Complete sequencing and characterization of 21,243 full-length human cDNAs.

Q6ZS62 COLC1_HUMAN Colorectal cancer-associated protein 1 COLCA1 C11orf92 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Human chromosome 11 DNA sequence and analysis including novel gene identification. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Identification of genes expressed by immune cells of the colon that are regulated by colorectal cancer-associated variants. TISSUE SPECIFICITY SUBCELLULAR LOCATION Membrane Single-pass membrane protein Co-localizes with crystalloid granules of eosinophils and granular organelles of mast cells, neutrophils, macrophages and dendritic cells. Expressed in gastrointestinal and immune tissue, as well as prostate, testis and ovary. Expressed in lamina propria and eosinophils but not in epithelial cells. Expression is greater in benign adjacent tissues than in colon tumors. Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MESCSVAQAGVLTSPFMWRWTGMAGALSALDNTIEDDADDQLPCGEGRPGWVRGELLGSQ GVCKDSKDLFVPTSSSLYGCFCVGLVSGMAISVLLLASDFRKLDFSRPEPCFEKEASLWF VAQH P14384 B2R800 Q9H2K9 CBPM_HUMAN Carboxypeptidase M CPM 3.4.17.12 CPM Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M. Comparison with carboxypeptidases A, B, H, and N. NUCLEOTIDE SEQUENCE [MRNA] PROTEIN SEQUENCE OF 18-48 Placenta SEQUENCE REVISION Type 2 diabetes locus on 12q15: further mapping and mutation screening of two candidate genes. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Molecular structure and alternative splicing of the human carboxypeptidase M gene. NUCLEOTIDE SEQUENCE [MRNA] Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Lung The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta Effect of mutation of two critical glutamic acid residues on the activity and stability of human carboxypeptidase M and characterization of its signal for glycosylphosphatidylinositol anchoring. PROTEIN SEQUENCE OF 18-21 GPI-ANCHOR AT SER-423 BIOPHYSICOCHEMICAL PROPERTIES FUNCTION CATALYTIC ACTIVITY SITE SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY MUTAGENESIS OF GLU-277; GLU-281 AND SER-423 Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115 AND ASN-164 Liver Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity. X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 18-443 IN COMPLEX WITH ZINC IONS DISULFIDE BONDS GLYCOSYLATION AT ASN-38 AND ASN-115 Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins. Cleavage of C-terminal arginine or lysine residues from polypeptides. Zn(2+) Binds 1 zinc ion per subunit. Inhibited by O-phenanthroline and MGTA and activated by cobalt. 59 uM for synthetic dansyl-Ala-Arg 57 uM for placental peptide hormones Optimum pH is 7.0. Cell membrane Lipid-anchor GPI-anchor Belongs to the peptidase M14 family. 3D-structure Carboxypeptidase Cell membrane Complete proteome Direct protein sequencing Disulfide bond Glycoprotein GPI-anchor Hydrolase Lipoprotein Membrane Metal-binding Metalloprotease Polymorphism Protease Reference proteome Signal Zinc R H V I E A E Q E Q S A T S P MDFPCLWLGLLLPLVAALDFNYHRQEGMEAFLKTVAQNYSSVTHLHSIGKSVKGRNLWVL VVGRFPKEHRIGIPEFKYVANMHGDETVGRELLLHLIDYLVTSDGKDPEITNLINSTRIH IMPSMNPDGFEAVKKPDCYYSIGRENYNQYDLNRNFPDAFEYNNVSRQPETVAVMKWLKT ETFVLSANLHGGALVASYPFDNGVQATGALYSRSLTPDDDVFQYLAHTYASRNPNMKKGD ECKNKMNFPNGVTNGYSWYPLQGGMQDYNYIWAQCFEITLELSCCKYPREEKLPSFWNNN KASLIEYIKQVHLGVKGQVFDQNGNPLPNVIVEVQDRKHICPYRTNKYGEYYLLLLPGSY IINVTVPGHDPHITKVIIPEKSQNFSALKKDILLPFQGQLDSIPVSNPSCPMIPLYRNLP DHSAATKPSLFLFLVSLLHIFFK P40259 Q53FS2 Q9BU06 CD79B_HUMAN B-cell antigen receptor complex-associated protein beta chain B-cell-specific glycoprotein B29 Ig-beta Immunoglobulin-associated B29 protein CD79b CD79B B29 IGB Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and sequencing of the cDNA encoding the human homologue of the murine immunoglobulin-associated protein B29. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG) Isolation and chromosomal mapping of the human immunoglobulin-associated B29 gene (IGB). NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG) The human Ig-beta cDNA sequence, a homologue of murine B29, is identical in B cell and plasma cell lines producing all the human Ig isotypes. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG) The complete sequence of the human CD79b (Ig beta/B29) gene: identification of a conserved exon/intron organization, immunoglobulin-like regulatory regions, and allelic polymorphism. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG) Alternative splicing of CD79a (Ig-alpha/mb-1) and CD79b (Ig-beta/B29) RNA transcripts in human B cells. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT) NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) Small intestine Spleen The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG) Lymph Isolation and chemical characterization of the human B29 and mb-1 proteins of the B cell antigen receptor complex. PROTEIN SEQUENCE OF 29-45 Cooperativity and segregation of function within the Ig-alpha/beta heterodimer of the B cell antigen receptor complex. FUNCTION B-cell antigen receptor-induced apoptosis requires both Ig alpha and Ig beta. FUNCTION B cell progenitors are arrested in maturation but have intact VDJ recombination in the absence of Ig-alpha and Ig-beta. FUNCTION Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Structural and functional studies of Igalphabeta and its assembly with the B cell antigen receptor. X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-159 SUBUNIT DISULFIDE BONDS A hypomorphic mutation in Igbeta (CD79b) in a patient with immunodeficiency and a leaky defect in B cell development. VARIANT AGM6 SER-137 Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation. Heterodimer of alpha and beta chains; disulfide-linked. Part of the B-cell antigen receptor complex where the alpha/beta chain heterodimer is non-covalently associated with an antigen-specific membrane-bound surface immunoglobulin of two heavy chains and two light chains. Interacts with LYN (By similarity). O43765 SGTA false 6 Cell membrane Single-pass type I membrane protein Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur outside lipid rafts. P40259-1 Long P40259-2 Short P40259-3 3 No experimental confirmation available. B-cells. Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-kinases such as BLK, LYN and SYK. Agammaglobulinemia 6, autosomal recessive AGM6 A primary immunodeficiency characterized by profoundly low or absent serum antibodies and low or absent circulating B-cells due to an early block of B-cell development. Affected individuals develop severe infections in the first years of life. The disease is caused by mutations affecting the gene represented in this entry. CD79B mutation db 3D-structure Adaptive immunity Alternative splicing Cell membrane Complete proteome Direct protein sequencing Disease mutation Disulfide bond Glycoprotein Immunity Immunoglobulin domain Membrane Phosphoprotein Reference proteome Signal Transmembrane Transmembrane helix A AA G S G A G R E A MARLALSPVPSHWMVALLLLLSAEPVPAARSEDRYRNPKGSACSRIWQSPRFIARKRGFT VKMHCYMNSASGNVSWLWKQEMDENPQQLKLEKGRMEESQNESLATLTIQGIRFEDNGIY FCQQKCNNTSEVYQGCGTELRVMGFSTLAQLKQRNTLKDGIIMIQTLLIILFIIVPIFLL LDKDDSKAGMEEDHTYEGLDIDQTATYEDIVTLRTGEVKWSVGEHPGQE P15169 B1AP59 CBPN_HUMAN Carboxypeptidase N catalytic chain CPN 3.4.17.3 Anaphylatoxin inactivator Arginine carboxypeptidase Carboxypeptidase N polypeptide 1 Carboxypeptidase N small subunit Kininase-1 Lysine carboxypeptidase Plasma carboxypeptidase B Serum carboxypeptidase N SCPN CPN1 ACBP Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1). NUCLEOTIDE SEQUENCE [MRNA] Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Liver NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Pancreas Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: comparison with other carboxypeptidases. PROTEIN SEQUENCE OF 21-67; 162-190; 329-343 AND 379-416 On the specificity of carboxypeptidase N, a comparative study. 3D-STRUCTURE MODELING Crystal structure of the human carboxypeptidase N (kininase I) catalytic domain. X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-458 SUBUNIT DISULFIDE BONDS GLYCOSYLATION AT THR-400; THR-402 AND THR-409 DNA polymorphism and mutations in CPN1, including the genomic basis of carboxypeptidase N deficiency. VARIANT CPND ASP-178 Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation. Release of a C-terminal basic amino acid, preferentially lysine. Zn(2+) Binds 1 zinc ion per subunit. Tetramer of two catalytic chains and two glycosylated inactive chains. Secreted Extracellular space Synthesized in the liver and secreted in plasma. Carboxypeptidase N deficiency CPND Patients affected present some combination of angioedema or chronic urticaria, as well as hay fever or asthma, and have also slightly depressed serum carboxy peptidase N, suggestive of autosomal recessive inheritance of this disorder. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the peptidase M14 family. 3D-structure Carboxypeptidase Complete proteome Direct protein sequencing Disease mutation Disulfide bond Glycoprotein Hydrolase Metal-binding Metalloprotease Protease Reference proteome Secreted Signal Zinc G D C R T E MSDLLSVFLHLLLLFKLVAPVTFRHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHL YVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRNQRIVQLIQD TRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPN HHLPLPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRT ASTPTPDDKLFQKLAKVYSYAHGWMFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHT NCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQVHQGIKGMVLDENYNNLANAVIS VSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGPAEPTLVNFHLKRSIP QVSPVRRAPSRRHGVRAKVQPQARKKEMEMRQLQRGPA P23508 D3DT05 Q6ZR04 CRCM_HUMAN Colorectal mutant cancer protein Protein MCC MCC Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of a gene located at chromosome 5q21 that is mutated in colorectal cancers. NUCLEOTIDE SEQUENCE [MRNA] VARIANTS ARG-190; GLN-506 AND VAL-698 Brain The DNA sequence and comparative analysis of human chromosome 5. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT ARG-190 Muscle Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-779 (ISOFORM 2) VARIANT ARG-190 Trachea Mutated in colorectal cancer, a putative tumor suppressor for serrated colorectal cancer, selectively represses beta-catenin-dependent transcription. FUNCTION IN WNT SIGNALING SUBCELLULAR LOCATION INTERACTION WITH CTNNB1 MCC, a new interacting protein for Scrib, is required for cell migration in epithelial cells. FUNCTION IN CELL MIGRATION SUBCELLULAR LOCATION INTERACTION WITH SCRIB; EZR; SNX27; SLC9A3R1 AND SLC9A3R2 Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell The PDZ-binding motif of MCC is phosphorylated at position -1 and controls lamellipodia formation in colon epithelial cells. FUNCTION PDZ-BINDING MOTIF PHOSPHORYLATION AT SER-828 INTERACTION WITH SCRIB AND MYH10 SUBCELLULAR LOCATION MUTAGENESIS OF SER-828 An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Mutations of chromosome 5q21 genes in FAP and colorectal cancer patients. VARIANTS LEU-267; LEU-486; LEU-490; GLN-506 AND VAL-698 MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in the cytoplasm. CHARACTERIZATION OF VARIANT GLN-506 FUNCTION SUBCELLULAR LOCATION INTERACTION WITH CCAR2 NUCLEAR LOCALIZATION SIGNAL MAGI2 mutations cause congenital nephrotic syndrome. VARIANT LYS-142 Candidate for the putative colorectal tumor suppressor gene located at 5q21. Suppresses cell proliferation and the Wnt/b-catenin pathway in colorectal cancer cells. Inhibits DNA binding of b-catenin/TCF/LEF transcription factors. Involved in cell migration independently of RAC1, CDC42 and p21-activated kinase (PAK) activation (PubMed:18591935, PubMed:19555689, PubMed:22480440). Represses the beta-catenin pathway (canonical Wnt signaling pathway) in a CCAR2-dependent manner by sequestering CCAR2 to the cytoplasm, thereby impairing its ability to inhibit SIRT1 which is involved in the deacetylation and negative regulation of beta-catenin (CTNB1) transcriptional activity (PubMed:24824780). Interacts with SCRIB (via phosphorylated PDZ-binding motif), EZR, SNX27, SLC9A3R1 and SLC9A3R2. Interacts with CTNNB1; the interaction is enhanced upon Wnt stimulation. Interacts with MYH10. Interacts with CCAR2. P49674 CSNK1E false 3 P29084 GTF2E2 false 2 P26045 PTPN3 false 2 Q14160 SCRIB false 14 Cell membrane Cell projection Lamellipodium Nucleus Cytoplasm Colocalizes with actin at the leading edge of polarized cells. P23508-1 1 P23508-2 2 Ref.5 (BAC87521) sequence is in conflict in position: 25:S->GSSSG. Expressed in a variety of tissues. Belongs to the MCC family. Alternative splicing Cell membrane Cell projection Complete proteome Cytoplasm Membrane Nucleus Phosphoprotein Polymorphism Reference proteome Tumor suppressor Wnt signaling pathway MNSGVAMKYGNDSSAELSE MMAAAAAAAAGSSSSGGGGGGSGSSSSSSDTSSTGEEERMRRLFQTCDGDGDGYISRNDLLMVCRQLNMEESVAEIMNQLGADENGKISFQDFTRCRMQLVREIRKEEVDLSAKSDNSCTKKLRDRIASWPTSSDNSLGALSAARESWEYDSGARDLQSPDVQSQSALQKLLEYGGSSLHQQAALHKLLTQSPHIGNSVGGSYLELANT E K K R R L P L S L R Q A V S C S A S D S G MNSGVAMKYGNDSSAELSELHSAALASLKGDIVELNKRLQQTERERDLLEKKLAKAQCEQ SHLMREHEDVQERTTLRYEERITELHSVIAELNKKIDRLQGTTIREEDEYSELRSELSQS QHEVNEDSRSMDQDQTSVSIPENQSTMVTADMDNCSDLNSELQRVLTGLENVVCGRKKSS CSLSVAEVDKHIEQLTTASEHCDLAIKTVEEIEGVLGRDLYPNLAEERSRWEKELAGLRE ENESLTAMLCSKEEELNRTKATMNAIREERDRLRRRVRELQTRLQSVQATGPSSPGRLTS TNRPINPSTGELSTSSSSNDIPIAKIAERVKLSKTRSESSSSDRPVLGSEISSIGVSSSV AEHLAHSLQDCSNIQEIFQTLYSHGSAISESKIREFEVETERLNSRIEHLKSQNDLLTIT LEECKSNAERMSMLVGKYESNATALRLALQYSEQCIEAYELLLALAESEQSLILGQFRAA GVGSSPGDQSGDENITQMLKRAHDCRKTAENAAKALLMKLDGSCGGAFAVAGCSVQPWES LSSNSHTSTTSSTASSCDTEFTKEDEQRLKDYIQQLKNDRAAVKLTMLELESIHIDPLSY DVKPRGDSQRLDLENAVLMQELMAMKEEMAELKAQLYLLEKEKKALELKLSTREAQEQAY LVHIEHLKSEVEEQKEQRMRSLSSTSSGSKDKPGKECADAASPALSLAELRTTCSENELA AEFTNAIRREKKLKARVQELVSALERLTKSSEIRHQQSAEFVNDLKRANSNLVAAYEKAK KKHQNKLKKLESQMMAMVERHETQVRMLKQRIALLEEENSRPHTNETSL Q6ZV80 CB091_HUMAN Uncharacterized protein C2orf91 C2orf91 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Hippocampus Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Complete proteome Reference proteome MVRMSRPLFLDWAWRPLCSPSQSLPLTYGPEGWILQWKGTCRQQTALHCPFDFPQAPLRG RHTLSQVPNKGHEKASAVQLPEKQGTDQSRRGPTSAVTKARTSYPESETFIVYLCSYFWN SSKGVYMSGST Q9NX46 Q53G94 Q6IAB8 Q9BY47 ARHL2_HUMAN ADP-ribose glycohydrolase ARH3 ADP-ribosylhydrolase 3 O-acetyl-ADP-ribose deacetylase ARH3 3.5.1.- Poly(ADP-ribose) glycohydrolase ARH3 3.2.1.143 [Protein ADP-ribosylarginine] hydrolase-like protein 2 [Protein ADP-ribosylserine] hydrolase 3.2.2.- ADPRHL2 ARH3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] A novel gene expressed in human liver cancer tissue. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Liver cancer Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT LYS-209 Thyroid The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Skin Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. FUNCTION TISSUE SPECIFICITY SUBCELLULAR LOCATION COFACTOR MUTAGENESIS OF 77-ASP--ASP-78; 238-GLU--GLU-239 AND 261-GLU--GLU-262 The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases. FUNCTION CATALYTIC ACTIVITY COFACTOR MUTAGENESIS OF 77-ASP-ASP-78; 261-GLU-GLU-262 AND 238-GLU-GLN-239 Functional localization of two poly(ADP-ribose)-degrading enzymes to the mitochondrial matrix. SUBCELLULAR LOCATION Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Hydrolysis of O-acetyl-ADP-ribose isomers by ADP-ribosylhydrolase 3. FUNCTION CATALYTIC ACTIVITY ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose). FUNCTION CATALYTIC ACTIVITY SUBCELLULAR LOCATION Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-64 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia Serine ADP-ribosylation reversal by the hydrolase ARH3. FUNCTION CATALYTIC ACTIVITY MUTAGENESIS OF ASP-77; 77-ASP--ASP-78 AND ASP-78 Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase. FUNCTION CATALYTIC ACTIVITY MUTAGENESIS OF GLU-41; ASP-77; 77-ASP-ASP-78; GLY-115; SER-148; TYR-149; HIS-182; ASP-314 AND THR-317 Biallelic mutations in ADPRHL2, encoding ADP-ribosylhydrolase 3, lead to a degenerative pediatric stress-induced epileptic ataxia syndrome. INVOLVEMENT IN CONDSIAS VARIANTS CONDSIAS ASN-34; PRO-79; 106-GLN--SER-363 DEL; LEU-177 AND 334-GLN--SER-363 DEL CHARACTERIZATION OF VARIANTS CONDSIAS PRO-79; 106-GLN--SER-363 DEL AND 334-GLN--SER-363 DEL Bi-allelic ADPRHL2 mutations cause neurodegeneration with developmental delay, ataxia, and axonal neuropathy. INVOLVEMENT IN CONDSIAS VARIANTS CONDSIAS 248-LYS-ILE-249 DELINS ASN; GLY-335 AND 346-TYR--SER-363 DEL FUNCTION CHARACTERIZATION OF VARIANTS CONDSIAS 248-LYS-ILE-249 DELINS ASN AND GLY-335 Serine is the major residue for ADP-ribosylation upon DNA damage. FUNCTION The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation. X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-363 SUBUNIT MUTAGENESIS OF GLU-41; ASP-77; SER-148; TYR-149; ASN-151; HIS-182; ASP-314 AND THR-317 The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase. X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 19-363 SUBSTRATE-BINDING SITE METAL-BINDING SITES Structure-function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation. X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 19-363 IN COMPLEX WITH MAGNESIUM AND ADP-RIBOSE FUNCTION COFACTOR ACTIVITY REGULATION SUBCELLULAR LOCATION MUTAGENESIS OF GLU-41; ASP-77; SER-148; TYR-149; HIS-182; ASP-314 AND THR-317 Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND ADP-RIBOSE FUNCTION SUBSTRATE SPECIFICITY ACTIVITY REGULATION COFACTOR MUTAGENESIS OF ASP-314 ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (PubMed:21498885, PubMed:30045870, PubMed:29907568, PubMed:30401461). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (PubMed:28650317, PubMed:29234005, PubMed:30045870). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:29480802). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (PubMed:16278211). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:16278211). Also hydrolyzes free poly(ADP-ribose) in mitochondria (PubMed:22433848). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (PubMed:17075046, PubMed:21498885). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (PubMed:21498885). [(1''->2')-ADP-alpha-D-ribose]n + H2O = [(1''->2')-ADP-alpha-D-ribose]n-1 + ADP-D-ribose 1''-O-acetyl-ADP-alpha-D-ribose + H2O = acetate + ADP-D-ribose + H(+) H2O + O-(ADP-D-ribosyl)-L-seryl-[protein] = ADP-D-ribose + L-seryl-[protein] Mg(2+) Binds 2 magnesium ions per subunit. The protein undergoes a dramatic conformational switch from closed to open states upon substrate-binding, which enables specific substrate recognition for the 1''-O-linkage (PubMed:29907568). The glutamate flap (Glu-41) blocks substrate entrance to Mg(2+) in the unliganded closed state (PubMed:30045870, PubMed:29907568). In presence of substrate, Glu-41 is ejected from the active site: this closed-to-open transition significantly widens the substrate-binding channel and precisely positions the scissile 1''-O-linkage for cleavage while securing tightly 2'- and 3'-hydroxyls of ADP-ribose (PubMed:30045870, PubMed:29907568). Monomer. Nucleus Cytoplasm Chromosome Mitochondrion matrix Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites. Ubiquitous. Neurodegeneration, childhood-onset, stress-induced, with variable ataxia and seizures CONDSIAS An autosomal recessive neurodegenerative disorder characterized by pediatric onset of progressive brain atrophy, developmental regression, and seizures in association with periods of stress, such as infections. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the ADP-ribosylglycohydrolase family. 3D-structure Chromosome Complete proteome Cytoplasm Disease mutation DNA damage DNA repair Hydrolase Magnesium Metal-binding Mitochondrion Neurodegeneration Nucleus Phosphoprotein Polymorphism Reference proteome D N T P S L E K KI N V G E A Q DD AA DD NN D N A D N G D S A Y A N A H Q A EE QQ EE QQ D A E D N T A T S K E MAAAAMAAAAGGGAGAARSLSRFRGCLAGALLGDCVGSFYEAHDTVDLTSVLRHVQSLEP DPGTPGSERTEALYYTDDTAMARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGV VTVFKKLLNPKCRDVFEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQL THASSLGYNGAILQALAVHLALQGESSSEHFLKQLLGHMEDLEGDAQSVLDARELGMEER PYSSRLKKIGELLDQASVTREEVVSELGNGIAAFESVPTAIYCFLRCMEPDPEIPSAFNS LQRTLIYSISLGGDTDTIATMAGAIAGAYYGMDQVPESWQQSCEGYEETDILAQSLHRVF QKS P41240 Q2M3N2 Q6FGZ6 CSK_HUMAN Tyrosine-protein kinase CSK 2.7.10.2 C-Src kinase Protein-tyrosine kinase CYL CSK Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo CYL encodes a putative cytoplasmic tyrosine kinase lacking the conserved tyrosine autophosphorylation site (Y416src). NUCLEOTIDE SEQUENCE [MRNA] PHOSPHORYLATION AT TYR-416 Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase. NUCLEOTIDE SEQUENCE [MRNA] Lung Isolation and characterization of a human gene that encodes a new subclass of protein tyrosine kinases. NUCLEOTIDE SEQUENCE [GENOMIC DNA] TISSUE SPECIFICITY Characterization of the human CSK locus. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS ASP-287; GLN-398 AND ARG-442 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Uterus The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity. FUNCTION IN PHOSPHORYLATION OF LCK CATALYTIC ACTIVITY COFACTOR Recombinant Csk expressed in Escherichia coli is autophosphorylated on tyrosine residue(s). AUTOPHOSPHORYLATION CATALYTIC ACTIVITY Expression, purification, and initial characterization of human Yes protein tyrosine kinase from a bacterial expression system. FUNCTION IN PHOSPHORYLATION OF YES1 CATALYTIC ACTIVITY COFACTOR Identification of csk tyrosine phosphorylation sites and a tyrosine residue important for kinase domain structure. PHOSPHORYLATION AT TYR-184 AND TYR-304 MUTAGENESIS OF TYR-184 AND TYR-304 Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn. INTERACTION WITH TGFB1I1 Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. INTERACTION WITH PAG1 Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein). INTERACTION WITH SIT1 Activation of the COOH-terminal Src kinase (Csk) by cAMP-dependent protein kinase inhibits signaling through the T cell receptor. PHOSPHORYLATION AT SER-364 BY PKA MUTAGENESIS OF SER-364 LIME: a new membrane raft-associated adaptor protein involved in CD4 and CD8 coreceptor signaling. INTERACTION WITH LIME1 A missense single-nucleotide polymorphism in a gene encoding a protein tyrosine phosphatase (PTPN22) is associated with rheumatoid arthritis. INTERACTION WITH PTPN22 C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK) -- endogenous negative regulators of Src-family protein kinases. REVIEW p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity. INTERACTION WITH SRCIN1 Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] The tyrosine kinase Csk dimerizes through Its SH3 domain. HOMODIMERIZATION Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] RhoH modulates pre-TCR and TCR signalling by regulating LCK. INTERACTION WITH RHOH SCIMP, a transmembrane adapter protein involved in major histocompatibility complex class II signaling. INTERACTION WITH SCIMP The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop. X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-71 Patterns of somatic mutation in human cancer genomes. VARIANT [LARGE SCALE ANALYSIS] LEU-45 Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN, CSK or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK. ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] Mg(2+) Mn(2+) Homodimer (via SH3-domain) (PubMed:19888460). Interacts with PTPN22 (PubMed:15208781). Interacts with phosphorylated SIT1, PAG1, LIME1 and TGFB1I1; these interactions serve to recruit CSK to the membrane where it can phosphorylate and inhibit Src-family kinases (PubMed:11433379, PubMed:10790433, PubMed:14610046, PubMed:10838081). Interacts with SRCIN1 (PubMed:17525734). Interacts with RHOH (PubMed:20851766). Interacts (via SH2 domain) with SCIMP (PubMed:21930792).Interacts (via SH2 domain) with PRAG1 (when phosphorylated at 'Tyr-391'); this interaction prevents translocation of CSK from the cytoplasm to the membrane leading to increased activity of CSK (By similarity). false 7 P08069 IGF1R false 5 Q9NWQ8 PAG1 false 3 P08575 PTPRC false 3 P49023 PXN false 2 P00523 SRC true 6 Cytoplasm Cell membrane Mainly cytoplasmic, also present in lipid rafts. Expressed in lung and macrophages. The architecture of this protein is similar to that of Src-family kinases (SFKs) with one N-terminal SH3 domain, one SH2 domain, and a C-terminal kinase domain. Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated. Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily. 3D-structure Acetylation Adaptive immunity ATP-binding Cell membrane Complete proteome Cytoplasm Immunity Kinase Magnesium Manganese Membrane Metal-binding Nucleotide-binding Phosphoprotein Polymorphism Reference proteome SH2 domain SH3 domain Transferase Tyrosine-protein kinase P L G D R Q H R Y F Y F S A MSAIQAAWPSGTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGII PANYVQKREGVKAGTKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCV SCDGKVEHYRIMYHASKLSIDEEVYFENLMQLVEHYTSDADGLCTRLIKPKVMEGTVAAQ DEFYRSGWALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVM TQLRHSNLVQLLGVIVEEKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCE AMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVKWTAPEALRE KKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYEVMK NCWHLDAAMRPSFLQLREQLEHIKTHELHL P35858 B4DZY8 E9PGU3 ALS_HUMAN Insulin-like growth factor-binding protein complex acid labile subunit ALS IGFALS ALS Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Structure and functional expression of the acid-labile subunit of the insulin-like growth factor-binding protein complex. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) PARTIAL PROTEIN SEQUENCE Liver Conservation of a growth hormone-responsive promoter element in the human and mouse acid-labile subunit genes. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Thymus The sequence and analysis of duplication-rich human chromosome 16. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] High molecular weight insulin-like growth factor binding protein complex. Purification and properties of the acid-labile subunit from human serum. PROTEIN SEQUENCE OF 28-35 Deficiency of the circulating insulin-like growth factor system associated with inactivation of the acid-labile subunit gene. INVOLVEMENT IN ACLSD Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-368 AND ASN-515 Plasma Total absence of functional acid labile subunit, resulting in severe insulin-like growth factor deficiency and moderate growth failure. VARIANT ACLSD ASN-440 Phenotypic effects of null and haploinsufficiency of acid-labile subunit in a family with two novel IGFALS gene mutations. VARIANTS ACLSD SER-LEU-ARG-197 INS AND ARG-540 Primary acid-labile subunit deficiency due to recessive IGFALS mutations results in postnatal growth deficit associated with low circulating insulin growth factor (IGF)-I, IGF binding protein-3 levels, and hyperinsulinemia. VARIANT ACLSD SER-276 Three novel IGFALS gene mutations resulting in total ALS and severe circulating IGF-I/IGFBP-3 deficiency in children of different ethnic origins. VARIANTS ACLSD SER-60; PHE-244 AND LEU-GLU-LEU-439 INS Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-368 Liver Acid-labile subunit deficiency and growth failure: description of two novel cases. VARIANTS ACLSD LEU-73 AND GLN-134 Acid-labile subunit (ALS) deficiency. INVOLVEMENT IN ACLSD A novel mutation in IGFALS, c.380T>C (p.L127P), associated with short stature, delayed puberty, osteopenia and hyperinsulinaemia in two siblings: insights into the roles of insulin growth factor-1 (IGF1). VARIANT IN ACLSD PRO-127 Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion. Forms a ternary complex of about 140 to 150 kDa with IGF-I or IGF-II and IGFBP-3. Secreted Extracellular space P35858-1 1 P35858-2 2 No experimental confirmation available. Plasma. Acid-labile subunit deficiency ACLSD A disorder characterized by severely reduced serum IGF-I and IGFBP-3 concentrations and mild growth retardation. Pubertal delay in boys and insulin insensitivity are common findings. The disease is caused by mutations affecting the gene represented in this entry. Alternative splicing Cell adhesion Complete proteome Direct protein sequencing Disease mutation Glycoprotein Leucine-rich repeat Polymorphism Reference proteome Repeat Secreted Signal K KAGDLEPQFTPERRFRLCWYQAHSGRALLGPPPQASPPA C S P L L F L P L Q R RSLR L F N S P L L LLEL D N P S C R R W L P MALRKGGLALALLLLSWVALGPRSLEGADPGTPGEAEGPACPAACVCSYDDDADELSVFC SSRNLTRLPDGVPGGTQALWLDGNNLSSVPPAAFQNLSSLGFLNLQGGQLGSLEPQALLG LENLCHLHLERNQLRSLALGTFAHTPALASLGLSNNRLSRLEDGLFEGLGSLWDLNLGWN SLAVLPDAAFRGLGSLRELVLAGNRLAYLQPALFSGLAELRELDLSRNALRAIKANVFVQ LPRLQKLYLDRNLIAAVAPGAFLGLKALRWLDLSHNRVAGLLEDTFPGLLGLRVLRLSHN AIASLRPRTFKDLHFLEELQLGHNRIRQLAERSFEGLGQLEVLTLDHNQLQEVKAGAFLG LTNVAVMNLSGNCLRNLPEQVFRGLGKLHSLHLEGSCLGRIRPHTFTGLSGLRRLFLKDN GLVGIEEQSLWGLAELLELDLTSNQLTHLPHRLFQGLGKLEYLLLSRNRLAELPADALGP LQRAFWLDVSHNRLEALPNSLLAPLGRLRYLSLRNNSLRTFTPQPPGLERLWLEGNPWDC GCPLKALRDFALQNPSAVPRFVQAICEGDDCQPPAYTYNNITCASPPEVVGLDLRDLSEA HFAPC Q5SW96 A2BHI5 Q6TQS9 Q8N2Y0 Q9UFI9 ARH_HUMAN Low density lipoprotein receptor adapter protein 1 Autosomal recessive hypercholesterolemia protein LDLRAP1 ARH Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Autosomal recessive hypercholesterolemia caused by mutations in a putative LDL receptor adaptor protein. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT PRO-202 VARIANT ARH HIS-202 Molecular mechanisms of autosomal recessive hypercholesterolemia. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT PRO-202 The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT PRO-202 Uterus The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT PRO-202 Brain ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2. INTERACTION WITH LDLR; CLATHRIN AND AP-2 COMPLEX MUTAGENESIS OF PHE-165; 212-LEU-LEU-213; ASP-214; GLU-216 AND ARG-266 MOTIF REGION The autosomal recessive hypercholesterolemia (ARH) protein interfaces directly with the clathrin-coat machinery. CHARACTERIZATION INTERACTION WITH CLATHRIN AND AP-2 COMPLEX SUBCELLULAR LOCATION Functional dissection of an AP-2 beta2 appendage-binding sequence within the autosomal recessive hypercholesterolemia protein. FUNCTION INTERACTION WITH AP2B1 Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly. INTERACTION WITH AP2B1 MUTAGENESIS OF ASP-256 A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-186 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly. X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 252-267 IN COMPLEX WITH AP2B1 DOMAIN A novel Thr56Met mutation of the autosomal recessive hypercholesterolemia gene associated with hypercholesterolemia. VARIANTS MET-56 AND PRO-202 Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytocis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface. Required for trafficking of LRP2 to the endocytic recycling compartment which is necessary for LRP2 proteolysis, releasing a tail fragment which translocates to the nucleus and mediates transcriptional repression (By similarity). Interacts (via PID domain) with LDLR (via NPXY motif) (PubMed:12221107). Binds to soluble clathrin trimers (PubMed:12221107). Interacts with AP2B1; the interaction mediates the association with the AP-2 complex (PubMed:12221107). Interacts with VLDLR (By similarity). Interacts with LRP2 (By similarity). P63010 AP2B1 false 4 P63010-2 AP2B1 false 4 P31273 HOXC8 false 4 Q9UPT6 MAPK8IP3 false 4 Q8NDX1-2 PSD4 false 5 Q9H668 STN1 false 8 Cytoplasm Expressed at high levels in the kidney, liver, and placenta, with lower levels detectable in brain, heart, muscle, colon, spleen, intestine, lung, and leukocytes. The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1. The PID domain mediates interaction with the NPXY internalization motif of LDLR. Hypercholesterolemia, autosomal recessive ARH A familial condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins. The disease is caused by mutations affecting the gene represented in this entry. 3D-structure Acetylation Atherosclerosis Cholesterol metabolism Complete proteome Cytoplasm Disease mutation Endocytosis Hyperlipidemia Lipid metabolism Phosphoprotein Polymorphism Reference proteome Steroid metabolism Sterol metabolism T M S H S P F A F V LL AA D A E A D R R A MDALKSAGRALIRSPSLAKQSWGGGGRHRKLPENWTDTRETLLEGMLFSLKYLGMTLVEQ PKGEELSAAAIKRIVATAKASGKKLQKVTLKVSPRGIILTDNLTNQLIENVSIYRISYCT ADKMHDKVFAYIAQSQHNQSLECHAFLCTKRKMAQAVTLTVAQAFKVAFEFWQVSKEEKE KRDKASQEGGDVLGARQDCTPSLKSLVATGNLLDLEETAKAPLSTVSANTTNMDEVPRPQ ALSGSSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLTAQDMHYAQCLSPVDWDKPDSSGT EQDDLFSF Q7Z6I8 D3DQA7 Q86Y53 Q8N1T9 CE024_HUMAN UPF0461 protein C5orf24 C5orf24 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Physical and hematopoietic transcript map of a 5q31 critical subregion associated with the 5q- syndrome. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) Blood Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Corpus callosum NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Skin ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic kidney Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-180 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia Uncovering global SUMOylation signaling networks in a site-specific manner. SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75 AND LYS-184 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] O95967 EFEMP2 false 3 Q7Z6I8-1 1 Q7Z6I8-2 2 Belongs to the UPF0461 family. Alternative splicing Complete proteome Isopeptide bond Phosphoprotein Reference proteome Ubl conjugation SIKALSRLADLGYGCGTAAFPYPMMHGRAVHGVEETSSEVKPPNE KKQQAFRCSSDA A V MMHPVASSNPAFCGPGKPSCLNEDAMRAADQFDIYSSQQSKYSHTVNHKPMVCQRQDPLN ETHLQTTSGRSIEIKDELKKKKNLNRSGKRGRPSGTTKSAGYRTSTGRPLGTTKAAGFKT SPGRPLGTTKAAGYKVSPGRPPGSIKALSRLADLGYGCGTAAFPYPMMHGRAVHGVEETS SEVKPPNE Q9BS16 Q9H4L0 CENPK_HUMAN Centromere protein K CENP-K Interphase centromere complex protein 37 Protein AF-5alpha p33 CENPK ICEN37 FKSG14 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Fusion of the MLL gene with two different genes, AF-6 and AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8 and 11 in infant leukemia. NUCLEOTIDE SEQUENCE [MRNA] CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1 TISSUE SPECIFICITY Molecular cloning of human p33. NUCLEOTIDE SEQUENCE [MRNA] Molecular cloning of FKSG14, a novel gene located on chromosome 5. NUCLEOTIDE SEQUENCE [MRNA] Carcinoma The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Gall bladder Comprehensive analysis of the ICEN (Interphase Centromere Complex) components enriched in the CENP-A chromatin of human cells. FUNCTION SUBCELLULAR LOCATION The CENP-H-I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres. IDENTIFICATION BY MASS SPECTROMETRY IDENTIFICATION IN A COMPLEX WITH CENPH; CENPI; CENPN; CENPO; CENPP; CENPQ; CENPR AND CENPU FUNCTION SUBCELLULAR LOCATION The human CENP-A centromeric nucleosome-associated complex. IDENTIFICATION BY MASS SPECTROMETRY IDENTIFICATION IN THE CENPA-CAD COMPLEX WITH CENPI; CENPL; CENPO; CENPP; CENPQ; CENPR AND CENPS KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly in vertebrates. FUNCTION CENP-K and CENP-H may form coiled-coils in the kinetochores. INTERACTION WITH CENPH Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Acts in coordination with KNL1 to recruit the NDC80 complex to the outer kinetochore. Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex interacts with the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Interacts directly with CENPH. Q86V28 false 3 Q9H3R5 CENPH false 5 Q96HT8 MRFAP1L1 false 3 Nucleus Chromosome Centromere Chromosome Centromere Kinetochore Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex. Detected in several fetal organs with highest levels in fetal liver. In adults, it is weakly expressed in lung and placenta. Chromosomal aberrations involving CENPK are a cause of acute leukemias. Translocation t(5;11)(q12;q23) with KMT2A/MLL1. Belongs to the CENP-K/MCM22 family. Centromere Chromosomal rearrangement Chromosome Coiled coil Complete proteome Kinetochore Nucleus Reference proteome I M L W C G W G T I MNQEDLDPDSTTDVGDVTNTEEELIRECEEMWKDMEECQNKLSLIGTETLTDSNAQLSLL IMQVKCLTAELSQWQKKTPETIPLTEDVLITLGKEEFQKLRQDLEMVLSTKESKNEKLKE DLEREQRWLDEQQQIMESLNVLHSELKNKVETFSESRIFNELKTKMLNIKEYKEKLLSTL GEFLEDHFPLPDRSVKKKKKNIQESSVNLITLHEMLEILINRLFDVPHDPYVKISDSFWP PYVELLLRNGIALRHPEDPTRIRLEAFHQ Q9BV29 A8KAL4 Q86TC4 Q8N788 Q8NAR7 CCD32_HUMAN Coiled-coil domain-containing protein 32 CCDC32 C15orf57 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) VARIANT ILE-2 Brain Uterus The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT ILE-2 Skeletal muscle NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Lung N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Q9NUX5 POT1 false 2 Q9BV29-1 1 Q9BV29-2 2 No experimental confirmation available. Q9BV29-3 3 No experimental confirmation available. Alternative splicing Coiled coil Complete proteome Polymorphism Reference proteome M MRGSGLRFQM S R K I MKMFESADSTATRSGQDLWAEICSCLPNPEQEDGANNAFSDSFVDSCPEGEGQREVADFA VQPAVKPWAPLQDSEVYLASLEKKLRRIKGLNQEVTSKDMLRTLAQAKKECWDRFLQEKL ASEFFVDGLDSDESTLEHFKRWLQPDKVAVSTEEVQYLIPPESQVEKPVAEDEPAAGDKP AAAEQ Q4G0S7 B3KXI4 B4E0P7 Q5BLP6 CC152_HUMAN Coiled-coil domain-containing protein 152 CCDC152 Chr5_400 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Substantia nigra Thymus The DNA sequence and comparative analysis of human chromosome 5. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis Comparative gene finding in chicken indicates that we are closing in on the set of multi-exonic widely expressed human genes. NUCLEOTIDE SEQUENCE [MRNA] OF 1-61 (ISOFORM 1) TISSUE SPECIFICITY Q4G0S7-1 1 Q4G0S7-2 2 No experimental confirmation available. Detected in stomach. Translation N-terminally shortened. Alternative splicing Coiled coil Complete proteome Polymorphism Reference proteome R H E V Q K MDQSSEGCMKKISSVNLDKLINDFSQIEKKMVETNGKNNILDIQLEKSNCLLKVMQAKEV SIKEECATLHNIIKGLQQTIEYQQNLKGENEQLKISADLIKEKLKSHEQEYKNNIAKLVS EMKIKEEGYKKEISKLYQDMQRKVELNEEKHKELIEKKEMEISELNAKLRSQEKEKQNEI IKLQLEFDAKLARVQTKSKSYQDSTVLPQSIYRRKLQHFQEEKNKEIAILRNTIRDLEQR LSVGKDSHLKRRRF P30443 O77964 O78171 Q9MYA3 Q9TP25 Q9TQP5 1A01_HUMAN HLA class I histocompatibility antigen, A-1 alpha chain Human leukocyte antigen A*01 HLA-A*01 HLA-A HLAA Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The HLA-A,B,C genotype of the class I negative cell line Daudi reveals novel HLA-A and -B alleles. NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*01:02) Diversity and diversification of HLA-A,B,C alleles. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01) Nucleotide sequence of an HLA-A1 gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01) A generic sequencing based typing approach for the identification of HLA-A diversity. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:03) A nucleotide insertion in exon 4 is responsible for the absence of expression of an HLA-A*01 allele. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01) Seventeen more novel HLA-A locus alleles. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:06) High frequency of HLA-A*0103 allele in a Somali population. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:03) Blood A new HLA-A*01 allele. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:07) NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01) The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE A*01:01) Brain A nonapeptide encoded by human gene MAGE-1 is recognized on HLA-A1 by cytolytic T lymphocytes directed against tumor antigen MZ2-E. FUNCTION HLA-A1 and HLA-A3 T cell epitopes derived from influenza virus proteins predicted from peptide binding motifs. FUNCTION INTERACTION WITH B2M AND PEPTIDE Endogenous peptides with distinct amino acid anchor residue motifs bind to HLA-A1 and HLA-B8. FUNCTION INTERACTION WITH B2M AND PEPTIDE Identification of a highly immunogenic HLA-A*01-binding T cell epitope of WT1. FUNCTION A mechanism for the HLA-A*01-associated risk for EBV+ Hodgkin lymphoma and infectious mononucleosis. FUNCTION Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110 Liver Production of an antigenic peptide by insulin-degrading enzyme. FUNCTION Nomenclature for factors of the HLA system, 2010. NOMENCLATURE An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352; SER-356 AND SER-359 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] A comprehensive analysis of peptides presented by HLA-A1. FUNCTION Measuring Antiviral Capacity of T Cell Responses to Adenovirus. FUNCTION Conformational changes within the HLA-A1:MAGE-A1 complex induced by binding of a recombinant antibody fragment with TCR-like specificity. X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-298 IN COMPLEX WITH B2M AND PEPTIDE FUNCTION DOMAIN DISULFIDE BOND Preexisting CD8+ T-cell immunity to the H7N9 influenza A virus varies across ethnicities. X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-308 IN COMPLEX WITH B2M AND PEPTIDE FUNCTION DOMAIN Direct molecular mimicry enables off-target cardiovascular toxicity by an enhanced affinity TCR designed for cancer immunotherapy. X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 25-298 IN COMPLEX WITH B2M AND PEPTIDE FUNCTION DOMAIN DISULFIDE BOND Initial characterization of the human central proteome. VARIANT [LARGE SCALE ANALYSIS] THR-166 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Antigen-presenting major histocompatibility complex class I (MHCI) molecule, HLA-A*01 serotype. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-A*01-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:1402688, PubMed:7504010, PubMed:17189421, PubMed:19177349, PubMed:26758806, PubMed:24395804). May also present self-peptides, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:25880248, PubMed:7506728). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells. Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome or via endopeptidase IDE/insulin-degrading enzyme (PubMed:17189421, PubMed:20364150). Can bind different peptides that share a common structural motif defined by the nature of the peptide anchor residues. HLA-A*01:01 presents a restricted peptide repertoire including viral epitopes derived from IAV NP/nucleoprotein (CTELKLSDY), IAV PB1/polymerase basic protein 1 (VSDGGPNLY), HAdV-11 capsid L3/hexon protein (LTDLGQNLLY) as well as tumor peptide antigens including MAGE1 (EADPTGHSY), MAGEA3 (EVDPIGHLY) and WT1 (TSEKRPFMCAY), all having in common a canonical motif with a negatively charged Asp or Glu residue at position 3 and a Tyr anchor residue at C-terminal (PubMed:1402688, PubMed:7504010, PubMed:17189421, PubMed:20364150, PubMed:25880248, PubMed:30530481, PubMed:24395804, PubMed:26758806). A number of HLA-A*01:01-restricted peptides carry a post-translational modification with oxidation and N-terminal acetylation being the most frequent (PubMed:25880248). Fails to present highly immunogenic peptides from the EBV latent antigens (PubMed:18779413). Heterotrimer that consists of an alpha chain HLA-A*01, a beta chain B2M and a peptide (peptide-HLA-A*01-B2M) (PubMed:19177349, PubMed:24395804, PubMed:26758806, PubMed:7504010, PubMed:7506728). Early in biogenesis, HLA-A-B2M dimer interacts with the components of the peptide-loading complex composed of TAPBP, TAP1-TAP2, TAPBPL, PDIA3/ERP57 and CALR. Interacts with TAP1-TAP2 transporter via TAPBP; this interaction is obligatory for the loading of peptide epitopes delivered to the ER by TAP1-TAP2 transporter. Interacts with TAPBPL; TAPBPL binds peptide-free HLA-A-B2M complexes or those loaded with low affinity peptides, likely facilitating peptide exchange for higher affinity peptides. Only optimally assembled peptide-HLA-A-B2M trimer translocates to the surface of antigen-presenting cells, where it interacts with TCR and CD8 coreceptor on the surface of T cells. HLA-A (via polymorphic alpha-1 and alpha-2 domains) interacts with antigen-specific TCR (via CDR3 domains). One HLA-A molecule (mainly via nonpolymorphic alpha-3 domain) interacts with one CD8A homodimer (via CDR-like loop); this interaction insures peptide-HLA-A-B2M recognition by CD8-positive T cells only (By similarity). Q14943 KIR3DS1 false 2 Cell membrane Single-pass type I membrane protein Endoplasmic reticulum membrane Single-pass type I membrane protein Ubiquitous. The alpha-1 domain is a structural part of the peptide-binding cleft. The alpha-2 domain is a structural part of the peptide-binding cleft (PubMed:19177349, PubMed:26758806, PubMed:24395804). Mediates the interaction with TAP1-TAP2 complex (By similarity). The alpha-3 Ig-like domain mediates the interaction with CD8 coreceptor. The HLA-A*01 allele group comprises at least 297 different alleles. Polymorphic residues encode for alpha-1 and alpha-2 domains of the peptide-binding cleft, where they contribute to variations in peptide binding and TCR recognition among different alleles. The sequence shown is that of HLA-A*01:01. Belongs to the MHC class I family. Immuno Polymorphism Database-ImMunoGeneTics/HLA The Immune Epitope Database 3D-structure Adaptive immunity Cell membrane Complete proteome Disulfide bond Endoplasmic reticulum Glycoprotein Host-virus interaction Immunity Immunoglobulin domain Membrane MHC I Phosphoprotein Polymorphism Reference proteome Signal Sulfation Transmembrane Transmembrane helix F S R S G R R G M V A E D A I M G W F L N K I T R H R L V A R H MAVMAPRTLLLLLSGALALTQTWAGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRF DSDAASQKMEPRAPWIEQEGPEYWDQETRNMKAHSQTDRANLGTLRGYYNQSEDGSHTIQ IMYGCDVGPDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAVHAAEQR RVYLEGRCVDGLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLT WQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEL SSQPTIPIVGIIAGLVLLGAVITGAVVAAVMWRRKSSDRKGGSYTQAASSDSAQGSDVSL TACKV Q9P1Z9 Q2KHR6 Q5VV25 Q68DP5 Q69YV9 Q6AHY0 CC180_HUMAN Coiled-coil domain-containing protein 180 CCDC180 C9orf174 KIAA1529 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Brain The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) Testis DNA sequence and analysis of human chromosome 9. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-583 (ISOFORM 2) Uterus Q9P1Z9-2 2 No experimental confirmation available. Q9P1Z9-3 3 No experimental confirmation available. Readthrough transcript which is the product of an upstream read-through pseudogene (SUGT1P4-STRA6LP) with CCDC180. Readthrough transcript which is the product of an upstream read-through pseudogene (SUGT1P4-STRA6LP) with CCDC180. Intron retention. Translation N-terminally shortened. Alternative splicing Coiled coil Complete proteome Polymorphism Reference proteome P H S R L H P R E K S C F L D N L F K M L P N I E D MRGGENRPPARVQSSSEELELRHQSLDAFPGRRLPGRGIQPAAKMSSVGKVTQVPNGKAY QQIFQAEVQLVHSLAATRKRAAERSVTLKSGRIPMMKKVETPEGEVMSPRQQKWMHSLPN DWIMENPVLHREKERAKREKARESENTIAAREVRGLMDTIVPEKISTSTFQRQAEHKRKS YESALASFQEEIAQVGKEMEPLIVDTGGLFLKKLTESDEEMNRLFLKVENDTNLEDYTIQ ALLELWDKVAGRLLLRKQEIKELDEALHSLEFSRTDKLKSVLKKYAEVIEKTSYLMRPEV YRLINEEAMVMNYALLGNRKALAQLFVNLMESTLQQELDSRHRWQGLVDTWKALKKEALL QSFSEFMASESIHTPPAVTKELEVMLKTQNVLQQRRLKHLCTICDLLPPSYSKTQLTEWH SSLNSLNKELDTYHVDCMMRIRLLYEKTWQECLMHVQNCKKQLLDWKAFTEEEAETLVNQ FFFQMVGALQGKVEEDLELLDKSFETLADQTEWQSSHLFKYFQEVVQLWEAHQSELLVQE LELEKRMEQHRQKHSLESQVQEAHLDRLLDQLRQQSDKETLAFHLEKVKDYLKNMKSRYE CFHTLLTKEVMEYPAIMLKELNSYSSALSQYFFVREIFEQNLAGEVIFKFRQPEAHEKPS QKRVKKLRKKQGSKEDMTRSEESISSGTSTARSVEEVEEENDQEMESFITEEVLGQQKKS PLHAKMDESKEGSIQGLEEMQVEREGSLNPSLNEENVKGQGEKKEESEEEDEKEEEEEEE KLEEEKEEKEAQEEQESLSVGEEEDKEEGLEEIYYEDMESFTISSGNTYFVFVPLEEEHC RKSHSTFSAMFINDTSSAKFIEQVTIPSRLILEIKKQLRAGFFEHLEKWFDQCSLNTRVT VATKINELDSELELHLHLHQPRAQQIEKDIHNVRAAELLLHQEQLDSHCAGVTETLKKKR LMFCQFQEEQNVRSKNFRLKIYDMEHIFLNATRSQKLVTLSNTLHQELLSYVDVTQVSLR SFRQYLEESLGKLRYSNIEFIKHCRLFSEGGNFSPKEINSLCSRLEKEAARIELVESVIM LNMEKLENEYLDQANDVINKFESKFHNLSVDLIFIEKIQRLLTNLQVKIKCQVAKSNSQT NGLNFSLQQLQNKIKTCQESRGEKTTVTTEELLSFVQTWKEKLSQRIQYLNCSLDRVSMT ELVFTNTILKDQEEDSDILTSSEALEEEAKLDVVTPESFTQLSRVGKPLIEDPAVDVIRK LLQLPNTKWPTHHCDKDPSQTGRGAWACGSRGSSEAGAGGAVCSPPVLCSCPGPSSPKGF KRHRCQPENSGKKAVPSASATSAGSFTPHPKPNKMERKYRVLGDKPPPAAEDFKGIILTL LWESSENLLTVAEEFYRKEKRPVTRPDCMCDTFDQCAENISKKILEYQSQANKYHNSCLI ELRIQIRRFEELLPQVCWLVMENFKEHHWKKFFTSVKEIRGQFEEQQKRLEKRKDKNAQK LHLNLGHPVHFQEMESLHLSEEERQEELDSMIRMNKEKLEECTRRNGQVFITNLATFTEK FLLQLDEVVTIDDVQVARMEPPKQKLSMLIRRKLAGLSLKEESEKPLIERGSRKWPGIKP TEVTIQNKILLQPTSSISTTKTTLGHLAAVEARDAVYLKYLASFEEELKRIQDDCTSQIK EAQRWKDSWKQSLHTIQGLYV P08861 B2RE44 P11423 Q5VU28 Q5VU29 Q5VU30 CEL3B_HUMAN Chymotrypsin-like elastase family member 3B 3.4.21.70 Elastase IIIB Elastase-3B Protease E CELA3B ELA3B Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of a novel class of elastase isozyme, human pancreatic elastase III, by cDNA and genomic gene cloning. NUCLEOTIDE SEQUENCE [MRNA] Pancreas Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT TRP-79 Urinary bladder The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANT TRP-79 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT TRP-79 Pancreas Primary structure of human pancreatic protease E determined by sequence analysis of the cloned mRNA. NUCLEOTIDE SEQUENCE [MRNA] OF 4-270 Pancreas Generation of a subunit III-like protein by autolysis of human and porcine proproteinase E in a binary complex with procarboxypeptidase A. PROTEIN SEQUENCE OF 18-57 Characterization of two glycoproteins of human pancreatic juice: P35, a truncated protease E and P19, precursor of protein X. PROTEIN SEQUENCE OF 31-63 Identification of a procarboxypeptidase A-truncated protease E binary complex in human pancreatic juice. PROTEIN SEQUENCE OF 31-50 Pancreas Localization and characterization of the glycosylation site of human pancreatic elastase 1. PROTEIN SEQUENCE OF 94-164 GLYCOSYLATION AT ASN-114 Pancreas Human elastase 1: evidence for expression in the skin and the identification of a frequent frameshift polymorphism. TISSUE SPECIFICITY Efficient protease with alanine specificity but only little elastolytic activity. Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin. Pancreas. Not detectable in keratinocytes. Belongs to the peptidase S1 family. Elastase subfamily. Was originally thought to be elastase 1. Complete proteome Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Polymorphism Protease Reference proteome Serine protease Signal Zymogen R W R G A G R P MMLRLLSSLLLVAVASGYGPPSSRPSSRVVNGEDAVPYSWPWQVSLQYEKSGSFYHTCGG SLIAPDWVVTAGHCISSSRTYQVVLGEYDRAVKEGPEQVIPINSGDLFVHPLWNRSCVAC GNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQEALL PVVDYEHCSRWNWWGSSVKKTMVCAGGDIRSGCNGDSGGPLNCPTEDGGWQVHGVTSFVS AFGCNTRRKPTVFTRVSAFIDWIEETIASH Q96M95 Q8N6Q0 CCD42_HUMAN Coiled-coil domain-containing protein 42 CCDC42 CCDC42A Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Brain Required for sperm development. Q9UJV3-2 MID2 false 3 Q9UBB9 TFIP11 false 3 Q96M95-1 1 Q96M95-2 2 No experimental confirmation available. Belongs to the CFAP73 family. Alternative splicing Coiled coil Complete proteome Polymorphism Reference proteome T P R C A T P L MSLGIMEEEDLAEYFRLQYGERLLQMLQKLPNVEGASESPSIWLLEKKKETEIMHQTMVQ KKKMFQRRMETLNLRWEELGVKEAQLKAHIQKSEQFIQENDQKRIRAMKKANKERELKCQ HMQELTKRKQEMVALRLEHQRLSAKLKDYYIFNKYLEKVVENSEFEEIHEVIARYKTLVS MRHDLMQSAQEGQEKIERAKARLARYMEEKDDEILQQNNELARLQMRFDRARSNVIFWES RWAHIQNTAAKKTLLLGTIKMATLNLFQIVSKHLKEVTEVALEDTHKQLDMIQQFIQDRS DIWAEVKKKEQQRVRI P15289 B2RCA6 B7XD04 F8WCC8 Q6ICI5 Q96CJ0 ARSA_HUMAN Arylsulfatase A ASA 3.1.6.8 Cerebroside-sulfatase Arylsulfatase A component B Arylsulfatase A component C ARSA Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and expression of human arylsulfatase A. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Structure of the arylsulfatase A gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Characterization of the arylsulfatase I (ARSI) gene preferentially expressed in the human retinal pigment epithelium cell line ARPE-19. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) A genome annotation-driven approach to cloning the human ORFeome. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) VARIANT SER-391 Testis NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS LEU-82; CYS-193; SER-350; VAL-356; SER-391; SER-440 AND HIS-496 The DNA sequence of human chromosome 22. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT SER-391 B-cell Proteolytic processing of human lysosomal arylsulfatase A. PROTEIN SEQUENCE OF 19-33 AND 434-479 SUBUNIT A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. PARTIAL PROTEIN SEQUENCE IDENTIFICATION BY MASS SPECTROMETRY OXOALANINE AT CYS-69 LACK OF OXOALANINE IN MSD Conversion of cysteine to formylglycine: a protein modification in the endoplasmic reticulum. OXOALANINE AT CYS-69 MUTAGENESIS OF CYS-69 AND 69-CYS-THR-70 SUBCELLULAR LOCATION Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency. INVOLVEMENT IN MSD Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158 AND ASN-350 Liver A new analytical bench assay for the determination of arylsulfatase a activity toward galactosyl-3-sulfate ceramide: implication for metachromatic leukodystrophy diagnosis. CATALYTIC ACTIVITY FUNCTION BIOPHYSICOCHEMICAL PROPERTIES Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OLIGOMERIZATION Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis. X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) MUTAGENESIS OF CYS-69 Crystal structure of a covalent intermediate of endogenous human arylsulfatase A. X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 19-507 SUBUNIT GLYCOSYLATION AT ASN-158 AND ASN-184 ACTIVE SITE ACTIVITY REGULATION CALCIUM-BINDING COFACTOR A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 69-73 IN COMPLEX WITH SUMF1 Molecular genetics of metachromatic leukodystrophy. REVIEW ON MLD VARIANTS Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site. INVOLVEMENT IN MLD VARIANT SER-350 CHARACTERIZATION OF VARIANT SER-350 Identification of a mutation in the arylsulfatase A gene of a patient with adult-type metachromatic leukodystrophy. VARIANT MLD ASP-99 Mutations in the arylsulfatase A pseudodeficiency allele causing metachromatic leukodystrophy. VARIANT MLD PHE-96 Molecular basis of different forms of metachromatic leukodystrophy. VARIANT MLD LEU-426 VARIANTS CYS-193 AND SER-391 Late-onset metachromatic leukodystrophy: molecular pathology in two siblings. VARIANT MLD GLN-84 High residual arylsulfatase A (ARSA) activity in a patient with late-infantile metachromatic leukodystrophy. VARIANT MLD SER-309 Mutations in the arylsulfatase A gene of Japanese patients with metachromatic leukodystrophy. VARIANT MLD ARG-245 Prevalence of common mutations in the arylsulphatase A gene in metachromatic leukodystrophy patients diagnosed in Britain. VARIANT MLD LEU-426 An adult-type metachromatic leukodystrophy caused by substitution of serine for glycine-122 in arylsulfatase A. VARIANT MLD SER-122 Missense mutations in the arylsulphatase A genes of metachromatic leukodystrophy patients. VARIANTS MLD VAL-212; VAL-224 AND TYR-295 An arylsulfatase A (ARSA) missense mutation (T274M) causing late-infantile metachromatic leukodystrophy. VARIANT MLD MET-274 Single exon mutation in arylsulfatase A gene has two effects: loss of enzyme activity and aberrant splicing. VARIANT MLD ILE-409 Multiple mutations are responsible for the high frequency of metachromatic leukodystrophy in a small geographic area. VARIANTS MLD ASP-86; LEU-96; HIS-190; MET-274 AND TRP-370 CHARACTERIZATION OF VARIANTS MLD ASP-86; LEU-96; HIS-190; MET-274 AND TRP-370 A missense mutation P136L in the arylsulfatase A gene causes instability and loss of activity of the mutant enzyme. VARIANT MLD LEU-136 Identification of seven novel mutations associated with metachromatic leukodystrophy. VARIANTS MLD LEU-82; TYR-172; CYS-201; GLN-311; VAL-335 AND TRP-390 Two novel mutations in a Japanese patient with the late-infantile form of metachromatic leukodystrophy. VARIANTS MLD HIS-153 AND VAL-308 CHARACTERIZATION OF VARIANTS MLD HIS-153 AND VAL-308 Characterization of two arylsulfatase A missense mutations D335V and T274M causing late infantile metachromatic leukodystrophy. CHARACTERIZATION OF VARIANTS MET-274 AND VAL-335 A T > C transition causing a Leu > Pro substitution in a conserved region of the arylsulfatase A gene in a late infantile metachromatic leukodystrophy patient. VARIANT MLD PRO-428 Metachromatic leukodystrophy: identification of the first deletion in exon 1 and of nine novel point mutations in the arylsulfatase A gene. VARIANTS MLD ASN-95; ARG-119; TYR-152; HIS-244; TYR-250; THR-314; ASN-367 AND CYS-384 VARIANT HIS-496 A 9-bp deletion (2320del9) on the background of the arylsulfatase A pseudodeficiency allele in a metachromatic leukodystrophy patient and in a patient with nonprogressive neurological symptoms. VARIANT MLD 406-SER--THR-408 DEL Molecular genetic characterization of two metachromatic leukodystrophy patients who carry the T799G mutation and show different phenotypes; description of a novel null-type mutation. VARIANTS MLD PRO-135 AND SER-179 ERRATUM The R496H mutation of arylsulfatase A does not cause metachromatic leukodystrophy. VARIANT HIS-496 Two novel mutations in the arylsulfatase A gene associated with juvenile (R390Q) and adult onset (H397Y) metachromatic leukodystrophy. VARIANTS MLD GLN-390 AND TYR-397 Prevalence of arylsulphatase A mutations in 11 Japanese patients with metachromatic leukodystrophy: identification of two novel mutations. VARIANT MLD SER-298 CHARACTERIZATION OF VARIANT MLD SER-298 Coincidence of two novel arylsulfatase A alleles and mutation 459+1G>A within a family with metachromatic leukodystrophy: molecular basis of phenotypic heterogeneity. VARIANTS PRO-76; CYS-193; SER-391 AND VAL-464 Metachromatic leucodystrophy in Portugal-finding of four new molecular lesions: C300F, P425T, g.1190-1191insC, and g.2408delC. VARIANTS MLD PHE-300 AND THR-425 Identification of 12 novel mutations and two new polymorphisms in the arylsulfatase A gene: haplotype and genotype-phenotype correlation studies in Spanish metachromatic leukodystrophy patients. VARIANTS MLD SER-32; PRO-68; TRP-84; ALA-94; VAL-99; SER-136; VAL-212; TYR-227; HIS-255; HIS-288; ASP-308; ILE-327 AND LEU-377 VARIANTS CYS-193; SER-350 AND SER-391 Metachromatic leucodystrophy: a newly identified mutation in arylsulphatase A, D281Y, found as a compound heterozygote with I179L in an adult onset case. VARIANTS MLD SER-179 AND TYR-281 Metachromatic leukodystrophy: subtype genotype/phenotype correlations and identification of novel missense mutations (P148L and P191T) causing the juvenile-onset disease. VARIANTS MLD LEU-148; THR-191; VAL-335; TYR-397 AND LEU-426 Characterization of four arylsulfatase A missense mutations G86D, Y201C, D255H, and E312D causing metachromatic leukodystrophy. VARIANTS MLD ASP-86; CYS-201; HIS-255 AND ASP-312 CHARACTERIZATION OF VARIANTS MLD ASP-86; CYS-201; HIS-255 AND ASP-312 FUNCTION CATALYTIC ACTIVITY Adult-onset MLD: a gene mutation with isolated polyneuropathy. VARIANT MLD PRO-286 VARIANT SER-391 Variable onset of metachromatic leukodystrophy in a Vietnamese family. VARIANT MLD GLY-143 CHARACTERIZATION OF VARIANT MLD GLY-143 Late-onset metachromatic leukodystrophy clinically presenting as isolated peripheral neuropathy: compound heterozygosity for the IVS2+1G-->A mutation and a newly identified missense mutation (Thr408Ile) in a Spanish family. VARIANT MLD ILE-408 VARIANTS CYS-193 AND SER-391 Contribution of arylsulfatase A mutations located on the same allele to enzyme activity reduction and metachromatic leukodystrophy severity. VARIANT MLD LYS-253 CHARACTERIZATION OF VARIANT MLD LYS-253 CHARACTERIZATION OF VARIANTS SER-350; SER-391 AND LEU-426 Biochemical characterization of two (C300F, P425T) arylsulfatase A missense mutations. CHARACTERIZATION OF VARIANTS MLD PHE-300 AND THR-425 Oligomerization capacity of two arylsulfatase A mutants: C300F and P425T. CHARACTERIZATION OF VARIANTS MLD PHE-300 AND THR-425 Identification of nine novel arylsulfatase A (ARSA) gene mutations in patients with metachromatic leukodystrophy (MLD). VARIANTS MLD LEU-155; GLN-181; VAL-212; HIS-306; SER-325; VAL-335; LEU-426 AND SER-429 Novel mutations in arylsulfatase A gene in three Ukrainian families with metachromatic leukodystrophy. VARIANTS MLD SER-136; SER-247; GLU-381 LEU-426 AND GLY-469 Novel mutations associated with metachromatic leukodystrophy: phenotype and expression studies in nine Czech and Slovak patients. VARIANTS MLD ASN-29; ARG-156; SER-179; SER-293; TYR-294; SER-309 AND LEU-426 VARIANTS CYS-193 AND SER-391 CHARACTERIZATION OF VARIANTS MLD ASN-29; ARG-156; SER-293 AND TYR-294 Late onset MLD with normal nerve conduction associated with two novel missense mutations in the ASA gene. VARIANTS MLD ASP-293 AND GLY-489 VARIANT SER-350 Adult onset metachromatic leukodystrophy without electroclinical peripheral nervous system involvement: a new mutation in the ARSA gene. VARIANT MLD VAL-219 CHARACTERIZATION OF VARIANT MLD VAL-219 Molecular analysis of ARSA and PSAP genes in twenty-one Italian patients with metachromatic leukodystrophy: identification and functional characterization of 11 novel ARSA alleles. VARIANTS MLD ASP-18; HIS-30; GLN-84; PRO-137 DEL; ASP-154; SER-179; CYS-201; PRO-212; HIS-217; LYS-253; SER-282; ASN-302; TRP-370; ASN-376; TRP-390 AND PRO-428 CHARACTERIZATION OF VARIANTS MLD ASP-18; HIS-30; PRO-212; HIS-217; SER-282; ASN-302; TRP-370 AND ASN-376 Characterization of new arylsulfatase A gene mutations reinforces genotype-phenotype correlation in metachromatic leukodystrophy. VARIANTS MLD PRO-52; ASP-138; PRO-212; MET-304; LYS-307 AND GLY-406 CHARACTERIZATION OF VARIANTS MLD PRO-52; ASP-138; PRO-212; MET-304; LYS-307 AND GLY-406 Molecular bases of metachromatic leukodystrophy in Polish patients. VARIANTS MLD SER-179; SER-247; CYS-288; VAL-335; LYS-382; GLN-390; TRP-390; TYR-397 AND LEU-426 Adult-type metachromatic leukodystrophy with compound heterozygous ARSA mutations: a case report and phenotypic comparison with a previously reported case. VARIANTS MLD ASP-99 AND ILE-409 Hydrolyzes cerebroside sulfate. H2O + N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine = a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H(+) + sulfate Ca(2+) Binds 1 Ca(2+) ion per subunit. Inhibited by phosphate. The phosphate forms a covalent bond with the active site 3-oxoalanine. 0.099 mM for galactosyl-3-sulfate ceramide kcat is 0,087 sec(-1) with galactosyl-3-sulfate ceramide as substrate. Optimum pH is 4.5. Homodimer at neutral pH and homooctamer at acidic pH. Exists both as a single chain of 58 kDa (component A) or as a chain of 50 kDa (component B) linked by disulfide bond(s) to a 7 kDa chain (component C). Interacts with SUMF1. Q9BQY4 RHOXF2 false 4 Q15645 TRIP13 false 12 Endoplasmic reticulum Lysosome P15289-1 1 P15289-2 2 No experimental confirmation available. The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD). Metachromatic leukodystrophy MLD An autosomal recessive disease caused by abnormal intralysosomal accumulation of cerebroside-3-sulfate in central and peripheral nervous systems, as well as other organs. MLD is clinically characterized by leukodystrophy, progressive demyelination and a variety of neurological symptoms, including gait disturbances, ataxias, optical atrophy, dementia, seizures, and spastic tetraparesis. Decreased arylsulfatase A activity is detected in urine, leukocytes, and fibroblasts of affected individuals. Several forms of the disease can be distinguished according to the age at onset and disease severity: late infantile, juvenile and adult forms, partial cerebroside sulfate deficiency, and pseudoarylsulfatase A deficiency. Individuals with pseudoarylsulfatase A deficiency have low arylsulfatase A activity but lack neurological manifestations and are apparently healthy. The disease is caused by mutations affecting the gene represented in this entry. Multiple sulfatase deficiency MSD A clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. The protein represented in this entry is involved in disease pathogenesis. Arylsulfatase A activity is impaired in multiple sulfatase deficiency due to mutations in SUMF1 (PubMed:15146462). SUMF1 mutations result in defective post-translational modification of ARSA at residue Cys-69 that is not converted to 3-oxoalanine (PubMed:7628016). The metal cofactor was first identified as magnesium ion, based on the structure of the recombinant protein, but when purified from human placenta, the protein contains 1 calcium ion per subunit. Belongs to the sulfatase family. Arylsulfatase A entry Leiden Open Variation Database (LOVD) 3D-structure Alternative splicing Calcium Complete proteome Direct protein sequencing Disease mutation Disulfide bond Endoplasmic reticulum Glycoprotein Hydrolase Ichthyosis Leukodystrophy Lysosome Metachromatic leukodystrophy Metal-binding Polymorphism Reference proteome Signal A D D N D H G S L P L P L P P L R Q R W G D P A S N S F S L G D G V G R G S L P P L P S H D R G P L D Y Q H G D P L P R C R P R D N C Y I S L Q Q H P T W C Y C A P A V R H F V A V H Y P T R C R H G R F S S Y E K D H T M D Y N S T P R C R H G D G S C Y S Y L S C F K N T M Y H E K G D G V G S R Q E D A T G S T I D V N S F V K N R Q R W Y N P L D E E K R C R Q R W T S H Y S G T I T I P T P L L P Y S N S A V A G C G R H CT TC C A C S S P MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFT DFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGM AGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIP LLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAE RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRC GKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSP LLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSL TAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARG EDPALQICCHPGCTPRPACCHCPDPHA Q5TBE3 Q5TBE4 CI153_HUMAN Uncharacterized protein C9orf153 C9orf153 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo DNA sequence and analysis of human chromosome 9. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Brain Q5TBE3-1 1 No experimental confirmation available. Derived from EST data. Q5TBE3-2 2 Alternative splicing Complete proteome Reference proteome SVNKMNKPGKHRKTPSPKINK RKTIHESKGSGMEIF MFLTGDTSPAEDNREATLPQCSLPELYACIENFNKESKKSNLLKMHGISLNEAQEVLARN LNVMSFTRGADVRGDLQPVISVNKMNKPGKHRKTPSPKINK Q9NRK6 Q13040 Q6P1Q8 Q9H3V0 ABCBA_HUMAN ATP-binding cassette sub-family B member 10, mitochondrial ATP-binding cassette transporter 10 ABC transporter 10 protein Mitochondrial ATP-binding cassette 2 M-ABC2 ABCB10 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo M-ABC2, a new human mitochondrial ATP-binding cassette membrane protein. NUCLEOTIDE SEQUENCE [MRNA] VARIANT ASN-545 Lymphoblast Human mono ATP-binding cassette protein. NUCLEOTIDE SEQUENCE [MRNA] The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Eye Characterization and mapping of three new mammalian ATP-binding transporter genes from an EST database. NUCLEOTIDE SEQUENCE [MRNA] OF 510-738 Lysine acetylation targets protein complexes and co-regulates major cellular functions. ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states. X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 152-738 ALONE AND IN COMPLEX WITH ATP ANALOGS ATP-BINDING REGION SUBUNIT Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population. VARIANT SER-150 The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] THR-471 May mediate critical mitochondrial transport functions related to heme biosynthesis. Homodimer or homooligomer. Mitochondrion inner membrane Multi-pass membrane protein Ubiquitous. Highly expressed in bone marrow, expressed at intermediate to high levels in skeletal muscle, small intestine, thyroid, heart, brain, placenta, liver, pancreas, prostate, testis, ovary, leukocyte, stomach, spinal cord, lymph node, trachea and adrenal gland, and low levels are found in lung, kidney, spleen, thymus and colon. Belongs to the ABC transporter superfamily. ABCB family. Mitochondrial peptide exporter (TC 3.A.1.212) subfamily. Database for mutations in ABC proteins 3D-structure Acetylation ATP-binding Complete proteome Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Polymorphism Reference proteome Transit peptide Transmembrane Transmembrane helix Transport A S R G R T D N F V Q K IRQLNP NPSAKPS VAEVAN GLKGQ FIRNFPQG SPEFPPR R S MRGPPAWPLRLLEPPSPAEPGRLLPVACVWAAASRVPGSLSPFTGLRPARLWGAGPALLW GVGAARRWRSGCRGGGPGASRGVLGLARLLGLWARGPGSCRCGAFAGPGAPRLPRARFPG GPAAAAWAGDEAWRRGPAAPPGDKGRLRPAAAGLPEARKLLGLAYPERRRLAAAVGFLTM SSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSG QRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQA SVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGN VRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLL MGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFNEG VILNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL LRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSVTA EEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA TSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS KPNGIYRKLMNKQSFISA Q12887 B2R6U5 B4DJ50 O15334 Q969F7 COX10_HUMAN Protoheme IX farnesyltransferase, mitochondrial 2.5.1.141 Heme O synthase COX10 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANTS GLN-159 AND ASP-340 Genomic structure and expression of the human heme A:farnesyltransferase (COX10) gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT GLN-159 Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) VARIANT GLN-159 Brain Substantia nigra Cloning of human full-length CDSs in BD Creator(TM) system donor vector. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT GLN-159 DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT GLN-159 Brain A mutation in the human heme A:farnesyltransferase gene (COX10) causes cytochrome c oxidase deficiency. VARIANT MT-C4D LYS-204 Mutations in COX10 result in a defect in mitochondrial heme A biosynthesis and account for multiple, early-onset clinical phenotypes associated with isolated COX deficiency. VARIANTS MT-C4D LYS-196; LEU-225; GLY-336 AND VAL-336 Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma. VARIANT HIS-258 A comprehensive genomic analysis reveals the genetic landscape of mitochondrial respiratory chain complex deficiencies. VARIANTS MT-C4D ARG-288 AND LEU-420 Converts protoheme IX and farnesyl diphosphate to heme O. (2E,6E)-farnesyl diphosphate + H2O + heme b = diphosphate + Fe(II)-heme o Mitochondrion membrane Multi-pass membrane protein Q12887-1 1 Q12887-2 2 No experimental confirmation available. Mitochondrial complex IV deficiency MT-C4D A disorder of the mitochondrial respiratory chain with heterogeneous clinical manifestations, ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Features include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental delay, delayed motor development and mental retardation. Some affected individuals manifest a fatal hypertrophic cardiomyopathy resulting in neonatal death. A subset of patients manifest Leigh syndrome. The disease is caused by mutations affecting the gene represented in this entry. Leigh syndrome LS An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the UbiA prenyltransferase family. Alternative splicing Complete proteome Disease mutation Heme biosynthesis Leigh syndrome Membrane Mitochondrion Polymorphism Primary mitochondrial disease Reference proteome Transferase Transit peptide Transmembrane Transmembrane helix MAASPHTLSSRLLTG MICQEFWLDYPKSNS T I T S Y C R Q T K N K P L L H G R D G D V G D P L A T Y H MAASPHTLSSRLLTGCVGGSVWYLERRTIQDSPHKFLHLLRNVNKQWITFQHFSFLKRMY VTQLNRSHNQQVRPKPEPVASPFLEKTSSGQAKAEIYEMRPLSPPSLSLSRKPNEKELIE LEPDSVIEDSIDVGKETKEEKRWKEMKLQVYDLPGILARLSKIKLTALVVSTTAAGFALA PGPFDWPCFLLTSVGTGLASCAANSINQFFEVPFDSNMNRTKNRPLVRGQISPLLAVSFA TCCAVPGVAILTLGVNPLTGALGLFNIFLYTCCYTPLKRISIANTWVGAVVGAIPPVMGW TAATGSLDAGAFLLGGILYSWQFPHFNALSWGLREDYSRGGYCMMSVTHPGLCRRVALRH CLALLVLSAAAPVLDITTWTFPIMALPINAYISYLGFRFYVDADRRSSRRLFFCSLWHLP LLLLLMLTCKRPSGGGDAGPPPS Q9Y615 B2RC83 Q5JSV0 ACL7A_HUMAN Actin-like protein 7A Actin-like-7-alpha ACTL7A Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning, mapping, and expression of two novel actin genes, actin-like-7A (ACTL7A) and actin-like-7B (ACTL7B), from the familial dysautonomia candidate region on 9q31. NUCLEOTIDE SEQUENCE [GENOMIC DNA] TISSUE SPECIFICITY Single nucleotide polymorphisms: discovery of the genetic causes of male infertility. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS CYS-45 AND MET-340 Blood Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis DNA sequence and analysis of human chromosome 9. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis Molecular recognition of the Tes LIM2-3 domains by the actin-related protein Arp7A. X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 1-65 IN COMPLEX WITH ENAH AND TES SUBUNIT MUTAGENESIS OF ALA-31 AND ALA-41 Interacts (via N-terminus) with TES (via LIM domain 2). Heterodimer with TES; the heterodimer interacts with ENAH to form a heterotrimer. Q9UGI8 TES false 9 Cytoplasm Cytoskeleton Golgi apparatus Cytoplasm Nucleus Detected at the Golgi apparatus during acrosome biogenesis. Detected at the subacrosomal layer in round spermatids. Detected in sperm head and tail. Strongly expressed in testis. Also expressed in other tissues. Belongs to the actin family. 3D-structure Complete proteome Cytoplasm Cytoskeleton Golgi apparatus Nucleus Polymorphism Reference proteome R C A P V M L V A Y A Y MWAPPAAIMGDGPTKKVGNQAPLQTQALQTASLRDGPAKRAVWVRHTSSEPQEPTESKAA KERPKQEVTKAVVVDLGTGYCKCGFAGLPRPTHKISTTVGKPYMETAKTGDNRKETFVGQ ELNNTNVHLKLVNPLRHGIIVDWDTVQDIWEYLFRQEMKIAPEEHAVLVSDPPLSPHTNR EKYAEMLFEAFNTPAMHIAYQSRLSMYSYGRTSGLVVEVGHGVSYVVPIYEGYPLPSITG RLDYAGSDLTAYLLGLLNSAGNEFTQDQMGIVEDIKKKCCFVALDPIEEKKVPLSEHTIR YVLPDGKEIQLCQERFLCSEMFFKPSLIKSMQLGLHTQTVSCLNKCDIALKRDLMGNILL CGGSTMLSGFPNRLQKELSSMCPNDTPQVNVLPERDSAVWTGGSILASLQGFQPLWVHRF EYEEHGPFFLYRRCF Q9UBX8 O60514 Q6NT09 B4GT6_HUMAN Beta-1,4-galactosyltransferase 6 Beta-1,4-GalTase 6 Beta4Gal-T6 b4Gal-T6 2.4.1.- Glucosylceramide beta-1,4-galactosyltransferase 2.4.1.274 Lactosylceramide synthase LacCer synthase UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 6 UDP-Gal:glucosylceramide beta-1,4-galactosyltransferase UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 6 B4GALT6 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The expanding beta 4-galactosyltransferase gene family: messages from the databanks. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) cDNA cloning and expression of human lactosylceramide synthase. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Brain Human beta-1,4-galactosyltransferase VI. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) DNA sequence and analysis of human chromosome 18. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Lung UDPgalactose:glucosylceramide beta 1->4-galactosyltransferase activity in human proximal tubular cells from normal and familial hypercholesterolemic homozygotes. FUNCTION AS GLUCOSYLCERAMIDE BETA-1,4-GALACTOSYLTRANSFERASE CATALYTIC ACTIVITY COFACTOR BIOPHYSICOCHEMICAL PROPERTIES Purification of uridine diphosphate-galactose:glucosyl ceramide, beta 1-4 galactosyltransferase from human kidney. FUNCTION AS GLUCOSYLCERAMIDE BETA-1,4-GALACTOSYLTRANSFERASE CATALYTIC ACTIVITY Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. REVIEW Establishment of HeLa cell mutants deficient in sphingolipid-related genes using TALENs. FUNCTION AS GLUCOSYLCERAMIDE BETA-1,4-GALACTOSYLTRANSFERASE Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (PubMed:3099851, PubMed:1551920, PubMed:24498430). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity). a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide(d18:1(4E)) + H(+) + UDP Mn(2+) Mg(2+) Inhibited by EDTA. 3 uM for glucosylceramide 0.5 uM for UDP-galactose 0.06 nmol/h/mg enzyme toward glucosylceramide 86 nmol/h/mg enzyme toward UDP-galactose Protein modification; protein glycosylation. Sphingolipid metabolism. Golgi apparatus Golgi stack membrane Single-pass type II membrane protein Trans cisternae of Golgi stack. Q9UBX8-1 1 Q9UBX8-2 2 No experimental confirmation available. High expression in brain and adrenal gland, lower in liver, lung, colon and peripheral white blood cells. Belongs to the glycosyltransferase 7 family. Beta-1,4-galactosyltransferase 6 Alternative splicing Calcium Complete proteome Disulfide bond Glycoprotein Glycosyltransferase Golgi apparatus Lipid biosynthesis Lipid metabolism Magnesium Manganese Membrane Metal-binding Polymorphism Reference proteome Signal-anchor Sphingolipid metabolism Transferase Transmembrane Transmembrane helix I V I V MSVLRRMMRVSNRSLLAFIFFFSLSSSCLYFIYVAPGIANTYLFMVQARGIMLRENVKTI GHMIRLYTNKNSTLNGTDYPEGNNSSDYLVQTTTYLPENFTYSPYLPCPEKLPYMRGFLN VNVSEVSFDEIHQLFSKDLDIEPGGHWRPKDCKPRWKVAVLIPFRNRHEHLPIFFLHLIP MLQKQRLEFAFYVIEQTGTQPFNRAMLFNVGFKEAMKDSVWDCVIFHDVDHLPENDRNYY GCGEMPRHFAAKLDKYMYILPYKEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNR VHYAGYNVTRPEGDLGKYKSIPHHHRGEVQFLGRYKLLRYSKERQYIDGLNNLIYRPKIL VDRLYTNISVNLMPELAPIEDY Q8TD86 A2A2M3 Q6Q2C4 CALL6_HUMAN Calmodulin-like protein 6 Calglandulin-like protein CALML6 CAGLP CALGP Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and characterization of human CAGLP gene encoding a novel EF-hand protein. NUCLEOTIDE SEQUENCE [MRNA] SUBCELLULAR LOCATION TISSUE SPECIFICITY Skeletal muscle SEQUENCE REVISION The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Cytoplasm Nucleus Expressed in prostate, thymus, heart, skeleton muscle, bone marrow and ovary. Belongs to the calmodulin family. Calglandulin subfamily. Calcium Complete proteome Cytoplasm Metal-binding Nucleus Polymorphism Reference proteome Repeat W R MGLQQEISLQPWCHHPAESCQTTTDMTERLSAEQIKEYKGVFEMFDEEGNGEVKTGELEW LMSLLGINPTKSELASMAKDVDRDNKGFFNCDGFLALMGVYHEKAQNQESELRAAFRVFD KEGKGYIDWNTLKYVLMNAGEPLNEVEAEQMMKEADKDGDRTIDYEEFVAMMTGESFKLI Q Q9NYQ6 O95722 Q5TH47 Q9BWQ5 Q9Y506 Q9Y526 CELR1_HUMAN Cadherin EGF LAG seven-pass G-type receptor 1 Cadherin family member 9 Flamingo homolog 2 hFmi2 CELSR1 CDHF9 FMI2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Large exons encoding multiple ectodomains are a characteristic feature of protocadherin genes. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) The DNA sequence of human chromosome 22. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 627-3014 (ISOFORM 2) VARIANTS TRP-664 AND ARG-1126 Kidney A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2764 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Mutations in the planar cell polarity genes CELSR1 and SCRIB are associated with the severe neural tube defect craniorachischisis. VARIANTS NTD VAL-773; GLN-2438; LEU-2964 AND ALA-2983 VARIANTS PRO-2312 AND THR-2739 CHARACTERIZATION OF VARIANTS NTD VAL-773; GLN-2438; LEU-2964 AND ALA-2983 CHARACTERIZATION OF VARIANTS PRO-2312 AND THR-2739 Receptor that may have an important role in cell/cell signaling during nervous system formation. Cell membrane Multi-pass membrane protein Q9NYQ6-1 1 Q9NYQ6-2 2 No experimental confirmation available. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. Neural tube defects NTD Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components. The disease may be caused by mutations affecting the gene represented in this entry. Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily. Alternative splicing Calcium Cell membrane Complete proteome Developmental protein Disease mutation Disulfide bond EGF-like domain G-protein coupled receptor Glycoprotein Hydroxylation Laminin EGF-like domain Membrane Phosphoprotein Polymorphism Receptor Reference proteome Repeat Signal Transducer Transmembrane Transmembrane helix GEH EIS I V S W A V C R V I Y H L P L P T M I V R H T A R P R Q N T C S E Q G S S L P A E D MAPPPPPVLPVLLLLAAAAALPAMGLRAAAWEPRVPGGTRAFALRPGCTYAVGAACTPRA PRELLDVGRDGRLAGRRRVSGAGRPLPLQVRLVARSAPTALSRRLRARTHLPGCGARARL CGTGARLCGALCFPVPGGCAAAQHSALAAPTTLPACRCPPRPRPRCPGRPICLPPGGSVR LRLLCALRRAAGAVRVGLALEAATAGTPSASPSPSPPLPPNLPEARAGPARRARRGTSGR GSLKFPMPNYQVALFENEPAGTLILQLHAHYTIEGEEERVSYYMEGLFDERSRGYFRIDS ATGAVSTDSVLDRETKETHVLRVKAVDYSTPPRSATTYITVLVKDTNDHSPVFEQSEYRE RVRENLEVGYEVLTIRASDRDSPINANLRYRVLGGAWDVFQLNESSGVVSTRAVLDREEA AEYQLLVEANDQGRNPGPLSATATVYIEVEDENDNYPQFSEQNYVVQVPEDVGLNTAVLR VQATDRDQGQNAAIHYSILSGNVAGQFYLHSLSGILDVINPLDFEDVQKYSLSIKAQDGG RPPLINSSGVVSVQVLDVNDNEPIFVSSPFQATVLENVPLGYPVVHIQAVDADSGENARL HYRLVDTASTFLGGGSAGPKNPAPTPDFPFQIHNSSGWITVCAELDREEVEHYSFGVEAV DHGSPPMSSSTSVSITVLDVNDNDPVFTQPTYELRLNEDAAVGSSVLTLQARDRDANSVI TYQLTGGNTRNRFALSSQRGGGLITLALPLDYKQEQQYVLAVTASDGTRSHTAHVLINVT DANTHRPVFQSSHYTVSVSEDRPVGTSIATLSANDEDTGENARITYVIQDPVPQFRIDPD SGTMYTMMELDYENQVAYTLTIMAQDNGIPQKSDTTTLEILILDANDNAPQFLWDFYQGS IFEDAPPSTSILQVSATDRDSGPNGRLLYTFQGGDDGDGDFYIEPTSGVIRTQRRLDREN VAVYNLWALAVDRGSPTPLSASVEIQVTILDINDNAPMFEKDELELFVEENNPVGSVVAK IRANDPDEGPNAQIMYQIVEGDMRHFFQLDLLNGDLRAMVELDFEVRREYVLVVQATSAP LVSRATVHILLVDQNDNPPVLPDFQILFNNYVTNKSNSFPTGVIGCIPAHDPDVSDSLNY TFVQGNELRLLLLDPATGELQLSRDLDNNRPLEALMEVSVSDGIHSVTAFCTLRVTIITD DMLTNSITVRLENMSQEKFLSPLLALFVEGVAAVLSTTKDDVFVFNVQNDTDVSSNILNV TFSALLPGGVRGQFFPSEDLQEQIYLNRTLLTTISTQRVLPFDDNICLREPCENYMKCVS VLRFDSSAPFLSSTTVLFRPIHPINGLRCRCPPGFTGDYCETEIDLCYSDPCGANGRCRS REGGYTCECFEDFTGEHCEVDARSGRCANGVCKNGGTCVNLLIGGFHCVCPPGEYERPYC EVTTRSFPPQSFVTFRGLRQRFHFTISLTFATQERNGLLLYNGRFNEKHDFIALEIVDEQ VQLTFSAGETTTTVAPKVPSGVSDGRWHSVQVQYYNKPNIGHLGLPHGPSGEKMAVVTVD DCDTTMAVRFGKDIGNYSCAAQGTQTGSKKSLDLTGPLLLGGVPNLPEDFPVHNRQFVGC MRNLSVDGKNVDMAGFIANNGTREGCAARRNFCDGRRCQNGGTCVNRWNMYLCECPLRFG GKNCEQAMPHPQLFSGESVVSWSDLNIIISVPWYLGLMFRTRKEDSVLMEATSGGPTSFR LQILNNYLQFEVSHGPSDVESVMLSGLRVTDGEWHHLLIELKNVKEDSEMKHLVTMTLDY GMDQNKADIGGMLPGLTVRSVVVGGASEDKVSVRRGFRGCMQGVRMGGTPTNVATLNMNN ALKVRVKDGCDVDDPCTSSPCPPNSRCHDAWEDYSCVCDKGYLGINCVDACHLNPCENMG ACVRSPGSPQGYVCECGPSHYGPYCENKLDLPCPRGWWGNPVCGPCHCAVSKGFDPDCNK TNGQCQCKENYYKLLAQDTCLPCDCFPHGSHSRTCDMATGQCACKPGVIGRQCNRCDNPF AEVTTLGCEVIYNGCPKAFEAGIWWPQTKFGQPAAVPCPKGSVGNAVRHCSGEKGWLPPE LFNCTTISFVDLRAMNEKLSRNETQVDGARALQLVRALRSATQHTGTLFGNDVRTAYQLL GHVLQHESWQQGFDLAATQDADFHEDVIHSGSALLAPATRAAWEQIQRSEGGTAQLLRRL EGYFSNVARNVRRTYLRPFVIVTANMILAVDIFDKFNFTGARVPRFDTIHEEFPRELESS VSFPADFFRPPEEKEGPLLRPAGRRTTPQTTRPGPGTEREAPISRRRRHPDDAGQFAVAL VIIYRTLGQLLPERYDPDRRSLRLPHRPIINTPMVSTLVYSEGAPLPRPLERPVLVEFAL LEVEERTKPVCVFWNHSLAVGGTGGWSARGCELLSRNRTHVACQCSHTASFAVLMDISRR ENGEVLPLKIVTYAAVSLSLAALLVAFVLLSLVRMLRSNLHSIHKHLAVALFLSQLVFVI GINQTENPFLCTVVAILLHYIYMSTFAWTLVESLHVYRMLTEVRNIDTGPMRFYYVVGWG IPAIVTGLAVGLDPQGYGNPDFCWLSLQDTLIWSFAGPIGAVIIINTVTSVLSAKVSCQR KHHYYGKKGIVSLLRTAFLLLLLISATWLLGLLAVNRDALSFHYLFAIFSGLQGPFVLLF HCVLNQEVRKHLKGVLGGRKLHLEDSATTRATLLTRSLNCNTTFGDGPDMLRTDLGESTA SLDSIVRDEGIQKLGVSSGLVRGSHGEPDASLMPRSCKDPPGHDSDSDSELSLDEQSSSY ASSHSSDSEDDGVGAEEKWDPARGAVHSTPKGDAVANHVPAGWPDQSLAESDSEDPSGKP RLKVETKVSVELHREEQGSHRGEYPPDQESGGAARLASSQPPEQRKGILKNKVTYPPPLT LTEQTLKGRLREKLADCEQSPTSSRTSSLGSGGPDCAITVKSPGREPGRDHLNGVAMNVR TGSAQADGSDSEKP P02649 B2RC15 C0JYY5 Q9P2S4 APOE_HUMAN Apolipoprotein E Apo-E APOE Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Synthesis, intracellular processing, and signal peptide of human apolipoprotein E. NUCLEOTIDE SEQUENCE [MRNA] (ALLELE APOE*3) Human apolipoprotein E mRNA. cDNA cloning and nucleotide sequencing of a new variant. NUCLEOTIDE SEQUENCE [MRNA] VARIANTS THR-117 AND PRO-170 Nucleotide sequence and structure of the human apolipoprotein E gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*4) VARIANT AD2 ARG-130 Genotyping and sequence analysis of apolipoprotein E isoforms. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*2) VARIANT CYS-176 Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene: PEREC1. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*3) Sequence diversity and large-scale typing of SNPs in the human apolipoprotein E gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*3) VARIANTS PRO-46; ARG-130; CYS-163 AND CYS-176 Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE APOE*3) Cerebellum NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*3) The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE APOE*3) Eye A new apolipoprotein E variant (Gln46-->His). NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-78 VARIANT HIS-64 Blood Identification and DNA sequence of a human apolipoprotein E cDNA clone. NUCLEOTIDE SEQUENCE [MRNA] OF 99-317 (ALLELE APOE*3) ERRATUM Human apolipoprotein E. The complete amino acid sequence. PROTEIN SEQUENCE OF 19-317 (ALLELE APOE*2) Cholesteryl ester and apolipoprotein E transfer between human high density lipoproteins and chylomicrons. FUNCTION IN LIPOPROTEINS CONVERSION Binding of a high reactive heparin to human apolipoprotein E: identification of two heparin-binding domains. HEPARIN-BINDING SITES Lipoproteins and their receptors in the central nervous system. Characterization of the lipoproteins in cerebrospinal fluid and identification of apolipoprotein B,E(LDL) receptors in the brain. TISSUE SPECIFICITY Soluble LR11 competes with amyloid beta in binding to cerebrospinal fluid-high-density lipoprotein. INTERACTION WITH SORL1 Site-specific mutagenesis of human apolipoprotein E. Receptor binding activity of variants with single amino acid substitutions. CHARACTERIZATION OF VARIANTS SER-154 AND PRO-170 MUTAGENESIS OF SER-157; HIS-158; LYS-161; LEU-162; LEU-167 AND ARG-168 Glycosylation of human apolipoprotein E. The carbohydrate attachment site is threonine 194. SUBCELLULAR LOCATION GLYCOSYLATION AT THR-212 MUTAGENESIS OF THR-212 Low density lipoprotein receptor-related protein mediates uptake of cholesteryl esters derived from apoprotein E-enriched lipoproteins. FUNCTION IN VLDL CLEARANCE Apolipoprotein E distribution among human plasma lipoproteins: role of the cysteine-arginine interchange at residue 112. REGION CHARACTERIZATION OF VARIANT ARG-130 AND ARG-176 Effects of exogenous apo E-3 and of cholesterol-enriched meals on the cellular metabolism of human chylomicrons and their remnants. FUNCTION IN CHYLOMICRONS CLEARANCE SUBCELLULAR LOCATION Mechanisms of inhibition by apolipoprotein C of apolipoprotein E-dependent cellular metabolism of human triglyceride-rich lipoproteins through the low density lipoprotein receptor pathway. FUNCTION IN VLDL AND IDL CLEARANCE Discrete carboxyl-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization. SUBUNIT SUBCELLULAR LOCATION REGION Binding of human apolipoprotein E to synthetic amyloid beta peptide: isoform-specific effects and implications for late-onset Alzheimer disease. INTERACTION WITH APP/A4 AMYLOID-BETA PEPTIDE CHARACTERIZATION OF VARIANT AD2 ARG-130 Isoform-specific interactions of apolipoprotein E with the microtubule-associated protein MAP2c: implications for Alzheimer's disease. INTERACTION WITH MAP2 CHARACTERIZATION OF VARIANT AD2 ARG-130 Isoform-specific interactions of apolipoprotein E with microtubule-associated protein tau: implications for Alzheimer disease. INTERACTION WITH MAPT CHARACTERIZATION OF VARIANT AD2 ARG-130 Identification of glycoprotein 330 as an endocytic receptor for apolipoprotein J/clusterin. FUNCTION LRP2-BINDING Apolipoprotein E-containing high density lipoprotein promotes neurite outgrowth and is a ligand for the low density lipoprotein receptor-related protein. FUNCTION IN NEURITE OUTGROWTH LRP-BINDING CHARACTERIZATION OF VARIANT AD2 ARG-130 Heparan sulfate proteoglycans participate in hepatic lipase and apolipoprotein E-mediated binding and uptake of plasma lipoproteins, including high density lipoproteins. FUNCTION IN HDL CLEARANCE HEPARAN SULFATE-BINDING The HepG2 extracellular matrix contains separate heparinase- and lipid-releasable pools of ApoE. Implications for hepatic lipoprotein metabolism. FUNCTION HEPARAN-SULFATE-BINDING SUBCELLULAR LOCATION Specific regional transcription of apolipoprotein E in human brain neurons. TISSUE SPECIFICITY Glycation of apolipoprotein E impairs its binding to heparin: identification of the major glycation site. GLYCATION AT LYS-93 IDENTIFICATION BY MASS SPECTROMETRY Apolipoprotein E fragments present in Alzheimer's disease brains induce neurofibrillary tangle-like intracellular inclusions in neurons. PTM CHARACTERIZATION OF VARIANT AD2 ARG-130 Domains of apoE required for binding to apoE receptor 2 and to phospholipids: implications for the functions of apoE in the brain. FUNCTION LRP8-BINDING CHARACTERIZATION OF VARIANT CYS-176 Molecular interactions between apoE and ABCA1: impact on apoE lipidation. FUNCTION IN REVERSE CHOLESTEROL TRANSPORT INTERACTION WITH ABCA1 Enrichment of glycopeptides for glycan structure and attachment site identification. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-212; THR-307 AND SER-308 STRUCTURE OF CARBOHYDRATES Cerebrospinal fluid Decoding of lipoprotein-receptor interactions: properties of ligand binding modules governing interactions with apolipoprotein E. FUNCTION LRP1-BINDING REGION Glycosylation and sialylation of macrophage-derived human apolipoprotein E analyzed by SDS-PAGE and mass spectrometry: evidence for a novel site of glycosylation on Ser290. GLYCOSYLATION AT SER-308 Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Resveratrol-induced changes of the human adipocyte secretion profile. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Apolipoproteins E and AV mediate lipoprotein clearance by hepatic proteoglycans. FUNCTION IN LIPOPROTEIN CLEARANCE HEPARAN-SULFATE PROTEOGLYCANS BINDING LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins. GLYCOSYLATION AT THR-26; THR-36 AND SER-314 IDENTIFICATION BY MASS SPECTROMETRY ApoE influences amyloid-beta (Abeta) clearance despite minimal apoE/Abeta association in physiological conditions. FUNCTION IN CHOLESTEROL EFFLUX INTERACTION WITH APP/A4 AMYLOID-BETA PEPTIDE An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver A single kinase generates the majority of the secreted phosphoproteome. PHOSPHORYLATION AT SER-147 ApoE2, ApoE3, and ApoE4 Differentially Stimulate APP Transcription and Abeta Secretion. FUNCTION IN APP TRANSCRIPTION CHARACTERIZATION OF VARIANT AD2 ARG-130 Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 41-184 FUNCTION REGION Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms. X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 41-184 OF VARIANT AD2 ARG-130 CHARACTERIZATION OF VARIANT AD2 ARG-130 MUTAGENESIS OF ARG-79 AND GLU-127 REGION Salt bridge relay triggers defective LDL receptor binding by a mutant apolipoprotein. X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 41-184 OF VARIANT CYS-176 CHARACTERIZATION OF VARIANT CYS-176 Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia. X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-209 OF VARIANT CYS-176 MUTAGENESIS OF ASP-172 CHARACTERIZATION OF VARIANT CYS-176 FUNCTION LDLR-BINDING Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding. X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-183 Interaction of the N-terminal domain of apolipoprotein E4 with heparin. X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 19-209 OF VARIANT AD2 ARG-130 Structure of the minimal interface between ApoE and LRP. STRUCTURE BY NMR OF 147-167 IN COMPLEX WITH LRP1 FUNCTION LRP1-BINDING Identification of human apolipoprotein E variant gene: apolipoprotein E7 (Glu244,245----Lys244,245). VARIANT HLPP3 262-GLU-GLU-263 DELINS LYS-LYS Molecular cloning of a human apolipoprotein E variant: E5 (Glu-3-->Lys). VARIANT LYS-21 Apolipoprotein E3-Leiden contains a seven-amino acid insertion that is a tandem repeat of residues 121-127. VARIANTS HLPP3 ARG-130 AND GLU-VAL-GLN-ALA-MET-LEU-GLY-145 INS Identification and characterization of a new variant of apolipoprotein E (apo E-Kochi). VARIANT HLPP3 HIS-163 Apolipoprotein E2-Dunedin (228 Arg replaced by Cys): an apolipoprotein E2 variant with normal receptor-binding activity. VARIANT CYS-246 Apolipoprotein E-4 Philadelphia (Glu-13-->Lys,Arg-145-->Cys). Homozygosity for two rare point mutations in the apolipoprotein E gene combined with severe type III hyperlipoproteinemia. VARIANTS HLPP3 LYS-31 AND CYS-163 Characterization of a new apolipoprotein E5 variant detected in two French-Canadian subjects. VARIANT APOE5 FRENCH-CANADIAN LYS-31 Site-directed mutagenesis of an apolipoprotein E mutant, apo E5(Glu3----Lys) and its binding to low density lipoprotein receptors. CHARACTERIZATION OF VARIANT LYS-21 FUNCTION LDLR-BINDING Familial apolipoprotein E deficiency and type III hyperlipoproteinemia due to a premature stop codon in the apolipoprotein E gene. VARIANT HLPP3 228-TRP--HIS-317 DEL Characterization of five new mutants in the carboxyl-terminal domain of human apolipoprotein E: no cosegregation with severe hyperlipidemia. VARIANTS GLU-254; GLY-269; GLU-270; HIS-292 AND ARG-314 Characterization of the gene for apolipoprotein E5-Frankfurt (Gln81->Lys, Cys112->Arg) by polymerase chain reaction, restriction isotyping, and temperature gradient gel electrophoresis. VARIANTS LYS-99 AND ARG-130 Preferential association of apolipoprotein E Leiden with very low density lipoproteins of human plasma. CHARACTERIZATION OF VARIANT GLU-VAL-GLN-ALA-MET-LEU-GLY-145 INS Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. INVOLVEMENT IN AD2 VARIANT AD2 ARG-130 Common and rare genotypes of human apolipoprotein E determined by specific restriction profiles of polymerase chain reaction-amplified DNA. VARIANTS HLPP3 ARG-130; ASP-145; SER-154; CYS-160 AND CYS-176 Dominant expression of type III hyperlipoproteinemia. Pathophysiological insights derived from the structural and kinetic characteristics of ApoE-1 (Lys146-->Glu). VARIANT HLPP3 GLU-164 CHARACTERIZATION OF VARIANT HLPP3 GLU-164 AND CYS-176 FUNCTION LDLR-BINDING HEPARIN-BINDING Characterization of a novel variant of apolipoprotein E, E2 Fukuoka (Arg-224 --> Gln) in a hyperlipidemic patient with xanthomatosis. VARIANT GLN-242 Apolipoprotein E Sendai (arginine 145-->proline): a new variant associated with lipoprotein glomerulopathy. VARIANT LPG PRO-163 Apolipoprotein E R112; R251G: a carboxy-terminal variant found in patients with hyperlipidemia and coronary heart disease. VARIANTS ARG-130 AND GLY-269 A novel apolipoprotein E mutation, E2 (Arg25Cys), in lipoprotein glomerulopathy. VARIANT LPG CYS-43 Virus-mediated transduction of apolipoprotein E (ApoE)-sendai develops lipoprotein glomerulopathy in ApoE-deficient mice. CHARACTERIZATION OF VARIANT LPG PRO-163 CHARACTERIZATION OF VARIANT AD2 ARG-130 Familial splenomegaly: macrophage hypercatabolism of lipoproteins associated with apolipoprotein E mutation [apolipoprotein E (delta149 Leu)]. VARIANT SBHD LEU-167 DEL Apolipoprotein E3Basel: new insights into a highly conserved protein region. VARIANT VAL-124 Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. VARIANTS ARG-130 AND CYS-176 Variable expressivity of the clinical and biochemical phenotype associated with the apolipoprotein E p.Leu149del mutation. VARIANT SBHD LEU-167 DEL APOE Kyoto mutation in European Americans with lipoprotein glomerulopathy. VARIANT LPG CYS-43 Quantitative detection of single amino acid polymorphisms by targeted proteomics. VARIANT HIS-64 IDENTIFICATION BY MASS SPECTROMETRY Apolipoprotein E gene mutations in subjects with mixed hyperlipidemia and a clinical diagnosis of familial combined hyperlipidemia. VARIANT HLPP3 SER-154 VARIANT LEU-167 DEL APOE p.Leu167del mutation in familial hypercholesterolemia. POSSIBLE INVOLVEMENT IN FH VARIANT FH LEU-167 DEL Description of a large family with autosomal dominant hypercholesterolemia associated with the APOE p.Leu167del mutation. POSSIBLE INVOLVEMENT IN FH VARIANT FH LEU-167 DEL Global molecular analysis and APOE mutations in a cohort of autosomal dominant hypercholesterolemia patients in France. POSSIBLE INVOLVEMENT IN FH VARIANTS FH PRO-46; ASP-145; CYS-163 AND LEU-167 DEL Genetic heterogeneity of apolipoprotein E and its influence on plasma lipid and lipoprotein levels. REVIEW VARIANTS LYS-31; ARG-102; ARG-130; GLN-152 AND CYS-154 Apolipoprotein E: structure and function in lipid metabolism, neurobiology, and Alzheimer's diseases. REVIEW POLYMORPHISM TISSUE SPECIFICITY Cell-specific production, secretion, and function of apolipoprotein E. REVIEW FUNCTION PTM APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids (PubMed:6860692, PubMed:1911868, PubMed:14754908). APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance (PubMed:6860692, PubMed:2762297, PubMed:1911868, PubMed:1917954, PubMed:9395455, PubMed:14754908, PubMed:23620513). Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma (PubMed:6860692, PubMed:2762297, PubMed:9395455). As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL) (PubMed:6860692, PubMed:1911868). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (PubMed:2762297, PubMed:1917954, PubMed:7768901, PubMed:8939961, PubMed:12950167, PubMed:20030366, PubMed:2063194, PubMed:8756331, PubMed:20303980, PubMed:1530612, PubMed:7635945). Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells (PubMed:9395455, PubMed:9488694, PubMed:23676495, PubMed:7635945). A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes (PubMed:1911868, PubMed:1917954, PubMed:9395455, PubMed:23676495, PubMed:29516132). APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues (PubMed:2762297, PubMed:29516132). By participating to the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis (PubMed:2762297, PubMed:1917954, PubMed:29516132). APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis (PubMed:9395455, PubMed:14754908, PubMed:23620513). First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues (PubMed:14754908, PubMed:23620513). Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes (PubMed:9395455). APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting (PubMed:8939961, PubMed:25173806). APOE in also involved in innate and adaptive immune responses, controlling for instance the survival of myeloid-derived suppressor cells (By similarity). APOE, may also play a role in transcription regulation through a receptor-dependent and cholesterol-independent mechanism, that activates MAP3K12 and a non-canonical MAPK signal transduction pathway that results in enhanced AP-1-mediated transcription of APP (PubMed:28111074). Homotetramer (PubMed:8340399). May interact with ABCA1; functionally associated with ABCA1 in the biogenesis of HDLs (PubMed:14754908). May interact with APP/A4 amyloid-beta peptide; the interaction is extremely stable in vitro but its physiological significance is unclear (PubMed:8367470, PubMed:23620513). May interact with MAPT (PubMed:7972031). May interact with MAP2 (PubMed:7891887). In the cerebrospinal fluid, interacts with secreted SORL1 (PubMed:30448281). P27958 true 4 P05067 APP false 3 Q16543 CDC37 false 3 Q9BQ95 ECSIT false 4 P00738 HP false 7 P01130 LDLR false 2 Q14114 LRP8 false 2 P10636 MAPT false 3 Q53EL6 PDCD4 false 3 P50502 ST13 false 3 O75069 TMCC2 false 5 Secreted Secreted Extracellular space Secreted Extracellular space Extracellular matrix In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins (PubMed:1911868, PubMed:8340399). Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner (PubMed:9488694). Lipidation induces the release from the extracellular matrix (PubMed:9488694). Produced by several tissues and cell types and mainly found associated with lipid particles in the plasma, the interstitial fluid and lymph (PubMed:25173806). Mainly synthesized by liver hepatocytes (PubMed:25173806). Significant quantities are also produced in brain, mainly by astrocytes and glial cells in the cerebral cortex, but also by neurons in frontal cortex and hippocampus (PubMed:3115992, PubMed:10027417). It is also expressed by cells of the peripheral nervous system (PubMed:10027417, PubMed:25173806). Also expressed by adrenal gland, testis, ovary, skin, kidney, spleen and adipose tissue and macrophages in various tissues (PubMed:25173806). APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma (PubMed:29516132). The extent of glycosylation and sialylation are tissue and context specific (PubMed:29516132). Plasma APOE undergoes desialylation and is less glycosylated and sialylated than the cellular form (PubMed:2498325, PubMed:19838169, PubMed:20511397, PubMed:23234360). Glycosylation is not required for proper expression and secretion (PubMed:2498325). O-glycosylated with core 1 or possibly core 8 glycans. Thr-307 and Ser-314 are minor glycosylation sites compared to Ser-308 (PubMed:19838169, PubMed:23234360). Glycated in plasma VLDL of normal subjects, and of hyperglycemic diabetic patients at a higher level (2-3 fold). Phosphorylated by FAM20C in the extracellular medium. Undergoes C-terminal proteolytic processing in neurons. C-terminally truncated APOE has a tendency to form neurotoxic intracellular neurofibrillary tangle-like inclusions in neurons. There are three common APOE alleles identified: APOE*2/APOE-epsilon2/E2, APOE*3/APOE-epsilon3/E3, and APOE*4/APOE-epsilon4/E4. The corresponding ApoE2, ApoE3 and ApoE4 isoforms differentially present Cys and Arg residues at positions 130 and 176. The most common allele in the human population is APOE*3 which sequence is the one displayed in that entry with a Cys at position 130 and an Arg at position 176. Common APOE variants influence lipoprotein metabolism in healthy individuals. Additional variants have been described and are described relative to the three common alleles. Hyperlipoproteinemia 3 HLPP3 A disorder characterized by the accumulation of intermediate-density lipoprotein particles (IDL or broad-beta-lipoprotein) rich in cholesterol. Clinical features include xanthomas, yellowish lipid deposits in the palmar crease, or less specific on tendons and on elbows. The disorder rarely manifests before the third decade in men. In women, it is usually expressed only after the menopause. The disease is caused by mutations affecting the gene represented in this entry. The vast majority of the patients are homozygous for APOE*2 alleles. More severe cases of HLPP3 have also been observed in individuals heterozygous for rare APOE variants. The influence of APOE on lipid levels is often suggested to have major implications for the risk of coronary artery disease (CAD). Individuals carrying the common APOE*4 variant are at higher risk of CAD. Alzheimer disease 2 AD2 A late-onset form of Alzheimer disease. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituents of these plaques are neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42, that are produced by the proteolysis of the transmembrane APP protein. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products, such as C31, are also implicated in neuronal death. Disease susceptibility is associated with variations affecting the gene represented in this entry. The APOE*4 allele (APOE form E4) is genetically associated with the common late onset familial and sporadic forms of Alzheimer disease. Risk for AD increased from 20% to 90% and mean age at onset decreased from 84 to 68 years with increasing number of APOE*4 alleles in 42 families with late onset AD. Thus APOE*4 gene dose is a major risk factor for late onset AD and, in these families, homozygosity for APOE*4 was virtually sufficient to cause AD by age 80. The mechanism by which APOE*4 participates in pathogenesis is not known. Sea-blue histiocyte disease SBHD Characterized by splenomegaly, mild thrombocytopenia and, in the bone marrow, numerous histiocytes containing cytoplasmic granules which stain bright blue with the usual hematologic stains. The syndrome is the consequence of an inherited metabolic defect analogous to Gaucher disease and other sphingolipidoses. The disease is caused by mutations affecting the gene represented in this entry. Lipoprotein glomerulopathy LPG Uncommon kidney disease characterized by proteinuria, progressive kidney failure, and distinctive lipoprotein thrombi in glomerular capillaries. The disease is caused by mutations affecting the gene represented in this entry. Familial hypercholesterolemia FH A common autosomal dominant disorder characterized by elevated serum low-density lipoprotein (LDL) cholesterol levels, which result in excess deposition of cholesterol in tissues and leads to xanthelasma, xanthomas, accelerated atherosclerosis and increased risk of premature coronary heart disease. The disorder occurs in 2 clinical forms: a mild form that becomes evident in the fourth or fifth decade in individuals carrying heterozygous LDLR mutations; a more severe form that usually manifests in the first two decades of life in individuals with homozygous LDLR mutations. The disease may be caused by mutations affecting the gene represented in this entry. Belongs to the apolipoprotein A1/A4/E family. The Singapore human mutation and polymorphism database Apolipoprotein E entry Tangled - Issue 83 of June 2007 3D-structure Alzheimer disease Amyloidosis Cholesterol metabolism Chylomicron Complete proteome Direct protein sequencing Disease mutation Extracellular matrix Glycation Glycoprotein HDL Heparin-binding Hyperlipidemia Lipid metabolism Lipid transport Lipid-binding Neurodegeneration Oxidation Phosphoprotein Polymorphism Reference proteome Repeat Secreted Signal Steroid metabolism Sterol metabolism Transport VLDL E K E K R C L P T A Q H Q K P R A T A V C R G D G GEVQAMLG R Q R C R S R C R C R H R P K E K Q A P R C R Q R C V E EE KK R G L E R H S R R T E A S R H A K A L P L A R A D A T A MKVLWAALLVTFLAGCQAKVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQT LSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQA RLGADMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVY QAGAREGAERGLSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMG SRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEK VQAAVGTSAAPVPSDNH Q6PH81 Q63HN9 CP087_HUMAN UPF0547 protein C16orf87 C16orf87 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Endometrium NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Q13547 HDAC1 false 3 P43365 MAGEA12 false 5 Q6PH81-1 1 Q6PH81-2 2 Belongs to the UPF0547 family. Alternative splicing Coiled coil Complete proteome Phosphoprotein Reference proteome MSATRAKKVKMATKSCPECDQQVPVACKSCPCGYIFISRKLLNAKHSEKSPPSTENKHEA KRRRTERVRREKINSTVNKDLENRKRSRSNSHSDHIRRGRGRPKSASAKKHEEEREKQEK EIDIYANLSDEKAFVFSVALAEINRKIINQRLIL Q96CM8 B4DFQ6 B4DHT5 B4DUF5 Q9H7G2 ACSF2_HUMAN Medium-chain acyl-CoA ligase ACSF2, mitochondrial 6.2.1.2 ACSF2 UNQ493/PRO1009 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4) Adipose tissue Amygdala Caudate nucleus DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT VAL-75 Kidney Skin Identification of novel PPARgamma target genes in primary human adipocytes. FUNCTION INDUCTION Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome. FUNCTION CATALYTIC ACTIVITY An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA (PubMed:17762044). Has some preference toward medium-chain substrates (PubMed:17762044). Plays a role in adipocyte differentiation (PubMed:16380219). a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA Q6RW13 AGTRAP false 3 Q15041 ARL6IP1 false 6 Q96DZ9 CMTM5 false 4 Mitochondrion Q96CM8-1 1 Q96CM8-2 2 No experimental confirmation available. Q96CM8-3 3 No experimental confirmation available. Q96CM8-4 4 No experimental confirmation available. By PPARG. Belongs to the ATP-dependent AMP-binding enzyme family. Acetylation Alternative splicing ATP-binding Complete proteome Fatty acid metabolism Ligase Lipid metabolism Mitochondrion Nucleotide-binding Polymorphism Reference proteome Transit peptide S SARGGMEAGRQRISVPSSFTASAAAH G V V M MAVYVGMLRLGRLCAGSSGVLGARAALSRSWQEARLQGVRFLSSREVDRMVSTPIGGLSY VQGCTKKHLNSKTVGQCLETTAQRVPEREALVVLHEDVRLTFAQLKEEVDKAASGLLSIG LCKGDRLGMWGPNSYAWVLMQLATAQAGIILVSVNPAYQAMELEYVLKKVGCKALVFPKQ FKTQQYYNVLKQICPEVENAQPGALKSQRLPDLTTVISVDAPLPGTLLLDEVVAAGSTRQ HLDQLQYNQQFLSCHDPINIQFTSGTTGSPKGATLSHYNIVNNSNILGERLKLHEKTPEQ LRMILPNPLYHCLGSVAGTMMCLMYGATLILASPIFNGKKALEAISRERGTFLYGTPTMF VDILNQPDFSSYDISTMCGGVIAGSPAPPELIRAIINKINMKDLVVAYGTTENSPVTFAH FPEDTVEQKAESVGRIMPHTEARIMNMEAGTLAKLNTPGELCIRGYCVMLGYWGEPQKTE EAVDQDKWYWTGDVATMNEQGFCKIVGRSKDMIIRGGENIYPAELEDFFHTHPKVQEVQV VGVKDDRMGEEICACIRLKDGEETTVEEIKAFCKGKISHFKIPKYIVFVTNYPLTISGKI QKFKLREQMERHLNL P84085 P26437 ARF5_HUMAN ADP-ribosylation factor 5 ARF5 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells. NUCLEOTIDE SEQUENCE [MRNA] Localization and characterization of the human ADP-ribosylation factor 5 (ARF5) gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Cloning of human full-length CDSs in BD Creator(TM) system donor vector. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Lung Skin Identification of a new Pyk2 target protein with Arf-GAP activity. INTERACTION WITH ASAP2 GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors. INTERACTION WITH GGA1; GGA2 AND GGA3 Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1. INTERACTION WITH RAB11FIP3 AND RAB11FIP4 Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta. INTERACTION WITH NCS1 SUBCELLULAR LOCATION Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Global profiling of co- and post-translationally N-myristoylated proteomes in human cells. MYRISTOYLATION AT GLY-2 CLEAVAGE OF INITIATOR METHIONINE IDENTIFICATION BY MASS SPECTROMETRY Structure of human ADP-ribosylation factor 5. X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 8-180 IN COMPLEX WITH GDP GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Interacts (when activated) with GGA1, GGA2 and GGA3; the interaction is required for proper subcellular location of GGA1, GGA2 and GGA3 (PubMed:11950392). Binds ASAP2 (PubMed:10022920). Interacts with NCS1/FREQ at the Golgi complex (PubMed:17555535). Interacts with RAB11FIP3 and RAB11FIP4 (PubMed:17030804). Golgi apparatus Cytoplasm Perinuclear region Membrane Lipid-anchor Golgi apparatus trans-Golgi network membrane Lipid-anchor Belongs to the small GTPase superfamily. Arf family. 3D-structure Complete proteome Cytoplasm ER-Golgi transport Golgi apparatus GTP-binding Lipoprotein Membrane Myristate Nucleotide-binding Protein transport Reference proteome Transport MGLTVSALFSRIFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKN ICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVQESADELQKMLQEDELRDAV LLVFANKQDMPNAMPVSELTDKLGLQHLRSRTWYVQATCATQGTGLYDGLDWLSHELSKR Q6JBY9 B1AK48 Q4G0E7 Q6IN93 Q8IZM2 Q96DX0 Q9NST4 CPZIP_HUMAN CapZ-interacting protein Protein kinase substrate CapZIP RCSD domain-containing protein 1 RCSD1 CAPZIP Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) FUNCTION INTERACTION WITH CAPZA2 AND CAPZB TISSUE SPECIFICITY PHOSPHORYLATION AT SER-68; SER-83; SER-108; SER-179; SER-216 AND SER-244 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Blood NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Blood Brain Lymph NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-406 (ISOFORM 1) Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] T-cell Large-scale proteomics analysis of the human kinome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-108; SER-116; SER-120; SER-123; SER-177; SER-179; SER-216; SER-267; SER-268 AND SER-284 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-68; SER-82; SER-83; SER-108; SER-116; SER-120; SER-123; SER-127; SER-177; SER-179; SER-216; SER-268; SER-284; SER-298; SER-333; THR-336 AND SER-351 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Stress-induced phosphorylation of CAPZIP may regulate the ability of F-actin-capping protein to remodel actin filament assembly. Interacts with CAPZA2 and CAPZB. Q6JBY9-1 1 Q6JBY9-2 2 Highly expressed in skeletal muscle and more weakly in cardiac muscle. Also expressed in several lymphoid organs, including spleen, thymus, peripheral blood leukocytes, lymph node and bone marrow. Dephosphorylation results in its dissociation from CAPZA2. Alternative splicing Complete proteome Phosphoprotein Polymorphism Reference proteome Q R P A H Q D E MEERPAETNANVDNSASPSVAQLAGRFREQAAAAKETPASKPTRRKPPCSLPLFPPKVDL GQNGEEKSPPNASHPPKFKVKSSPLIEKLQANLTFDPAALLPGASPKSPGLKAMVSPFHS PPSTPSSPGVRSRPSEAEEVPVSFDQPPEGSHLPCYNKVRTRGSIKRRPPSRRFRRSQSD CGELGDFRAVESSQQNGAKEEDGDEVLPSKSKAPGSPLSSEGAAGEGVRTLGPAEKPPLR RSPSRTEKQEEDRATEEAKNGEKARRSSEEVDGQHPAQEEVPESPQTSGPEAENRCGSPR EEKPAGEEAEMEKATEVKGERVQNEEVGPEHDSQETKKLEEGAAVKETPHSPPGGVKGGD VPKQEKGKEKQQEGAVLEPGCSPQTGPAQLETSSEVQSEPAVPKPEDDTPVQDTKM Q07973 Q15807 Q32ML3 Q5I2W7 CP24A_HUMAN 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial 24-OHase Vitamin D(3) 24-hydroxylase 1.14.15.16 Cytochrome P450 24A1 Cytochrome P450-CC24 CYP24A1 CYP24 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Isolation and expression of human 1,25-dihydroxyvitamin D3 24-hydroxylase cDNA. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Alternative splicing of vitamin D-24-hydroxylase: a novel mechanism for the regulation of extrarenal 1,25-dihydroxyvitamin D synthesis. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3) The DNA sequence and comparative analysis of human chromosome 20. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Cloning of the human 1 alpha,25-dihydroxyvitamin D-3 24-hydroxylase gene promoter and identification of two vitamin D-responsive elements. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104 Human 25-hydroxyvitamin D 24-hydroxylase cytochrome P450 subunit maps to a different chromosomal location than that of pseudovitamin D-deficient rickets. NUCLEOTIDE SEQUENCE [MRNA] OF 258-514 (ISOFORM 1) Metabolism of vitamin D3 by cytochromes P450. FUNCTION CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY Mutations in CYP24A1 and idiopathic infantile hypercalcemia. VARIANTS HCINF1 GLU-143 DEL; GLN-159; LYS-322; TRP-396 AND SER-409 CHARACTERIZATION OF VARIANTS HCINF1 GLU-143 DEL; GLN-159; LYS-322; TRP-396 AND SER-409 Has a role in maintaining calcium homeostasis. Catalyzes the adrenodoxin-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3)). The enzyme can perform up to 6 rounds of hydroxylation of calcitriol leading to calcitroic acid. It also shows 23-hydroxylating activity leading to 1-alpha,25-dihydroxyvitamin D(3)-26,23-lactone as end product. calcitriol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitetrol + H2O + 2 oxidized [adrenodoxin] calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = H2O + 2 oxidized [adrenodoxin] + secalciferol heme Mitochondrion Q07973-1 1 Q07973-2 2 No experimental confirmation available. Q07973-3 3 CYP24-SV Specifically expressed in macrophages. Lacks the transit peptide. May be a dominant negative-acting isoform possibly by sequestering vitamin D metabolites. Hypercalcemia, infantile, 1 HCINF1 A disorder characterized by abnormally high level of calcium in the blood, failure to thrive, vomiting, dehydration, and nephrocalcinosis. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the cytochrome P450 family. Alternative splicing Complete proteome Disease mutation Heme Iron Metal-binding Mitochondrion Monooxygenase Oxidoreductase Polymorphism Reference proteome Transit peptide MSSPISKS MYSCFSHR R Q R Q E K M T R W L S G A AY V D G V R A E S G F S MSSPISKSRSLAAFLQQLRSPRQPPRLVTSTAYTSPQPREVPVCPLTAGGETQNAAALPG PTSWPLLGSLLQILWKGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYR TESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKIN EVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIM AIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSAD FLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL PENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGTVLMLNTQ VLGSSEDNFEDSSQFRPERWLQEKEKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIV RKYDIQATDNEPVEMLHSGTLVPSRELPIAFCQR Q504U0 B3KNH7 CD046_HUMAN Renal cancer differentiation gene 1 protein C4orf46 RCDG1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Pancreas Placenta Expression and clinical significance of RCDG1 in renal cell carcinoma: a novel renal cancer-associated gene. SUBCELLULAR LOCATION TISSUE SPECIFICITY Q01850 CDR2 false 5 Q86X02 CDR2L false 4 O60921 HUS1 false 4 Q9BQD3 KXD1 false 5 P0C1Z6-2 TFPT false 3 Cytoplasm Expressed in the kidney, in epithelial cells in both proximal tubules and distal convoluted tubules. Complete proteome Cytoplasm Reference proteome MADPEELQVSSPPPPPPSSPSSSDASAASSPGGPVSLGWPVPSRSSGPTVDQLEEVELQI GDAAFSLTKLLEATSAVSAQVEELAFKCTENARFLKTWRDLLKEGYDSLKPDD Q9P291 Q53HK2 Q9H2Q0 ARMX1_HUMAN Armadillo repeat-containing X-linked protein 1 ARM protein lost in epithelial cancers on chromosome X 1 Protein ALEX1 ARMCX1 ALEX1 AD032 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo ALEX1, a novel human armadillo repeat protein that is expressed differentially in normal tissues and carcinomas. NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Adrenal gland Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Coronary artery The DNA sequence of the human X chromosome. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Uterus Regulates mitochondrial transport during axon regeneration. Increases the proportion of motile mitochondria by recruiting stationary mitochondria into the motile pool. Enhances mitochondria movement and neurite growth in both adult axons and embryonic neurons. Promotes neuronal survival and axon regeneration after nerve injury. May link mitochondria to the Trak1-kinesin motor complex via its interaction with MIRO1. Interacts with MIRO1. P38432 COIL false 3 Q9UBB9 TFIP11 false 3 Q96BR9 ZBTB8A false 5 Mitochondrion Mitochondrion outer membrane Single-pass membrane protein Expressed at high levels ovary, heart, testis, prostate, brain, spleen and colon. Expressed at very low levels in liver and thymus. Not expressed in peripheral blood leukocytes. Not or reduced expressed in lung, prostate, colon, pancreas and ovarian carcinomas. Belongs to the eutherian X-chromosome-specific Armcx family. Complete proteome Membrane Mitochondrion Mitochondrion outer membrane Reference proteome Repeat Signal-anchor Transmembrane Transmembrane helix C R N Y MGRTREAGCVAAGVVIGAGACYCVYRLAWGRDENEKIWDEDEESTDTSEIGVETVKGAKT NAGAGSGAKLQGDSEVKPEVSLGLEDCPGVKEKAHSGSHSGGGLEAKAKALFNTLKEQAS AKAGKGARVGTISGNRTLAPSLPCPGGRGGGCHPTRSGSRAGGRASGKSKGKARSKSTRA PATTWPVRRGKFNFPYKIDDILSAPDLQKVLNILERTNDPFIQEVALVTLGNNAAYSFNQ NAIRELGGVPIIAKLIKTKDPIIREKTYNALNNLSVNAENQGKIKTYISQVCDDTMVCRL DSAVQMAGLRLLTNMTVTNHYQHLLSYSFPDFFALLFLGNHFTKIQIMKLIINFTENPAM TRELVSCKVPSELISLFNKEWDREILLNILTLFENINDNIKNEGLASSRKEFSRSSLFFL FKESGVCVKKIKALANHNDLVVKVKVLKVLTKL Q8N283 A6NEU0 B4DL62 Q3MJ10 Q96LS3 ANR35_HUMAN Ankyrin repeat domain-containing protein 35 ANKRD35 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT SER-428 Brain Tongue The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) VARIANT SER-428 Heart Lung Tongue Q8N283-1 1 Q8N283-2 2 No experimental confirmation available. Alternative splicing ANK repeat Coiled coil Complete proteome Polymorphism Reference proteome Repeat HGANEDAVDAENRSPLHWAASSGCASSVL PPLAVPQVCSCCVTTKPSWTCWIMMDVHP N K P S R Q N D S A E G MKRIFSCSSTQVAVERWNRHDQKLLEAVHRGDVGRVAALASRKSARPTKLDSNGQSPFHL AASKGLTECLTILLANGADINSKNEDGSTALHLATISCQPQCVKVLLQHGANEDAVDAEN RSPLHWAASSGCASSVLLLCDHEAFLDVLDNDGRTPLMIASLGGHAAICSQLLQRGARVN VTDKNDKSALILACEKGSAEVAELLLSHGADAGAVDSTGHDALHYALHTQDKALWRHLQQ ALSRRRRGGQRLVQHPDLASQASPSEPQAGSPPKSSWRAEPEEEQEEKEDEDPCSEEWRW KYEEERRKVVRLEQELVQKTEECKTQAAAYLDLENQIREQAQELGVLLSWEPRASGKQGS SLRPGGDGMEQGCPKDLLAESTQELKKQQQAAATVNPVLAPKKAEDSAPGKIQYEVHGRS QPEEQGPPQSPASETIRKATGQQLTTNGAQTFGPDHADQLPAGQKESSQVLGVEPGGTVA EPVGPAAMNQLLLQLREELAAVWREKDAARGALSRPVMEGALGTPRAEAAAAAWEKMEAR LERVLARLEWAKAGLQVKPEVPSQESREGALKAAPGSIKQDEEKEKRVPGARGEPLGALG GEKALGGLAKGQLEKEMSVLRLSNSNLLEELGELGRERQRLQRELQSLSQRLQREFVPKP EAQVQLQQLRQSVGLLTNELAMEKEATEKLRKLLASQSSGLRGLWDCLPADLVGERSAQS KAAESLEELRACISTLVDRHREAQQVLARLQEENQQLRGSLSPCREPGTSLKAPASPQVA ALEQDLGKLEEELRAVQATMSGKSQEIGKLKQLLYQATEEVAELRAREAASLRQHEKTRG SLVAQAQAWGQELKALLEKYNTACREVGRLREAVAEERRRSGDLAAQAAEQERQASEMRG RSEQFEKTAELLKEKMEHLIGACRDKEAKIKELLKKLEQLSEEVLAIRGENARLALQLQD SQKNHEEIISTYRNHLLNAARGYMEHEVYNILLQILSMEEE Q92481 Q5JYX6 Q9NQ63 Q9NU99 Q9UJI7 Q9Y214 Q9Y3K3 AP2B_HUMAN Transcription factor AP-2-beta AP2-beta Activating enhancer-binding protein 2-beta TFAP2B Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Enhanced apoptotic cell death of renal epithelial cells in mice lacking transcription factor AP-2beta. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1) The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Skin Characterisation of the human AP-2beta and AP-2gamma genes. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27 Chromosomal mapping of the human and mouse homologues of two new members of the AP-2 family of transcription factors. NUCLEOTIDE SEQUENCE [MRNA] OF 2-460 (ISOFORM 1) Mammary tumor Cardiac malformations, adrenal agenesis, neural crest defects and exencephaly in mice lacking Cited2, a new Tfap2 co-activator. FUNCTION INTERACTION WITH CITED2 Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2. INTERACTION WITH CITED4 Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. INTERACTION WITH UBE2I SUMOYLATION AT LYS-21 Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2. INTERACTION WITH CITED2 Syndromic patent ductus arteriosus: evidence for haploinsufficient TFAP2B mutations and identification of a linked sleep disorder. INVOLVEMENT IN CHAR The interaction of KCTD1 with transcription factor AP-2alpha inhibits its transactivation. INTERACTION WITH KCTD1 Novel TFAP2B mutation in nonsyndromic patent ductus arteriosus. INVOLVEMENT IN PDA2 Familial nonsyndromic patent ductus arteriosus caused by mutations in TFAP2B. INVOLVEMENT IN PDA2 Mutations in TFAP2B cause Char syndrome, a familial form of patent ductus arteriosus. VARIANTS CHAR ASP-275 AND CYS-300 Novel TFAP2B mutations that cause Char syndrome provide a genotype-phenotype correlation. VARIANTS CHAR ARG-73; CYS-236; SER-236 AND GLN-285 Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-beta appears to be required for normal face and limb development and for proper terminal differentiation and function of renal tubular epithelia. Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Interacts with CITED4. Interacts with UBE2I. Interacts with KCTD1; this interaction represses transcription activation. Interacts with CITED2 (via C-terminus); the interaction stimulates TFAP2B-transcriptional activity. Nucleus Q92481-1 1 Q92481-2 2 No experimental confirmation available. Sumoylated on Lys-21; which inhibits transcriptional activity. Char syndrome CHAR An autosomal dominant disorder characterized by patent ductus arteriosus (PDA), facial dysmorphism and hand anomalies. The disease is caused by mutations affecting the gene represented in this entry. Patent ductus arteriosus 2 PDA2 A congenital heart defect characterized by the persistent opening of fetal ductus arteriosus that fails to close after birth. Fetal ductus arteriosus connects the pulmonary artery to the descending aorta, allowing unoxygenated blood to bypass the lung and flow to the placenta. Normally, the ductus occludes shortly after birth. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the AP-2 family. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Activating protein 2 entry Activator Alternative splicing Complete proteome Disease mutation DNA-binding Isopeptide bond Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation Ubl conjugation E EMLVHTYSSM P R R C R S A D R Q R C S A QLCKEFTDLLAQDRTPIGNSRPSPILEPGIQSCLTHFSLITHGFGAPAICAALTALQNYLTEALKGMDKMFLNNTTTNRHTSGEGPGSKTGDKEEKHRK GNFVKNLRIYWRRTGHR MHSPPRDQAAIMLWKLVENVKYEDIYEDRHDGVPSHSSRLSQLGSVSQGPYSSAPPLSHT PSSDFQPPYFPPPYQPLPYHQSQDPYSHVNDPYSLNPLHQPQQHPWGQRQRQEVGSEAGS LLPQPRAALPQLSGLDPRRDYHSVRRPDVLLHSAHHGLDAGMGDSLSLHGLGHPGMEDVQ SVEDANNSGMNLLDQSVIKKVPVPPKSVTSLMMNKDGFLGGMSVNTGEVFCSVPGRLSLL SSTSKYKVTVGEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLRERLEKIGLNLPAGRR KAANVTLLTSLVEGEAVHLARDFGYICETEFPAKAVSEYLNRQHTDPSDLHSRKNMLLAT KQLCKEFTDLLAQDRTPIGNSRPSPILEPGIQSCLTHFSLITHGFGAPAICAALTALQNY LTEALKGMDKMFLNNTTTNRHTSGEGPGSKTGDKEEKHRK Q96MT8 D3DND8 D3DND9 D3DNE0 Q96CR0 Q9H8F5 Q9H8N0 CEP63_HUMAN Centrosomal protein of 63 kDa Cep63 CEP63 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4) Placenta Teratocarcinoma NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) Pancreas Proteomic characterization of the human centrosome by protein correlation profiling. IDENTIFICATION (ISOFORM 3) IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] Lymphoblast Cep63 recruits Cdk1 to the centrosome: implications for regulation of mitotic entry, centrosome amplification, and genome maintenance. FUNCTION INTERACTION WITH CDK1 AND CDK2 SUBCELLULAR LOCATION A primary microcephaly protein complex forms a ring around parental centrioles. INVOLVEMENT IN SCKL6 FUNCTION INTERACTION WITH CEP152 SUBCELLULAR LOCATION N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia Proximity interactions among centrosome components identify regulators of centriole duplication. SUBCELLULAR LOCATION INTERACTION WITH CCDC14 AND KIAA0753 Centriolar satellites assemble centrosomal microcephaly proteins to recruit CDK2 and promote centriole duplication. FUNCTION INTERACTION WITH CDK5RAP2; CEP152; WDR62; CEP90; CCDC14 AND CDK2 SUBCELLULAR LOCATION Required for normal spindle assembly. Plays a key role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication. Reported to be required for centrosomal recruitment of CEP152; however, this function has been questioned (PubMed:21983783, PubMed:26297806). Also recruits CDK1 to centrosomes (PubMed:21406398). Plays a role in DNA damage response. Following DNA damage, such as double-strand breaks (DSBs), is removed from centrosomes; this leads to the inactivation of spindle assembly and delay in mitotic progression (PubMed:21406398). Interacts with CEP152 and CDK1; these interactions recruit both ligands to centrosomes (PubMed:21406398). Interacts with CDK2, CDK5RAP2, WDR62, CEP90, KIAA0753/moonraker and CCDC14. CEP63, CDK5RAP2, CEP152, WDR62 are proposed to form a stepwise assembled complex at the centrosome forming a ring near parental centrioles (PubMed:21406398, PubMed:26297806). P09917 ALOX5 false 5 P53365 ARFIP2 false 3 Q49A88 CCDC14 false 5 A2AUM9 Cep152 true 3 Q86XR8 CEP57 false 3 Q86XR8-3 CEP57 false 3 Q8IYX8 CEP57L1 false 3 Q8IYX8-2 CEP57L1 false 3 Q9NRI5 DISC1 false 8 O60941 DTNB false 4 Q86Y13 DZIP3 false 3 Q15910 EZH2 false 3 Q3B820 FAM161A false 3 Q8TES7-6 FBF1 false 3 Q96CS2 HAUS1 false 4 O14964 HGS false 5 Q9NPJ8 NXT2 false 3 Q8WXW3 PIBF1 false 6 Q9BT08 POLR3C false 3 Q969G3 SMARCE1 false 4 Q99909 SSX3 false 3 Q9BSW7 SYT17 false 3 Q92844 TANK false 4 P03410 tax true 4 P14079 tax true 5 Q8TC07 TBC1D15 false 5 Q63HK5 TSHZ3 false 3 P40222 TXLNA false 4 Q8N3L3 TXLNB false 3 Q8TBK6 ZCCHC10 false 3 Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Centriole Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Centriolar satellite Colocalizes with CDK5RAP2, CEP152 and WDR62 in a discrete ring around the proximal end of the parental centriole. At this site, a cohesive structure is predicted to engage parental centrioles and procentrioles. Q96MT8-1 1 Q96MT8-2 2 Q96MT8-3 3 Q96MT8-4 4 Seckel syndrome 6 SCKL6 A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and mental retardation. The disease is caused by mutations affecting the gene represented in this entry. CEP63 and DEUP1 paralogs are both involved in centriole amplification: while CEP63 mediates mother-centriole-dependent centriole duplication, DEUP1 mediates de novo centriole amplification in multiciliated cells. Belongs to the CEP63 family. 3D-structure Acetylation Alternative splicing Cell cycle Cell division Coiled coil Complete proteome Cytoplasm Cytoskeleton DNA damage Dwarfism Mental retardation Mitosis Phosphoprotein Polymorphism Reference proteome AKEISLADLQENYIEALNKLVSENQQLQKDLM RWGFTMLSSLVLNFGIQAIRQPQRPKVLELQV S L K R MEALLEGIQNRGHGGGFLTSCEAELQELMKQIDIMVAHKKSEWEGRTHALETCLKIREQE LKSLRSQLDVTHKEVGMLHQQVEEHEKIKQEMTMEYKQELKKLHEELCILKRSYEKLQKK QMREFRGNTKNHREDRSEIERLTAKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQ SEIIQAQLVNRKQKLESVELSSQSEIQHLSSKLERANDTICANELEIERLTMRVNDLVGT SMTVLQEQQQKEEKLRESEKLLEALQEEKRELKAALQSQENLIHEARIQKEKLQEKVKAT NTQHAVEAIRPREESLAEKKYTSQGQGDLDSVLSQLNFTHTSEDLLQAEVTCLEGSLESV SATCKQLSQELMEKYEELKRMEAHNNEYKAEIKKLKEQILQGEQSYSSALEGMKMEISHL TQELHQRDITIASTKGSSSDMEKRLRAEMQKAEDKAVEHKEILDQLESLKLENRHLSEMV MKLELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMNTKSQLEISTQMCKKQNDR IFKPTHSRTTEFKNTEFKPTHGQHRHDGIKTEHYKTDLHSPRGQASDSINPMSRVLSPLS PQISPCSSTRSLTSYSLCKTHSLPSALDTNEANFSDTMSESMNDQEEFISSCSLPVSPLG SIATRFLEEEELRSHHILERLDAHIEELKRESEKTVRQFTALK Q7L5N1 A4D2A3 O15387 CSN6_HUMAN COP9 signalosome complex subunit 6 SGN6 Signalosome subunit 6 JAB1-containing signalosome subunit 6 MOV34 homolog Vpr-interacting protein hVIP COPS6 CSN6 HVIP Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Human chromosome 7: DNA sequence and biology. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly. NUCLEOTIDE SEQUENCE [MRNA] OF 22-327 A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits. PARTIAL PROTEIN SEQUENCE FUNCTION SUBCELLULAR LOCATION Biochemical mechanism of HIV-I Vpr function. Specific interaction with a cellular protein. INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION) HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular factor linked to the G2/M phase transition of the mammalian cell cycle. SUBCELLULAR LOCATION TISSUE SPECIFICITY INTERACTION WITH HUMAN VPR (MICROBIAL INFECTION) COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. FUNCTION Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome. FUNCTION COMPOSITION OF THE CSN COMPLEX INTERACTION WITH RBX1 Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome. INTERACTION WITH EIF3S6 Carboxyl terminus of hVIP/mov34 is critical for HIV-1-Vpr interaction and glucocorticoid-mediated signaling. INTERACTION WITH VPR (MICROBIAL INFECTION) The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. FUNCTION Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome. FUNCTION Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. IDENTIFICATION IN THE CSN COMPLEX Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3 ubiquitin ligase for 14-3-3sigma. FUNCTION INTERACTION WITH COP1 AND SFN An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver CSNAP is a stoichiometric subunit of the COP9 signalosome. COMPOSITION OF THE CSN COMPLEX INTERACTION WITH COPS9 Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Has some glucocorticoid receptor-responsive activity. Stabilizes COP1 through reducing COP1 auto-ubiquitination and decelerating COP1 turnover rate, hence regulates the ubiquitination of COP1 targets. Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 isoform 1 (PubMed:18850735, PubMed:26456823). In the complex, it probably interacts directly with COPS2, COPS4, COPS5, COPS7 (COPS7A or COPS7B) and COPS9 isoform 1 (PubMed:11337588, PubMed:26456823). Interacts with the translation initiation factor EIF3S6 (PubMed:12220626). Interacts weakly with RBX1 (PubMed:11337588). Directly interacts with COP1 and 14-3-3 protein sigma/SFN (PubMed:21625211). (Microbial infection) Interacts with the HIV-1 protein Vpr. Q9BX70 BTBD2 false 2 Q8NHY2 COP1 false 3 Q9UNS2 COPS3 false 18 Q9BT78 COPS4 false 12 Q92905 COPS5 false 15 P28482 MAPK1 false 2 P31947 SFN false 7 Nucleus Cytoplasm The interaction with HIV-1 Vpr protein possibly leads its translocation to a perinuclear region. Widely expressed. Belongs to the peptidase M67A family. CSN6 subfamily. Although related to the peptidase M67A family, it lacks the JAMM motif that probably constitutes the catalytic center and therefore it probably does not have a protease activity. Translation N-terminally extended. 3D-structure Complete proteome Cytoplasm Direct protein sequencing Host-virus interaction Nucleus Reference proteome Signalosome MAAAAAAAAATNGTGGSSGMEVDAAVVPSVMACGVTGSVSVALHPLVILNISDHWIRMRS QEGRPVQVIGALIGKQEGRNIEVMNSFELLSHTVEEKIIIDKEYYYTKEEQFKQVFKELE FLGWYTTGGPPDPSDIHVHKQVCEIIESPLFLKLNPMTKHTDLPVSVFESVIDIINGEAT MLFAELTYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVKLILE YVKASEAGEVPFNHEILREAYALCHCLPVLSTDKFKTDFYDQCNDVGLMAYLGTITKTCN TMNQFVNKFNVLYDRQGIGRRMRGLFF Q99440 Q17R65 CD006_HUMAN Uncharacterized protein encoded by LINC01587 Protein AC1 LINC01587 AC1 C4orf6 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Fluorescent differential display analysis of gene expression in differentiating neuroblastoma cells. NUCLEOTIDE SEQUENCE [MRNA] Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Expressed in neuroblastoma. Complete proteome Polymorphism Reference proteome N K MDTQKQIHKTHNSKNQFFTIFFFLSVEFGKEGTRKNFYLLLSIGHYGRKSRRADLGTADT ADKTEPECFAASWTFDPNPSVTVSGAHSTAVHQ Q6UWU4 B4DTT1 B7Z9L9 F4NAR0 F4NAR1 Q5TDC5 Q6ZMG5 Q7Z356 Q8IZ35 CF089_HUMAN Bombesin receptor-activated protein C6orf89 Amfion C6orf89 BRAP UNQ177/PRO203 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo C6orf89 encodes three distinct HDAC enhancers that function in the nucleolus, the Golgi and the midbody. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2) FUNCTION SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 3) INTERACTION WITH SIN3B TOPOLOGY GLYCOSYLATION SUBUNIT Adipocyte The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3) Placenta The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Colon endothelium The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Muscle Placenta Cloning of a novel protein interacting with BRS-3 and its effects in wound repair of bronchial epithelial cells. FUNCTION INTERACTION WITH BRS3 SUBCELLULAR LOCATION (ISOFORM 2) Exhibits histone deacetylase (HDAC) enhancer properties (PubMed:23460338). May play a role in cell cycle progression and wound repair of bronchial epithelial cells (PubMed:21857995). Homodimer (PubMed:23460338). Interacts with BRS3 (PubMed:21857995). Interacts (via N-terminus) with SIN3B (PubMed:23460338). Isoform 1 Golgi apparatus membrane Single-pass type II membrane protein Midbody Isoform 2 Golgi apparatus membrane Single-pass type II membrane protein Midbody Isoform 3 Cytoplasm Nucleus Nucleolus Retained in nucleolar organiser regions (NORs) in mitotic cells (PubMed:23460338). Q6UWU4-1 1 42/116mp Q6UWU4-2 2 Q6UWU4-3 3 34/64sp Glycosylated. Named amfion, after 'the 4 Amfion heroes in Greek mythology and their deeds in different locations within the mother land. Translation N-terminally shortened. Translation N-terminally shortened. Alternative splicing Complete proteome Cytoplasm Glycoprotein Golgi apparatus Membrane Nucleus Reference proteome Signal-anchor Transmembrane Transmembrane helix M MDFILEDM A V D H P A Y C MDLAANEISIYDKLSETVDLVRQTGHQCGMSEKAIEKFIRQLLEKNEPQRPPPQYPLLIV VYKVLATLGLILLTAYFVIQPFSPLAPEPVLSGAHTWRSLIHHIRLMSLPIAKKYMSENK GVPLHGGDEDRPFPDFDPWWTNDCEQNESEPIPANCTGCAQKHLKVMLLEDAPRKFERLH PLVIKTGKPLLEEEIQHFLCQYPEATEGFSEGFFAKWWRCFPERWFPFPYPWRRPLNRSQ MLRELFPVFTHLPFPKDASLNKCSFLHPEPVVGSKMHKMPDLFIIGSGEAMLQLIPPFQC RRHCQSVAMPIEPGDIGYVDTTHWKVYVIARGVQPLVICDGTAFSEL A6NNH2 F90AR_HUMAN Protein FAM90A27P FAM90A27P Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence and biology of human chromosome 19. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Belongs to the FAM90 family. Complete proteome Reference proteome MARHSVHHQAQRPPRAKNPQEQQRRPMGQTTLPAEQEESRVKCKNCGAFGHSARSKTCPI KRWSGALPLQALGSHKEKENLKPAKAQLPFTTPGPFTTNDREKERSPSPQQQQSEAPTQT FPRTPQEKMQEAWKEPAEDCLFLRHPTMPLPVHTTKKRSVLGPVSTGPPPVNKPEMRLLC PSGHNDSPQLSTCGPTKGHGRDVTASLLPVLKSSHQTPTLSARLPANRPDMSSHGALQPA MQALALGPGLKSQAEIKHPDADAKPRPQQVRKQCGQDSRTQAPDKEPAPVPTQTFQNPAK KARFSSFQTPALRTQLPDVGAVQTLQPPRTATGLGSKEAPKATAETAATKTATLQPRVNL QPAPSSPFLGPAQGCPVLQPGPPIHVPGRPGSVTFMRGDKGQKSPRFRMPPTSRPPENSA SAQSPRFSRQPEGQGPQVSTSVLYEDLLVTSSSEDSDSD Q13685 Q8WUJ9 Q96H92 AAMP_HUMAN Angio-associated migratory cell protein AAMP Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of a new immunoglobulin superfamily protein expressed in blood vessels with a heparin-binding consensus sequence. NUCLEOTIDE SEQUENCE [MRNA] PARTIAL PROTEIN SEQUENCE TISSUE SPECIFICITY Brain Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Ovary Skin Angio-associated migratory cell protein is expressed as an extracellular protein by blood-vessel-associated mesenchymal cells. FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY Blockade of angio-associated migratory cell protein inhibits smooth muscle cell migration and neointima formation in accelerated atherosclerosis. FUNCTION SUBCELLULAR LOCATION Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Plays a role in angiogenesis and cell migration. In smooth muscle cell migration, may act through the RhoA pathway. Cell membrane Cytoplasm Expressed in metastatic melanoma, liver, skin, kidney, heart, lung, lymph node, skeletal muscle and brain, and also in A2058 melanoma cells and activated T-cells (at protein level). Expressed in blood vessels. Strongly expressed in endothelial cells, cytotrophoblasts, and poorly differentiated. colon adenocarcinoma cells found in lymphatics. Angiogenesis Cell membrane Complete proteome Cytoplasm Developmental protein Differentiation Direct protein sequencing Membrane Phosphoprotein Polymorphism Reference proteome Repeat WD repeat I V MESESESGAAADTPPLETLSFHGDEEIIEVVELDPGPPDPDDLAQEMEDVDFEEEEEEEG NEEGWVLEPQEGVVGSMEGPDDSEVTFALHSASVFCVSLDPKTNTLAVTGGEDDKAFVWR LSDGELLFECAGHKDSVTCAGFSHDSTLVATGDMSGLLKVWQVDTKEEVWSFEAGDLEWM EWHPRAPVLLAGTADGNTWMWKVPNGDCKTFQGPNCPATCGRVLPDGKRAVVGYEDGTIR IWDLKQGSPIHVLKGTEGHQGPLTCVAANQDGSLILTGSVDCQAKLVSATTGKVVGVFRP ETVASQPSLGEGEESESNSVESLGFCSVMPLAAVGYLDGTLAIYDLATQTLRHQCQHQSG IVQLLWEAGTAVVYTCSLDGIVRLWDARTGRLLTDYRGHTAEILDFALSKDASLVVTTSG DHKAKVFCVQRPDR Q8N4F0 Q6UWN3 Q6ZME0 Q8NFQ7 BPIB2_HUMAN BPI fold-containing family B member 2 Bactericidal/permeability-increasing protein-like 1 BPI-like 1 Long palate, lung and nasal epithelium carcinoma-associated protein 2 RYSR BPIFB2 BPIL1 C20orf184 LPLUNC2 UNQ2489/PRO5776 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Three new human members of the lipid transfer/lipopolysaccharide binding protein family (LT/LBP). NUCLEOTIDE SEQUENCE [MRNA] Trachea The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The DNA sequence and comparative analysis of human chromosome 20. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Lung Testis Signal peptide prediction based on analysis of experimentally verified cleavage sites. PROTEIN SEQUENCE OF 21-35 Expansion of the BPI family by duplication on human chromosome 20: characterization of the RY gene cluster in 20q11.21 encoding olfactory transporters/antimicrobial-like peptides. SUBCELLULAR LOCATION TISSUE SPECIFICITY Fetal brain A single kinase generates the majority of the secreted phosphoproteome. PHOSPHORYLATION AT THR-52 AND SER-60 Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96; ASN-293 AND ASN-332 Saliva The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] VAL-20 Secreted Highly expressed in tonsils, especially in hypertrophic tonsils. Detected at very low levels in fetal liver. Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family. Complete proteome Direct protein sequencing Disulfide bond Glycoprotein Phosphoprotein Polymorphism Reference proteome Secreted Signal A V K M A V K N V G MAWASRLGLLLALLLPVVGASTPGTVVRLNKAALSYVSEIGKAPLQRALQVTVPHFLDWS GEALQPTRIRILNVHVPRLHLKFIAGFGVRLLAAANFTFKVFRAPEPLELTLPVELLADT RVTQSSIRTPVVSISACSLFSGHANEFDGSNSTSHALLVLVQKHIKAVLSNKLCLSISNL VQGVNVHLGTLIGLNPVGPESQIRYSMVSVPTVTSDYISLEVNAVLFLLGKPIILPTDAT PFVLPRHVGTEGSMATVGLSQQLFDSALLLLQKAGALNLDITGQLRSDDNLLNTSALGRL IPEVARQFPEPMPVVLKVRLGATPVAMLHTNNATLRLQPFVEVLATASNSAFQSLFSLDV VVNLRLQLSVSKVKLQGTTSVLGDVQLTVASSNVGFIDTDQVRTLMGTVFEKPLLDHLNA LLAMGIALPGVVNLHYVAPEIFVYEGYVVISSGLFYQS P54802 ANAG_HUMAN Alpha-N-acetylglucosaminidase 3.2.1.50 N-acetyl-alpha-glucosaminidase NAG Alpha-N-acetylglucosaminidase 82 kDa form Alpha-N-acetylglucosaminidase 77 kDa form NAGLU UFHSD1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The molecular basis of Sanfilippo syndrome type B. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] VARIANT GLY-737 Testis Cloning and expression of the gene involved in Sanfilippo B syndrome (mucopolysaccharidosis III B). NUCLEOTIDE SEQUENCE [MRNA] PARTIAL PROTEIN SEQUENCE CHARACTERIZATION VARIANT GLY-737 Molecular dissection of a cosmid from a gene-rich region in 17q21 and characterization of a candidate gene for alpha-N-acetylglucosaminidase with two cDNA isoforms. NUCLEOTIDE SEQUENCE [MRNA] VARIANT GLY-737 DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT GLY-737 Skin Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-532 Liver Crystal structure of N-acetylglucosaminidase. X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 24-743 GLYCOSYLATION AT ASN-261; ASN-272; ASN-435; ASN-503; ASN-526 AND ASN-532 Adult-onset painful axonal polyneuropathy caused by a dominant NAGLU mutation. INVOLVEMENT IN CMT2V VARIANT CMT2V THR-403 Genotype-phenotype correspondence in Sanfilippo syndrome type B. VARIANTS MPS3B CYS-140; CYS-455; LEU-521; GLY-612; CYS-674 AND HIS-674 NAGLU mutations underlying Sanfilippo syndrome type B. VARIANTS MPS3B HIS-92; SER-115; CYS-140; LYS-153; LEU-358; VAL-664 AND ARG-682 Identification of 12 novel mutations in the alpha-N-acetylglucosaminidase gene in 14 patients with Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB). VARIANTS MPS3B CYS-48; CYS-140; CYS-234; ARG-268; LEU-521; TRP-565; PRO-591 AND LYS-705 Mucopolysaccharidosis type IIIB (Sanfilippo B): identification of 18 novel alpha-N-acetylglucosaminidase gene mutations. VARIANTS MPS3B CYS-79; ARG-100; CYS-140; PHE-142 DEL; LEU-243; PHE-277; PRO-280; ARG-292; LYS-452; TRP-482; ARG-561; GLN-565; HIS-674 AND LYS-705 VARIANT GLY-737 Sanfilippo type B syndrome (mucopolysaccharidosis III B): allelic heterogeneity corresponds to the wide spectrum of clinical phenotypes. VARIANTS MPS3B LEU-48; SER-69; PRO-227; ARG-248; ARG-292; PHE-334; SER-410; ARG-414; LEU-521; PRO-560; PRO-565; TRP-565; PHE-617; CYS-643; GLU-650; CYS-674 AND PRO-676 VARIANT GLY-737 Mucopolysaccharidosis type IIIB: characterisation and expression of wild-type and mutant recombinant alpha-N-acetylglucosaminidase and relationship with sanfilippo phenotype in an attenuated patient. VARIANT MPS3B LEU-48 CHARACTERIZATION OF VARIANT MPS3B LEU-48 Molecular defects in the alpha-N-acetylglucosaminidase gene in Italian Sanfilippo type B patients. VARIANTS MPS3B PHE-35; ASP-82; CYS-140; CYS-156; CYS-234; ARG-292; GLY-501; TRP-520; TYR-534 AND CYS-649 CHARACTERIZATION OF VARIANTS MPS3B PHE-35; ASP-82; CYS-156; GLY-501; TRP-520; TYR-534 AND CYS-649 Allelic heterogeneity in Spanish patients with Sanfilippo disease type B. Identification of eight new mutations. VARIANTS MPS3B SER-79; CYS-234; GLY-474; TRP-565 AND PHE-658 Sanfilippo syndrome in Turkey: identification of novel mutations in subtypes A and B. VARIANTS MPS3B LYS-153; ARG-248; ILE-437 AND ARG-682 Molecular analysis of the alpha-N-acetylglucosaminidase gene in seven Japanese patients from six unrelated families with mucopolysaccharidosis IIIB (Sanfilippo type B), including two novel mutations. VARIANTS MPS3B MET-241; LEU-314; TRP-482; PRO-565 AND TRP-565 Identification and characterisation of mutations underlying Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB). VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412 AND TRP-565 CHARACTERIZATION OF VARIANTS MPS3B CYS-130; ARG-154; CYS-309; GLU-412 AND TRP-565 Sanfilippo B syndrome: molecular defects in Greek patients. VARIANTS MPS3B CYS-140; PRO-242; ARG-292; ARG-414; LYS-446; LYS-452; GLN-482 AND LEU-516 CHARACTERIZATION OF VARIANTS MPS3B PRO-242; ARG-414; LYS-446; GLN-482 AND LEU-516 Sanfilippo type B syndrome: five patients with an R565P homozygous mutation in the alpha-N-acetylglucosaminidase gene from the Okinawa islands in Japan. VARIANT MPS3B PRO-565 Molecular defects in Sanfilippo syndrome type B (mucopolysaccharidosis IIIB). VARIANTS MPS3B TRP-38; GLY-77; CYS-79; CYS-130; PRO-246; CYS-309; CYS-335; ARG-414; LYS-452; TRP-482; TRP-520; LEU-521 AND TRP-565 CHARACTERIZATION OF VARIANTS MPS3B TRP-38; GLY-77 AND CYS-335 Update of the spectrum of mucopolysaccharidoses type III in Tunisia: identification of three novel mutations and in silico structural analysis of the missense mutations. VARIANTS MPS3B 153-GLU--TRP-743 DEL AND PRO-550 Involved in the degradation of heparan sulfate. Hydrolysis of terminal non-reducing N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides. Monomer and homodimer. Lysosome Liver, ovary, peripheral blood leukocytes, testis, prostate, spleen, colon, lung, placenta and kidney. Mucopolysaccharidosis 3B MPS3B A form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life. The disease is caused by mutations affecting the gene represented in this entry. Charcot-Marie-Tooth disease 2V CMT2V An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2V is an autosomal dominant sensory neuropathy with late onset. The main clinical feature is recurrent leg pain that progresses to constant painful paraesthesias in the feet and later the hands. As it evolves, some patients develop a mild sensory ataxia. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the glycosyl hydrolase 89 family. A MPS3B mutation at position 100 was erroneously reported (PubMed:9950362) as an amino acid change from Arg to His. The right amino acid change is from His to Arg. 3D-structure Charcot-Marie-Tooth disease Complete proteome Direct protein sequencing Disease mutation Glycoprotein Glycosidase Hydrolase Lysosome Mucopolysaccharidosis Neurodegeneration Neuropathy Polymorphism Reference proteome Signal L F R W F C F L G S V G G C G S G D Y H H R P S R C Y C E K I R W C H P R C V M L P P L A P H R W R C F L P G R Y C F L V F Y C P L I T F S G E H R T I E K E K Y C W G R Q R W V G P L R W P L S Y L P L P L R R P R Q R W L P S G L F R C R H W C G E Y F A V R C R H R P L R E K R G A L S L MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKP GLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGE LTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYL ALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTP VLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELI KEFGTDHIYGADTFNEMQPPSSEPSYLAAATTAVYEAMTAVDTEAVWLLQGWLFQHQPQF WGPAQIRAVLGAVPRGRLLVLDLFAESQPVYTRTASFQGQPFIWCMLHNFGGNHGLFGAL EAVNGGPEAARLFPNSTMVGTGMAPEGISQNEVVYSLMAELGWRKDPVPDLAAWVTSFAA RRYGVSHPDAGAAWRLLLRSVYNCSGEACRGHNRSPLVRRPSLQMNTSIWYNRSDVFEAW RLLLTSAPSLATSPAFRYDLLDLTRQAVQELVSLYYEEARSAYLSKELASLLRAGGVLAY ELLPALDEVLASDSRFLLGSWLEQARAAAVSEAEADFYEQNSRYQLTLWGPEGNILDYAN KQLAGLVANYYTPRWRLFLEALVDSVAQGIPFQQHQFDKNVFQLEQAFVLSKQRYPSQPR GDTVDLAKKIFLKYYPRWVAGSW O00189 D6W5U1 Q8WV65 Q9UHK9 AP4M1_HUMAN AP-4 complex subunit mu-1 AP-4 adaptor complex mu subunit Adaptor-related protein complex 4 subunit mu-1 Mu subunit of AP-4 Mu-adaptin-related protein 2 mu-ARP2 Mu4-adaptin mu4 AP4M1 MUARP2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of two new mu-adaptin-related proteins, mu-ARP1 and mu-ARP2. NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY Brain Characterization of a fourth adaptor-related protein complex. NUCLEOTIDE SEQUENCE [MRNA] FUNCTION SUBUNIT Brain Signal-binding specificity of the mu4 subunit of the adaptor protein complex, AP-4. NUCLEOTIDE SEQUENCE [MRNA] FUNCTION INTERACTION WITH LAMP2 SUBCELLULAR LOCATION Spleen NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain AP-4, a novel protein complex related to clathrin adaptors. FUNCTION SUBUNIT Mutation in the AP4M1 gene provides a model for neuroaxonal injury in cerebral palsy. INVOLVEMENT IN SPG50 AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells. FUNCTION SUBUNIT Association between rare variants in AP4E1, a component of intracellular trafficking, and persistent stuttering. FUNCTION INTERACTION WITH NAGPA Sorting of the Alzheimer's disease amyloid precursor protein mediated by the AP-4 complex. X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 160-453 IN COMPLEX WITH APP PEPTIDE FUNCTION SUBCELLULAR LOCATION MUTAGENESIS OF PHE-255 AND ARG-283 SUBUNIT Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways (PubMed:10436028, PubMed:11139587, PubMed:10066790, PubMed:11802162, PubMed:20230749). AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system (PubMed:11139587, PubMed:20230749). It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons (By similarity). Within AP-4, the mu-type subunit AP4M1 is directly involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos (PubMed:10436028, PubMed:11139587, PubMed:26544806, PubMed:20230749). The adaptor protein complex 4 (AP-4) may also recognize other types of sorting signal (By similarity). Adaptor protein complex 4 (AP-4) is a heterotetramer composed of two large adaptins (epsilon-type subunit AP4E1 and beta-type subunit AP4B1), a medium adaptin (mu-type subunit AP4M1) and a small adaptin (sigma-type AP4S1) (PubMed:10436028, PubMed:10066790, PubMed:11802162). Interacts with tyrosine-based sorting signals on the cytoplasmic tail of cargo proteins such as APP, LAMP2 and NAGPA (PubMed:11139587, PubMed:26544806, PubMed:20230749). Interacts with the C-terminal domain of GRID2 (By similarity). Interacts with GRIA1 and GRIA2; the interaction is indirect via CACNG3 (By similarity). Interacts with CACNG3; CACNG3 associates GRIA1 and GRIA2 with the adaptor protein complex 4 (AP-4) to target them to the somatodendritic compartment of neurons (By similarity). Q96K76 USP47 false 3 Golgi apparatus trans-Golgi network membrane Peripheral membrane protein Early endosome Found in soma and dendritic shafts of neuronal cells. Ubiquitous. Highly expressed in testis and lowly expressed in brain and lung. Spastic paraplegia 50, autosomal recessive SPG50 A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG50 affected individuals present postnatally with early infantile hypotonia, delayed psychomotor development, strabismus, lack of independent walking and severe mental retardation. They develop progressive spasticity of all limbs with generalized hypertonia, hyperreflexia, and extensor plantar responses by the end of the first year of life. Speech is absent or limited. Pseudobulbar signs, such as drooling, stereotypic laughter, and exaggerated jaw jerk, are part of the clinical picture. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the adaptor complexes medium subunit family. 3D-structure Complete proteome Endosome Golgi apparatus Hereditary spastic paraplegia Membrane Neurodegeneration Protein transport Reference proteome Transport F A R D R G Q R L M S C MISQFFILSSKGDPLIYKDFRGDSGGRDVAELFYRKLTGLPGDESPVVMHHHGRHFIHIR HSGLYLVVTTSENVSPFSLLELLSRLATLLGDYCGSLGEGTISRNVALVYELLDEVLDYG YVQTTSTEMLRNFIQTEAVVSKPFSLFDLSSVGLFGAETQQSKVAPSSAASRPVLSSRSD QSQKNEVFLDVVERLSVLIASNGSLLKVDVQGEIRLKSFLPSGSEMRIGLTEEFCVGKSE LRGYGPGIRVDEVSFHSSVNLDEFESHRILRLQPPQGELTVMRYQLSDDLPSPLPFRLFP SVQWDRGSGRLQVYLKLRCDLLSKSQALNVRLHLPLPRGVVSLSQELSSPEQKAELAEGA LRWDLPRVQGGSQLSGLFQMDVPGPPGPPSHGLSTSASPLGLGPASLSFELPRHTCSGLQ VRFLRLAFRPCGNANPHKWVRHLSHSDAYVIRI Q96SW2 B2R6H4 C9IZA9 C9JAH6 Q6AI62 Q6NVZ0 Q9UHW4 CRBN_HUMAN Protein cereblon CRBN AD-006 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain The DNA sequence, annotation and analysis of human chromosome 3. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Brain Lung Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-442 Adrenal gland The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-250 Fetal kidney A mutation in a novel ATP-dependent Lon protease gene in a kindred with mild mental retardation. INVOLVEMENT IN MRT2A TISSUE SPECIFICITY Primary function analysis of human mental retardation related gene CRBN. TISSUE SPECIFICITY Dysregulation of large-conductance Ca2+-activated K+ channel expression in nonsyndromal mental retardation due to a cereblon p.R419X mutation. FUNCTION Identification of a primary target of thalidomide teratogenicity. FUNCTION SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY IDENTIFICATION IN A DCX COMPLEX WITH DDB1; RBX1 AND CUL4A THALIDOMIDE-BINDING UBIQUITINATION MUTAGENESIS OF TYR-384 AND TRP-386 Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia Immunomodulatory agents lenalidomide and pomalidomide co-stimulate T cells by inducing degradation of T cell repressors Ikaros and Aiolos via modulation of the E3 ubiquitin ligase complex CRL4(CRBN.). FUNCTION MISCELLANEOUS Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with thalidomide. FUNCTION INTERACTION WITH DDB1 UBIQUITINATION Structure of the human cereblon-DDB1-lenalidomide complex reveals basis for responsiveness to thalidomide analogs. X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 48-428 IN COMPLEX WITH DDB1; S-LENALIDOMIDE AND ZINC FUNCTION INTERACTION WITH DDB1 DOMAIN MUTAGENESIS OF TRP-386 MISCELLANEOUS A missense mutation in the CRBN gene that segregates with intellectual disability and self-mutilating behaviour in a consanguineous Saudi family. INVOLVEMENT IN MRT2A VARIANT MRT2A ARG-391 Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. May play a role in memory and learning by regulating the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1. Binding of pomalidomide and other thalidomide-related drugs changes the substrate specificity of the human protein, leading to decreased degradation of MEIS2 and other target proteins and increased degradation of MYC, IRF4, IKZF1 and IKZF3. Protein modification; protein ubiquitination. Interacts with KCNT1 (By similarity). Component of a DCX (DDB1-CUL4-X-box) protein ligase complex, at least composed of CRBN, CUL4A, DDB1 and RBX1. Interacts directly with DDB1 (PubMed:25043012, PubMed:25108355). Interacts (in pomalidomide-bound form) with IKZF1 and IKZF3 (PubMed:24328678). P48729 CSNK1A1 false 3 Q16531 DDB1 false 7 Q13422-7 IKZF1 false 2 Q9P286 PAK5 false 3 Q93062 RBPMS false 3 Cytoplasm Nucleus Membrane Peripheral membrane protein Q96SW2-1 1 Q96SW2-2 2 No experimental confirmation available. Widely expressed. Highly expressed in brain. The CULT domain binds thalidomide and related drugs, such as pomalidomide and lenalidomide. Drug binding leads to a change in substrate specificity of the human DCX (DDB1-CUL4-X-box) E3 protein ligase complex, while no such change is observed in rodents. Ubiquitinated, ubiquitination is mediated by its own DCX protein ligase complex. Mental retardation, autosomal recessive 2A MRT2A A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs. MRT2A patients display mild mental retardation with a standard IQ ranged from 50 to 70. IQ scores are lower in males than females. Developmental milestones are mildly delayed. There are no dysmorphic or autistic features. The disease is caused by mutations affecting the gene represented in this entry. Thalidomide was widely prescribed to pregnant women in the late 1950s as a sedative and as treatment against morning sickness. Thalidomide was found to be teratogenic, causing multiple birth defects. Recently, thalidomide use has increased for the treatment of multiple myeloma and erythema nodosum leprosum, a painful complication of leprosy. Thalidomide binding leads to a change in substrate specificity of the human DCX (DDB1-CUL4-X-box) E3 protein ligase complex, and this is probably the underlying cause of the teratogenic activity of thalidomide, possibly due to abnormal regulation of the BMP and FGF8 signaling pathways (PubMed:20223979). The thalidomide-induced change in substrate specificity leads to increased degradation of MYC, IRF4, IKZF1 and IKZF3, and this is probably the reason for the anti-proliferative and immunomodulatory effects of thalidomide and related drugs (PubMed:25108355). Thalidomide is also teratogenic in chicken and zebrafish, but not in mice. Belongs to the CRBN family. Although it contains a Lon N-terminal domain also found in proteases of the peptidase S16 family, it does not contain the ATP-binding and catalytic domains, suggesting that it has no protease activity. Translation N-terminally extended. A short story - Issue 117 of May 2010 3D-structure Alternative splicing Complete proteome Cytoplasm Disease mutation Membrane Mental retardation Metal-binding Nucleus Phosphoprotein Reference proteome Ubl conjugation Ubl conjugation pathway Zinc C R Y A W A K R L P D G E G MAGEGDQQDAAHNMGNHLPLLPAESEEEDEMEVEDQDSKEAKKPNIINFDTSLPTSHTYL GADMEEFHGRTLHDDDSCQVIPVLPQVMMILIPGQTLPLQLFHPQEVSMVRNLIQKDRTF AVLAYSNVQEREAQFGTTAEIYAYREEQDFGIEIVKVKAIGRQRFKVLELRTQSDGIQQA KVQILPECVLPSTMSAVQLESLNKCQIFPSKPVSREDQCSYKWWQKYQKRKFHCANLTSW PRWLYSLYDAETLMDRIKKQLREWDENLKDDSLPSNPIDFSYRVAACLPIDDVLRIQLLK IGSAIQRLRCELDIMNKCTSLCCKQCQETEITTKNEIFSLSLCGPMAAYVNPHGYVHETL TVYKACNLNLIGRPSTEHSWFPGYAWTVAQCKICASHIGWKFTATKKDMSPQKFWGLTRS ALLPTIPDTEDEISPDKVILCL O75718 B2RBL6 CRTAP_HUMAN Cartilage-associated protein CRTAP CASP Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo cDNA cloning, characterization and chromosome mapping of the gene encoding human cartilage associated protein (CRTAP). NUCLEOTIDE SEQUENCE [MRNA] Fetal brain Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT ASP-137 Kidney CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta. FUNCTION INVOLVEMENT IN OI7 Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Deficiency of CRTAP in non-lethal recessive osteogenesis imperfecta reduces collagen deposition into matrix. INVOLVEMENT IN OI7 N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] CRTAP and LEPRE1 mutations in recessive osteogenesis imperfecta. VARIANT OI7 PRO-67 CRTAP mutations in lethal and severe osteogenesis imperfecta: the importance of combining biochemical and molecular genetic analysis. VARIANTS OI7 GLU-13 AND GLU-157 Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues. Secreted Extracellular space Extracellular matrix Found in articular chondrocytes. Expressed in a variety of tissues. Osteogenesis imperfecta 7 OI7 A form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI7 is an autosomal recessive, severe form. Multiple fractures are present at birth and patients have short stature, short humeri and femora, coxa vara, and white sclera. Dentinogenesis imperfecta is absent. Death can occur in the perinatal period due to secondary respiratory insufficiency. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the leprecan family. Cartilage-associated protein (CRTAP) Complete proteome Disease mutation Dwarfism Extracellular matrix Glycoprotein Hydroxylation Osteogenesis imperfecta Polymorphism Reference proteome Secreted Signal A E L P E D K E L V MEPGRRGAAALLALLCVACALRAGRAQYERYSFRSFPRDELMPLESAYRHALDKYSGEHW AESVGYLEISLRLHRLLRDSEAFCHRNCSAAPQPEPAAGLASYPELRLFGGLLRRAHCLK RCKQGLPAFRQSQPSREVLADFQRREPYKFLQFAYFKANNLPKAIAAAHTFLLKHPDDEM MKRNMAYYKSLPGAEDYIKDLETKSYESLFIRAVRAYNGENWRTSITDMELALPDFFKAF YECLAACEGSREIKDFKDFYLSIADHYVEVLECKIQCEENLTPVIGGYPVEKFVATMYHY LQFAYYKLNDLKNAAPCAVSYLLFDQNDKVMQQNLVYYQYHRDTWGLSDEHFQPRPEAVQ FFNVTTLQKELYDFAKENIMDDDEGEVVEYVDDLLELEETS P68106 Q13664 Q16645 Q53TM2 Q9BQ40 FKB1B_HUMAN Peptidyl-prolyl cis-trans isomerase FKBP1B PPIase FKBP1B 5.2.1.8 12.6 kDa FK506-binding protein 12.6 kDa FKBP FKBP-12.6 FK506-binding protein 1B FKBP-1B Immunophilin FKBP12.6 Rotamase h-FKBP-12 FKBP1B FKBP12.6 FKBP1L FKBP9 OTK4 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning and expression of a novel human gene that is highly homologous to human FK506-binding protein 12kDa (hFKBP-12) and characterization of two alternatively spliced transcripts. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2) Fetal brain A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Brain Heart muscle FKBP9: an alternative splice variant of the FK506-binding protein FKBP12.6 expressed in the human heart. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) Genomic organization, chromosomal localization, and promoter of human gene for FK506-binding protein 12.6. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Brain PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. IDENTIFICATION IN A COMPLEX WITH RYR2; PP1; PP2A AKAP6 AND PKA INTERACTION WITH RYR2 TISSUE SPECIFICITY Structure of FKBP12.6 in complex with rapamycin. X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Inhibited by both FK506 and rapamycin. Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1. Interacts directly with RYR2. Q6UY14-3 ADAMTSL4 false 3 P62161 Calm3 true 2 Q13557 CAMK2D false 3 Q53SE7 FLJ13057 false 3 Q15323 KRT31 false 3 Q6A162 KRT40 false 3 Q04864 REL false 3 P11716 RYR1 true 2 Q92736 RYR2 false 5 Q86WT6 TRIM69 false 3 Cytoplasm Sarcoplasmic reticulum P68106-1 Q16645-1 1 P68106-2 Q16645-2 2 Detected in heart muscle (at protein level). Isoform 1 and isoform 2 are ubiquitous with highest levels in brain and thymus. Belongs to the FKBP-type PPIase family. FKBP1 subfamily. 3D-structure Alternative splicing Complete proteome Cytoplasm Isomerase Reference proteome Rotamase Sarcoplasmic reticulum MSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE LGPLSPLPICPHPC MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGF EEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE O75129 A2A2T7 A2A2T9 Q52LQ2 Q5JVX8 Q5JVX9 Q5JVY1 Q5VXG8 Q5VZX6 Q8N6P8 Q8WV47 Q96FL4 Q9UHW6 ASTN2_HUMAN Astrotactin-2 ASTN2 KIAA0634 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Brain DNA sequence and analysis of human chromosome 9. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 6) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 532-1339 (ISOFORM 3) Brain Cervix Eye Molecular cloning of human astrotactin-2. NUCLEOTIDE SEQUENCE [MRNA] OF 227-1339 (ISOFORM 2) Uterus Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 274-470 (ISOFORM 1) Structure of astrotactin-2: a conserved vertebrate-specific and perforin-like membrane protein involved in neuronal development. X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 768-1339 DISULFIDE BONDS GLYCOSYLATION AT ASN-770 AND ASN-783 CALCIUM-BINDING FUNCTION MUTAGENESIS OF ARG-1175 DOMAIN The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] LEU-1293 Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma. VARIANT VAL-229 Mediates recycling of the neuronal cell adhesion molecule ASTN1 to the anterior pole of the cell membrane in migrating neurons. Promotes ASTN1 internalization and intracellular transport of endocytosed ASTN1 (By similarity). Selectively binds inositol-4,5-bisphosphate, inositol-3,4,5-trisphosphate and inositol-1,3,4,5-tetrakisphosphate, suggesting it is recruited to membranes that contain lipids with a phosphoinositide headgroup (Ref.6). Interacts with ASTN1; the interaction is not calcium-dependent. Membrane Multi-pass membrane protein Perikaryon Cytoplasm Cell cortex Early endosome Late endosome Cytoplasmic vesicle Clathrin-coated vesicle Cytoplasmic vesicle Integral membrane protein not detected at the cell membrane. Detected in cytoplasmic vesicles in the cell cortex, close to the anterior pole of migrating neurons. Detected at the base of the leading process in migrating neurons. O75129-1 1 O75129-2 2 O75129-3 3 O75129-4 4 No experimental confirmation available. O75129-6 6 The C-terminal region after the fibronectin type-III domain presents structural similarity to annexin domains and binds calcium ions. Belongs to the astrotactin family. Translation N-terminally extended. Translation N-terminally shortened. 3D-structure Alternative splicing Calcium Complete proteome Cytoplasm Cytoplasmic vesicle Disulfide bond EGF-like domain Endosome Glycoprotein Membrane Metal-binding Polymorphism Protein transport Reference proteome Repeat Signal Transmembrane Transmembrane helix Transport YGSHYIAEALYGSELTCIIHFPSKKVQQQLWLQYQK MNTLLCKGMFCLLSWEADSRGRLGEYTLQPLSLQTE GESKGR YLTLSKVSPF V I A V R H V I V L R T T M MAAAGARLSPGPGSGLRGRPRLCFHPGPPPLLPLLLLFLLLLPPPPLLAGATAAASREPD SPCRLKTVTVSTLPALRESDIGWSGARAGAGAGTGAGAAAAAASPGSPGSAGTAAESRLL LFVRNELPGRIAVQDDLDNTELPFFTLEMSGTAADISLVHWRQQWLENGTLYFHVSMSSS GQLAQATAPTLQEPSEIVEEQMHILHISVMGGLIALLLLLLVFTVALYAQRRWQKRRRIP QKSASTEATHEIHYIPSVLLGPQARESFRSSRLQTHNSVIGVPIRETPILDDYDCEEDEE PPRRANHVSREDEFGSQVTHTLDSLGHPGEEKVDFEKKAAAEATQETVESLMQKFKESFR ANTPIEIGQLQPPLRSTSAGKRKRRSKSRGGISFGRAKGTSGSEADDETQLTFYTEQYRS RRRSKGLLKSPVNKTALTLIAVSSCILAMVCGSQMSCPLTVKVTLHVPEHFIADGSSFVV SEGSYLDISDWLNPAKLSLYYQINATSPWVRDLCGQRTTDACEQLCDPETGECSCHEGYA PDPVHRHLCVRSDWGQSEGPWPYTTLERGYDLVTGEQAPEKILRSTFSLGQGLWLPVSKS FVVPPVELSINPLASCKTDVLVTEDPADVREEAMLSTYFETINDLLSSFGPVRDCSRNNG GCTRNFKCVSDRQVDSSGCVCPEELKPMKDGSGCYDHSKGIDCSDGFNGGCEQLCLQQTL PLPYDATSSTIFMFCGCVEEYKLAPDGKSCLMLSDVCEGPKCLKPDSKFNDTLFGEMLHG YNNRTQHVNQGQVFQMTFRENNFIKDFPQLADGLLVIPLPVEEQCRGVLSEPLPDLQLLT GDIRYDEAMGYPMVQQWRVRSNLYRVKLSTITLAAGFTNVLKILTKESSREELLSFIQHY GSHYIAEALYGSELTCIIHFPSKKVQQQLWLQYQKETTELGSKKELKSMPFITYLSGLLT AQMLSDDQLISGVEIRCEEKGRCPSTCHLCRRPGKEQLSPTPVLLEINRVVPLYTLIQDN GTKEAFKSALMSSYWCSGKGDVIDDWCRCDLSAFDANGLPNCSPLLQPVLRLSPTVEPSS TVVSLEWVDVQPAIGTKVSDYILQHKKVDEYTDTDLYTGEFLSFADDLLSGLGTSCVAAG RSHGEVPEVSIYSVIFKCLEPDGLYKFTLYAVDTRGRHSELSTVTLRTACPLVDDNKAEE IADKIYNLYNGYTSGKEQQMAYNTLMEVSASMLFRVQHHYNSHYEKFGDFVWRSEDELGP RKAHLILRRLERVSSHCSSLLRSAYIQSRVETVPYLFCRSEEVRPAGMVWYSILKDTKIT CEEKMVSMARNTYGESKGR Q8N319 E9PB59 Q8N575 CF223_HUMAN Uncharacterized protein C6orf223 C6orf223 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Lymph Q8N319-3 1 Q8N319-4 2 Gene prediction based on EST data. Intron retention. Alternative splicing Complete proteome Polymorphism Reference proteome KTPRHKQPTLLMVRASRRSGKTSAVLKAGRQSVSGRKNSTSKDLVTLGASSLREERGHPLHPRHRKAVHLRTRGRTRGWVQTLARMSRRTRGPVERAAAAAAAAAGGDAGHAPFPPPPAADGARAPRSPGQVTPRGLRLRLPRRESLLRGLCRPLRPLLGFRESDSAKPASLRLLQHTPSARRNYRIAGARLMRSNYPPPLSSAALRGAGPTRRN LLRKEGVDGGLFSPEDPQAQAAHLTDGQSIQKKWQDFSCPQSRKTECFWQKEQHKQRSGNPRCLQFEGGERTPPPPQT K E V M A AA MMPLAEAGALAQGGGPSATEWACILRRKTPRHKQPTLLMVRASRRSGKTSAVLKAGRQSV SGRKNSTSKDLVTLGASSLREERGHPLHPRHRKAVHLRTRGRTRGWVQTLARMSRRTRGP VERAAAAAAAAAGGDAGHAPFPPPPAADGARAPRSPGQVTPRGLRLRLPRRESLLRGLCR PLRPLLGFRESDSAKPASLRLLQHTPSARRNYRIAGARLMRSNYPPPLSSAALRGAGPTR RN Q9UHK6 A5YM47 B8Y916 B8Y918 F8W9N1 O43673 Q3KT79 Q96GH1 Q9Y3Q1 AMACR_HUMAN Alpha-methylacyl-CoA racemase 5.1.99.4 2-methylacyl-CoA racemase AMACR Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA racemase in humans. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANTS ASP-175; SER-201; THR-261 AND LYS-277 SUBCELLULAR LOCATION MICROBODY TARGETING Mutations in the gene encoding peroxisomal alpha-methylacyl-CoA racemase cause adult-onset sensory motor neuropathy. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) FUNCTION CATALYTIC ACTIVITY VARIANT AMACRD PRO-52 VARIANT CBAS4 PRO-107 VARIANTS SER-201 AND LYS-277 CHARACTERIZATION OF VARIANT AMACRD PRO-52 CHARACTERIZATION OF VARIANT CBAS4 PRO-107 A variant of the alpha-methyl-acyl-CoA racemase gene created by a deletion in exon 5 and its expression in prostate cancer. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4) VARIANTS SER-201 AND LYS-277 Prostate cancer Human alpha-methylacyl-CoA racemase cDNA sequence. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANTS MET-9; ASP-175; SER-201; THR-261 AND LYS-277 Expression of alpha-methylacyl-CoA racemase spliced variants in normal and malignant prostate tissue. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) VARIANT MET-9 Cloning of human full-length CDSs in BD Creator(TM) system donor vector. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) VARIANT MET-9 The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Salivary gland The DNA sequence and comparative analysis of human chromosome 5. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANT MET-9 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) VARIANT MET-9 Kidney Purification and characterization of an alpha-methylacyl-CoA racemase from human liver. FUNCTION CATALYTIC ACTIVITY SUBUNIT SUBCELLULAR LOCATION BIOPHYSICOCHEMICAL PROPERTIES Liver Subcellular localization and physiological role of alpha-methylacyl-CoA racemase. FUNCTION CATALYTIC ACTIVITY SUBCELLULAR LOCATION An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver disease caused by failure to racemize trihydroxycholestanoic acid: gene mutation and effect of bile acid therapy. VARIANT CBAS4 PRO-52 Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters (PubMed:7649182, PubMed:10655068, PubMed:11060359). Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs (PubMed:7649182, PubMed:10655068, PubMed:11060359). (2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA = (25S)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA (2R,6)-dimethylheptanoyl-CoA = (2S,6)-dimethylheptanoyl-CoA 172 uM for pristanoyl-CoA 31.6 uM for trihydroxycoprostanoyl-CoA 0.1 umol/min/mg enzyme for pristanoyl-CoA 0.3 umol/min/mg enzyme for trihydroxycoprostanoyl-CoA Optimum pH is 7-8. Lipid metabolism; bile acid biosynthesis. Lipid metabolism; fatty acid metabolism. Monomer. Peroxisome Mitochondrion Q9UHK6-1 1 Q9UHK6-2 2 IBLi May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Q9UHK6-4 3 Q9UHK6-5 4 Expression is elevated in prostate cancer. Alpha-methylacyl-CoA racemase deficiency AMACRD A rare autosomal recessive peroxisomal disorder characterized by elevated plasma concentrations of pristanic acid C27-bile-acid intermediates, and adult onset of variable neurodegenerative symptoms affecting the central and peripheral nervous systems. Features may include seizures, visual failure, sensorimotor neuropathy, spasticity, migraine, and white matter hyperintensities on brain imaging. The disease is caused by mutations affecting the gene represented in this entry. Congenital bile acid synthesis defect 4 CBAS4 A disorder characterized by the presence of trihydroxycoprostanic acid in the bile and absence of cholic acid. Patients manifest neonatal jaundice, intrahepatic cholestasis and bile duct deficiency. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the CoA-transferase III family. Aberrant splicing. Aberrant splicing. Acetylation Alternative splicing Complete proteome Disease mutation Intrahepatic cholestasis Isomerase Mitochondrion Peroxisome Polymorphism Reference proteome VLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDANMVEGTAYLSSFLWKTQKLSLWEAPRGQNMLDGGAPFYTTYRTADGE GRNSIFKFFSVENSEIESVGSTSRTEHVGWWSTFLYDLQDSRWGIHGCWSNRTPVLRAADQRSLIPYFNLYLQFLNISMQNLFKVHTLLRPCYFLGQK VLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDANMVEGTAYLSSFLWKT GRNSIFKFFSVENSEIESVGSTSRTEHVGWWSTFLYDLQDSRWGIHGCWSNRTPVLRAADQRTWTKV VKASL AGSKFWILYPTHSNIQK V M S P L P R Q G D L S P S Q H M I M T E K P R A T L V N D N S P L FKR SKG MALQGISVVELSGLAPGPFCAMVLADFGARVVRVDRPGSRYDVSRLGRGKRSLVLDLKQP RGAAVLRRLCKRSDVLLEPFRRGVMEKLQLGPEILQRENPRLIYARLSGFGQSGSFCRLA GHDINYLALSGVLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVI DANMVEGTAYLSSFLWKTQKLSLWEAPRGQNMLDGGAPFYTTYRTADGEFMAVGAIEPQF YELLIKGLGLKSDELPNQMSMDDWPEMKKKFADVFAEKTKAEWCQIFDGTDACVTPVLTF EEVVHHDHNKERGSFITSEEQDVSPRPAPLLLNTPAIPSFKRDPFIGEHTEEILEEFGFS REEIYQLNSDKIIESNKVKASL Q9H8M5 Q5T569 Q5T570 Q8WU59 Q9H952 Q9NRK5 Q9NXT4 CNNM2_HUMAN Metal transporter CNNM2 Ancient conserved domain-containing protein 2 Cyclin-M2 CNNM2 ACDP2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 242-875 (ISOFORM 1) Colon Placenta Teratocarcinoma The DNA sequence and comparative analysis of human chromosome 10. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) B-cell Molecular cloning and characterization of a novel gene family of four ancient conserved domain proteins (ACDP). NUCLEOTIDE SEQUENCE [MRNA] OF 210-875 (ISOFORM 1) CNNM2, encoding a basolateral protein required for renal Mg2+ handling, is mutated in dominant hypomagnesemia. TISSUE SPECIFICITY VARIANT HOMG6 ILE-568 CHARACTERIZATION OF VARIANT HOMG6 ILE-568 VARIANT GLN-38 Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-761 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia CNNM2 mutations cause impaired brain development and seizures in patients with hypomagnesemia. INVOLVEMENT IN HOMGSMR1 VARIANTS HOMGSMR1 LYS-122; TRP-269; PHE-330 AND LYS-357 CHARACTERIZATION OF VARIANTS HOMGSMR1 LYS-122; TRP-269 AND LYS-357 Divalent metal cation transporter. Mediates transport of divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+) (By similarity). Cell membrane Multi-pass membrane protein Q9H8M5-1 1 Q9H8M5-2 2 Q9H8M5-3 3 No experimental confirmation available. Widely expressed. Expressed at higher level in brain, kidney and placenta, while it is weakly expressed in skeletal muscle. In the kidney, it is expressed in the distal convoluted tubule and the thick ascending limb of Henle loop. Hypomagnesemia 6 HOMG6 A renal disease characterized by severely lowered serum magnesium levels in the absence of other electrolyte disturbances. Affected individuals show an inappropriately normal urinary magnesium excretion, demonstrating a defect in tubular reabsorption. Age of clinical onset is highly variable and some affected individuals are asymptomatic. The disease is caused by mutations affecting the gene represented in this entry. Hypomagnesemia, seizures, and mental retardation 1 HOMGSMR1 A disease characterized by renal wasting of magnesium, low serum magnesium, seizures, and variable degrees of delayed psychomotor development. The disease is caused by mutations affecting the gene represented in this entry. Shares weak sequence similarity with the cyclin family, hence its name. However, it has no cyclin-like function in vivo. Belongs to the ACDP family. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. 3D-structure Alternative splicing CBS domain Cell membrane Complete proteome Disease mutation Epilepsy Glycoprotein Ion transport Membrane Mental retardation Phosphoprotein Polymorphism Primary hypomagnesemia Reference proteome Repeat Transmembrane Transmembrane helix Transport GKSHLAIVQRVN EHTNKKPKSYQH R Q E K S W L F E K T I K N I V E V MIGCGACEPKVKMAGGQAAAALPTWKMAARRSLSARGRGILQAAAGRLLPLLLLSCCCGA GGCAAVGENEETVIIGLRLEDTNDVSFMEGGALRVSERTRVKLRVYGQNINNETWSRIAF TEHERRRHSPGERGLGGPAPPEPDSGPQRCGIRTSDIIILPHIILNRRTSGIIEIEIKPL RKMEKSKSYYLCTSLSTPALGAGGSGSTGGAVGGKGGSGVAGLPPPPWAETTWIYHDGED TKMIVGEEKKFLLPFWLQVIFISLLLCLSGMFSGLNLGLMALDPMELRIVQNCGTEKEKN YAKRIEPVRRQGNYLLCSLLLGNVLVNTTLTILLDDIAGSGLVAVVVSTIGIVIFGEIVP QAICSRHGLAVGANTIFLTKFFMMMTFPASYPVSKLLDCVLGQEIGTVYNREKLLEMLRV TDPYNDLVKEELNIIQGALELRTKTVEDVMTPLRDCFMITGEAILDFNTMSEIMESGYTR IPVFEGERSNIVDLLFVKDLAFVDPDDCTPLKTITKFYNHPLHFVFNDTKLDAMLEEFKK GKSHLAIVQRVNNEGEGDPFYEVLGIVTLEDVIEEIIKSEILDETDLYTDNRTKKKVAHR ERKQDFSAFKQTDSEMKVKISPQLLLAMHRFLATEVEAFSPSQMSEKILLRLLKHPNVIQ ELKYDEKNKKAPEYYLYQRNKPVDYFVLILQGKVEVEAGKEGMKFEASAFSYYGVMALTA SPVPLSLSRTFVVSRTELLAAGSPGENKSPPRPCGLNHSDSLSRSDRIDAVTPTLGSSNN QLNSSLLQVYIPDYSVRALSDLQFVKISRQQYQNALMASRMDKTPQSSDSENTKIELTLT ELHDGLPDETANLLNEQNCVTHSKANHSLHNEGAI O15072 A1L3U9 Q9BXZ8 ATS3_HUMAN A disintegrin and metalloproteinase with thrombospondin motifs 3 ADAM-TS 3 ADAM-TS3 ADAMTS-3 3.4.24.- Procollagen II N-proteinase PC II-NP Procollagen II amino propeptide-processing enzyme ADAMTS3 KIAA0366 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT LYS-138 Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis. NUCLEOTIDE SEQUENCE [MRNA] OF 1-227 VARIANT LYS-138 Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1205 VARIANT LYS-138 Brain Loss of ADAMTS3 activity causes Hennekam lymphangiectasia-lymphedema syndrome 3. INVOLVEMENT IN HKLLS3 VARIANTS HKLLS3 PRO-168 AND THR-291 CHARACTERIZATION OF VARIANTS HKLLS3 PRO-168 AND THR-291 SUBCELLULAR LOCATION Cleaves the propeptides of type II collagen prior to fibril assembly. Does not act on types I and III collagens. Zn(2+) Binds 1 zinc ion per subunit. Secreted Secreted Extracellular space Extracellular matrix Found in cartilage and skin. The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. The precursor is cleaved by a furin endopeptidase. Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). Hennekam lymphangiectasia-lymphedema syndrome 3 HKLLS3 A form of Hennekam lymphangiectasia-lymphedema syndrome, a generalized lymph-vessels dysplasia characterized by intestinal lymphangiectasia with severe lymphedema of the limbs, genitalia and face. In addition, affected individuals have unusual facies and some manifest mental retardation. HKLLS3 is characterized by widespread congenital edema, facial dysmorphism and protein-losing enteropathy of variable severity. HKLLS3 transmission pattern is consistent with autosomal recessive inheritance. The disease is caused by mutations affecting the gene represented in this entry. Has sometimes been referred to as ADAMTS4. Cleavage on pair of basic residues Complete proteome Disease mutation Disulfide bond Extracellular matrix Glycoprotein Heparin-binding Hydrolase Metal-binding Metalloprotease Polymorphism Protease Reference proteome Repeat Secreted Signal Zinc Zymogen R K L P I T S P C V MVLLSLWLIAAALVEVRTSADGQAGNEEMVQIDLPIKRYREYELVTPVSTNLEGRYLSHT LSASHKKRSARDVSSNPEQLFFNITAFGKDFHLRLKPNTQLVAPGAVVEWHETSLVPGNI TDPINNHQPGSATYRIRRTEPLQTNCAYVGDIVDIPGTSVAISNCDGLAGMIKSDNEEYF IEPLERGKQMEEEKGRIHVVYKRSAVEQAPIDMSKDFHYRESDLEGLDDLGTVYGNIHQQ LNETMRRRRHAGENDYNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVH INVVLVRMIMLGYAKSISLIERGNPSRSLENVCRWASQQQRSDLNHSEHHDHAIFLTRQD FGPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCGDETA MGSVMAPLVQAAFHRYHWSRCSGQELKRYIHSYDCLLDDPFDHDWPKLPELPGINYSMDE QCRFDFGVGYKMCTAFRTFDPCKQLWCSHPDNPYFCKTKKGPPLDGTECAAGKWCYKGHC MWKNANQQKQDGNWGSWTKFGSCSRTCGTGVRFRTRQCNNPMPINGGQDCPGVNFEYQLC NTEECQKHFEDFRAQQCQQRNSHFEYQNTKHHWLPYEHPDPKKRCHLYCQSKETGDVAYM KQLVHDGTHCSYKDPYSICVRGECVKVGCDKEIGSNKVEDKCGVCGGDNSHCRTVKGTFT RTPRKLGYLKMFDIPPGARHVLIQEDEASPHILAIKNQATGHYILNGKGEEAKSRTFIDL GVEWDYNIEDDIESLHTDGPLHDPVIVLIIPQENDTRSSLTYKYIIHEDSVPTINSNNVI QEELDTFEWALKSWSQCSKPCGGGFQYTKYGCRRKSDNKMVHRSFCEANKKPKPIRRMCN IQECTHPLWVAEEWEHCTKTCGSSGYQLRTVRCLQPLLDGTNRSVHSKYCMGDRPESRRP CNRVPCPAQWKTGPWSECSVTCGEGTEVRQVLCRAGDHCDGEKPESVRACQLPPCNDEPC LGDKSIFCQMEVLARYCSIPGYNKLCCESCSKRSSTLPPPYLLEAAETHDDVISNPSDLP RSLVMPTSLVPYHSETPAKKMSLSSISSVGGPNAYAAFRPNSKPDGANLRQRSAQQAGSK TVRLVTVPSSPPTKRVHLSSASQMAAASFFAASDSIGASSQARTSKKDGKIIDNRRPTRS STLER P98194 B2RAT7 B4DSW3 B7Z3X9 G3XAH8 G8JLN9 O76005 Q86V72 Q86V73 Q8N6V1 Q8NCJ7 AT2C1_HUMAN Calcium-transporting ATPase type 2C member 1 ATPase 2C1 7.2.2.10 ATP-dependent Ca(2+) pump PMR1 ATP2C1 KIAA1347 PMR1L HUSSY-28 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2) VARIANTS HHD THR-304; PRO-318; ARG-641; ARG-645; MET-709 AND ARG-744 Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4) VARIANTS HHD LEU-201; TYR-344 AND ILE-570 Keratinocyte Effect of Hailey-Hailey Disease mutations on the function of a new variant of human secretory pathway Ca2+/Mn2+-ATPase (hSPCA1). NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6) SUBCELLULAR LOCATION MUTAGENESIS Keratinocyte Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 6; 7 AND 8) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 360-919 (ISOFORM 1) Mammary gland Neuron Thalamus The DNA sequence, annotation and analysis of human chromosome 3. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Blood Characterization of 16 novel human genes showing high similarity to yeast sequences. NUCLEOTIDE SEQUENCE [MRNA] OF 424-919 A quantitative atlas of mitotic phosphorylation. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia Hailey-Hailey disease: molecular and clinical characterization of novel mutations in the ATP2C1 gene. VARIANTS HHD CYS-309; PRO-341; ARG-411; VAL-580; TYR-742 AND ARG-789 Analysis of ATP2C1 gene mutation in 10 unrelated Japanese families with Hailey-Hailey disease. VARIANTS HHD PHE-490 AND PRO-584 Mendelian Disorders of Cornification Caused by Defects in Intracellular Calcium Pumps: Mutation Update and Database for Variants in ATP2A2 and ATP2C1 associated with Darier disease and Hailey-Hailey disease. VARIANTS HHD GLU-220; VAL-309; 609-GLN--VAL-919 DEL; 730-ASN-ALA-731 DEL AND ASP-731 This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate Golgi apparatus membrane Multi-pass membrane protein P98194-1 1 ATP2C1A P98194-2 2 ATP2C1B ATP2C1C P98194-3 3 ATP2C1B P98194-4 4 ATP2C1A P98194-5 5 ATP2C1B P98194-6 6 ATP2C1D P98194-7 7 No experimental confirmation available. P98194-8 8 No experimental confirmation available. P98194-9 9 No experimental confirmation available. Isoform 1 and isoform 2 are expressed in the same tissues. Found in most tissues except colon, thymus, spleen and leukocytes. Most abundant in keratinocytes and kidney. Hailey-Hailey disease HHD Autosomal dominant disorder characterized by persistent blisters and suprabasal cell separation (acantholysis) of the epidermis, due to impaired keratinocyte adhesion. Patients lacking all isoforms except isoform 2 have HHD. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily. Alternative splicing ATP-binding Calcium Calcium transport Complete proteome Disease mutation Golgi apparatus Ion transport Magnesium Membrane Metal-binding Nucleotide-binding Polymorphism Reference proteome Translocase Transmembrane Transmembrane helix Transport MK MDSLLPPSRFSYFKKYPLHAIRRYLSTLRNQRAEEQ DLLFLLGLTSSVCIVAEIIKKVERSREKIQKHVSSTSSSFLEV GLALGEEWTAAG SSTSSSFLEV WLWERSGQQLVEIHPHLETGLPLTEDVSCV V VSSTSSSFLEVWLWERSGQQLVEIHPHLETGLPLTEDVSCV V VWLWERSGQQLVEIHPHLETGLPLTEDVSCV P L G E A T G C G V L P L P C Y C R A T C F T I I V L P M R G R T M A D D Y P R G R E K I F T I V A A T R H A T F L S G MKVARFQKIPNGENETMIPVLTSKKASELPVSEVASILQADLQNGLNKCEVSHRRAFHGW NEFDISEDEPLWKKYISQFKNPLIMLLLASAVISVLMHQFDDAVSITVAILIVVTVAFVQ EYRSEKSLEELSKLVPPECHCVREGKLEHTLARDLVPGDTVCLSVGDRVPADLRLFEAVD LSIDESSLTGETTPCSKVTAPQPAATNGDLASRSNIAFMGTLVRCGKAKGVVIGTGENSE FGEVFKMMQAEEAPKTPLQKSMDLLGKQLSFYSFGIIGIIMLVGWLLGKDILEMFTISVS LAVAAIPEGLPIVVTVTLALGVMRMVKKRAIVKKLPIVETLGCCNVICSDKTGTLTKNEM TVTHIFTSDGLHAEVTGVGYNQFGEVIVDGDVVHGFYNPAVSRIVEAGCVCNDAVIRNNT LMGKPTEGALIALAMKMGLDGLQQDYIRKAEYPFSSEQKWMAVKCVHRTQQDRPEICFMK GAYEQVIKYCTTYQSKGQTLTLTQQQRDVYQQEKARMGSAGLRVLALASGPELGQLTFLG LVGIIDPPRTGVKEAVTTLIASGVSIKMITGDSQETAVAIASRLGLYSKTSQSVSGEEID AMDVQQLSQIVPKVAVFYRASPRHKMKIIKSLQKNGSVVAMTGDGVNDAVALKAADIGVA MGQTGTDVCKEAADMILVDDDFQTIMSAIEEGKGIYNNIKNFVRFQLSTSIAALTLISLA TLMNFPNPLNAMQILWINIIMDGPPAQSLGVEPVDKDVIRKPPRNWKDSILTKNLILKIL VSSIIIVCGTLFVFWRELRDNVITPRDTTMTFTCFVFFDMFNALSSRSQTKSVFEIGLCS NRMFCYAVLGSIMGQLLVIYFPPLQKVFQTESLSILDLLFLLGLTSSVCIVAEIIKKVER SREKIQKHVSSTSSSFLEV Q3C1V1 Q3C1V2 CK091_HUMAN Uncharacterized protein C11orf91 C11orf91 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Human chromosome 11 DNA sequence and analysis including novel gene identification. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-185 (ISOFORM 1) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-193 (ISOFORM 2) Q3C1V1-1 1 Q3C1V1-2 2 Alternative splicing Complete proteome Reference proteome YTFLKALKDEKLQGLKTKQPGKKSASLS FLGLWTTCADAGRIPQPTS V F R L K Q MPKGRRGSHSPTMSQRSAPPLYFPSLYDRGISSSPLSDFNIWKKLFVPLKAGGAPVGGAA GARSLSQALPAPAPPPPPPPGLGPSSERPWPSPWPSGLASIPYEPLRFFYSPPPGPEVVA SPLVPCPSTPRLASASHPEELCELEIRIKELELLTITGDGFDSQSYTFLKALKDEKLQGL KTKQPGKKSASLS P0DKL9 A14EL_HUMAN ARL14 effector protein-like ARL14EPL Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence and comparative analysis of human chromosome 5. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Complete proteome Reference proteome MNEQSEKNNSIQERHTDHSFPEKNCQIGQKQLQQIERQLKCLAFRNPGPQVADFNPETRQ QKKKARMSKMNEYFSTKYKIMRKYDKSGRLICNDADLCDCLEKNCLGCFYPCPKCNSNKC GPECRCNRRWVYDAIVTESGEVISTLPFNVPD Q9H4R4 A2RUA0 CT191_HUMAN Putative nuclear receptor corepressor 1-like protein NCOR1P1 Nuclear receptor corepressor 1 pseudogene 1 NCOR1P1 C20orf191 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence and comparative analysis of human chromosome 20. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis Belongs to the N-CoR nuclear receptor corepressors family. Could be the product of a pseudogene. Highly similar to the N-terminus of NCOR1, but may encode a non-functional truncated protein. Coiled coil Complete proteome Reference proteome MSSSGYPPNQGAFSTEQSHYPPHSVKYTFPSTHHQQDPAFGGKHEAPSSPILGQPCGDDQ NASPSKLSKEELIECMDRVDREIAKVEQQILKLKKKQVKVFV L0R819 ASURF_HUMAN ASNSD1 upstream open reading frame protein ASNSD1 small/short open reading frame-encoded polypeptide ASNSD1-SEP ASDURF Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Direct detection of alternative open reading frames translation products in human significantly expands the proteome. NUCLEOTIDE SEQUENCE [GENOMIC DNA] ALTERNATIVE INITIATION (ISOFORM 2) Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Peptidomic discovery of short open reading frame-encoded peptides in human cells. ALTERNATIVE INITIATION (ISOFORM 2) SUBCELLULAR LOCATION (ISOFORM 2) IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2) Identification and characterization of sORF-encoded polypeptides. ALTERNATIVE INITIATION (ISOFORM 2) Cytoplasm L0R819-1 2 uORF Product of the upstream open reading frame of this bicistronic gene. Q9NWL6-1 1 Alternative initiation Coiled coil Complete proteome Cytoplasm Reference proteome MPSRGTRPEDSSVLIPTDNSTPHKEDLSSKIKEQKIVVDELSNLKKNRKVYRQQQNSNIF FLADRTEMLSESKNILDELKKEYQEIENLDKTKIKK P35555 B2RUU0 D2JYH6 Q15972 Q75N87 FBN1_HUMAN Fibrillin-1 Asprosin FBN1 FBN Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome. NUCLEOTIDE SEQUENCE [MRNA] Placenta Three novel mutations of the fibrillin-1 gene and ten single nucleotide polymorphisms of the fibrillin-3 gene in Marfan syndrome patients. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT MFS SER-2663 VARIANT CYS-472 NUCLEOTIDE SEQUENCE [GENOMIC DNA] Analysis of the DNA sequence and duplication history of human chromosome 15. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Fibrillin binds calcium and is coded by cDNAs that reveal a multidomain structure and alternatively spliced exons at the 5' end. NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55 Fibroblast Placenta Partial sequence of a candidate gene for the Marfan syndrome. NUCLEOTIDE SEQUENCE [MRNA] OF 899-2871 Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes. NUCLEOTIDE SEQUENCE [MRNA] OF 813-1313 The skipping of constitutive exons in vivo induced by nonsense mutations. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2086-2194 Initial steps in assembly of microfibrils. Formation of disulfide-cross-linked multimers containing fibrillin-1. PROTEIN SEQUENCE OF 25-36 AND 45-56 CLEAVAGE OF SIGNAL PEPTIDE AFTER GLY-24 Evidence for furin-type activity-mediated C-terminal processing of profibrillin-1 and interference in the processing by certain mutations. PROTEIN SEQUENCE OF 2732-2746 PROTEOLYTIC PROCESSING MUTAGENESIS OF ARG-2728; ARG-2731 AND SER-2732 CHARACTERIZATION OF VARIANT TRP-2726 Association of mitral valve prolapse and systemic abnormalities of connective tissue: a phenotypic continuum. INVOLVEMENT IN OCTD Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils. FUNCTION Interactions of fibrillin-1 with heparin/heparan sulfate, implications for microfibrillar assembly. HEPARIN-BINDING N-TERMINAL REGION DOMAIN C-TERMINAL REGION DOMAIN SUBCELLULAR LOCATION Cell adhesion to fibrillin-1 molecules and microfibrils is mediated by alpha 5 beta 1 and alpha v beta 3 integrins. FUNCTION CELL ATTACHMENT SITE MUTAGENESIS OF GLY-1542 INTERACTION WITH ITGA5; ITGAV; ITGB1 AND ITGB3 MAGP-2 has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrils. INTERACTION WITH MFAP2 AND MFAP5 Molecular structure and interaction of recombinant human type XVI collagen. INTERACTION WITH COL16A1 Fibulin-5 interacts with fibrillin-1 molecules and microfibrils. INTERACTION WITH FBLN5 AND ELN alphaVbeta6 is a novel receptor for human fibrillin-1. Comparative studies of molecular determinants underlying integrin-rgd affinity and specificity. FUNCTION INTERACTION WITH ITGA5; ITGAV; ITGB1 AND ITGB6 Fibrillin-1 interactions with fibulins depend on the first hybrid domain and provide an adaptor function to tropoelastin. INTERACTION WITH ELN; FBLN2; FBLN4 AND FBLN5 LTBP-2 specifically interacts with the amino-terminal region of fibrillin-1 and competes with LTBP-1 for binding to this microfibrillar protein. INTERACTION WITH LTBP1 AND LTBP2 TISSUE SPECIFICITY Targeting of bone morphogenetic protein growth factor complexes to fibrillin. INTERACTION WITH BMP2; BMP4; BMP7; BMP10 AND GDF5 Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-448; ASN-1067; ASN-1484 AND ASN-1581 Liver Marfan syndrome with neonatal progeroid syndrome-like lipodystrophy associated with a novel frameshift mutation at the 3' terminus of the FBN1-gene. INVOLVEMENT IN MFLS (ASPROSIN) Further evidence for a marfanoid syndrome with neonatal progeroid features and severe generalized lipodystrophy due to frameshift mutations near the 3' end of the FBN1 gene. INVOLVEMENT IN MFLS (ASPROSIN) Progeroid facial features and lipodystrophy associated with a novel splice site mutation in the final intron of the FBN1 gene. INVOLVEMENT IN MFLS (ASPROSIN) ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts. INTERACTION WITH ADAMTS10 A disintegrin-like and metalloprotease domain containing thrombospondin type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-, and heparin-binding member of the ADAMTS superfamily containing a netrin-like module. INTERACTION WITH ADAMTSL5 Fibrillin-1 directly regulates osteoclast formation and function by a dual mechanism. FUNCTION INTERACTION WITH TNFSF11 De novo heterozygous FBN1 mutations in the extreme C-terminal region cause progeroid fibrillinopathy. INVOLVEMENT IN MFLS (ASPROSIN) VARIANT MFLS THR-2741 Severe congenital lipodystrophy and a progeroid appearance: Mutation in the penultimate exon of FBN1 causing a recognizable phenotype. INVOLVEMENT IN MFLS (ASPROSIN) Neonatal progeroid variant of Marfan syndrome with congenital lipodystrophy results from mutations at the 3' end of FBN1 gene. INVOLVEMENT IN MFLS (ASPROSIN) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2702 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver C-terminal propeptide is required for fibrillin-1 secretion and blocks premature assembly through linkage to domains cbEGF41-43. SUBCELLULAR LOCATION PROTEOLYTIC PROCESSING CHARACTERIZATION OF VARIANTS 2776-ARG--LEU-2781 DEL; PRO-2780; 2849-TYR--HIS-2871 DEL AND 2867-GLN--HIS-2871 DEL A single kinase generates the majority of the secreted phosphoproteome. PHOSPHORYLATION AT SER-2702 New insights into the structure, assembly and biological roles of 10-12 nm connective tissue microfibrils from fibrillin-1 studies. REVIEW Asprosin, a fasting-induced glucogenic protein hormone. FUNCTION (ASPROSIN) SUBCELLULAR LOCATION (ASPROSIN) INVOLVEMENT IN MFLS (ASPROSIN) Marfanoid-progeroid-lipodystrophy syndrome: a newly recognized fibrillinopathy. INVOLVEMENT IN MFLS (ASPROSIN) Characterization of microfibrillar-associated protein 4 (MFAP4) as a tropoelastin- and fibrillin-binding protein involved in elastic fiber formation. INTERACTION WITH MFAP4 Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils. STRUCTURE BY NMR OF 2054-2125 DISULFIDE BONDS Calcium binding properties of an epidermal growth factor-like domain pair from human fibrillin-1. STRUCTURE BY NMR OF 2124-2205 Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders. STRUCTURE BY NMR OF 2124-2205 Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1. STRUCTURE BY NMR OF 1069-1154 IN COMPLEX WITH CALCIUM DISULFIDE BONDS Structure of the integrin binding fragment from fibrillin-1 gives new insights into microfibril organization. X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1486-1647 IN COMPLEX WITH CALCIUM IONS FUNCTION INTERACTION WITH INTEGRIN ALPHA-V/BETA-3 DISULFIDE BONDS Structure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins. X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 807-951 IN COMPLEX WITH CALCIUM DISULFIDE BONDS Structure of the fibrillin-1 N-terminal domains suggests that heparan sulfate regulates the early stages of microfibril assembly. STRUCTURE BY NMR OF 45-178 DISULFIDE BONDS Software and database for the analysis of mutations in the human FBN1 gene. REVIEW ON MFS VARIANTS The molecular genetics of Marfan syndrome and related microfibrillopathies. REVIEW ON MFS Mutations of FBN1 and genotype-phenotype correlations in Marfan syndrome and related fibrillinopathies. REVIEW ON VARIANTS Marfan syndrome caused by a recurrent de novo missense mutation in the fibrillin gene. VARIANT MFS PRO-1137 Clustering of fibrillin (FBN1) missense mutations in Marfan syndrome patients at cysteine residues in EGF-like domains. VARIANTS MFS SER-1249; ARG-1663; SER-2221 AND SER-2307 Marfan phenotype variability in a family segregating a missense mutation in the epidermal growth factor-like motif of the fibrillin gene. VARIANT MFS SER-2307 Four novel FBN1 mutations: significance for mutant transcript level and EGF-like domain calcium binding in the pathogenesis of Marfan syndrome. VARIANTS MFS ILE-548 AND ALA-723 A novel fibrillin mutation in the Marfan syndrome which could disrupt calcium binding of the epidermal growth factor-like module. VARIANT MFS SER-2144 Mutation screening of complete fibrillin-1 coding sequence: report of five new mutations, including two in 8-cysteine domains. VARIANTS MFS ARG-862; TYR-1117; PRO-1137 AND PHE-1589 VARIANT ALA-1148 A compound-heterozygous Marfan patient: two defective fibrillin alleles result in a lethal phenotype. VARIANTS MFS GLY-217 AND ARG-2627 A novel mutation of the fibrillin gene causing ectopia lentis. VARIANT ECTOL1 LYS-2447 Two novel mutations and a neutral polymorphism in EGF-like domains of the fibrillin gene (FBN1): SSCP screening of exons 15-21 in Marfan syndrome patients. VARIANT MFS CYS-627 Substitution of a cysteine residue in a non-calcium binding, EGF-like domain of fibrillin segregates with the Marfan syndrome in a large kindred. VARIANT MFS GLY-476 Identification of a novel nonsense mutation in the fibrillin gene (FBN1) using nonisotopic techniques. VARIANT 2776-ARG--LEU-2781 DEL An extra cysteine in one of the non-calcium-binding epidermal growth factor-like motifs of the FBN1 polypeptide is connected to a novel variant of Marfan syndrome. VARIANT MFS CYS-122 A new missense mutation of fibrillin in a patient with Marfan syndrome. VARIANT MFS TYR-1223 A novel mutation in the fibrillin gene (FBN1) in familial arachnodactyly. VARIANT MFS HIS-1170 Mutations in the fibrillin gene responsible for dominant ectopia lentis and neonatal Marfan syndrome. VARIANTS MFS GLY-217; ASN-1023; ARG-1074; TYR-1242; ARG-1513; GLU-2127; TRP-2151; LYS-2447 AND ARG-2511 A Gly1127Ser mutation in an EGF-like domain of the fibrillin-1 gene is a risk factor for ascending aortic aneurysm and dissection. VARIANT MFS SER-1127 Fifteen novel FBN1 mutations causing Marfan syndrome detected by heteroduplex analysis of genomic amplicons. VARIANTS MFS TYR-129; PHE-166; CYS-746; ARG-926; ARG-1013; LYS-1073; SER-1382 AND ARG-1928 The phenotypic continuum associated with FBN1 mutations includes the Shprintzen-Goldberg syndrome. VARIANT MFS TYR-1223 A mutation in FBN1 disrupts profibrillin processing and results in isolated skeletal features of the Marfan syndrome. VARIANT TRP-2726 CHARACTERIZATION OF VARIANT TRP-2726 INVOLVEMENT IN MFS Delineation of the Marfan phenotype associated with mutations in exons 23-32 of the FBN1 gene. VARIANTS MFS ARG-1053; GLY-1072; LYS-1073 AND GLY-1117 Characterisation of four novel fibrillin-1 (FBN1) mutations in Marfan syndrome. VARIANTS MFS THR-705; TYR-711; GLY-1055 AND TYR-1153 A novel de novo mutation in exon 14 of the fibrillin-1 gene associated with delayed secretion of fibrillin in a patient with a mild Marfan phenotype. VARIANT MFS TYR-587 The pathogenicity of the Pro1148Ala substitution in the FBN1 gene: causing or predisposing to Marfan syndrome and aortic aneurysm, or clinically innocent? VARIANT ALA-1148 Mutation screening of all 65 exons of the fibrillin-1 gene in 60 patients with Marfan syndrome: report of 12 novel mutations. VARIANTS MFS ARG-111; CYS-545; CYS-627; GLY-750; ARG-1074; HIS-1170; TRP-1171; LYS-1173; TYR-1404; GLY-1610; LYS-1893; TRP-2099; TYR-2111; ARG-2258; TRP-2282 AND ARG-2489 P1148A in fibrillin-1 is not a mutation leading to Shprintzen-Goldberg syndrome. VARIANT ALA-1148 Fibrillin-1 mutations in Marfan syndrome and other type-1 fibrillinopathies. VARIANTS MFS ARG-996; THR-1048; THR-1048 DEL; CYS-1058 INS; TRP-1086; SER-1837 AND CYS-2680 P1148A in fibrillin-1 is not a mutation anymore. VARIANT ALA-1148 Marfan Database (second edition): software and database for the analysis of mutations in the human FBN1 gene. VARIANTS MFS ARG-661; ARG-1043 AND ARG-2511 Multiple molecular mechanisms underlying subdiagnostic variants of Marfan syndrome. VARIANT MFS ARG-1265 Correlation of a recurrent FBN1 mutation (R122C) with an atypical familial Marfan syndrome phenotype. VARIANT MFS CYS-122 A novel mutation in the neonatal region of the fibrillin (FBN) 1 gene associated with a classical phenotype of Marfan syndrome (MfS). VARIANT MFS ILE-984 Demonstration of the recurrence of Marfan-like skeletal and cardiovascular manifestations due to germline mosaicism for an FBN1 mutation. VARIANT MFS GLU-985 Identification of 9 novel FBN1 mutations in German patients with Marfan syndrome. VARIANTS MFS PHE-504; TYR-1129; CYS-1261; SER-1833 AND TYR-2142 Genotype and phenotype analysis of 171 patients referred for molecular study of the fibrillin-1 gene FBN1 because of suspected Marfan syndrome. VARIANTS MFS PHE-89; CYS-122; CYS-240; CYS-366; CYS-545; SER-560; TYR-570; ASP-592; TRP-598; TYR-776; ARG-781; GLY-913; ARG-985; ARG-1013; TRP-1055; TYR-1055; CYS-1101; PRO-1337; TYR-1339; SER-1429; PRO-1790; TYR-1791; TYR-1835; THR-1909; SER-1915; TYR-1971; TYR-1977; HIS-2223; TRP-2282; TYR-2406; PHE-2581; THR-2585; ARG-2618; LYS-2624 AND CYS-2668 VARIANTS ECTOL1 CYS-1530 AND ARG-2154 VARIANT MITRAL VALVE PROLAPSE ILE-1128 TGGE screening of the entire FBN1 coding sequence in 126 individuals with Marfan syndrome and related fibrillinopathies. VARIANTS MFS CYS-62; TYR-587; TYR-596; ASN-654; TYR-681; ARG-683; TRP-685; VAL-723; PHE-734; TYR-748; GLY-776; ARG-781; ARG-908; GLY-921; PRO-1790; SER-1806; VAL-1931 DEL; TYR-1998; GLY-2221; THR-2269 AND TRP-2335 VARIANTS ECTOL1 CYS-115; TYR-661 AND TYR-2339 VARIANT MET-2101 Mutation screening of the fibrillin-1 (FBN1) gene in 76 unrelated patients with Marfan syndrome or Marfanoid features leads to the identification of 11 novel and three previously reported mutations. VARIANTS MFS 429-ARG--HIS-2871 DEL; ILE-449; SER-880; CYS-1101; TYR-1806; ILE-1908; ASP-1919 AND ARG-2251 Sensitivity of conformation sensitive gel electrophoresis in detecting mutations in Marfan syndrome and related conditions. VARIANTS MFS CYS-114; ARG-890; GLY-1200; TYR-1835; ARG-2111; CYS-2474 AND GLY-2652 VARIANT ECTOL1 CYS-240 Twelve novel FBN1 mutations in Marfan syndrome and Marfan related phenotypes test the feasibility of FBN1 mutation testing in clinical practice. VARIANTS MFS CYS-627; ASN-654; TYR-748; 1541-ARG--HIS-2871 DEL; TYR-1835; ARG-1977; TYR-2258; 2394-ARG--HIS-2871 DEL; 2466-TYR--HIS-2871 DEL AND 2467-GLN--HIS-2871 DEL VARIANT PRO-2780 In frame fibrillin-1 gene deletion in autosomal dominant Weill-Marchesani syndrome. VARIANT WMS2 1692-ARG--TYR-1699 DEL Detection of thirty novel FBN1 mutations in patients with Marfan syndrome or a related fibrillinopathy. VARIANTS MFS SER-154; SER-166; CYS-240; SER-652; THR-705; TYR-711; SER-816; ARG-1013; TYR-1044; GLY-1055; CYS-1101; TYR-1117; TYR-1153; ASN-1155; GLN-1325; LYS-1366; SER-1374; ARG-1389; 1394-GLY--THR-1396 DEL; ALA-1424; CYS-1530; TYR-1564; PHE-1770; TRP-1793; GLU-1796; TRP-2442; THR-2585 AND PRO-2623 Consequences of cysteine mutations in calcium-binding epidermal growth factor modules of fibrillin-1. CHARACTERIZATION OF VARIANTS MFS CYS-627; GLY-750 AND ARG-926 Identification of sixty-two novel and twelve known FBN1 mutations in eighty-one unrelated probands with Marfan syndrome and other fibrillinopathies. VARIANTS MFS CYS-20; TYR-123; ARG-177; ARG-224; GLY-439; 629-VAL--GLY-633 DEL; CYS-635; ILE-636; TYR-832; GLY-890; ASP-1058; SER-1153; PHE-1211 DEL; CYS-1219; ASP-1261; SER-1278; SER-1333; ARG-1402; SER-1424; PHE-1564; GLY-1631; TYR-1663; TYR-1876; ILE-1887; ARG-1895; TYR-1900; PRO-2160; PHE-2221; THR-2385; ARG-2500; TYR-2500; TRP-2535; LYS-2570; ARG-2571; SER-2592; LYS-2610 AND CYS-2629 Identification of 29 novel and nine recurrent fibrillin-1 (FBN1) mutations and genotype-phenotype correlations in 76 patients with Marfan syndrome. VARIANTS MFS ASN-507 DEL; TYR-541; CYS-627; TYR-781; ARG-985; ARG-1013; VAL-1113; GLY-1284; SER-1475; GLU-1475; THR-1576; ARG-1791; GLY-1928; TYR-1928; TYR-2038; ARG-2085; SER-2144; ARG-2536 AND TYR-2605 The importance of mutation detection in Marfan syndrome and Marfan-related disorders: report of 193 FBN1 mutations. VARIANTS MFS CYS-122; SER-214; 248-ASP--HIS-2871 DEL; 351-GLN--HIS-2871 DEL; ARG-365; 366-TRP--HIS-2871 DEL; TRP-474; CYS-545; TRP-546; 565-ARG--HIS-2871 DEL; TYR-727; CYS-828; TYR-832; 861-ARG--HIS-2871 DEL; VAL-882; CYS-974; HIS-976; 994-GLU--HIS-2871 DEL; TYR-1032; THR-1048; TYR-1074; ILE-1088; 1125-ARG--HIS-2871 DEL; TYR-1138; 1140-CYS--HIS-2871 DEL; GLY-1158; HIS-1170; ARG-1223; ARG-1249; TYR-1307; ARG-1326; LEU-1346; LYS-1366; TYR-1402; ALA-1424; ASP-1427; ARG-1485; TYR-1528; 1541-ARG--HIS-2871 DEL; ARG-1622; TYR-1720; TYR-1793; VAL-1796; SER-1806; LYS-1811; CYS-1830; PHE-1835; TRP-1847; ASP-1879; ARG-1987; 2053-CYS--HIS-2871 DEL; MET-2118; GLU-2127; ASP-2144; PRO-2145; TYR-2153; THR-2185; 2220-ARG--HIS-2871 DEL; THR-2269; TRP-2274; LYS-2447; ARG-2489; MET-2520; ARG-2536; 2542-GLN--HIS-2871 DEL; VAL-2555; 2571-CYS--HIS-2871 DEL; TYR-2577; THR-2585; LYS-2610 AND ARG-2618 VARIANTS ECTOL1 CYS-63; SER-68; CYS-240; TRP-365; CYS-545; ARG-596; PRO-634; VAL-882; 1086-CYS--HIS-2871 DEL; ASN-1155; ARG-1692 DEL; GLY-2250; CYS-2272; LYS-2447 AND ARG-2448 VARIANTS ASP-127; ARG-160; SER-164; 215-ARG--HIS-2871 DEL; 364-ARG--HIS-2871 DEL; ARG-504; TYR-652; 653-VAL--HIS-2871 DEL; 752-SER--HIS-2871 DEL; CYS-954; 966-GLU--HIS-2871 DEL; 988-TRP--HIS-2871 DEL; GLY-1028; GLY-1406; SER-1633; 1644-ARG--HIS-2871 DEL; PHE-1777; 1796-GLY--HIS-2871 DEL; TYR-1812; SER-1907; HIS-1930; LYS-2105; ASP-2136; 2169-GLU--HIS-2871 DEL; ARG-2195; PRO-2224; 2229-GLU--HIS-2871 DEL; MET-2234; THR-2273; TRP-2289; TYR-2302; TYR-2365; TRP-2470; ILE-2516; SER-2526; PHE-2541; TRP-2554; TRP-2726 AND 2840-LYS--HIS-2871 DEL FBN1 mutation screening of patients with Marfan syndrome and related disorders: detection of 46 novel FBN1 mutations. VARIANTS MFS TYR-123; SER-136; SER-177; TYR-177; SER-214; 348-GLN--HIS-2871 DEL; 429-ARG--HIS-2871 DEL; ARG-488; TYR-576; ARG-582; PHE-623; CYS-635; TYR-684; CYS-721; ARG-816; SER-880; GLU-884; TYR-1008; SER-1042; 1125-ARG--HIS-2871 DEL; 1136-TYR--HIS-2871 DEL; TRP-1182; TYR-1265; ARG-1320; 1534-CYS--HIS-2871 DEL; 1539-ARG--HIS-2871 DEL; 1541-ARG--HIS-2871 DEL; GLY-1631; ARG-1672; TYR-1672; GLY-1674; 1735-GLN--HIS-2871 DEL; LYS-1811; ARG-1847; TYR-1860; LYS-1894; TYR-1900; GLY-1934; TRP-1977; 2057-ARG--HIS-2871 DEL; 2062-TYR--HIS-2871 DEL; 2064-LYS--HIS-2871 DEL; TYR-2084; LYS-2130; ARG-2221; TYR-2232; THR-2269; THR-2284; TYR-2470; PRO-2561; LYS-2570; ARG-2577 AND 2694-ARG--HIS-2871 DEL VARIANTS PRO-39; ARG-937; ALA-1020; TRP-2726 AND 2774-LYS--HIS-2871 DEL Identification of novel FBN1 and TGFBR2 mutations in 65 probands with Marfan syndrome or Marfan-like phenotypes. VARIANTS MFS ASP-57; TYR-100; TYR-129; 861-ARG--HIS-2871 DEL; HIS-910; 921-CYS--HIS-2871 DEL; PRO-1130; 1790-ARG--HIS-2871 DEL; ARG-1812; SER-1826; TRP-2084; LYS-2130; SER-2144; 2298-LYS--HIS-2871 DEL; TYR-2522 AND SER-2708 Identification of the minimal combination of clinical features in probands for efficient mutation detection in the FBN1 gene. VARIANT 2867-GLN--HIS-2871 DEL Central nervous system abnormalities in two cases with neonatal Marfan syndrome with novel mutations in the fibrillin-1 gene. VARIANT MFS GLY-1068 Identification of a novel lethal fibrillin-1 gene mutation in a Chinese Marfan family and correlation of 3' fibrillin-1 gene mutations with phenotype. VARIANT 2849-TYR--HIS-2871 DEL Paucity of skeletal manifestations in Hispanic families with FBN1 mutations. VARIANTS MFS 515-CYS-ARG-516 DELINS TRP-GLY AND CYS-1530 A Japanese-specific allele in the GALNT11 gene. VARIANT ALA-1148 Mutations in fibrillin-1 cause congenital scleroderma: stiff skin syndrome. VARIANTS SSKS SER-1564; CYS-1570; GLY-1577 AND ASP-1594 Mutations in the TGFbeta binding-protein-like domain 5 of FBN1 are responsible for acromicric and geleophysic dysplasias. VARIANTS GPHYSD2 CYS-1696; ASP-1699; CYS-1699; TYR-1706; TRP-1719; THR-1728; VAL-1728; TYR-1733 AND SER-1762 VARIANTS ACMICD CYS-1699; CYS-1700; ARG-1714; CYS-1722; VAL-1726; THR-1728; GLN-1735 INS; ARG-1750 AND VAL-1758 Applying massive parallel sequencing to molecular diagnosis of Marfan and Loeys-Dietz syndromes. VARIANTS MFS GLY-80; TYR-490; TYR-499; ARG-611; GLY-617; TRP-685; TYR-685; TYR-790; TYR-811; SER-853; TYR-926; SER-1090; ASP-1185; TYR-1284; PHE-1350; ALA-1401; TRP-1431; TYR-1431; ALA-1487; LYS-1489; CYS-1838; TYR-1900; THR-1909; SER-1934; GLY-1976; ARG-1984; ASN-2166; THR-2185; GLY-2247; ARG-2318; TYR-2406; SER-2442; ARG-2511; VAL-2606 DEL; LYS-2610 AND ARG-2646 VARIANTS GLY-1481 AND HIS-2793 Exon 47 skipping of fibrillin-1 leads preferentially to cardiovascular defects in patients with thoracic aortic aneurysms and dissections. VARIANTS MFS GLU-55; GLN-219; SER-699; SER-880; TYR-908; ARG-1117; ALA-1199; 1539-ARG--HIS-2871 DEL; GLY-1642; ARG-1865; 2081-GLN--HIS-2871 DEL AND 2220-ARG--HIS-2871 DEL Fibrillin-1: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093). Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921). Asprosin: Hormone that targets the liver to increase plasma glucose levels. Secreted by white adipose tissue and circulates in the plasma. Acts in response to fasting and promotes blood glucose elevation by binding to the surface of hepatocytes. Promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation. Interacts with COL16A1 (PubMed:15165854). Interacts with integrin alpha-V/beta-3 (PubMed:15062093). Interacts with ADAMTS10; this interaction promotes microfibril assembly (PubMed:21402694). Interacts with THSD4; this interaction promotes fibril formation (By similarity). Interacts (via N-terminal domain) with FBLN2, FBLN4 and FBLN5 (PubMed:15790312, PubMed:17255108). Interacts with ELN (PubMed:15790312). Forms a ternary complex with ELN and FBLN2 or FBLN5 and a significant interaction with ELN seen only in the presence of FBLN2 or FBLN5 (PubMed:17255108). Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in a Ca(+2)-dependent manner (PubMed:17293099). Interacts (via N-terminal domain) with LTBP1 (via C-terminal domain) (PubMed:17293099). Interacts with integrins ITGA5:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6 (PubMed:17158881, PubMed:12807887). Interacts (via N-terminal domain) with BMP2, BMP4, BMP7, BMP10 and GDF5 (PubMed:18339631). Interacts (via N-terminal domain) with MFAP2 and MFAP5 (PubMed:15131124). Interacts with ADAMTSL5 (PubMed:23010571). Interacts with MFAP4 (PubMed:26601954). Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent manner (PubMed:24039232). false 6 O95967 EFEMP2 false 3 Q9UBX5 FBLN5 false 3 P35556 FBN2 false 2 P02751 FN1 false 2 P28300 LOX false 2 Q14766-2 LTBP1 false 2 Secreted Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin (PubMed:24982166). Asprosin Secreted Secreted into the plasma. Fibrillin-1 Secreted Extracellular space Extracellular matrix Fibrillin-1: Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils (PubMed:27026396). The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide (PubMed:24982166). Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils (PubMed:24982166). Fibrillin-1: Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils. Marfan syndrome MFS A hereditary disorder of connective tissue that affects the skeletal, ocular, and cardiovascular systems. A wide variety of skeletal abnormalities occurs with Marfan syndrome, including scoliosis, chest wall deformity, tall stature, abnormal joint mobility. Ectopia lentis occurs in most of the patients and is almost always bilateral. The leading cause of premature death is progressive dilation of the aortic root and ascending aorta, causing aortic incompetence and dissection. Neonatal Marfan syndrome is the most severe form resulting in death from cardiorespiratory failure in the first few years of life. The disease is caused by mutations affecting the gene represented in this entry. The majority of the more than thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations. Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini. Ectopia lentis 1, isolated, autosomal dominant ECTOL1 An ocular abnormality characterized by partial or complete displacement of the lens from its space resulting from defective zonule formation. The disease is caused by mutations affecting the gene represented in this entry. Weill-Marchesani syndrome 2 WMS2 A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma. The disease is caused by mutations affecting the gene represented in this entry. Overlap connective tissue disease OCTD Heritable disorder of connective tissue characterized by involvement of the mitral valve, aorta, skeleton, and skin. MASS syndrome is closely resembling both the Marfan syndrome and the Barlow syndrome. However, no dislocation of the lenses or aneurysmal changes occur in the aorta, and the mitral valve prolapse is by no means invariable. The disease is caused by mutations affecting the gene represented in this entry. Stiff skin syndrome SSKS A syndrome characterized by hard, thick skin, usually over the entire body, which limits joint mobility and causes flexion contractures. Other occasional findings include lipodystrophy and muscle weakness. The disease is caused by mutations affecting the gene represented in this entry. Geleophysic dysplasia 2 GPHYSD2 An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have characteristic facial features including a 'happy' face with full cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin upper lip. Other distinctive features include progressive cardiac valvular thickening often leading to an early death, toe walking, tracheal stenosis, respiratory insufficiency, and lysosomal-like storage vacuoles in various tissues. The disease is caused by mutations affecting the gene represented in this entry. Acromicric dysplasia ACMICD An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening. Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies. Affected individuals have distinct facial features, including round face, well-defined eyebrows, long eyelashes, bulbous nose with anteverted nostrils, long and prominent philtrum, and thick lips with a small mouth. Other characteristic features include hoarse voice and pseudomuscular build, and there are distinct skeletal features as well, including an internal notch of the femoral head, internal notch of the second metacarpal, and external notch of the fifth metacarpal. The disease is caused by mutations affecting the gene represented in this entry. Marfanoid-progeroid-lipodystrophy syndrome MFLS An autosomal dominant syndrome characterized by congenital lipodystrophy, a progeroid facial appearance due to lack of subcutaneous fat, and variable signs of Marfan syndrome. Clinical features include premature birth with an accelerated linear growth disproportionate to the weight gain, ectopia lentis, aortic dilatation, dural ectasia, and arachnodactyly. Mental and motor development are within normal limits. The disease is caused by mutations affecting the gene represented in this entry. Asprosin: Mutations specifically affect Asprosin, a hormone peptide present at the C-terminus of Fibrillin-1 chain, which is cleaved from Fibrillin-1 following secretion (PubMed:27087445). Asprosin: Was named after the Greek word for white, because of the reduction in subcutaneous white adipose tissue that is displayed by asprosin-deficient patients. Belongs to the fibrillin family. Translation N-terminally shortened. 3D-structure Aortic aneurysm Calcium Complete proteome Direct protein sequencing Disease mutation Disulfide bond Dwarfism EGF-like domain Extracellular matrix Glycoprotein Heparin-binding Hormone Phosphoprotein Polymorphism Reference proteome Repeat Secreted Signal Y C A T A P G E N D R C Y C C S C G C F C Y C R R C S C R C C Y G D C Y H Q C S C S C R N S C F C S C R C S C Y G S W G H Q C R R C I T G S C R C W W C R G V I Y C C W C G C R D Y C Y C F C R CR WG C Y R C C W N I G S C Y C Y C R C Y G D C R C Y C W C R C G C F R C S P Y C R I C S C Y D N C R C Y S Y C R C Y C W C Y C S A T C Y G C D A D V C Y C F Y C C Y C G C G C Y C R C Y C Y C Y C R C S F C C Y C S C R G S A V G E C G C R C R C Y D H E G C G C R C Y C R R C R C R H V I G E G R C R C Y G R T A K N D G C Y G S K R C Y I T I V C R C G C W C Y G D G GC C G D G E K C R C Y C W N I P S Y C D G D V C G C R C Y G S V I C Y H P N Y R P C Y P A C S C Y D N E G R H C W N K C W G D D A E G Y C C R C Y C Y C R C S Y C Y D C R C Y C S N S C G C Y C Y C R E Q C R C S A P C Y F L C F E K C S N S C R T A C R C Y D Y D G P A P S Y D C S C W C Y G E G S S G C R D A N K C R D Y R C C F C S C Y W C M T C G C F G D C G C R C G C S D G C R C Y C F C R C Y C G Y C Y C Y D Y C C Y M R C W C Y S C G V A T A V C Y Q QQ S R D V G S C F C F R P C R C Y C W C Y G E G V C S C Y E K C R C Y N S S C C S C F C Y P S G C C R C W C Y C R C Y G D T I N K E K C R C Y N S T I I T R S G D C G C R C Y D H C G C S C Y E G C R C W C Y C R G R C Y V I C Y C F C W C Y C R C W T M E K C R C Y Y F I M D E E K V D C Y N D N S T P C W C Y P R A P D N C F I T G R C F C G C R C S N H T P C Y V M D G E G C R C R C Y I T Y C M T C W P S R W P T C W C Y C S C R D E R W C Y C Y A T C Y C S C W E K C R C W C Y Y C C R C R C Y C R T I T M C Y N S C W G R C F R W G V T P E K C R C R C Y C F I T C S C Y E K G R H P N K G R Y C C R C G C S G C R C N S R W I T L P Y H G D R A R K S T T Q I T MRRGRLLEIALGFTVLLASYTSHGADANLEAGNVKETRASRAKRRGGGGHDALKGPNVCG SRYNAYCCPGWKTLPGGNQCIVPICRHSCGDGFCSRPNMCTCPSGQIAPSCGSRSIQHCN IRCMNGGSCSDDHCLCQKGYIGTHCGQPVCESGCLNGGRCVAPNRCACTYGFTGPQCERD YRTGPCFTVISNQMCQGQLSGIVCTKTLCCATVGRAWGHPCEMCPAQPHPCRRGFIPNIR TGACQDVDECQAIPGLCQGGNCINTVGSFECKCPAGHKLNEVSQKCEDIDECSTIPGICE GGECTNTVSSYFCKCPPGFYTSPDGTRCIDVRPGYCYTALTNGRCSNQLPQSITKMQCCC DAGRCWSPGVTVAPEMCPIRATEDFNKLCSVPMVIPGRPEYPPPPLGPIPPVLPVPPGFP PGPQIPVPRPPVEYLYPSREPPRVLPVNVTDYCQLVRYLCQNGRCIPTPGSYRCECNKGF QLDLRGECIDVDECEKNPCAGGECINNQGSYTCQCRAGYQSTLTRTECRDIDECLQNGRI CNNGRCINTDGSFHCVCNAGFHVTRDGKNCEDMDECSIRNMCLNGMCINEDGSFKCICKP GFQLASDGRYCKDINECETPGICMNGRCVNTDGSYRCECFPGLAVGLDGRVCVDTHMRST CYGGYKRGQCIKPLFGAVTKSECCCASTEYAFGEPCQPCPAQNSAEYQALCSSGPGMTSA GSDINECALDPDICPNGICENLRGTYKCICNSGYEVDSTGKNCVDINECVLNSLLCDNGQ CRNTPGSFVCTCPKGFIYKPDLKTCEDIDECESSPCINGVCKNSPGSFICECSSESTLDP TKTICIETIKGTCWQTVIDGRCEININGATLKSQCCSSLGAAWGSPCTLCQVDPICGKGY SRIKGTQCEDIDECEVFPGVCKNGLCVNTRGSFKCQCPSGMTLDATGRICLDIRLETCFL RYEDEECTLPIAGRHRMDACCCSVGAAWGTEECEECPMRNTPEYEELCPRGPGFATKEIT NGKPFFKDINECKMIPSLCTHGKCRNTIGSFKCRCDSGFALDSEERNCTDIDECRISPDL CGRGQCVNTPGDFECKCDEGYESGFMMMKNCMDIDECQRDPLLCRGGVCHNTEGSYRCEC PPGHQLSPNISACIDINECELSAHLCPNGRCVNLIGKYQCACNPGYHSTPDRLFCVDIDE CSIMNGGCETFCTNSEGSYECSCQPGFALMPDQRSCTDIDECEDNPNICDGGQCTNIPGE YRCLCYDGFMASEDMKTCVDVNECDLNPNICLSGTCENTKGSFICHCDMGYSGKKGKTGC TDINECEIGAHNCGKHAVCTNTAGSFKCSCSPGWIGDGIKCTDLDECSNGTHMCSQHADC KNTMGSYRCLCKEGYTGDGFTCTDLDECSENLNLCGNGQCLNAPGGYRCECDMGFVPSAD GKACEDIDECSLPNICVFGTCHNLPGLFRCECEIGYELDRSGGNCTDVNECLDPTTCISG NCVNTPGSYICDCPPDFELNPTRVGCVDTRSGNCYLDIRPRGDNGDTACSNEIGVGVSKA SCCCSLGKAWGTPCEMCPAVNTSEYKILCPGGEGFRPNPITVILEDIDECQELPGLCQGG KCINTFGSFQCRCPTGYYLNEDTRVCDDVNECETPGICGPGTCYNTVGNYTCICPPDYMQ VNGGNNCMDMRRSLCYRNYYADNQTCDGELLFNMTKKMCCCSYNIGRAWNKPCEQCPIPS TDEFATLCGSQRPGFVIDIYTGLPVDIDECREIPGVCENGVCINMVGSFRCECPVGFFYN DKLLVCEDIDECQNGPVCQRNAECINTAGSYRCDCKPGYRFTSTGQCNDRNECQEIPNIC SHGQCIDTVGSFYCLCHTGFKTNDDQTMCLDINECERDACGNGTCRNTIGSFNCRCNHGF ILSHNNDCIDVDECASGNGNLCRNGQCINTVGSFQCQCNEGYEVAPDGRTCVDINECLLE PRKCAPGTCQNLDGSYRCICPPGYSLQNEKCEDIDECVEEPEICALGTCSNTEGSFKCLC PEGFSLSSSGRRCQDLRMSYCYAKFEGGKCSSPKSRNHSKQECCCALKGEGWGDPCELCP TEPDEAFRQICPYGSGIIVGPDDSAVDMDECKEPDVCKHGQCINTDGSYRCECPFGYILA GNECVDTDECSVGNPCGNGTCKNVIGGFECTCEEGFEPGPMMTCEDINECAQNPLLCAFR CVNTYGSYECKCPVGYVLREDRRMCKDEDECEEGKHDCTEKQMECKNLIGTYMCICGPGY QRRPDGEGCVDENECQTKPGICENGRCLNTRGSYTCECNDGFTASPNQDECLDNREGYCF TEVLQNMCQIGSSNRNPVTKSECCCDGGRGWGPHCEICPFQGTVAFKKLCPHGRGFMTNG ADIDECKVIHDVCRNGECVNDRGSYHCICKTGYTPDITGTSCVDLNECNQAPKPCNFICK NTEGSYQCSCPKGYILQEDGRSCKDLDECATKQHNCQFLCVNTIGGFTCKCPPGFTQHHT SCIDNNECTSDINLCGSKGICQNTPGSFTCECQRGFSLDQTGSSCEDVDECEGNHRCQHG CQNIIGGYRCSCPQGYLQHYQWNQCVDENECLSAHICGGASCHNTLGSYKCMCPAGFQYE QFSGGCQDINECGSAQAPCSYGCSNTEGGYLCGCPPGYFRIGQGHCVSGMGMGRGNPEPP VSGEMDDNSLSPEACYECKINGYPKRGRKRRSTNETDASNIEDQSETEANVSLASWDVEK TAIFAFNISHVSNKVRILELLPALTTLTNHNRYLIESGNEDGFFKINQKEGISYLHFTKK KPVAGTYSLQISSTPLYKKKELNQLEDKYDKDYLSGELGDNLKMKIQVLLH Q92484 B7Z729 Q8WV13 ASM3A_HUMAN Acid sphingomyelinase-like phosphodiesterase 3a ASM-like phosphodiesterase 3a 3.1.4.- SMPDL3A ASML3A Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Synovium The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Placenta Acid sphingomyelinase is a member of a multi-gene family and shares motifs with a large family of metallo-phosphoesterases. NUCLEOTIDE SEQUENCE [MRNA] OF 277-453 (ISOFORM 1/2) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-222; ASN-263 AND ASN-356 Liver Sphingomyelin phosphodiesterase acid-like 3A (SMPDL3A) is a novel nucleotide phosphodiesterase regulated by cholesterol in human macrophages. CATALYTIC ACTIVITY FUNCTION LACK OF SPHINGOMYELIN PHOSPHODIESTERASE ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES ACTIVITY REGULATION SUBCELLULAR LOCATION GLYCOSYLATION INDUCTION BY CHOLESTEROL TISSUE SPECIFICITY The structure and catalytic mechanism of human sphingomyelin phosphodiesterase like 3a - an acid sphingomyelinase homolog with a novel nucleotide hydrolase activity. X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 34-443 IN COMPLEX WITH CMP; PHOSPHORIBOSE AND ZINC IONS FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES COFACTOR SUBUNIT DISULFIDE BONDS GLYCOSYLATION AT ASN-69; ASN-131 AND ASN-356 ACTIVITY REGULATION Has in vitro nucleotide phosphodiesterase activity with nucleoside triphosphates, such as ATP (PubMed:25288789, PubMed:26783088). Has in vitro activity with p-nitrophenyl-TMP (PubMed:25288789). Has lower activity with nucleoside diphosphates, and no activity with nucleoside monophosphates (PubMed:25288789, PubMed:26783088). Has in vitro activity with CDP-choline, giving rise to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine (PubMed:26783088). Does not have sphingomyelin phosphodiesterase activity (PubMed:25288789, PubMed:26783088). Zn(2+) Binds 2 Zn(2+) per subunit. Requires micromolar levels of Zn(2+) for activity (PubMed:26783088). Inhibited by millimolar levels of Zn(2+) (PubMed:25288789, PubMed:26783088). 326 uM for ATP 306 uM for ADP 348 uM for ADP-ribose 390 uM for CDP-ethanolamine 262 uM for CDP-choline Optimum pH is 4-6. Monomer. Secreted Q92484-1 1 Q92484-2 2 No experimental confirmation available. Detected in blood serum. Detected in macrophages (at protein level). Up-regulated in macrophages in response to cholesterol accumulation. Up-regulated by cAMP. N-glycosylated. Belongs to the acid sphingomyelinase family. 3D-structure Alternative splicing Complete proteome Disulfide bond Glycoprotein Hydrolase Metal-binding Polymorphism Reference proteome Secreted Signal Zinc H Y P S N K MALVRALVCCLLTAWHCRSGLGLPVAPAGGRNPPPAIGQFWHVTDLHLDPTYHITDDHTK VCASSKGANASNPGPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDSPPHVPVPEL STDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVTSKVYNAVANLWKPWLD EEAISTLRKGGFYSQKVTTNPNLRIISLNTNLYYGPNIMTLNKTDPANQFEWLESTLNNS QQNKEKVYIIAHVPVGYLPSSQNITAMREYYNEKLIDIFQKYSDVIAGQFYGHTHRDSIM VLSDKKGSPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEA NLKGESIWKLEYILTQTYDIEDLQPESLYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTC DKTCKAFQICAIMNLDNISYADCLKQLYIKHNY Q8TCG5 A8K0Z8 Q5K6N5 Q8N6Q9 Q8NDS6 Q8TE84 CPT1C_HUMAN Carnitine O-palmitoyltransferase 1, brain isoform CPT1-B 2.3.1.21 CPT IC Carnitine O-palmitoyltransferase I, brain isoform CPTI-B Carnitine palmitoyltransferase 1C CPT1C CATL1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A novel brain-expressed protein related to carnitine palmitoyltransferase I. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) TISSUE SPECIFICITY Eye Molecular characterization, chromosomal localization and expression analysis of a gene, CATL1, encoding for a new member of the human carnitine acyltransferase family. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain Kidney epithelium Subthalamic nucleus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Eye The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 375-803 (ISOFORM 3) Brain Mutation in CPT1C Associated with pure autosomal dominant spastic paraplegia. FUNCTION INTERACTION WITH ATL1 SUBCELLULAR LOCATION TISSUE SPECIFICITY INVOLVEMENT IN SPG73 VARIANT SPG73 CYS-37 CHARACTERIZATION OF VARIANT SPG73 CYS-37 May play a role in lipid metabolic process. (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine Lipid metabolism; fatty acid beta-oxidation. Peripherally associated with AMPAR complex. AMPAR complex consists of an inner core made of 4 pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged in a twofold symmetry. One of the two pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR complex is complemented by outer core constituents binding directly to the GluA/GRIA proteins at sites distinct from the interaction sites of the inner core constituents. Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the inner and outer core serve as a platform for other, more peripherally associated AMPAR constituents, including CPT1C. Alone or in combination, these auxiliary subunits control the gating and pharmacology of the AMPAR complex and profoundly impact their biogenesis and protein processing (By similarity). Interacts with ATL1 (PubMed:25751282). Mitochondrion outer membrane Multi-pass membrane protein Cell junction Synapse Cell projection Dendrite Cell projection Axon Endoplasmic reticulum Localized in the soma and dendritic and axonal projections. Q8TCG5-1 1 Q8TCG5-2 2 No experimental confirmation available. Q8TCG5-3 3 No experimental confirmation available. Expressed predominantly in brain and testis. Expressed in motor neurons. Spastic paraplegia 73, autosomal dominant SPG73 A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the carnitine/choline acetyltransferase family. Translation N-terminally extended. Translation N-terminally extended. 3D-structure Acyltransferase Alternative splicing Cell junction Cell projection Complete proteome Disease mutation Endoplasmic reticulum Fatty acid metabolism Hereditary spastic paraplegia Lipid metabolism Membrane Mitochondrion Mitochondrion outer membrane Neurodegeneration Reference proteome Synapse Transferase Transmembrane Transmembrane helix R C S G HEEH RTRG D G MAEAHQAVGFRPSLTSDGAEVELSAPVLQEIYLSGLRSWKRHLSRFWNDFLTGVFPASPL SWLFLFSAIQLAWFLQLDPSLGLMEKIKELLPDWGGQHHGLRGVLAAALFASCLWGALIF TLHVALRLLLSYHGWLLEPHGAMSSPTKTWLALVRIFSGRHPMLFSYQRSLPRQPVPSVQ DTVRKYLESVRPILSDEDFDWTAVLAQEFLRLQASLLQWYLRLKSWWASNYVSDWWEEFV YLRSRNPLMVNSNYYMMDFLYVTPTPLQAARAGNAVHALLLYRHRLNRQEIPPTLLMGMR PLCSAQYEKIFNTTRIPGVQKDYIRHLHDSQHVAVFHRGRFFRMGTHSRNSLLSPRALEQ QFQRILDDPSPACPHEEHLAALTAAPRGTWAQVRTSLKTQAAEALEAVEGAAFFVSLDAE PAGLTREDPAASLDAYAHALLAGRGHDRWFDKSFTLIVFSNGKLGLSVEHSWADCPISGH MWEFTLATECFQLGYSTDGHCKGHPDPTLPQPQRLQWDLPDQIHSSISLALRGAKILSEN VDCHVVPFSLFGKSFIRRCHLSSDSFIQIALQLAHFRDRGQFCLTYESAMTRLFLEGRTE TVRSCTREACNFVRAMEDKEKTDPQCLALFRVAVDKHQALLKAAMSGQGVDRHLFALYIV SRFLHLQSPFLTQVHSEQWQLSTSQIPVQQMHLFDVHNYPDYVSSGGGFGPADDHGYGVS YIFMGDGMITFHISSKKSSTKTDSHRLGQHIEDALLDVASLFQAGQHFKRRFRGSGKENS RHRCGFLSRQTGASKASMTSTDF A6NM45 F5H040 CLD24_HUMAN Putative claudin-24 Claudin-21 CLDN24 CLDN21 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Cell junction Tight junction Cell membrane Multi-pass membrane protein Belongs to the claudin family. Could be the product of a pseudogene. Cell junction Cell membrane Complete proteome Membrane Polymorphism Reference proteome Tight junction Transmembrane Transmembrane helix L F MALIFRTAMQSVGLLLSLLGWILSIITTYLPHWKNLNLDLNEMENWTMGLWQTCVIQEEV GMQCKDFDSFLALPAELRVSRILMFLSNGLGFLGLLVSGFGLDCLRIGESQRDLKRRLLI LGGILSWASGITALVPVSWVAHKTVQEFWDENVPDFVPRWEFGEALFLGWFAGLSLLLGG CLLNCAACSSHAPLALGHYAVAQMQTQCPYLEDGTADPQV Q8N5K1 Q7Z3D5 CISD2_HUMAN CDGSH iron-sulfur domain-containing protein 2 Endoplasmic reticulum intermembrane small protein MitoNEET-related 1 protein Miner1 Nutrient-deprivation autophagy factor-1 NAF-1 CISD2 CDGSH2 ERIS ZCD2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A homozygous mutation in a novel zinc-finger protein, ERIS, is responsible for Wolfram syndrome 2. NUCLEOTIDE SEQUENCE [MRNA] FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY INVOLVEMENT IN WFS2 Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Synovium The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Retina NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Cervix PROTEIN SEQUENCE OF 21-32; 82-95 AND 117-131 IDENTIFICATION BY MASS SPECTROMETRY B-cell lymphoma MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity. COFACTOR SUBCELLULAR LOCATION Antagonism of Beclin 1-dependent autophagy by BCL-2 at the endoplasmic reticulum requires NAF-1. FUNCTION SUBCELLULAR LOCATION INTERACTION WITH BCL2; BCL2L1 AND ITPR1 MUTAGENESIS OF CYS-99; CYS-101; CYS-110 AND HIS-114 Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminome analysis of the human mitochondrial proteome. CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Crystal structure of Miner1: The redox-active 2Fe-2S protein causative in Wolfram Syndrome 2. X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 57-135 OF MUTANT CYS-92 IN COMPLEX WITH 2FE-2S BIOPHYSICOCHEMICAL PROPERTIES MUTAGENESIS OF CYS-92 Regulator of autophagy that contributes to antagonize BECN1-mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of BCL2 with BECN1 and is required for BCL2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy. Contributes to BIK-initiated autophagy, while it is not involved in BIK-dependent activation of caspases. Involved in life span control, probably via its function as regulator of autophagy. [2Fe-2S] cluster Binds 1 [2Fe-2S] cluster. E is 0 +/- 10 mV for 2Fe-2S at pH 7.5. Homodimer. Interacts with BCL2; the interaction is direct and disrupted by BIK interaction with BCL2. Interacts with BCL2L1. Interacts with ITPR1. P10415 BCL2 false 2 Endoplasmic reticulum membrane Single-pass membrane protein Mitochondrion outer membrane Single-pass membrane protein According to PubMed:20010695, it mainly localizes to the endoplasmic reticulum. However, experiments in mouse showed that it mainly localizes to the mitochondrion outer membrane. Testis, small intestine, kidney, lung, brain, heart, pancreas and platelets. Wolfram syndrome 2 WFS2 A rare disorder characterized by juvenile-onset insulin-dependent diabetes mellitus with optic atrophy. Other manifestations include diabetes insipidus, sensorineural deafness, dementia, psychiatric illnesses. WFS2 patients additionally show a strong bleeding tendency and gastrointestinal ulceration. Diabetes insipidus may be absent. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the CISD protein family. CISD2 subfamily. Although initially thought (PubMed:17846994) to be a zinc-finger protein, it was later shown (PubMed:17376863) that it binds 1 2Fe-2S cluster instead. 2Fe-2S 3D-structure Autophagy Complete proteome Deafness Diabetes mellitus Direct protein sequencing Endoplasmic reticulum Iron Iron-sulfur Membrane Metal-binding Mitochondrion Mitochondrion outer membrane Reference proteome Transmembrane Transmembrane helix C S C S C S C S H Q MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFL PKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNEL TGDNVGPLILKKKEV Q9BYF1 C7ECU1 Q6UWP0 Q86WT0 Q9NRA7 Q9UFZ6 ACE2_HUMAN Angiotensin-converting enzyme 2 3.4.17.23 ACE-related carboxypeptidase Angiotensin-converting enzyme homolog ACEH Metalloprotease MPROT15 Processed angiotensin-converting enzyme 2 ACE2 UNQ868/PRO1885 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) TISSUE SPECIFICITY FUNCTION ACTIVITY REGULATION Heart A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) TISSUE SPECIFICITY GLYCOSYLATION FUNCTION ACTIVITY REGULATION Lymphoma The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is selectively expressed by adult Leydig cells of the testis. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) ACTIVITY REGULATION SUBCELLULAR LOCATION TISSUE SPECIFICITY Testis Identification of an alternative 5'-untranslated exon and new polymorphisms of angiotensin-converting enzyme 2 gene: lack of association with SARS in the Vietnamese population. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANT SER-638 Lung Testis Cloning, expression analysis and chromosomal localization of a novel ACE like enzyme. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) MPROT15 polypeptide and MPROT15 polynucleotide. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Comparative susceptibility to SARS-CoV mediated by ACE2 protein of 15 different species. NUCLEOTIDE SEQUENCE [MRNA] The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT ARG-26 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain Testis The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-805 (ISOFORM 1) Testis Interaction of ACE2 and integrin beta1 in failing human heart. PROTEIN SEQUENCE OF 679-689 IDENTIFICATION BY MASS SPECTROMETRY INTERACTION WITH ITGB1 Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme. TISSUE SPECIFICITY Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase. FUNCTION BIOPHYSICOCHEMICAL PROPERTIES ACTIVITY REGULATION COFACTOR Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. FUNCTION (MICROBIAL INFECTION) INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN GLYCOSYLATION IDENTIFICATION BY MASS SPECTROMETRY ACE2 gene expression is up-regulated in the human failing heart. INDUCTION Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis. TISSUE SPECIFICITY Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2. FUNCTION (MICROBIAL INFECTION) INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN A proteomic analysis of human bile. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90 Bile Myocardial infarction increases ACE2 expression in rat and humans. TISSUE SPECIFICITY INDUCTION Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2. FUNCTION (MICROBIAL INFECTION) INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN MUTAGENESIS Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2). PROTEOLYTIC CLEAVAGE Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry. FUNCTION (MICROBIAL INFECTION) INTERACTION WITH HCOV-NL63 SPIKE GLYCOPROTEIN A protein complex in the brush-border membrane explains a Hartnup disorder allele. FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546 Liver Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. FUNCTION MUTAGENESIS OF ARG-273 Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site identification: determinants and constraints. PROTEOLYTIC CLEAVAGE A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry. SUBCELLULAR LOCATION PROTEOLYTIC CLEAVAGE INTERACTION WITH TMPRSS2 TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein. FUNCTION (MICROBIAL INFECTION) SUBCELLULAR LOCATION PROTEOLYTIC CLEAVAGE ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-615 X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-615 IN COMPLEX WITH MLN-4760 DISULFIDE BONDS GLYCOSYLATION AT ASN-53; ASN-90; ASN-103; ASN-322; ASN-432 AND ASN-546 Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator (PubMed:10969042, PubMed:10924499, PubMed:11815627). Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency (PubMed:11815627). By cleavage of angiotensin II, may be an important regulator of heart function (PubMed:10969042, PubMed:10924499). By cleavage of angiotensin II, may also have a protective role in acute lung injury (By similarity). Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SL6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity (PubMed:18424768, PubMed:19185582). (Microbial infection) Acts as a receptor for SARS coronavirus/SARS-CoV. (Microbial infection) Acts as a receptor for Human coronavirus NL63/HCoV-NL63. angiotensin II + H2O = angiotensin-(1-7) + L-phenylalanine Zn(2+) Binds 1 zinc ion per subunit. chloride Binds 1 Cl(-) ion per subunit. Activated by chloride and fluoride, but not bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the ACE inhibitors linosipril, captopril and enalaprilat. 6.9 uM for angiotensin I 2 uM for angiotensin II 6.8 uM for apelin-13 5.5 uM for dynorphin-13 Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6 to 9. Interacts with ITGB1 (PubMed:15276642). Interacts with the catalytically active form of TMPRSS2 (PubMed:21068237). Interacts with SLC6A19; this interaction is essential for expression and function of SLC6A19 in intestine (By similarity). (Microbial infection) Interacts with SARS coronavirus/SARS-CoV. (Microbial infection) Interacts with Human coronavirus NL63/HCoV-NL63 spike glycoprotein. Q6Q1S2 S true 3 Processed angiotensin-converting enzyme 2 Secreted Cell membrane Single-pass type I membrane protein Cytoplasm Detected in both cell membrane and cytoplasm in neurons. Q9BYF1-1 1 Q9BYF1-2 2 No experimental confirmation available. Expressed in endothelial cells from small and large arteries, and in arterial smooth muscle cells (at protein level) (PubMed:15141377). Expressed in lung alveolar epithelial cells, enterocytes of the small intestine, Leydig cells and Sertoli cells (at protein level) (PubMed:15141377). Expressed in the renal proximal tubule and the small intestine (at protein level) (PubMed:18424768). Expressed in heart, kidney, testis, and gastrointestinal system (PubMed:10969042, PubMed:10924499, PubMed:15231706, PubMed:12459472, PubMed:15671045). Up-regulated in failing heart. N-glycosylation on Asn-90 may limit SARS infectivity. Proteolytic cleavage by ADAM17 generates a secreted form. Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1. Belongs to the peptidase M2 family. 3D-structure Alternative splicing Carboxypeptidase Cell membrane Chloride Complete proteome Cytoplasm Direct protein sequencing Disulfide bond Glycoprotein Host cell receptor for virus entry Host-virus interaction Hydrolase Membrane Metal-binding Metalloprotease Polymorphism Protease Receptor Reference proteome Secreted Signal Transmembrane Transmembrane helix Zinc F L K R N S QAK KAE K D E A D A Y A K D MYP NFS E P PD SM E R R D R D H Q R Q K D E A T A NVQ DDR D A K H A D D A R A L K A M A P A R A SPD PSN KGE QDK R S F T Q H N D K R MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQ NMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTIL NTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLY EEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHL HAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQ AWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILM CTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKS IGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEM KREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLH KCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNK NSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKN QMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDN SLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENP YASIDISKGENNPGFQNTDDVQTSF Q15822 A8KAX3 B4DK19 J3KMY9 Q9HAQ3 ACHA2_HUMAN Neuronal acetylcholine receptor subunit alpha-2 CHRNA2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4 nicotinic acetylcholine receptor subunits and functional expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANT ALA-125 Hypothalamus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANT ALA-125 Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) VARIANT ALA-125 Thalamus DNA sequence and analysis of human chromosome 8. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Crystal structure of a human neuronal nAChR extracellular domain in pentameric assembly: Ligand-bound alpha2 homopentamer. X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 59-265 SUBUNIT MUTAGENESIS OF TRP-115 AND TYR-225 Increased sensitivity of the neuronal nicotinic receptor alpha2 subunit causes familial epilepsy with nocturnal wandering and ictal fear. VARIANT ENFL4 ASN-279 CHARACTERIZATION OF VARIANT ENFL4 ASN-279 Mutation of CHRNA2 in a family with benign familial infantile seizures: Potential role of nicotinic acetylcholine receptor in various phenotypes of epilepsy. VARIANT BFIS6 TRP-376 After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. Neuronal AChR seems to be composed of two different types of subunits: alpha and non-alpha (beta). Alpha-2 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. The alpha-2:beta-2 nAChR complex is proposed to be a heteropentamer with two subtypes: LS (low agonist sensitivity) with a (alpha-2)3:(beta-2)2 and HS (high agonist sensitivity) with a (alpha-2)2:(beta-2)3 stoichiometry; the subtypes differ in their subunit binding interfaces which are involved in ligand binding. Cell junction Synapse Postsynaptic cell membrane Multi-pass membrane protein Cell membrane Multi-pass membrane protein Q15822-1 1 Q15822-2 2 No experimental confirmation available. Epilepsy, nocturnal frontal lobe, 4 ENFL4 An autosomal dominant focal epilepsy characterized by nocturnal seizures associated with fear sensation, tongue movements, and nocturnal wandering, closely resembling nightmares and sleep walking. The disease is caused by mutations affecting the gene represented in this entry. Seizures, benign familial infantile, 6 BFIS6 A form of benign familial infantile epilepsy, a neurologic disorder characterized by afebrile seizures occurring in clusters during the first year of life, without neurologic sequelae. BFIS6 inheritance is autosomal dominant. The disease may be caused by mutations affecting the gene represented in this entry. Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-2/CHRNA2 sub-subfamily. With the use of epibatidine as high affinity ligand, an alpha-2 homopentamer has been purified and crystallized. Its physiological relevance has not been proven. 3D-structure Alternative splicing Cell junction Cell membrane Complete proteome Disease mutation Disulfide bond Epilepsy Glycoprotein Ion channel Ion transport Ligand-gated ion channel Membrane Polymorphism Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport T I T A I N R W W A Y F MGPSCPVFLSFTKLSLWWLLLTPAGGEEAKRPPPRAPGDPLSSPSPTALPQGGSHTETED RLFKHLFRGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWSDYKL RWNPTDFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFSTGTVHWVPPAIYK SSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMEQTVDLKDYWESGEWAIVNATGTY NSKKYDCCAEIYPDVTYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSDCGEKITLC ISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTH TMPHWVRGALLGCVPRWLLMNRPPPPVELCHPLRLKLSPSYHWLESNVDAEEREVVVEEE DRWACAGHVAPSVGTLCSHGHLHSGASGPKAEALLQEGELLLSPHMQKALEGVHYIADHL RSEDADSSVKEDWKYVAMVIDRIFLWLFIIVCFLGTIGLFLPPFLAGMI Q9H4D0 B2RCW5 D3DNF4 Q3SX54 Q3ZB76 Q5UE56 Q96HZ2 Q9BSS0 CSTN2_HUMAN Calsyntenin-2 Alcadein-gamma Alc-gamma CLSTN2 CS2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The calsyntenins - a family of postsynaptic membrane proteins with distinct neuronal expression patterns. NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY VARIANT ILE-366 Fetal brain Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism. NUCLEOTIDE SEQUENCE [MRNA] VARIANT ILE-366 Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Uterus The DNA sequence, annotation and analysis of human chromosome 3. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANT ILE-366 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Lung Coordinated metabolism of Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation. PROTEOLYTIC CLEAVAGE The consensus coding sequences of human breast and colorectal cancers. VARIANTS [LARGE SCALE ANALYSIS] ILE-193 AND GLN-765 May modulate calcium-mediated postsynaptic signals. Cell membrane Single-pass type I membrane protein Endoplasmic reticulum membrane Golgi apparatus membrane Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. Restricted to the brain. Binds synaptic Ca(2+) with its cytoplasmic domain. Proteolytically processed under normal cellular conditions. A primary zeta-cleavage generates a large extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal transmembrane fragment (CTF1). A secondary cleavage catalyzed by gamma-secretase within the transmembrane domain releases the beta-Alc-gamma chain in the extracellular milieu and produces an intracellular fragment (AlcICD). This processing is strongly suppressed in the tripartite complex formed with APBA2 and APP, which seems to prevent the association with PSEN1 (By similarity). Calcium Cell adhesion Cell membrane Complete proteome Endoplasmic reticulum Glycoprotein Golgi apparatus Membrane Polymorphism Reference proteome Repeat Signal Transmembrane Transmembrane helix S I I T V I R Q V D L P MLPGRLCWVPLLLALGVGSGSGGGGDSRQRRLLAAKVNKHKPWIETSYHGVITENNDTVI LDPPLVALDKDAPVPFAGEICAFKIHGQELPFEAVVLNKTSGEGRLRAKSPIDCELQKEY TFIIQAYDCGAGPHETAWKKSHKAVVHIQVKDVNEFAPTFKEPAYKAVVTEGKIYDSILQ VEAIDEDCSPQYSQICNYEIVTTDVPFAIDRNGNIRNTEKLSYDKQHQYEILVTAYDCGQ KPAAQDTLVQVDVKPVCKPGWQDWTKRIEYQPGSGSMPLFPSIHLETCDGAVSSLQIVTE LQTNYIGKGCDRETYSEKSLQKLCGASSGIIDLLPSPSAATNWTAGLLVDSSEMIFKFDG RQGAKVPDGIVPKNLTDQFTITMWMKHGPSPGVRAEKETILCNSDKTEMNRHHYALYVHN CRLVFLLRKDFDQADTFRPAEFHWKLDQICDKEWHYYVINVEFPVVTLYMDGATYEPYLV TNDWPIHPSHIAMQLTVGACWQGGEVTKPQFAQFFHGSLASLTIRPGKMESQKVISCLQA CKEGLDINSLESLGQGIKYHFNPSQSILVMEGDDIGNINRALQKVSYINSRQFPTAGVRR LKVSSKVQCFGEDVCISIPEVDAYVMVLQAIEPRITLRGTDHFWRPAAQFESARGVTLFP DIKIVSTFAKTEAPGDVKTTDPKSEVLEEMLHNLDFCDILVIGGDLDPRQECLELNHSEL HQRHLDATNSTAGYSIYGVGSMSRYEQVLHHIRYRNWRPASLEARRFRIKCSELNGRYTS NEFNLEVSILHEDQVSDKEHVNHLIVQPPFLQSVHHPESRSSIQHSSVVPSIATVVIIIS VCMLVFVVAMGVYRVRIAHQHFIQETEAAKESEMDWDDSALTITVNPMEKHEGPGHGEDE TEGEEEEEAEEEMSSSSGSDDSEEEEEEEGMGRGRHGQNGARQAQLEWDDSTLPY O43520 Q9BTP8 AT8B1_HUMAN Phospholipid-transporting ATPase IC 7.6.2.1 ATPase class I type 8B member 1 Familial intrahepatic cholestasis type 1 P4-ATPase flippase complex alpha subunit ATP8B1 ATP8B1 ATPIC FIC1 PFIC Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis. NUCLEOTIDE SEQUENCE [MRNA] VARIANTS PFIC1 SER-288; VAL-308; 645-ILE--ILE-699 DEL AND ARG-892 VARIANTS BRIC1 THR-661 AND 795-GLY--ARG-797 DEL VARIANT THR-1152 Intestine Liver DNA sequence and analysis of human chromosome 18. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Multiple members of a third subfamily of P-type ATPases identified by genomic sequences and ESTs. NUCLEOTIDE SEQUENCE [MRNA] OF 388-661 Colon tumor The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-1251 VARIANT THR-1152 Uterus ATP8B1 requires an accessory protein for endoplasmic reticulum exit and plasma membrane lipid flippase activity. FUNCTION SUBUNIT SUBCELLULAR LOCATION CDC50A plays a key role in the uptake of the anticancer drug perifosine in human carcinoma cells. FUNCTION A flippase-independent function of ATP8B1, the protein affected in familial intrahepatic cholestasis type 1, is required for apical protein expression and microvillus formation in polarized epithelial cells. FUNCTION SUBCELLULAR LOCATION Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases. INTERACTION WITH TMEM30A AND TMEM30B SUBCELLULAR LOCATION CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery. INTERACTION WITH TMEM30A AND TMEM30B SUBCELLULAR LOCATION ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent manner. INTERACTION WITH TMEM30A AND TMEM30B SUBCELLULAR LOCATION Recurrent familial intrahepatic cholestasis in the Faeroe Islands. Phenotypic heterogeneity but genetic homogeneity. VARIANT BRIC1 THR-661 A missense mutation in FIC1 is associated with Greenland familial cholestasis. VARIANT PFIC1 ASN-554 Characterization of mutations in ATP8B1 associated with hereditary cholestasis. VARIANTS PFIC1 PRO-127; TYR-403; PRO-412; MET-456; HIS-500; PHE-529 DEL; LEU-535; ASN-554; THR-661; GLY-688; ARG-733; SER-853; ARG-892 AND ARG-1040 VARIANTS BRIC1 ASN-70; ASP-308; PHE-344; TYR-453; GLY-454; TRP-600; GLN-600; TRP-628; THR-661; THR-694 AND ARG-892 VARIANT ALA-429 Sequence variation in the ATP8B1 gene and intrahepatic cholestasis of pregnancy. VARIANTS ICP1 THR-45 AND GLU-203 VARIANT GLN-952 ATP8B1 mutations in British cases with intrahepatic cholestasis of pregnancy. VARIANT ICP1 CYS-867 VARIANTS ASN-70; ILE-305 AND GLN-952 The consensus coding sequences of human breast and colorectal cancers. VARIANTS [LARGE SCALE ANALYSIS] VAL-886 AND MET-1178 Differential effects of progressive familial intrahepatic cholestasis type 1 and benign recurrent intrahepatic cholestasis type 1 mutations on canalicular localization of ATP8B1. CHARACTERIZATION OF VARIANTS PFIC1 VAL-308; ASN-554; THR-661 AND ARG-1040 CHARACTERIZATION OF VARIANTS BRIC1 ASN-70 AND THR-661 CHARACTERIZATION OF VARIANT ICP1 CYS-867 MUTAGENESIS OF ASP-454 Characterization of ATP8B1 gene mutations and a hot-linked mutation found in Chinese children with progressive intrahepatic cholestasis and low GGT. VARIANT PFIC1 THR-209 Novel ATP8B1 mutation in an adult male with progressive familial intrahepatic cholestasis. VARIANT PFIC1 ILE-1012 Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May play a role in asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both. In cooperation with ABCB4 may be involved in establishing integrity of the canalicular membrane thus protecting hepatocytes from bile salts. Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine. Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity. Required for the preservation of cochlear hair cells in the inner ear. May act as cardiolipin transporter during inflammatory injury. ATP + H(2)O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2). Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit (Probable). The probable flippase ATP8B1:TMEM30A complex can form an intermediate phosphoenzyme in vitro. Also interacts with beta subunit TMEM30B. Q9NV96 TMEM30A false 3 Cell membrane Multi-pass membrane protein Apical cell membrane Cell projection Stereocilium Endoplasmic reticulum Golgi apparatus Exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B (PubMed:20947505). Localizes to apical membranes in epithelial cells (PubMed:20512993). Found in most tissues except brain and skeletal muscle. Most abundant in pancreas and small intestine. Cholestasis, progressive familial intrahepatic, 1 PFIC1 A disorder characterized by early onset of cholestasis that progresses to hepatic fibrosis, cirrhosis, and end-stage liver disease before adulthood. The disease is caused by mutations affecting the gene represented in this entry. Cholestasis, benign recurrent intrahepatic, 1 BRIC1 A disorder characterized by intermittent episodes of cholestasis without progression to liver failure. There is initial elevation of serum bile acids, followed by cholestatic jaundice which generally spontaneously resolves after periods of weeks to months. The cholestatic attacks vary in severity and duration. Patients are asymptomatic between episodes, both clinically and biochemically. The disease is caused by mutations affecting the gene represented in this entry. Cholestasis of pregnancy, intrahepatic 1 ICP1 A liver disorder of pregnancy. It presents during the second or, more commonly, the third trimester of pregnancy with intense pruritus which becomes more severe with advancing gestation and cholestasis. Cholestasis results from abnormal biliary transport from the liver into the small intestine. ICP1 causes fetal distress, spontaneous premature delivery and intrauterine death. ICP1 patients have spontaneous and progressive disappearance of cholestasis after delivery. The disease may be caused by mutations affecting the gene represented in this entry. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. ATP-binding Cell membrane Cell projection Complete proteome Disease mutation Endoplasmic reticulum Golgi apparatus Hearing Intrahepatic cholestasis Lipid transport Magnesium Membrane Metal-binding Nucleotide-binding Phosphoprotein Polymorphism Reference proteome Translocase Transmembrane Transmembrane helix Transport N T D N H Q L P K E P T L S F I G D G V I F R H I V S Y R P E A S Y D G T M Y H H L D N I V S N R Q R W R W I T M T D G I T G R K N F S R C A V G R R Q S I G R A T I M D A P L MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRK ECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAA NLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEV IKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFK MSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVI RNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLILLSAGLAIGHA YWEAQVGNSSWYLYDGEDDTPSYRGFLIFWGYIIVLNTMVPISLYVSVEVIRLGQSHFIN WDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHR DASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVD RTDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDR KRMSIIVRTPEGNIKLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKE IEEKEFTEWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISK LAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYA KFAPPVQESFFPPGGNRALIITGSWLNEILLEKKTKRNKILKLKFPRTEEERRMRTQSKR RLEAKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNM IKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFA FTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYTSLPVLLMGLLDQDVSDKLSLRFPGLYI VGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASAL VITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNAL RQPYIWLTIILAVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRR GVSTRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS Q4AC94 C9JR55 E2QRD1 Q2NLE1 Q3C1U9 Q6ZU92 Q8IYM4 Q8NB87 Q8NDH7 Q9Y4M2 C2CD3_HUMAN C2 domain-containing protein 3 C2CD3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of novel human genes predicted by combining multiple gene-finders. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT GLN-1219 Human chromosome 11 DNA sequence and analysis including novel gene identification. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-2352 (ISOFORM 1) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1067-2352 (ISOFORM 2) VARIANT GLN-1219 Brain Testis The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 716-2353 (ISOFORM 1) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1245-2353 (ISOFORM 4) VARIANT GLN-997 Eye The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1193-2353 (ISOFORM 3) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1999-2353 (ISOFORM 5) VARIANT GLN-1219 Testis Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2114 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Discovering regulators of centriole biogenesis through siRNA-based functional genomics in human cells. FUNCTION SUBCELLULAR LOCATION Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728; SER-1891; SER-2114 AND SER-2132 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia The oral-facial-digital syndrome gene C2CD3 encodes a positive regulator of centriole elongation. INVOLVEMENT IN OFD14 VARIANT OFD14 GLY-1029 FUNCTION SUBCELLULAR LOCATION INTERACTION WITH OFD1 Joubert Syndrome in French Canadians and Identification of Mutations in CEP104. VARIANT CYS-1743 Component of the centrioles that acts as a positive regulator of centriole elongation (PubMed:24997988). Promotes assembly of centriolar distal appendage, a structure at the distal end of the mother centriole that acts as an anchor of the cilium, and is required for recruitment of centriolar distal appendages proteins CEP83, SCLT1, CEP89, FBF1 and CEP164. Not required for centriolar satellite integrity or RAB8 activation. Required for primary cilium formation (PubMed:23769972). Required for sonic hedgehog/SHH signaling and for proteolytic processing of GLI3. Interacts with IFT88, BBS4 and PCM1 (By similarity). Interacts with OFD1; OFD1 may act as a negative regulator of C2CD3. Associates with the BBSome complex. O75665 OFD1 false 3 Cytoplasm Cytoskeleton Cilium basal body Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Centriole Localizes to centrioles and procentrioles both in interphase and mitosis. Localizes to centriolar satellites, localization is dependent on PCM1 and dynein-mediated retrograde transport. Also localizes to the distal ends of the mother and daughter centrioles. Q4AC94-5 5 Q4AC94-1 1 Q4AC94-2 2 No experimental confirmation available. Q4AC94-3 3 No experimental confirmation available. Q4AC94-4 4 No experimental confirmation available. Orofaciodigital syndrome 14 OFD14 A form of orofaciodigital syndrome, a group of heterogeneous disorders characterized by malformations of the oral cavity, face and digits, and associated phenotypic abnormalities that lead to the delineation of various subtypes. OFD14 patients show severe microcephaly, cerebral malformations the molar tooth sign, and intellectual disability in addition to canonical OFDS features. The disease is caused by mutations affecting the gene represented in this entry. Translation N-terminally extended. Translation N-terminally extended. Alternative splicing Cell projection Ciliopathy Cilium biogenesis/degradation Complete proteome Cytoplasm Cytoskeleton Disease mutation Mental retardation Phosphoprotein Polymorphism Reference proteome Repeat SILTSLRKNLSELDQIQRYFRQKLTKPF PEAWRRGDCLMWYRGSWRASGFGKKKT KNLSELDQIQRYFRQKLTKPFLPLSPQTQTAISQ SSPSLSYPSALRLKRPSHSTRRAVGTILGQVPAA DLQTITRD LPAPNDS DLQ GSY P R R Q C G R Q Y C S N G C G W R G I T M V V A T A H R P S Q R A E MKQRKGQGSGGSRGRKKRGLSDISPSTSLPPLVEGQLRCFLKLTVNRVIWKIAKPPTCVL VRVRWWGETSDGTLFCPRDALQTEPKAVRTTTRYAIRCGPKQFTSYLTDMAVLVLEVITK LDGLPIGRVQINGLAQLSPTHQINGFFTIVSSTSKKLGELQVSLALEPLSETYDSYHPLP TTDMTENVLLSKQGFRENTEPSSTQFQVPSRPRDIHTIKIDGKELAANSSRSTTPRGKDH VCFAENPDTIKDSSFGLQHSLNSGQSLESVTLKGRAPRKQMSLLNSSEFQPQIRTVAKSH SDSCILSSNNLPTKDLLSALLEQGNKLRNAMVISAMKSSPETSMLLDQVHPPINEDSLRA STQIRAFSRNRFKDHIEDHLLPSTENTFWRHDTKADTRAIQLLLGSAELSQGNFWDGLGS PPDSPSPGSDVYCISELNDPQYDQSLLENLFYTAPKSDTSISDFLSEEDDIVPSKKISQS TALARSSKVLESSDHKLKKRSAGKRNRNLVEQQMLSETPEDAQTMTLSVDRLALLGRTHS VRIIIETMGVPPDSPQMTPGKKSYAGPPPKVTTAKKRTFFVEYHFPVGFSESGLGKTALI TEVVRLASSKITDGKVKFQQRFVFPVQFGGPMIEHWWNSNLTFQIYVKKTPQKKPEVIGS VSLSLRAVIQSELLSFSDQLPVQQENGQSPFGPLKVTMELITDNKDFTGINTKLSGNTHY TPLCAPTSPNKALPELNQDMTCTKNPQNLNQIHEETAKKAQNLVLPNRKSPSPVAPHPST FVATPASHNLVNQTNGTTKESALLLHVLLMVPDGKDFISGESEKQSPCNVYLNCKLFSTE EVTRSVIAWGTTQPVFNFSQVIPVSLSSKYLERLKNNVMVIETWNKVRSPGQDKLLGLVK LPLHQFYMSFKDAKISRLLLDAQYPVVAVDSYMPVIDVFSGHQNGSLRVFLAMGSSNQIM ALQRLKNEEGTLPPFSPRPAHFLDQPTAASVAMAEDRGNGLMEHCFEIHIEMVKGLAPLQ ATVWGEADCYVQYYFPVQHSQSSVLKGPEFLENGITLKPFRTATTLCVPDPIFNSEHHHS LLLPAEVPVQRLLLSAFSAQGLVPGGGVQFEIWCRYYYPNVRDQKVAKGTLPLSRICAMV TTQHREDVGIQTFNLPLTPRIENRKELRNQSSGLLDVGLRYRRSPRTAEGVLAARTVSIS VQIIRACGLQAAAKALAEREPALQFSATVGVNASVTTHLSFLPQGEQRRTHPVACSFCPE FSHHVEFTCNLVTQHCSGEACFLAELLEFAEVIFAVYHENTKSASDIISIESCKEYLLGV VKVPTKELLIKRSGITGWYPIILPEDGGLPHGLELMQKIVGGLELSISFTHRGDRERVLE AAEHLGWSFENSLKDFVRMDEGEPATVTISTPRLWLPIHCVLLAGHNHIHKNTYCYLRYK FYDHEAFWTPLKKPKESVNKKQIMVTFKASKRAEVTRGPSLLWYFREERLEIQVWRAYGN DSVERPHQTDSWIGSAYVDLARLGERSARTLTVSGVYPLFGRNASNLSGAALRVHVVLSS LSSHLEPTHELDSMDCSSHSESEQLPRRNDEVQLSPPEVISCHQKSPASTQVPCSSTTAE VRLTQEGPADLDGTFAVSILVERAMHLSLKGSPLTERKVSIPSCCVSFATADESSPVYTQ VVENTDSPIWNFQQQSRLSKELLLDPQQTLVFKVWHKGDEERVIGFASVDLSPLLSGFQF VCGWYNITDFSGECQGQIKVAVSPLESLIHFKEERQARRGVETSKSLIPIYSPFSFPASD TYAAFSSHMARQTLDQLAHASSKELDFSSPGRSDTTRSQASRHEEHVQNIRRFHESLHLQ GEAPLPCDDKLTTSPLSSQTSILTSLRKNLSELDQIQRYFRQKLTKPFLPLSPQTQTAIS QHQESCRDHLGPGASSLDPGSQCILEKSSNLVLQVSSLITDLQTITRDSQAALSSHRARS RSNKATTLPDAQDTEALQERCTMPDEPLVRAPDKGTDSPSPPPLEETSNGGRMLHESLRH AVPITRMQSSEDTEAGPAYSDEDYEEDIIEPRTLNEITTVTDKTSPWSSVISDTSEVISP QPDEVQREGPSCPSPGPFCREELMVKSSFLSSPERAVNPHLPRQGSPSQSLVACECEASK ARVGGESASANPQPIPCPTLSGAQQSSTFVGWSSPQTDQNKEPKSEAPAENEAATSELGD SADSFKKLPLNLASQSRRENHKGPPIDSSDIRQRQVTTGSETSTKQSLLLPGPIVVPNFF LPPQQLEASLRMLSLSATLPPAATTDQDKSEATRGALSQRPCRPRPNSLPLNLPEEETLR IARIFSSQYSQKD Q14CW9 Q8IY68 Q96N40 Q9NPU5 AT7L3_HUMAN Ataxin-7-like protein 3 SAGA-associated factor 11 homolog ATXN7L3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-347 (ISOFORM 2) Lymph Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-347 (ISOFORM 1) Teratocarcinoma The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-347 Amygdala A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing. FUNCTION IDENTIFICATION BY MASS SPECTROMETRY IDENTIFICATION IN THE SAGA COMPLEX INTERACTION WITH ENY2 AND USP22 DOMAIN Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-281 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-326 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements. FUNCTION IDENTIFICATION IN THE SAGA COMPLEX System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-131 AND SER-281 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-281 AND SER-326 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Cytoplasmic ATXN7L3B interferes with nuclear functions of the SAGA deubiquitinase module. FUNCTION IDENTIFICATION IN THE SAGA COMPLEX INTERACTION WITH ENY2 AND USP22 SUBCELLULAR LOCATION The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties. STRUCTURE BY NMR OF 197-276 IN COMPLEX WITH ZINC Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates both histones H2A and H2B (PubMed:18206972, PubMed:21746879). The SAGA complex is recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Within the complex, it is required to recruit USP22 and ENY2 into the SAGA complex (PubMed:18206972). Regulates H2B monoubiquitination (H2Bub1) levels. Affects subcellular distribution of ENY2, USP22 and ATXN7L3B (PubMed:27601583). Component of some SAGA transcription coactivator-HAT complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H, TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3, and USP22 form an additional subcomplex of SAGA called the DUB module (deubiquitination module) (PubMed:18206972, PubMed:21746879, PubMed:27601583). Interacts directly with ENY2 and USP22 (PubMed:18206972). Nucleus Q14CW9-1 1 Q14CW9-2 2 The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module. The C-terminal SGF11-type zinc-finger domain together with the C-terminal catalytic domain of USP22 forms the 'catalytic lobe' of the SAGA deubiquitination module. Belongs to the SGF11 family. 3D-structure Activator Alternative splicing Chromatin regulator Complete proteome Metal-binding Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation Zinc Zinc-finger K KLWYLPFQ MKMEEMSLSGLDNSKLEAIAQEIYADLVEDSCLGFCFEVHRAVKCGYFFLDDTDPDSMKD FEIVDQPGLDIFGQVFNQWKSKECVCPNCSRSIAASRFAPHLEKCLGMGRNSSRIANRRI ANSNNMNKSESDQEDNDDINDNDWSYGSEKKAKKRKSDKNPNSPRRSKSLKHKNGELSNS DPFKYNNSTGISYETLGPEELRSLLTTQCGVISEHTKKMCTRSLRCPQHTDEQRRTVRIY FLGPSAVLPEVESSLDNDSFDMTDSQALISRLQWDGSSDLSPSDSGSSKTSENQGWGLGT NSSESRKTKKKKSHLSLVGTASGLGSNKKKKPKPPAPPTPSIYDDIN Q17RA5 CMAS1_HUMAN Putative uncharacterized protein C21orf62-AS1 C21orf62 antisense RNA 1 C21orf62 antisense gene protein 1 C21orf62-AS1 C21orf49 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence of human chromosome 21. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Product of a dubious CDS prediction. Complete proteome Reference proteome MHHVRQLMMPICPMALNSTTSSSTTFGAFRIMTLNVEEWATAWKVLILLEAAVEEEKRSE EKRILVCGTCGTRSSQKNL P0C2W7 A6NM97 CT47B_HUMAN Cancer/testis antigen 47B Cancer/testis antigen 47.13 CT47.13 CT47B1 CT47.13 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence of the human X chromosome. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Identification of a new cancer/testis gene family, CT47, among expressed multicopy genes on the human X chromosome. IDENTIFICATION Analysis of the chromosome X exome in patients with autism spectrum disorders identified novel candidate genes, including TMLHE. VARIANT GLU-99 DEL Coiled coil Complete proteome Polymorphism Reference proteome MSATGDRHPTQGDQEAPVSQEGAQAEAAGAGNQEGGDSGPDSSDMVPAAEVVGVAGPVEG LGEEEGEQAAGLAAVPQGGSAEEDSDIGPATEEEEEEEEGNEAANFDLAVATRRYPAAGI GFVFLYLVHSLLRRLYHNDHIQIANRHLSRLMVGPHAAVPNLWDNPPLLLLSQRLGAGAA APEGEGLGLIQEAASVQEAASVPEPAVPADLAEMAREPAEEAADEKPPEEAAEEKLTEEA TEEPAAEEPTSEEAVAPEEVTKSQPEKWDEEAQDAAGEEEKEQEKEKDVENKVKNSKGT Q96PC3 B4DQZ1 Q8WTY1 Q96DD1 AP1S3_HUMAN AP-1 complex subunit sigma-3 Adaptor protein complex AP-1 subunit sigma-1C Adaptor-related protein complex 1 subunit sigma-1C Clathrin assembly protein complex 1 sigma-1C small chain Golgi adaptor HA1/AP1 adaptin sigma-1C subunit Sigma 1C subunit of AP-1 clathrin Sigma-adaptin 1C Sigma1C-adaptin AP1S3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Adaptins: the final recount. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4) Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) Brain Lymph AP1S3 mutations are associated with pustular psoriasis and impaired Toll-like receptor 3 trafficking. FUNCTION INVOLVEMENT IN PSORS15 VARIANTS PSORS15 CYS-4 AND TRP-33 CHARACTERIZATION OF VARIANTS PSORS15 CYS-4 AND TRP-33 VARIANTS LYS-17; ALA-22; ILE-32; VAL-79; THR-83 AND GLU-124 Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Involved in TLR3 trafficking (PubMed:24791904). Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Q6PD74 AAGAB false 3 Golgi apparatus Cytoplasmic vesicle membrane Peripheral membrane protein Cytoplasmic side Membrane Clathrin-coated pit Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. Q96PC3-1 1 Q96PC3-2 2 May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Q96PC3-4 4 No experimental confirmation available. Q96PC3-3 3 May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Widely expressed. Psoriasis 15, pustular PSORS15 A form of pustular psoriasis, a life-threatening disease defined by repeated flares of sudden onset consisting of diffuse erythematous skin eruption characterized by rapid coverage with pustules, high-grade fever, asthenia, marked leukocytosis, and elevated serum levels of C-reactive protein. Disease susceptibility is associated with variations affecting the gene represented in this entry. Belongs to the adaptor complexes small subunit family. 3D-structure Alternative splicing Coated pit Complete proteome Cytoplasmic vesicle Disease mutation Golgi apparatus Membrane Polymorphism Protein transport Reference proteome Transport VCELDII TWPFARA VSTVSQTMGER NRLSPRGRDCSEPRSCHCTLA VSTVSQTMGER TMEEYMNKPTF F C Q K T A T I R W L V I T Q E MIHFILLFSRQGKLRLQKWYITLPDKERKKITREIVQIILSRGHRTSSFVDWKELKLVYK RYASLYFCCAIENQDNELLTLEIVHRYVELLDKYFGNVCELDIIFNFEKAYFILDEFIIG GEIQETSKKIAVKAIEDSDMLQEVSTVSQTMGER P04745 A6NJS5 A8K8H6 Q13763 Q5T083 AMY1_HUMAN Alpha-amylase 1 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase 1 Salivary alpha-amylase AMY1A AMY1 AMY1B AMY1 AMY1C AMY1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Primary structure of human salivary alpha-amylase gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases. NUCLEOTIDE SEQUENCE [GENOMIC DNA] ERRATUM SEQUENCE REVISION Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Thyroid Concerted evolution of human amylase genes. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56 AND 408-448 Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-293 AND 450-511 Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase. GLYCOSYLATION AT ASN-427 DEAMIDATION AT ASN-365; ASN-427 AND ASN-474 Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-427 Saliva Structure of human salivary alpha-amylase at 1.6-A resolution: implications for its role in the oral cavity. X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 17-511 IN COMPLEX WITH CALCIUM AND CHLORIDE DISULFIDE BONDS COFACTOR Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 16-511 OF WILD-TYPE AND MUTANT 321-GLY--ALA-325 DEL IN COMPLEX WITH CALCIUM AND CHLORIDE CATALYTIC ACTIVITY DISULFIDE BONDS Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Ca(2+) Binds 1 Ca(2+) ion per subunit. chloride Binds 1 Cl(-) ion per subunit. Monomer. Q8TAX7 MUC7 false 2 Secreted Belongs to the glycosyl hydrolase 13 family. Amylase entry 3D-structure Calcium Carbohydrate metabolism Chloride Complete proteome Disulfide bond Glycoprotein Glycosidase Hydrolase Metal-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal N T MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP NENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGL LDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEG SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG FMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP RYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQP FTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGI KIYVSDDGKAHFSISNSAEDPFIAIHAESKL Q5CZ79 A6NC18 AN20B_HUMAN Ankyrin repeat domain-containing protein 20B Ankyrin repeat domain-containing protein 20A pseudogene ANKRD20A8P ANKRD20B Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Testis Q5CZ79-1 1 Q5CZ79-2 2 No experimental confirmation available. Translation N-terminally shortened. Alternative splicing ANK repeat Coiled coil Complete proteome Reference proteome Repeat FPKKLKEEHDK MNFKINVFICR G C MKLFGFGSRRGQTAEGSIDHVYTGSGYRIRDSELQKIHRAAVKGDAAEVERCLARRSGDL DARDKQHRTALHLACASGHVQVVTLLVNRKCQIDICDKENRTPLIQAVHCQEEACAVILL KHGANPNLKDIYGNTALHYAVYSESTSLAEKLLSHGAHIEALDKDSNTPLLFAIICKKEK MVEFLLKKKASTHAVDRLRRSALMLAVYYDSPGIVSILLKQNIDVFAQDMCGRDAEDYAI SHHLTKIQQQILEHKQKILKKEKSDVGSSDESAVSIFHELRVDSLPASDDKDLSVATKQC VPEKVSEPLPGPSHEKGNRIVNGQGEGPPAKHPSLKPTTGVEDPAVKGAVQRKNVQTLRA EQALPVASEEEQERHERSEKKQPQVKKGNNTNKSEKIQLSENICDSTSSAAAGRLTQQRK IGKTYPQQFPKKLKEEHDKCTLKQENEEKTNVNMLYKKNREELERKEKQYKKEVEAKQLE PTVQSLEMKSKTARNTPNRDFHNHEETKGLMDENCILKADIAILRQEICTMKNDNLEKEN KYLKDIKIVKETNAALEKYIKLNEEMITETAFRYQQELNDLKAENTRLNAELLKEKESKK RLEADIESYQSRLAAAIGKHSESVKTERNVKLALERTQDVSVQVEMSSAISKVKDENEFL TEQLSETQIKFNALKDKFRKTRDSLRKKSLALETVQNDLRKTQQQTQEMKEMYQNAEAKV NNSTGKWNCVEERICHLQRENAWLVQQLDDVHQKEDHKEIVTNIQRGFIESGKKDLVLEE KSKKLMNECDHLKESLFQYEREKAEGVVSIKEDKYFQTSRKKI Q09666 A1A586 AHNK_HUMAN Neuroblast differentiation-associated protein AHNAK Desmoyokin AHNAK PM227 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Human chromosome 11 DNA sequence and analysis including novel gene identification. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) A human gene (AHNAK) encoding an unusually large protein with a 1.2-microns polyionic rod structure. NUCLEOTIDE SEQUENCE [MRNA] OF 114-1930 (ISOFORM 1) NUCLEOTIDE SEQUENCE [MRNA] OF 4614-5890 (ISOFORM 1) Placenta ERRATUM Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-93; THR-490; SER-511; THR-4100; THR-4766; SER-5077; SER-5110; SER-5448; SER-5552 AND SER-5752 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-511; SER-5731 AND SER-5763 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration. INTERACTION WITH DYSF Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-490; SER-511; SER-4986; SER-5099; SER-5110 AND SER-5552 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5749 AND SER-5752 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] T-cell Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-511 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-93; SER-511; SER-570; SER-793; SER-4903; SER-4960; SER-4993; THR-5009; SER-5099; THR-5415; SER-5731; SER-5749; SER-5752; SER-5763; SER-5780; SER-5782; SER-5793; THR-5794; SER-5830 AND SER-5841 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Large-scale proteomics analysis of the human kinome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511 AND SER-5752 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511; SER-570; SER-2397; SER-5448; SER-5731; SER-5749; SER-5752 AND SER-5763 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-93; THR-101; SER-135; SER-177; SER-210; SER-212; SER-216; THR-490; SER-511; SER-559; SER-570; SER-793; SER-1068; THR-1192; SER-1286; THR-1986; THR-2181; THR-2309; SER-2397; SER-2670; SER-2798; THR-2832; THR-2845; SER-3054; SER-3182; SER-3409; SER-3412; SER-3426; THR-3716; SER-3836; SER-3964; SER-4092; THR-4100; SER-4220; THR-4430; SER-4516; SER-4684; SER-4812; SER-4960; SER-4986; SER-5077; SER-5099; SER-5110; SER-5125; SER-5332; SER-5386; SER-5400; SER-5448; SER-5552; SER-5620; SER-5731; SER-5739; SER-5752; SER-5763; SER-5780; SER-5782; SER-5790; THR-5824; SER-5830; SER-5841 AND SER-5857 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-135; SER-177; THR-490; SER-511; SER-559; SER-5731 AND SER-5841 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-93; SER-135; THR-158; SER-177; SER-210; SER-212; SER-216; SER-220; SER-332; SER-337; SER-379; THR-490; SER-511; THR-551; THR-553; SER-570; SER-572; SER-658; SER-793; SER-819; SER-1068; SER-1196; SER-1286; SER-1298; SER-1654; SER-1856; SER-1923; SER-1990; SER-2092; SER-2118; SER-2287; SER-2397; SER-2580; SER-2670; SER-2798; THR-2845; SER-3054; SER-3182; SER-3362; SER-3412; SER-3426; THR-3716; SER-3836; SER-3964; SER-4002; SER-4092; THR-4100; SER-4220; SER-4258; SER-4360; THR-4430; SER-4460; SER-4520; THR-4564; SER-4684; THR-4766; SER-4812; SER-4900; SER-4908; SER-4953; SER-4986; SER-5099; SER-5110; SER-5318; SER-5332; SER-5369; SER-5393; SER-5400; SER-5448; SER-5519; SER-5530; SER-5552; SER-5620; SER-5641; SER-5731; SER-5739; SER-5749; SER-5752; SER-5762; SER-5763; THR-5824; SER-5830; SER-5841; THR-5845 AND SER-5857 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-115; SER-135; SER-210; SER-212; THR-218; SER-256; SER-337; SER-379; SER-470; THR-490; SER-511; SER-570; SER-1010; SER-1042; SER-1068; SER-1170; SER-1580; SER-2138; SER-2600; SER-2708; SER-2728; SER-3092; SER-3220; SER-3412; SER-3544; SER-3746; SER-3766; SER-3874; SER-4022; THR-4100; SER-4150; SER-4278; SER-4406; SER-4425; SER-4480; SER-4486; THR-4564; SER-4722; SER-4960; SER-5099; SER-5110; SER-5261; SER-5400; SER-5448; SER-5577; SER-5620; SER-5641; SER-5731; SER-5739; SER-5749; SER-5752; SER-5780; SER-5782; SER-5830; SER-5841; SER-5851; SER-5857 AND SER-5863 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. METHYLATION [LARGE SCALE ANALYSIS] AT ARG-270; LYS-1208; LYS-1666; LYS-1868; LYS-1935; LYS-2002 AND LYS-2130 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Colon carcinoma Uncovering global SUMOylation signaling networks in a site-specific manner. SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-134 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-134; LYS-942; LYS-961; LYS-2132; LYS-2575; LYS-2594; LYS-2703; LYS-2722; LYS-2959; LYS-3087; LYS-3215; LYS-3667; LYS-3760; LYS-3869; LYS-3997; LYS-4016; LYS-4253; LYS-4272; LYS-4381; LYS-4400; LYS-4455 AND LYS-4474 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-712 AND LYS-961 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-181; LYS-712; LYS-763; LYS-891; LYS-1726; LYS-2062; LYS-2524; LYS-2908 AND LYS-5623 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] May be required for neuronal cell differentiation. Interacts with DYSF; the interaction is direct and Ca(2+)-independent. P00533 EGFR false 3 Q5SY16 NOL9 false 3 P60903 S100A10 false 2 Nucleus Q09666-1 1 Q09666-2 2 Translation N-terminally extended. 3D-structure Acetylation Alternative splicing Complete proteome Isopeptide bond Methylation Nucleus Phosphoprotein Polymorphism Reference proteome Repeat Ubl conjugation SGDDEEYQRIYTTKIKPRLKSEDGVEGDLGETQSR NTPQPSALECKDQNKQKEASSQAGAVSVSTPNAGL G V A T K T P L Q K V I S P D G G D M V I V D G T A A P G A V D P R F L S T V A RD KG DV NT Q H A P G V F V A P P S MEKEETTRELLLPNWQGSGSHGLTIAQRDDGVFVQEVTQNSPAARTGVVKEGDQIVGATI YFDNLQSGEVTQLLNTMGHHTVGLKLHRKGDRSPEPGQTWTREVFSSCSSEVVLSGDDEE YQRIYTTKIKPRLKSEDGVEGDLGETQSRTITVTRRVTAYTVDVTGREGAKDIDISSPEF KIKIPRHELTEISNVDVETQSGKTVIRLPSGSGAASPTGSAVDIRAGAISASGPELQGAG HSKLQVTMPGIKVGGSGVNVNAKGLDLGGRGGVQVPAVDISSSLGGRAVEVQGPSLESGD HGKIKFPTMKVPKFGVSTGREGQTPKAGLRVSAPEVSVGHKGGKPGLTIQAPQLEVSVPS ANIEGLEGKLKGPQITGPSLEGDLGLKGAKPQGHIGVDASAPQIGGSITGPSVEVQAPDI DVQGPGSKLNVPKMKVPKFSVSGAKGEETGIDVTLPTGEVTVPGVSGDVSLPEIATGGLE GKMKGTKVKTPEMIIQKPKISMQDVDLSLGSPKLKGDIKVSAPGVQGDVKGPQVALKGSR VDIETPNLEGTLTGPRLGSPSGKTGTCRISMSEVDLNVAAPKVKGGVDVTLPRVEGKVKV PEVDVRGPKVDVSAPDVEAHGPEWNLKMPKMKMPTFSTPGAKGEGPDVHMTLPKGDISIS GPKVNVEAPDVNLEGLGGKLKGPDVKLPDMSVKTPKISMPDVDLHVKGTKVKGEYDVTVP KLEGELKGPKVDIDAPDVDVHGPDWHLKMPKMKMPKFSVPGFKAEGPEVDVNLPKADVDI SGPKIDVTAPDVSIEEPEGKLKGPKFKMPEMNIKVPKISMPDVDLHLKGPNVKGEYDVTM PKVESEIKVPDVELKSAKMDIDVPDVEVQGPDWHLKMPKMKMPKFSMPGFKAEGPEVDVN LPKADVDISGPKVGVEVPDVNIEGPEGKLKGPKFKMPEMNIKAPKISMPDVDLHMKGPKV KGEYDMTVPKLEGDLKGPKVDVSAPDVEMQGPDWNLKMPKIKMPKFSMPSLKGEGPEFDV NLSKANVDISAPKVDTNAPDLSLEGPEGKLKGPKFKMPEMHFRAPKMSLPDVDLDLKGPK MKGNVDISAPKIEGEMQVPDVDIRGPKVDIKAPDVEGQGLDWSLKIPKMKMPKFSMPSLK GEGPEVDVNLPKADVVVSGPKVDIEAPDVSLEGPEGKLKGPKFKMPEMHFKTPKISMPDV DLHLKGPKVKGDVDVSVPKVEGEMKVPDVEIKGPKMDIDAPDVEVQGPDWHLKMPKMKMP KFSMPGFKGEGREVDVNLPKADIDVSGPKVDVEVPDVSLEGPEGKLKGPKFKMPEMHFKA PKISMPDVDLNLKGPKLKGDVDVSLPEVEGEMKVPDVDIKGPKVDISAPDVDVHGPDWHL KMPKVKMPKFSMPGFKGEGPEVDVKLPKADVDVSGPKMDAEVPDVNIEGPDAKLKGPKFK MPEMSIKPQKISIPDVGLHLKGPKMKGDYDVTVPKVEGEIKAPDVDIKGPKVDINAPDVE VHGPDWHLKMPKVKMPKFSMPGFKGEGPEVDMNLPKADLGVSGPKVDIDVPDVNLEAPEG KLKGPKFKMPSMNIQTHKISMPDVGLNLKAPKLKTDVDVSLPKVEGDLKGPEIDVKAPKM DVNVGDIDIEGPEGKLKGPKFKMPEMHFKAPKISMPDVDLHLKGPKVKGDMDVSVPKVEG EMKVPDVDIKGPKVDIDAPDVEVHDPDWHLKMPKMKMPKFSMPGFKAEGPEVDVNLPKAD IDVSGPSVDTDAPDLDIEGPEGKLKGSKFKMPKLNIKAPKVSMPDVDLNLKGPKLKGEID ASVPELEGDLRGPQVDVKGPFVEAEVPDVDLECPDAKLKGPKFKMPEMHFKAPKISMPDV DLHLKGPKVKGDADVSVPKLEGDLTGPSVGVEVPDVELECPDAKLKGPKFKMPDMHFKAP KISMPDVDLHLKGPKVKGDVDVSVPKLEGDLTGPSVGVEVPDVELECPDAKLKGPKFKMP EMHFKTPKISMPDVDLHLKGPKVKGDMDVSVPKVEGEMKVPDVDIKGPKMDIDAPDVDVH GPDWHLKMPKMKMPKFSMPGFKAEGPEVDVNLPKADVVVSGPKVDVEVPDVSLEGPEGKL KGPKLKMPEMHFKAPKISMPDVDLHLKGPKVKGDVDVSLPKLEGDLTGPSVDVEVPDVEL ECPDAKLKGPKFKMPEMHFKTPKISMPDVNLNLKGPKVKGDMDVSVPKVEGEMKVPDVDI RGPKVDIDAPDVDVHGPDWHLKMPKMKMPKFSMPGFKGEGPEVDVNLPKADVDVSGPKVD VEVPDVSLEGPEGKLKGPKFKMPEMHFKTPKISMPDVDFNLKGPKIKGDVDVSAPKLEGE LKGPELDVKGPKLDADMPEVAVEGPNGKWKTPKFKMPDMHFKAPKISMPDLDLHLKSPKA KGEVDVDVPKLEGDLKGPHVDVSGPDIDIEGPEGKLKGPKFKMPDMHFKAPNISMPDVDL NLKGPKIKGDVDVSVPEVEGKLEVPDMNIRGPKVDVNAPDVQAPDWHLKMPKMKMPKFSM PGFKAEGPEVDVNLPKADVDISGPKVDIEGPDVNIEGPEGKLKGPKLKMPEMNIKAPKIS MPDFDLHLKGPKVKGDVDVSLPKVEGDLKGPEVDIKGPKVDINAPDVGVQGPDWHLKMPK VKMPKFSMPGFKGEGPDGDVKLPKADIDVSGPKVDIEGPDVNIEGPEGKLKGPKFKMPEM NIKAPKISMPDIDLNLKGPKVKGDVDVSLPKVEGDLKGPEVDIKGPKVDIDAPDVDVHGP DWHLKMPKIKMPKISMPGFKGEGPDVDVNLPKADIDVSGPKVDVECPDVNIEGPEGKWKS PKFKMPEMHFKTPKISMPDIDLNLTGPKIKGDVDVTGPKVEGDLKGPEVDLKGPKVDIDV PDVNVQGPDWHLKMPKMKMPKFSMPGFKAEGPEVDVNLPKADVDVSGPKVDVEGPDVNIE GPEGKLKGPKFKMPEMNIKAPKIPMPDFDLHLKGPKVKGDVDISLPKVEGDLKGPEVDIR GPQVDIDVPDVGVQGPDWHLKMPKVKMPKFSMPGFKGEGPDVDVNLPKADLDVSGPKVDI DVPDVNIEGPEGKLKGPKFKMPEMNIKAPKISMPDIDLNLKGPKVKGDMDVSLPKVEGDM KVPDVDIKGPKVDINAPDVDVQGPDWHLKMPKIKMPKISMPGFKGEGPEVDVNLPKADLD VSGPKVDVDVPDVNIEGPDAKLKGPKFKMPEMNIKAPKISMPDLDLNLKGPKMKGEVDVS LANVEGDLKGPALDIKGPKIDVDAPDIDIHGPDAKLKGPKLKMPDMHVNMPKISMPEIDL NLKGSKLKGDVDVSGPKLEGDIKAPSLDIKGPEVDVSGPKLNIEGKSKKSRFKLPKFNFS GSKVQTPEVDVKGKKPDIDITGPKVDINAPDVEVQGKVKGSKFKMPFLSISSPKVSMPDV ELNLKSPKVKGDLDIAGPNLEGDFKGPKVDIKAPEVNLNAPDVDVHGPDWNLKMPKMKMP KFSVSGLKAEGPDVAVDLPKGDINIEGPSMNIEGPDLNVEGPEGGLKGPKFKMPDMNIKA PKISMPDIDLNLKGPKVKGDVDISLPKLEGDLKGPEVDIKGPKVDINAPDVDVHGPDWHL KMPKVKMPKFSMPGFKGEGPEVDVTLPKADIDISGPNVDVDVPDVNIEGPDAKLKGPKFK MPEMNIKAPKISMPDFDLNLKGPKMKGDVVVSLPKVEGDLKGPEVDIKGPKVDIDTPDIN IEGSEGKFKGPKFKIPEMHLKAPKISMPDIDLNLKGPKVKGDVDVSLPKMEGDLKGPEVD IKGPKVDINAPDVDVQGPDWHLKMPKVKMPKFSMPGFKGEGPDVDVNLPKADLDVSGPKV DIDVPDVNIEGPEGKLKGPKFKMPEMNIKAPKISMPDIDLNLKGPKVKGDMDVSLPKVEG DMQVPDLDIKGPKVDINAPDVDVRGPDWHLKMPKIKMPKISMPGFKGEGPEVDVNLPKAD LDVSGPKVDVDVPDVNIEGPDAKLKGPKFKMPEMNIKAPKISMPDFDLHLKGPKVKGDVD VSLPKMEGDLKAPEVDIKGPKVDIDAPDVDVHGPDWHLKMPKVKMPKFSMPGFKGEGPEV DVNLPKADIDVSGPKVDIDTPDIDIHGPEGKLKGPKFKMPDLHLKAPKISMPEVDLNLKG PKMKGDVDVSLPKVEGDLKGPEVDIKGPKVDIDVPDVDVQGPDWHLKMPKVKMPKFSMPG FKGEGPDVDVNLPKADLDVSGPKVDIDVPDVNIEGPDAKLKGPKFKMPEMNIKAPKISMP DFDLHLKGPKVKGDVDVSLPKVEGDLKGPEVDIKGPKVDIDAPDVDVHGPDWHLKMPKVK MPKFSMPGFKGEGPDVDVTLPKADIEISGPKVDIDAPDVSIEGPDAKLKGPKFKMPEMNI KAPKISMPDIDFNLKGPKVKGDVDVSLPKVEGDLKGPEIDIKGPSLDIDTPDVNIEGPEG KLKGPKFKMPEMNIKAPKISMPDFDLHLKGPKVKGDVDVSLPKVESDLKGPEVDIEGPEG KLKGPKFKMPDVHFKSPQISMSDIDLNLKGPKIKGDMDISVPKLEGDLKGPKVDVKGPKV GIDTPDIDIHGPEGKLKGPKFKMPDLHLKAPKISMPEVDLNLKGPKVKGDMDISLPKVEG DLKGPEVDIRDPKVDIDVPDVDVQGPDWHLKMPKVKMPKFSMPGFKGEGPDVDVNLPKAD IDVSGPKVDVDVPDVNIEGPDAKLKGPKFKMPEMSIKAPKISMPDIDLNLKGPKVKGDVD VTLPKVEGDLKGPEADIKGPKVDINTPDVDVHGPDWHLKMPKVKMPKFSMPGFKGEGPDV DVSLPKADIDVSGPKVDVDIPDVNIEGPDAKLKGPKFKMPEINIKAPKISIPDVDLDLKG PKVKGDFDVSVPKVEGTLKGPEVDLKGPRLDFEGPDAKLSGPSLKMPSLEISAPKVTAPD VDLHLKAPKIGFSGPKLEGGEVDLKGPKVEAPSLDVHMDSPDINIEGPDVKIPKFKKPKF GFGAKSPKADIKSPSLDVTVPEAELNLETPEISVGGKGKKSKFKMPKIHMSGPKIKAKKQ GFDLNVPGGEIDASLKAPDVDVNIAGPDAALKVDVKSPKTKKTMFGKMYFPDVEFDIKSP KFKAEAPLPSPKLEGELQAPDLELSLPAIHVEGLDIKAKAPKVKMPDVDISVPKIEGDLK GPKVQANLGAPDINIEGLDAKVKTPSFGISAPQVSIPDVNVNLKGPKIKGDVPSVGLEGP DVDLQGPEAKIKFPKFSMPKIGIPGVKMEGGGAEVHAQLPSLEGDLRGPDVKLEGPDVSL KGPGVDLPSVNLSMPKVSGPDLDLNLKGPSLKGDLDASVPSMKVHAPGLNLSGVGGKMQV GGDGVKVPGIDATTKLNVGAPDVTLRGPSLQGDLAVSGDIKCPKVSVGAPDLSLEASEGS IKLPKMKLPQFGISTPGSDLHVNAKGPQVSGELKGPGVDVNLKGPRISAPNVDFNLEGPK VKGSLGATGEIKGPTVGGGLPGIGVQGLEGNLQMPGIKSSGCDVNLPGVNVKLPTGQISG PEIKGGLKGSEVGFHGAAPDISVKGPAFNMASPESDFGINLKGPKIKGGADVSGGVSAPD ISLGEGHLSVKGSGGEWKGPQVSSALNLDTSKFAGGLHFSGPKVEGGVKGGQIGLQAPGL SVSGPQGHLESGSGKVTFPKMKIPKFTFSGRELVGREMGVDVHFPKAEASIQAGAGDGEW EESEVKLKKSKIKMPKFNFSKPKGKGGVTGSPEASISGSKGDLKSSKASLGSLEGEAEAE ASSPKGKFSLFKSKKPRHRSNSFSDEREFSGPSTPTGTLEFEGGEVSLEGGKVKGKHGKL KFGTFGGLGSKSKGHYEVTGSDDETGKLQGSGVSLASKKSRLSSSSSNDSGNKVGIQLPE VELSVSTKKE Q96IK1 B4DXH8 Q9BTW1 BOD1_HUMAN Biorientation of chromosomes in cell division protein 1 Biorientation defective protein 1 Protein FAM44B BOD1 FAM44B Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Lung Muscle Bod1, a novel kinetochore protein required for chromosome biorientation. FUNCTION SUBCELLULAR LOCATION Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles. Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Chromosome Centromere Kinetochore Localizes at the centrosomes throughout the cell cycle, only dissociating during cytokinesis. Localizes at the kinetochore from prometaphase until anaphase. Q96IK1-1 1 Q96IK1-2 2 No experimental confirmation available. Belongs to the BOD1 family. Alternative splicing Cell cycle Cell division Centromere Chromosome Complete proteome Cytoplasm Cytoskeleton Kinetochore Mitosis Reference proteome SGMLEAGV IRQTPFES MADGGGGGGTGAVGGGGTSQASAGAATGATGASGGGGPINPASLPPGDPQLIALIVEQLK SRGLFDSFRRDCLADVDTKPAYQNLRQKVDNFVSTHLDKQEWNPTMNKNQLRNGLRQSVV QSGMLEAGVDRIISQVVDPKLNHIFRPQIERAIHEFLAAQKKAAVPAPPPEPEGQDPPAP SQDTS Q96DG6 D3DTC7 Q8TED6 CMBL_HUMAN Carboxymethylenebutenolidase homolog 3.1.-.- CMBL Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Full length sequencing of some human and murine muscular transcripts (Telethon Italy project B41). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Skeletal muscle Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Adipose tissue NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta PROTEIN SEQUENCE OF 2-31; 150-168; 206-217 AND 236-245 CLEAVAGE OF INITIATOR METHIONINE ACETYLATION AT ALA-2 IDENTIFICATION BY MASS SPECTROMETRY Cervix carcinoma Lysine acetylation targets protein complexes and co-regulates major cellular functions. ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Human carboxymethylenebutenolidase as a bioactivating hydrolase of olmesartan medoxomil in liver and intestine. FUNCTION TISSUE SPECIFICITY SUBCELLULAR LOCATION BIOPHYSICOCHEMICAL PROPERTIES MUTAGENESIS OF CYS-132 IDENTIFICATION BY MASS SPECTROMETRY Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Cysteine hydrolase. Can convert the prodrug olmesartan medoxomil into its pharmacologically active metabolite olmerstatan, an angiotensin receptor blocker, in liver and intestine. May also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. Strongly inhibited by p-chloromercuribenzoate (PCMB). Partially inhibited by bis-p-nitrophenylphosphate (BNPP). Not inhibited by DFP, PMSF, eserine or EDTA. 170 uM for olmesartan medoxomil 283 uM for faropenem medoxomil 63.4 uM for lenampicillin 24.6 nmol/min/mg enzyme toward olmesartan medoxomil 16.4 nmol/min/mg enzyme toward faropenem medoxomil 4 nmol/min/mg enzyme toward lenampicillin Cytoplasm Cytosol Widely expressed, with highest levels in liver, followed by kidney, small intestine and colon. Present in liver and intestine (at protein level). Belongs to the dienelactone hydrolase family. Acetylation Complete proteome Cytoplasm Direct protein sequencing Hydrolase Phosphoprotein Polymorphism Reference proteome Y C C A C S K N Q H MANEAYPCPCDIGHRLEYGGLGREVQVEHIKAYVTKSPVDAGKAVIVIQDIFGWQLPNTR YIADMISGNGYTTIVPDFFVGQEPWDPSGDWSIFPEWLKTRNAQKIDREISAILKYLKQQ CHAQKIGIVGFCWGGTAVHHLMMKYSEFRAGVSVYGIVKDSEDIYNLKNPTLFIFAENDV VIPLKDVSLLTQKLKEHCKVEYQIKTFSGQTHGFVHRKREDCSPADKPYIDEARRNLIEW LNKYM Q14CN2 A8MQC9 B7Z1Q5 Q6UX81 Q9UNF7 CLCA4_HUMAN Calcium-activated chloride channel regulator 4 3.4.-.- Calcium-activated chloride channel family member 4 hCLCA4 Calcium-activated chloride channel protein 2 CaCC-2 hCaCC-2 Chloride channel accessory 4 Calcium-activated chloride channel regulator 4, 110 kDa form Calcium-activated chloride channel regulator 4, 30 kDa form CLCA4 CaCC2 UNQ562/PRO1124 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of three novel members of the calcium-dependent chloride channel (CaCC) family predominantly expressed in the digestive tract and trachea. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANT 877-PRO-THR-878 DEL TISSUE SPECIFICITY Colon The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Cerebellum The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANTS LEU-810 AND 877-PRO-THR-878 DEL The CLCA gene locus as a modulator of the gastrointestinal basic defect in cystic fibrosis. TISSUE SPECIFICITY Expression and distribution of ion transport mRNAs in human nasal mucosa and nasal polyps. TISSUE SPECIFICITY Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-811 Saliva Transcriptomic dissection of tongue squamous cell carcinoma. INDUCTION May be involved in mediating calcium-activated chloride conductance. Cell membrane Single-pass membrane protein Apical cell membrane Secreted The C-terminus 30 kDa form is anchored to the membrane. The N-terminus 110 kDa form is released from the membrane triggered by an unknown stimulus. Q14CN2-1 1 Q14CN2-2 2 No experimental confirmation available. Primarily expressed in the digestive tract, mainly in colon. Detected in smaller amounts in brain, urogenital organs, testis, and salivary and mammary glands. Highly expressed in the epithelial layer and submucosal gland of the inferior turbinate mucosa. Lower levels in the epithelial layer of nasal polyp. Down-regulated in oral tongue squamous cell carcinomas. The metalloprotease region is responsible for autoproteolytic processing. It can also cross-cleave other CLCA substrates. The translation product is autoproteolytically cleaved by the metalloprotease domain in the endoplasmic reticulum into a N-terminal and a C-terminal products that remain physically associated with each other. The cleavage is necessary for calcium-activated chloride channel (CaCC) activation activity. Belongs to the CLCR family. Alternative splicing Autocatalytic cleavage Cell membrane Chloride Complete proteome Glycoprotein Hydrolase Membrane Metal-binding Metalloprotease Polymorphism Protease Reference proteome Secreted Signal Transmembrane Transmembrane helix Transport Zinc LESKGLTLNSNAWMNDTVIIDSTVGKDTFFLITWN VRVLIPWVFMFTFATRKNHLVVISFEFHIFLKVNF P S D V M L V L S R MGLFRGFVFLLVLCLLHQSNTSFIKLNNNGFEDIVIVIDPSVPEDEKIIEQIEDMVTTAS TYLFEATEKRFFFKNVSILIPENWKENPQYKRPKHENHKHADVIVAPPTLPGRDEPYTKQ FTECGEKGEYIHFTPDLLLGKKQNEYGPPGKLFVHEWAHLRWGVFDEYNEDQPFYRAKSK KIEATRCSAGISGRNRVYKCQGGSCLSRACRIDSTTKLYGKDCQFFPDKVQTEKASIMFM QSIDSVVEFCNEKTHNQEAPSLQNIKCNFRSTWEVISNSEDFKNTIPMVTPPPPPVFSLL KISQRIVCLVLDKSGSMGGKDRLNRMNQAAKHFLLQTVENGSWVGMVHFDSTATIVNKLI QIKSSDERNTLMAGLPTYPLGGTSICSGIKYAFQVIGELHSQLDGSEVLLLTDGEDNTAS SCIDEVKQSGAIVHFIALGRAADEAVIEMSKITGGSHFYVSDEAQNNGLIDAFGALTSGN TDLSQKSLQLESKGLTLNSNAWMNDTVIIDSTVGKDTFFLITWNSLPPSISLWDPSGTIM ENFTVDATSKMAYLSIPGTAKVGTWAYNLQAKANPETLTITVTSRAANSSVPPITVNAKM NKDVNSFPSPMIVYAEILQGYVPVLGANVTAFIESQNGHTEVLELLDNGAGADSFKNDGV YSRYFTAYTENGRYSLKVRAHGGANTARLKLRPPLNRAAYIPGWVVNGEIEANPPRPEID EDTQTTLEDFSRTASGGAFVVSQVPSLPLPDQYPPSQITDLDATVHEDKIILTWTAPGDN FDVGKVQRYIIRISASILDLRDSFDDALQVNTTDLSPKEANSKESFAFKPENISEENATH IFIAIKSIDKSNLTSKVSNIAQVTLFIPQANPDDIDPTPTPTPTPTPDKSHNSGVNISTL VLSVIGSVVIVNFILSTTI Q8NCG5 Q8IV46 Q9Y5R3 CHST4_HUMAN Carbohydrate sulfotransferase 4 2.8.2.- Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3 GST-3 High endothelial cells N-acetylglucosamine 6-O-sulfotransferase HEC-GlcNAc6ST L-selectin ligand sulfotransferase LSST N-acetylglucosamine 6-O-sulfotransferase 2 GlcNAc6ST-2 Gn6st-2 CHST4 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin. NUCLEOTIDE SEQUENCE [MRNA] FUNCTION TISSUE SPECIFICITY Tonsil Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase. NUCLEOTIDE SEQUENCE [MRNA] Chromosomal localization and genomic organization for the galactose/ N-acetylgalactosamine/N-acetylglucosamine 6-O-sulfotransferase gene family. NUCLEOTIDE SEQUENCE [MRNA] Tonsil Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Teratocarcinoma The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain CHST1 and CHST2 sulfotransferase expression by vascular endothelial cells regulates shear-resistant leukocyte rolling via L-selectin. TISSUE SPECIFICITY INDUCTION Ectopic expression of a GlcNAc 6-O-sulfotransferase, GlcNAc6ST-2, in colonic mucinous adenocarcinoma. TISSUE SPECIFICITY Specificities of N-acetylglucosamine-6-O-sulfotransferases in relation to L-selectin ligand synthesis and tumor-associated enzyme expression. SUBSTRATE SPECIFICITY Golgi localization of carbohydrate sulfotransferases is a determinant of L-selectin ligand biosynthesis. SUBCELLULAR LOCATION The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant of substrate specificity. SUBUNIT Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within mucin-associated glycans that ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X on receptors SPN/CD43, GLYCAM1 and MADCAM1. Also involved in biosynthesis of SELL ligand recognized by MECA-79 antibody. Plays a central role in lymphocyte trafficking during chronic inflammation. Has a catalytic preference for core 2-branched mucin-type O-glycans. Can use GlcNAcbeta1-6[Galbeta1-3]GalNAc-pNP (core 2), GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man oligosaccharide structures as acceptors. Has also activity toward core 3 of GlcNAcbeta1-3GalNAc-pNP. Its substrate specificity may be influenced by its subcellular location. Monomer. Golgi apparatus membrane Single-pass type II membrane protein Specifically expressed in HEV. Weakly expressed in spleen. Not expressed in other tissues. Expressed in colonic mucinous adenocarcinoma. Upon cytokine activation, it is expressed at low level. May serve as an antiinflammatory target. Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc subfamily. Carbohydrate metabolism Complete proteome Glycoprotein Golgi apparatus Inflammatory response Membrane Polymorphism Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix H Q S N MLLPKKMKLLLFLVSQMAILALFFHMYSHNISSLSMKAQPERMHVLVLSSWRSGSSFVGQ LFGQHPDVFYLMEPAWHVWMTFKQSTAWMLHMAVRDLIRAVFLCDMSVFDAYMEPGPRRQ SSLFQWENSRALCSAPACDIIPQDEIIPRAHCRLLCSQQPFEVVEKACRSYSHVVLKEVR FFNLQSLYPLLKDPSLNLHIVHLVRDPRAVFRSRERTKGDLMIDSRIVMGQHEQKLKKED QPYYVMQVICQSQLEIYKTIQSLPKALQERYLLVRYEDLARAPVAQTSRMYEFVGLEFLP HLQTWVHNITRGKGMGDHAFHTNARDALNVSQAWRWSLPYEKVSRLQKACGDAMNLLGYR HVRSEQEQRNLLLDLLSTWTVPEQIH Q9BRR6 Q49AU7 Q8NBI1 Q8WZ90 Q96NF8 Q9H0A7 ADPGK_HUMAN ADP-dependent glucokinase ADP-GK ADPGK 2.7.1.147 RbBP-35 ADPGK PSEC0260 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo RbBP-35 interacted with pRb. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5) Lymph node Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4) Testis Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) Heart Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4) Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Teratocarcinoma The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6) Brain Kidney Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. GDP and CDP can replace ADP, but with reduced efficiency (By similarity). ADP + D-glucose = AMP + D-glucose 6-phosphate + H(+) Mg(2+) Binds 1 Mg(2+) ion per subunit. Carbohydrate degradation; glycolysis. Monomer. Secreted Q9BRR6-1 1 Q9BRR6-2 2 Q9BRR6-3 3 Q9BRR6-4 4 Q9BRR6-5 5 Q9BRR6-6 6 No experimental confirmation available. Belongs to the ADP-dependent glucokinase family. Alternative splicing Complete proteome Glycolysis Kinase Magnesium Metal-binding Polymorphism Reference proteome Secreted Signal Transferase RKRLLE MAASCR AAGARVAGTQACATETIDTSRVSLRAPQEFMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLV LGSSCGWDTGLRHRNHRHQPSVSEGTPRVHDFPFGGRLQDCIKPKQASSRMAQRGNILPLHTSIGV K R MALWRGSAYAGFLALAVGCVFLLEPELPGSALRSLWSSLCLGPAPAPPGPVSPEGRLAAA WDALIVRPVRRWRRVAVGVNACVDVVLSGVKLLQALGLSPGNGKDHSILHSRNDLEEAFI HFMGKGAAAERFFSDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAANSDLKVLLCGP VGPKLHELLDDNVFVPPESLQEVDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAM NMLEVFVSSLEEFQPDLVVLSGLHMMEGQSKELQRKRLLEVVTSISDIPTGIPVHLELAS MTNRELMSSIVHQQVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWNGVPDVGMVSDILF WILKEHGRSKSRASDLTRIHFHTLVYHILATVDGHWANQLAAVAAGARVAGTQACATETI DTSRVSLRAPQEFMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLG DAISAEGLFYSEVHPHY Q9P003 A8K1Q8 B2R553 Q9H0X8 CNIH4_HUMAN Protein cornichon homolog 4 CNIH-4 Cornichon family AMPA receptor auxiliary protein 4 CNIH4 HSPC163 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Umbilical cord blood Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Uterus Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Cerebellum Hippocampus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] CNIH4 interacts with newly synthesized GPCR and controls their export from the endoplasmic reticulum. FUNCTION SUBCELLULAR LOCATION INTERACTION WITH CCR5; ADRB2; SEC24B AND SEC24D Involved in G protein-coupled receptors (GPCRs) trafficking from the endoplasmic reticulum to the cell surface; it promotes the exit of GPCRs from the early secretory pathway, likely through interaction with the COPII machinery (PubMed:24405750). Interacts with Sec23/24 complex components SEC24B and SEC24D (PubMed:24405750). Interacts with CCR5 (PubMed:24405750). Interacts with ADRB2 in the early secretory pathway (PubMed:24405750). Membrane Multi-pass membrane protein Endoplasmic reticulum Endoplasmic reticulum-Golgi intermediate compartment Q9P003-1 1 Q9P003-2 2 Belongs to the cornichon family. Alternative splicing Complete proteome Endoplasmic reticulum ER-Golgi transport Membrane Polymorphism Protein transport Reference proteome Transmembrane Transmembrane helix Transport A G MEAVVFVFSLLDCCALIFLSVYFIITLSDLECDYINARSCCSKLNKWVIPELIGHTIVTV LLLMSLHWFIFLLNLPVATWNIYRYIMVPSGNMGVFDPTEIHNRGQLKSHMKEAMIKLGF HLLCFFMYLYSMILALIND Q96NS8 Q9BW88 CLUP3_HUMAN Putative protein CLUHP3 Clustered mitochondria (cluA/CLU1) homolog pseudogene 3 KIAA0664-like protein 3 CLUHP3 C16orf67 KIAA0664L3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Cerebellum The sequence and analysis of duplication-rich human chromosome 16. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Lung Product of a dubious CDS prediction. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Complete proteome Reference proteome A V MFLNGNCLETLKKKEPEGGRRRLSHPGNMGWMRPSQETTPPDRSHHSGFGLFCGDPGPEI EPFSLWVFPQEMVLEIHQLFMDHEYPCHHITSHCTWVAAHWTTSQSCAAWQGCRRACCST WWKSPAQCTRPTVMSATFETAQEPGPS Q86U37 A8MT64 CN023_HUMAN Uncharacterized protein encoded by LINC01551 LINC01551 C14orf23 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Full-length cDNA libraries and normalization. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Fetal brain The DNA sequence and analysis of human chromosome 14. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Complete proteome Reference proteome MELSSMKICAAIPTSRALPEVVRRMPRKRISGLEWLLQQDPGFSLVNTVKAGMIISFPSN NIYSSVCCCQSEIFKYEFSNSKKSSWIQEERHLGKNNVLYSAHDVSPEKVTSALKKTNKQ TTTINNFPLQYLPGSKLLDRFLSLSRSLLCLNSWSSSLPLAPQVKKK P08034 B2R8R2 D3DVV2 Q5U0S4 CXB1_HUMAN Gap junction beta-1 protein Connexin-32 Cx32 GAP junction 28 kDa liver protein GJB1 CX32 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and characterization of human and rat liver cDNAs coding for a gap junction protein. NUCLEOTIDE SEQUENCE [MRNA] Liver Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Subthalamic nucleus Cloning of human full-length CDSs in BD Creator(TM) system donor vector. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Liver Placenta Skin NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17 Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations. TOPOLOGY An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-266 AND SER-277 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver A Calpha model for the transmembrane alpha helices of gap junction intercellular channels. 3D-STRUCTURE MODELING OF 19-209 STRUCTURE BY ELECTRON CRYOMICROSCOPY (20 ANGSTROMS) Mutations in the peripheral myelin genes and associated genes in inherited peripheral neuropathies. REVIEW ON CMTX1 VARIANTS Connexin mutations in X-linked Charcot-Marie-Tooth disease. VARIANTS CMTX1 SER-12; MET-139; TRP-142; ARG-156; SER-172 AND LYS-186 Mutational studies in X-linked Charcot-Marie-Tooth disease (CMTX). VARIANTS CMTX1 MET-35; ALA-158; THR-182 AND 111-HIS--HIS-116 DEL Mutations in the connexin 32 gene in X-linked dominant Charcot-Marie-Tooth disease (CMTX1). VARIANTS CMTX1 GLN-15; PHE-60; ILE-63; LEU-143 DEL; LYS-208 AND TRP-215 Point mutations of the connexin32 (GJB1) gene in X-linked dominant Charcot-Marie-Tooth neuropathy. VARIANTS CMTX1 GLY-102 AND TRP-142 X-linked dominant Charcot-Marie-Tooth neuropathy: valine-38-methionine substitution of connexin32. VARIANT CMTX1 MET-38 New connexin32 mutations associated with X-linked Charcot-Marie-Tooth disease. VARIANTS CMTX1 LEU-13; ASN-30; CYS-65; MET-95; ARG-133 AND ARG-156 Correlation between connexin 32 gene mutations and clinical phenotype in X-linked dominant Charcot-Marie-Tooth neuropathy. VARIANTS CMTX1 SER-3; GLN-22; SER-77; ARG-80; GLY-102; TRP-142 AND TRP-164 X-linked dominant Charcot-Marie-Tooth neuropathy (CMTX): new mutations in the connexin32 gene. VARIANTS CMTX1 GLY-22; PRO-22 AND TRP-215 Novel mutations in the connexin 32 gene associated with X-linked Charcot-Marie tooth disease. VARIANTS CMTX1 THR-34; GLN-75 AND TRP-107 Novel missense mutation of the connexin32 (GJB1) gene in X-linked dominant Charcot-Marie-Tooth neuropathy. VARIANT CMTX1 CYS-7 Two novel mutations (C53S, S26L) in the connexin32 of Charcot-Marie-Tooth disease type X families. VARIANTS CMTX1 LEU-26 AND SER-53 A point mutation in codon 3 of connexin-32 is associated with X-linked Charcot-Marie-Tooth neuropathy. VARIANT CMTX1 SER-3 Arginine-164-tryptophan substitution in connexin32 associated with X linked dominant Charcot-Marie-Tooth disease. VARIANT CMTX1 TRP-164 Linkage and mutation analysis of Charcot-Marie-Tooth neuropathy type 2 families with chromosomes 1p35-p36 and Xq13. VARIANT CMTX1 TYR-49 New mutations in the X-linked form of Charcot-Marie-Tooth disease. VARIANTS CMTX1 VAL-34; HIS-90; TRP-107; TRP-142; PHE-156 AND LYS-186 Connexin32 gene mutations in X-linked dominant Charcot-Marie-Tooth disease (CMTX1). VARIANTS CMTX1 TRP-15; ILE-63; CYS-65; SER-87; PRO-89; MET-139 AND ARG-199 Mutational analysis of the MPZ, PMP22 and Cx32 genes in patients of Spanish ancestry with Charcot-Marie-Tooth disease and hereditary neuropathy with liability to pressure palsies. VARIANTS CMTX1 ALA-23; SER-64; SER-87; TRP-164; GLN-164; SER-183; HIS-183; CYS-183 AND TRP-215 Screening for connexin 32 mutations in Charcot-Marie-Tooth disease families with possible X-linked inheritance. VARIANTS CMTX1 GLN-22; GLN-75; TRP-75; TRY-107; MET-139 AND VAL-194 Mutation analysis of the connexin 32 (Cx32) gene in Charcot-Marie-Tooth neuropathy type 1: identification of five new mutations. VARIANTS CMTX1 PHE-25; LEU-26; ALA-87 AND HIS-238 Charcot-Marie-Tooth disease with intermediate motor nerve conduction velocities: characterization of 14 Cx32 mutations in 35 families. VARIANTS THR-34; ILE-84; MET-95; TRP-107; ARG-133; LEU-141; ALA-158; ASN-203; SER-205 AND 213-ILE-ILE-214 DELINS LEU Connexin32 and X-linked Charcot-Marie-Tooth disease. VARIANTS CMTX1 ARG-3; SER-3; CYS-7; SER-12; LEU-13; MET-13; LYS-14; GLN-15; TRP-15; PRO-16; SER-20; ASP-21; GLN-22; PRO-22; GLY-22; ALA-23; PHE-25; LEU-26; ASN-28; THR-28; LEU-29; ASN-30; THR-34; VAL-34; MET-35; MET-38; VAL-40; LYS-41; LEU-44; TYR-49; SER-53; PHE-56; PHE-60; ILE-63; SER-64; CYS-65; GLN-75; PRO-75; TRP-75; SER-77; ARG-80; CYS-85; PHE-85; ALA-86; ASN-86; SER-86; ALA-87; LEU-87; SER-87; PRO-89; HIS-90; VAL-93; GLN-94; TYR-94; MET-95; TYR-100; GLY-102; GLU-103; TRP-107; HIS-111--116-HIS DEL; ASN-124; PRO-128; ARG-133; MET-139; TRP-142; GLU-142; LEU-143 DEL; ARG-156; PHE-156; CYS-157; ALA-158; ARG-158; HIS-160; PRO-161; TRP-164; GLN-164; SER-172; LEU-172; TYR-178; ARG-179; LEU-180; MET-181; THR-182; CYS-183; SER-183; HIS-183; THR-185 DEL; LYS-186; GLU-187; GLY-189; ILE-189; 191-THR--PHE-193 DEL; CYS-193; PHE-198; ARG-199; ARG-201; VAL-204; SER-205; LYS-208; TRP-215; CYS-219; HIS-219; GLY-220; CYS-230; LEU-230; CYS-235 AND HIS-238 Mutations in the X-linked form of Charcot-Marie-Tooth disease in the French population. VARIANTS CMTX1 PRO-22; GLY-22; VAL-34; PRO-50; PHE-56; TRP-75; HIS-90; TRP-107; ARG-133; TRP-142; PHE-156; SER-159; ARG-184; LYS-186 AND TRP-215 Four novel mutations of the connexin 32 gene in four Japanese families with Charcot-Marie-Tooth disease type 1. VARIANTS CMTX1 MET-37; HIS-57; LEU-172 AND ALA-177 X-linked Charcot-Marie-Tooth disease and connexin32. VARIANTS CMTX1 SER-3; GLN-22; ALA-70; SER-77; ARG-80; MET-95; GLY-102; TRP-142; TRP-164 AND SER-180 A novel mutation (C201R) in the transmembrane domain of connexin 32 in severe X-linked Charcot-Marie-Tooth disease. VARIANT CMTX1 ARG-201 Mutation analysis in Charcot-Marie-Tooth disease type 1 (CMT1). VARIANTS CMTX1 TRP-15; PHE-60; ALA-86; TYR-100; CYS-133 AND SER-205 Spectrum of mutations in Finnish patients with Charcot-Marie-Tooth disease and related neuropathies. VARIANTS CMTX1 GLN-22; ARG-58; ILE-63; LEU-172; ASP-175 AND PHE-204 Mutations of connexin32 in Charcot-Marie-Tooth disease type X interfere with cell-to-cell communication but not cell proliferation and myelin-specific gene expression. VARIANTS CMTX1 SER-53 AND ARG-172 CHARACTERIZATION OF VARIANTS CMTX1 SER-53 AND ARG-172 Efficient neurophysiologic selection of X-linked Charcot-Marie-Tooth families: ten novel mutations. VARIANTS CMTX1 TRP-9; GLN-22; THR-28; THR-30; THR-34; MET-35; TRP-107; MET-127; PRO-131; ALA-158; THR-182; PHE-192 AND ILE-239 HMSN and HNPP. Laboratory service provision in the south west of England -- two years' experience. VARIANTS CMTX1 GLN-22; VAL-39; MET-43; PHE-60; THR-104; MET-139; GLN-142; TRP-142; VAL-149 AND GLU-177 Three novel mutations in the gap junction beta 1 (GJB1) gene coding region identified in Charcot-Marie-Tooth patients of Greek origin: T55I, R164Q, V120E. VARIANTS CMTX1 ILE-55; GLU-120 AND GLN-164 Central visual, acoustic, and motor pathway involvement in a Charcot-Marie-Tooth family with an Asn205Ser mutation in the connexin 32 gene. VARIANT CMTX1 SER-205 Altered formation of hemichannels and gap junction channels caused by C-terminal connexin-32 mutations. CHARACTERIZATION OF VARIANTS CMTX1 LYS-208; GLN-215; TRP-215; HIS-238 AND GLY-280 Mutational analysis and genotype/phenotype correlation in Turkish Charcot-Marie-Tooth type 1 and HNPP patients. VARIANTS CMTX1 MET-91 AND HIS-211 A family with X-linked dominant Charcot-Marie-Tooth caused by a connexin32 mutation. VARIANT CMTX1 TYR-126 Severe X-linked Charcot-Marie-Tooth neuropathy due to new mutations [G59R(G-->C), W44X(G-->A)] in the connexin 32 gene. VARIANT CMTX1 ARG-59 Screening for mutations in the peripheral myelin genes PMP22, MPZ and Cx32 (GJB1) in Russian Charcot-Marie-Tooth neuropathy patients. VARIANTS CMTX1 20-ASN-SER-21; LYS-34; ARG-80; VAL-90; VAL-93; TRP-107; TRP-142; GLN-164; HIS-183; LYS-186; LEU-193 AND LYS-208 ERRATUM Mutations in the peripheral myelin protein zero and connexin32 genes detected by non-isotopic RNase cleavage assay and their phenotypes in Japanese patients with Charcot-Marie-Tooth disease. VARIANTS CMTX1 LEU-69; GLN-142 AND GLN-164 A new de novo mutation of the connexin-32 gene in a patient with X-linked Charcot-Marie-Tooth type 1 disease. VARIANT CMTX1 ILE-8 Clinical, electrophysiological and molecular genetic characteristics of 93 patients with X-linked Charcot-Marie-Tooth disease. VARIANTS CMTX1 GLY-22; THR-34; VAL-34; PHE-56; ILE-84; MET-91; ASP-94; GLN-94; MET-95; TRP-107; ILE-130; ARG-133; LEU-141; GLN-142; ALA-158; ASP-159; TRP-164; GLN-164; LYS-186; ARG-199; ASN-203; SER-205; 213-ILE-ILE-214 DELINS LEU AND TRP-215 CHARACTERIZATION OF VARIANTS CMTX1 GLY-22; THR-34; PHE-56; GLN-94; MET-95; LYS-186 AND TRP-215 A novel connexin 32 missense mutation (E208G) causing Charcot-Marie-Tooth disease. VARIANT CMTX1 GLY-208 Charcot-Marie-Tooth disease type I and related demyelinating neuropathies: mutation analysis in a large cohort of Italian families. VARIANTS CMTX1 CYS-7; PRO-8; GLN-22; PRO-25; ASN-30; CYS-59; MET-139; LEU-143 DEL; SER-151; TRP-164 AND LEU-184 Charcot-Marie-Tooth type X: a novel mutation in the Cx32 gene with central conduction slowing. VARIANT CMTX1 HIS-65 Mutation analysis in Chariot-Marie Tooth disease type 1: point mutations in the MPZ gene and the GJB1 gene cause comparable phenotypic heterogeneity. VARIANTS CMTX1 TRP-26; PHE-64; TRP-142; TRP-164 AND TRP-215 Episodes of generalized weakness in two sibs with the C164T mutation of the connexin 32 gene. VARIANT CMTX1 ILE-55 Charcot-Marie-Tooth disease and related neuropathies: mutation distribution and genotype-phenotype correlation. VARIANTS CMTX1 TRP-15; GLN-22; GLY-102; PRO-108; ILE-205 AND TRP-215 Transient central nervous system white matter abnormality in X-linked Charcot-Marie-Tooth disease. VARIANTS CMTX1 TRP-142 AND TYR-168 Molecular analysis in Japanese patients with Charcot-Marie-Tooth disease: DGGE analysis for PMP22, MPZ, and Cx32/GJB1 mutations. VARIANTS CMTX1 TRP-75; GLN-75; VAL-120 DEL; MET-139; LYS-146; ASP-147; VAL-209 DEL AND CYS-264 Six novel connexin32 (GJB1) mutations in X-linked Charcot-Marie-Tooth disease. VARIANTS CMTX1 CYS-24; ARG-55; ASP-125 AND SER-153 Diverse trafficking abnormalities of connexin32 mutants causing CMTX. CHARACTERIZATION OF VARIANTS CMTX ILE-34; LYS-34; THR-34; VAL-34; MET-35; MET-37; MET-38; VAL-40; GLN-75; PRO-75; TRP-75; ILE-205; VAL-213; CYS-219; HIS-219; GLY-220; CYS-230; LEU-230; HIS-238 AND ILE-239 X-linked Charcot-Marie-Tooth disease caused by a novel point mutation in the connexin-32 gene. VARIANT CMTX1 THR-40 Charcot-Marie-Tooth neuropathy: clinical phenotypes of four novel mutations in the MPZ and Cx 32 genes. VARIANT CMTX1 PRO-49 Voltage opens unopposed gap junction hemichannels formed by a connexin 32 mutant associated with X-linked Charcot-Marie-Tooth disease. CHARACTERIZATION OF VARIANT CMTX1 CYS-85 Transient, recurrent, white matter lesions in X-linked Charcot-Marie-Tooth disease with novel connexin 32 mutation. VARIANT CMTX1 GLU-102 DEL Demyelinating and axonal features of Charcot-Marie-Tooth disease with mutations of myelin-related proteins (PMP22, MPZ and Cx32): a clinicopathological study of 205 Japanese patients. VARIANTS CMTX1 LEU-26; ALA-55; HIS-57; ILE-63; LEU-69; MET-139; GLN-142; TRP-142; ARG-172; ALA-177; HIS-183; ALA-191 AND TYR-201 Novel mutations in the Charcot-Marie-Tooth disease genes PMP22, MPZ, and GJB1. VARIANTS CMTX1 7-TYR-THR-8 DELINS SER; ASN-138; GLN-164; ALA-172 AND SER-205 Pathogenesis of X-linked Charcot-Marie-Tooth disease: differential effects of two mutations in connexin 32. VARIANTS CMTX1 GLY-102 AND ALA-181 CHARACTERIZATION OF VARIANTS CMTX1 GLY-102 AND ALA-181 Mutational analysis of PMP22, MPZ, GJB1, EGR2 and NEFL in Korean Charcot-Marie-Tooth neuropathy patients. VARIANTS CMTX1 ALA-136; GLN-164 AND ARG-168 ERRATUM Severe neuropathy with leaky connexin32 hemichannels. VARIANT CMTX1 CYS-235 CHARACTERIZATION OF VARIANT CMTX1 CYS-235 X-linked Charcot-Marie-Tooth disease: phenotypic expression of a novel mutation Ile127Ser in the GJB1 (connexin 32) gene. VARIANT CMTX1 SER-127 Two missense mutations of EGR2 R359W and GJB1 V136A in a Charcot-Marie-Tooth disease family. VARIANT DSS ALA-136 Improved diagnostic yield of neuromuscular disorders applying clinical exome sequencing in patients arising from a consanguineous population. VARIANT CMTX1 GLU-124 One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. A connexon is composed of a hexamer of connexins. Interacts with CNST (By similarity). Cell membrane Multi-pass membrane protein Cell junction Gap junction Charcot-Marie-Tooth disease, X-linked dominant, 1 CMTX1 A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies characterized by severely reduced motor nerve conduction velocities (NCVs) (less than 38m/s) and segmental demyelination and remyelination, and primary peripheral axonal neuropathies characterized by normal or mildly reduced NCVs and chronic axonal degeneration and regeneration on nerve biopsy. CMTX1 has both demyelinating and axonal features. Central nervous system involvement may occur. The disease is caused by mutations affecting the gene represented in this entry. Dejerine-Sottas syndrome DSS A severe degenerating neuropathy of the demyelinating Charcot-Marie-Tooth disease category, with onset by age 2 years. Characterized by motor and sensory neuropathy with very slow nerve conduction velocities, increased cerebrospinal fluid protein concentrations, hypertrophic nerve changes, delayed age of walking as well as areflexia. There are both autosomal dominant and autosomal recessive forms of Dejerine-Sottas syndrome. The gene represented in this entry may act as a disease modifier. Belongs to the connexin family. Beta-type (group I) subfamily. 3D-structure Cell junction Cell membrane Charcot-Marie-Tooth disease Complete proteome Dejerine-Sottas syndrome Disease mutation Gap junction Membrane Neurodegeneration Neuropathy Phosphoprotein Reference proteome Transmembrane Transmembrane helix W R W S YT S Y C T I T P L W S G G S V L V M N K R Q R W H P IG NS I S G D R G R P R Q V A W C L F L P S L S W I IIF I N I T F L I N I T M I M K M T M V V M V M V M A P A V A T A V E K V M W L S P S Y S P C S T A T I T R L F Q H P R G C G R C F V I C F C S Y C Y H F L P A R P R Q R W W S Q R L F L P V I S C S F T A T N T S P A P L P S L P L H L V V M M V H D H Q H Y V M H Y E G K E K T R W L P V E K E K N V D H Y I M I S S P T I L P W C W R Y C V A S N V M F L R E R Q R W E K A D F I F V Y S F S L F L R Y C P A P R P S G D G S Y H A P R Q R W C R C Y P A P L P R P S C R N D V A V E D Y C R F L F S V A V M S T R C R H R S P L P R E K K E V G V I T A V F F C F L M V S F G R C R C Y I N L F L V N I N S E G E K Y H II L I V R Q R W R C R H R G R C R L F C R H L I R C C G HS IL MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGC NSVCYDQFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPLHLEEV KRHKVHISGTLWWTYVISVVFRLLFEAVFMYVFYLLYPGYAMVRLVKCDVYPCPNTVDCF VSRPTEKTVFTVFMLAASGICIILNVAEVVYLIIRACARRAQRRSNPPSRKGSGFGHRLS PEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC Q9H0C2 ADT4_HUMAN ADP/ATP translocase 4 ADP,ATP carrier protein 4 Adenine nucleotide translocator 4 ANT 4 Solute carrier family 25 member 31 Sperm flagellar energy carrier protein SLC25A31 AAC4 ANT4 SFEC Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A fourth ADP/ATP carrier isoform in man: identification, bacterial expression, functional characterization and tissue distribution. NUCLEOTIDE SEQUENCE [MRNA] SUBCELLULAR LOCATION TISSUE SPECIFICITY Liver Compartmentalization of a unique ADP/ATP carrier protein SFEC (sperm flagellar energy carrier, AAC4) with glycolytic enzymes in the fibrous sheath of the human sperm flagellar principal piece. NUCLEOTIDE SEQUENCE [MRNA] FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in insulin-producing adenomas. VARIANT GLU-303 Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. May serve to mediate energy generating and energy consuming processes in the distal flagellum, possibly as a nucleotide shuttle between flagellar glycolysis, protein phosphorylation and mechanisms of motility. Mitochondrion inner membrane Multi-pass membrane protein Cell projection Cilium Flagellum In sperm flagellum this protein is located in the fibrous sheath, a non-mitochondrial region. Expressed in brain, liver, sperm and testis. The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue. Belongs to the mitochondrial carrier (TC 2.A.29) family. Cell projection Cilium Complete proteome Flagellum Membrane Mitochondrion Mitochondrion inner membrane Polymorphism Reference proteome Repeat Transmembrane Transmembrane helix Transport K E MHREPAKKKAEKRLFDASSFGKDLLAGGVAAAVSKTAVAPIERVKLLLQVQASSKQISPE ARYKGMVDCLVRIPREQGFFSFWRGNLANVIRYFPTQALNFAFKDKYKQLFMSGVNKEKQ FWRWFLANLASGGAAGATSLCVVYPLDFARTRLGVDIGKGPEERQFKGLGDCIMKIAKSD GIAGLYQGFGVSVQGIIVYRASYFGAYDTVKGLLPKPKKTPFLVSFFIAQVVTTCSGILS YPFDTVRRRMMMQSGEAKRQYKGTLDCFVKIYQHEGISSFFRGAFSNVLRGTGGALVLVL YDKIKEFFHIDIGGR P01036 Q9UBI5 Q9UCS9 CYTS_HUMAN Cystatin-S Cystatin-4 Cystatin-SA-III Salivary acidic protein 1 CST4 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Human salivary cystatin S. Cloning, sequence analysis, hybridization in situ and immunocytochemistry. NUCLEOTIDE SEQUENCE [MRNA] Submandibular gland Characterization of two members (CST4 and CST5) of the cystatin gene family and molecular evolution of cystatin genes. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Acquisition of complex patterns of differential expression in epithelial cell populations during the evolution of type 2 cystatin genes. NUCLEOTIDE SEQUENCE [GENOMIC DNA] The DNA sequence and comparative analysis of human chromosome 20. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Thyroid Identification of a long form of cystatin from human saliva by rapid microbore HPLC mapping. PROTEIN SEQUENCE OF 21-51 Large-scale purification and characterization of the major phosphoproteins and mucins of human submandibular-sublingual saliva. PROTEIN SEQUENCE OF 21-55 PHOSPHORYLATION AT SER-23 Saliva Identification of full-sized forms of salivary (S-type) cystatins (cystatin SN, cystatin SA, cystatin S, and two phosphorylated forms of cystatin S) in human whole saliva and determination of phosphorylation sites of cystatin S. PROTEIN SEQUENCE OF 21-36 PHOSPHORYLATION AT SER-21 AND SER-23 Saliva The effects of human salivary cystatins and statherin on hydroxyapatite crystallization. PROTEIN SEQUENCE OF 21-36 PHOSPHORYLATION AT SER-23 Saliva Isolation and amino acid sequence of SAP-1, an acidic protein of human whole saliva, and sequence homology with human gamma-trace. PROTEIN SEQUENCE OF 29-141 Human basal tear peptidome characterization by CID, HCD, and ETD followed by in silico and in vitro analyses for antimicrobial peptide identification. PROTEIN SEQUENCE OF 85-141 IDENTIFICATION BY MASS SPECTROMETRY Tear Cystatin S: a cysteine proteinase inhibitor of human saliva. INHIBITOR SPECIFICITY Salivary cystatin SA-III, a potential precursor of the acquired enamel pellicle, is phosphorylated at both its amino- and carboxyl-terminal regions. PHOSPHORYLATION Confident assignment of intact mass tags to human salivary cystatins using top-down Fourier-transform ion cyclotron resonance mass spectrometry. PHOSPHORYLATION AT SER-21 AND SER-23 DISULFIDE BONDS TISSUE SPECIFICITY SUBCELLULAR LOCATION MASS SPECTROMETRY Saliva The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] ASN-77 This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively. Secreted Expressed in submandibular and sublingual saliva but not in parotid saliva (at protein level). Expressed in saliva, tears, urine and seminal fluid. Phosphorylated at both its N- and C-terminal regions. Monophosphorylated at Ser-23, also called form S1. Diphosphorylated at Ser-21 and Ser-23, also called form S2. Belongs to the cystatin family. Complete proteome Direct protein sequencing Disulfide bond Phosphoprotein Polymorphism Protease inhibitor Reference proteome Secreted Signal Thiol protease inhibitor D N T N N D MARPLCTLLLLMATLAGALASSSKEENRIIPGGIYDADLNDEWVQRALHFAISEYNKATE DEYYRRPLQVLRAREQTFGGVNYFFDVEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSF EIYEVPWEDRMSLVNSRCQEA Q9Y6V7 E7ENA0 Q53FJ1 Q9BVQ8 DDX49_HUMAN Probable ATP-dependent RNA helicase DDX49 3.6.4.13 DEAD box protein 49 DDX49 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Synovial cell The DNA sequence and biology of human chromosome 19. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Cervix Uterus Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ATP + H2O = ADP + H(+) + phosphate Q9Y6V7-1 1 Q9Y6V7-2 2 No experimental confirmation available. Belongs to the DEAD box helicase family. DDX49/DBP8 subfamily. Alternative splicing ATP-binding Complete proteome Helicase Hydrolase Nucleotide-binding Polymorphism Reference proteome RNA-binding LDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVH ADQPPLPPGAWTSLRYRWSSTTTPPGSPRSTSTESAGRPVQGGRVRPSRW R H S A R W A V MAGFAELGLSSWLVEQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPI LQKLSEDPYGIFCLVLTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRK PHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLEQGCTDFTVDLEAILAAVPARR QTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPEKVKDAYLVHLIQ RFQDEHEDWSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYR ILIATDVASRGLDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLV HAIEEQIKKKLEEFSVEEAEVLQILTQVNVVRRECEIKLEAAHFDEKKEINKRKQLILEG KDPDLEAKRKAELAKIKQKNRRFKEKVEETLKRQKAGRAGHKGRPPRTPSGSHSGPVPSQ GLV Q8NEG4 Q96FD6 FA83F_HUMAN Protein FAM83F FAM83F Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence of human chromosome 22. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Cervix Testis System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] VAL-418 Q8NEG4-1 1 Q8NEG4-2 2 No experimental confirmation available. Belongs to the FAM83 family. Acetylation Alternative splicing Complete proteome Phosphoprotein Polymorphism Reference proteome R S G S A V R G R W MAESQLNCLDEAHVNEKVTEAQAAFYYCERRRAALEALLGGGEQAYRERLKEEQLRDFLS SPERQALRAAWSPYEDAVPAANARGKSKAKAKAPAPAPAESGESLAYWPDRSDTEVPPLD LGWTDTGFYRGVSRVTLFTHPPKDEKAPHLKQVVRQMIQQAQKVIAVVMDLFTDGDIFQD IVDAACKRRVPVYIILDEAGVKYFLEMCQDLQLTDFRIRNIRVRSVTGVGFYMPMGRIKG TLSSRFLMVDGDKVATGSYRFTWSSSHVDRNLLLLLTGQNVEPFDTEFRELYAISEEVDL YRQLSLAGRVGLHYSSTVARKLINPKYALVSGCRHPPGEMMRWAARQQREAGGNPEGQEE GASGGESAWRLESFLKDLVTVEQVLPPVEPIPLGELSQKDGRMVSHMHRDLKPKSREAPS RNGMGEAARGEAAPARRFSSRLFSRRAKRPAAPNGMASSVSTETSEVEFLTGKRPNENSS ADISGKTSPSSAKPSNCVIS Q6ZRV2 A0JLS2 Q8N4W0 FA83H_HUMAN Protein FAM83H FAM83H Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo DNA sequence and analysis of human chromosome 8. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-1179 Testis The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 861-1179 Placenta Prostate Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1003 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma FAM83H mutations in families with autosomal-dominant hypocalcified amelogenesis imperfecta. FUNCTION TISSUE SPECIFICITY INVOLVEMENT IN AI3A Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-647; SER-785 AND SER-1003 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647; SER-881; THR-883; SER-892; SER-903; SER-936; SER-945; SER-1003; SER-1024 AND SER-1025 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Large-scale proteomics analysis of the human kinome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-914 AND SER-1003 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-465; SER-523; SER-647; SER-759; SER-785; SER-870; SER-881; SER-892; SER-903; SER-914; SER-936; SER-945; SER-1003; THR-1040 AND SER-1048 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] A novel mechanism of keratin cytoskeleton organization through casein kinase Ialpha and FAM83H in colorectal cancer. FUNCTION INTERACTION WITH CSNK1A1 AND KRT18 SUBCELLULAR LOCATION REGION MUTAGENESIS OF PHE-251 AND PHE-274 Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-514; SER-516; SER-523; SER-647; SER-667; SER-785; SER-870; SER-881; SER-892; SER-903; SER-914; SER-925; SER-936; SER-1003; SER-1025 AND SER-1147 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; THR-756; SER-813; SER-914; SER-1003 AND SER-1068 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Novel missense mutation of the FAM83H gene causes retention of amelogenin and a mild clinical phenotype of hypocalcified enamel. VARIANT AI3A CYS-557 May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688). Interacts with CSNK1A1; recruits CSNK1A1 to keratin filaments. Interacts with KRT18 and probably other keratins. Cytoplasm Cytoskeleton Colocalizes with keratin filaments. Expressed in the tooth follicle. Amelogenesis imperfecta 3A AI3A An autosomal dominant hypomineralized form of amelogenesis imperfecta, a defect of enamel formation. AI3A is characterized by enamel of normal thickness but soft and with cheesy consistency. Enamel is lost from tooth soon after eruption. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the FAM83 family. Translation N-terminally extended. Amelogenesis imperfecta Biomineralization Complete proteome Cytoplasm Cytoskeleton Disease mutation Phosphoprotein Polymorphism Reference proteome Q H G C F A F A E V MARRSQSSSQGDNPLAPGYLPPHYKEYYRLAVDALAEGGSEAYSRFLATEGAPDFLCPEE LEHVSRHLRPPQYVTREPPEGSLLDVDMDGSSGTYWPVNSDQAVPELDLGWPLTFGFQGT EVTTLVQPPPPDSPSIKDEARRMIRSAQQVVAVVMDMFTDVDLLSEVLEAAARRVPVYIL LDEMNAQHFLDMADKCRVNLQHVDFLRVRTVAGPTYYCRTGKSFKGHVKEKFLLVDCAVV MSGSYSFMWSFEKIHRSLAHVFQGELVSSFDEEFRILFAQSEPLVPSAAALARMDAYALA PYAGAGPLVGVPGVGAPTPFSFPKRAHLLFPPPREEGLGFPSFLDPDRHFLSAFRREEPP RMPGGALEPHAGLRPLSRRLEAEAGPAGELAGARGFFQARHLEMDAFKRHSFATEGAGAV ENFAAARQVSRQTFLSHGDDFRFQTSHFHRDQLYQQQYQWDPQLTPARPQGLFEKLRGGR AGFADPDDFTLGAGPRFPELGPDGHQRLDYVPSSASREVRHGSDPAFAPGPRGLEPSGAP RPNLTQRFPCQAAARPGPDPAPEAEPERRGGPEGRAGLRRWRLASYLSGCHGEDGGDDGL PAPMEAEAYEDDVLAPGGRAPAGDLLPSAFRVPAAFPTKVPVPGPGSGGNGPEREGPEEP GLAKQDSFRSRLNPLVQRSSRLRSSLIFSTSQAEGAAGAAAATEKVQLLHKEQTVSETLG PGGEAVRSAASTKVAELLEKYKGPARDPGGGAGAITVASHSKAVVSQAWREEVAAPGAVG GERRSLESCLLDLRDSFAQQLHQEAERQPGAASLTAAQLLDTLGRSGSDRLPSRFLSAQS HSTSPQGLDSPLPLEGSGAHQVLHNESKGSPTSAYPERKGSPTPGFSTRRGSPTTGFIEQ KGSPTSAYPERRGSPVPPVPERRSSPVPPVPERRGSLTLTISGESPKAGPAEEGPSGPME VLRKGSLRLRQLLSPKGERRMEDEGGFPVPQENGQPESPRRLSLGQGDSTEAATEERGPR ARLSSATANALYSSNLRDDTKAILEQISAHGQKHRAVPAPSPGPTHNSPELGRPPAAGVL APDMSDKDKCSAIFRSDSLGTQGRLSRTLPASAEERDRLLRRMESMRKEKRVYSRFEVFC KKEEASSPGAGEGPAEEGTRDSKVGKFVPKILGTFKSKK P42830 Q96QE1 CXCL5_HUMAN C-X-C motif chemokine 5 ENA-78(1-78) Epithelial-derived neutrophil-activating protein 78 Neutrophil-activating peptide ENA-78 Small-inducible cytokine B5 ENA-78(8-78) ENA-78(9-78) CXCL5 ENA78 SCYB5 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning of a full-length cDNA encoding the neutrophil-activating peptide ENA-78 from human platelets. NUCLEOTIDE SEQUENCE [MRNA] Cloning and characterization of the human neutrophil-activating peptide (ENA-78) gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Characterization of the gene for human neutrophil-activating peptide 78 (ENA-78). NUCLEOTIDE SEQUENCE [GENOMIC DNA] Localization of distal regulatory domains in the megakaryocyte-specific platelet basic protein/platelet factor 4 gene locus. NUCLEOTIDE SEQUENCE [GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Kidney Novel polymorphism in ENA-78 gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-80 Structure and neutrophil-activating properties of a novel inflammatory peptide (ENA-78) with homology to interleukin 8. NUCLEOTIDE SEQUENCE [MRNA] OF 43-114 Epithelium Isolation of the CXC chemokines ENA-78, GRO alpha and GRO gamma from tumor cells and leukocytes reveals NH2-terminal heterogeneity. Functional comparison of different natural isoforms. PROTEIN SEQUENCE OF 37-51 IDENTIFICATION OF ENA-78(8-78) AND ENA-78(9-78) PROTEOLYTIC PROCESSING OF N-TERMINUS FUNCTION Peripheral blood monocyte Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. PROTEIN SEQUENCE OF 37-45 Platelet Regulation of the immune response by the interaction of chemokines and proteases. REVIEW Solution structure of CXCL5--a novel chemokine and adipokine implicated in inflammation and obesity. STRUCTURE BY NMR OF 37-114 DISULFIDE BONDS SUBUNIT Involved in neutrophil activation. In vitro, ENA-78(8-78) and ENA-78(9-78) show a threefold higher chemotactic activity for neutrophil granulocytes. Monomer (PubMed:24695525). Homodimer (PubMed:24695525). Secreted N-terminal processed forms ENA-78(8-78) and ENA-78(9-78) are produced by proteolytic cleavage after secretion from peripheral blood monocytes. Belongs to the intercrine alpha (chemokine CxC) family. CXCL5 entry 3D-structure Complete proteome Cytokine Direct protein sequencing Disulfide bond Reference proteome Secreted Signal MSLLSSRAARVPGPSSSLCALLVLLLLLTQPGPIASAGPAAAVLRELRCVCLQTTQGVHP KMISNLQVFAIGPQCSKVEVVASLKNGKEICLDPEAPFLKKVIQKILDGGNKEN Q9NVM6 DJC17_HUMAN DnaJ homolog subfamily C member 17 DNAJC17 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] T-cell A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. METHYLATION [LARGE SCALE ANALYSIS] AT LYS-264 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Colon carcinoma Solution structure of RNA binding domain in hypothetical protein FLJ10634. STRUCTURE BY NMR OF 162-258 May negatively affect PAX8-induced thyroglobulin/TG transcription. Cytoplasm Nucleus Predominantly nuclear. 3D-structure Chaperone Complete proteome Cytoplasm Methylation Nucleus Phosphoprotein Reference proteome RNA-binding Transcription Transcription regulation MAVTKELLQMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQAL EVLTDAAARAAYDKVRKAKKQAAERTQKLDEKRKKVKLDLEARERQAQAQESEEEEESRS TRTLEQEIERLREEGSRQLEEQQRLIREQIRQERDQRLRGKAENTEGQGTPKLKLKWKCK KEDESKGGYSKDVLLRLLQKYGEVLNLVLSSKKPGTAVVEFATVKAAELAVQNEVGLVDN PLKISWLEGQPQDAVGRSHSGLSKGSVLSERDYESLVMMRMRQAAERQQLIARMQQEDQE GPPT Q4G0N7 B8ZZ33 F229B_HUMAN Protein FAM229B FAM229B C6orf225 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Belongs to the FAM229 family. Complete proteome Reference proteome MPFQFGTQPRRFPVEGGDSSIELEPGLSSSAACNGKEMSPTRQLRRCPGSHCLTITDVPV TVYATTRKPPAQSSKEMHPK A0A1B0GUQ0 F236A_HUMAN Protein FAM236A FAM236A Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence of the human X chromosome. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Belongs to the FAM236 family. Complete proteome Reference proteome MIFTPFLPPADLSVFQNVKGLQNDPEEWVAVSDATEDPSGGTGLPREPALLRGSWRSRFQ RALACFTKCFRGGYRALGI Q96IJ6 A6NJ74 A8K3Q6 B3KMT4 Q53GI0 Q9NWC3 Q9Y5P5 GMPPA_HUMAN Mannose-1-phosphate guanyltransferase alpha GDP-mannose pyrophosphorylase A GMPP-alpha GTP-mannose-1-phosphate guanylyltransferase alpha GMPPA Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Human homolog of GDP-mannose pyrophosphorylase. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Kidney Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Lymph Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Mutations in GMPPA cause a glycosylation disorder characterized by intellectual disability and autonomic dysfunction. VARIANTS AAMR ASP-182; MET-334; PRO-334; PRO-390 AND THR-401 FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY May serve as a regulatory subunit and allow allosteric feedback inhibition of GMPPB by GDP-mannose. Associates with GMPPB. P35070 BTC false 6 P02741 CRP false 3 Q9Y5P6 GMPPB false 6 A0A0S2Z4D7 NCK1 false 3 A0A0S2Z6P0 ZNF688 false 3 Cytoplasm Myc-tagged GMPPA shows a diffuse cytoplasmic and nuclear pattern in transfected COS-7 cells. Q96IJ6-1 1 Q96IJ6-2 2 Expressed in fibroblasts (at protein level). Alacrima, achalasia, and mental retardation syndrome AAMR An autosomal recessive disorder characterized by onset of alacrima, achalasia, and mental retardation at birth or in early infancy. More variable features include hypotonia, gait abnormalities, anisocoria, and visual or hearing deficits. The disorder shows similarity to the triple A syndrome, but patients with AAMR do not have adrenal insufficiency. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the transferase hexapeptide repeat family. GMPPA is a close homolog of GMPPB, that has been shown to catalyze the formation of GDP-mannose, an essential precursor of glycan moieties of glycoproteins and glycolipids. However, lymphocytes from AAMR patients, that exhibit very low GMPPA protein levels, have unchanged GDP-mannose pyrophosphorylase activity and higher GDP-mannose levels than those from healthy controls. Affected individuals and control subjects show similar N-glycosylation profiles, both for transferrin glycosylation and for N-glycans derived from either total serum protein or immunoglobulin G. These observations led to the hypothesis that GMPPA might serve as a regulatory subunit and allow allosteric feedback inhibition of GMPPB by GDP-mannose. Alignment of GMPPAs and GMPPBs from various species shows that GMPPAs are characterized by a 2 amino acid-insertion (residues 11-12) in a highly conserved motif that borders the catalytic pocket and binds the nucleotide substrate in homologous enzymes. This insertion might inactivate the ancestral catalytic site, converting it to an allosteric site (PubMed:24035193). Alternative splicing Complete proteome Cytoplasm Disease mutation Mental retardation Polymorphism Reference proteome G GTQPAPIPNLWLPPQPSEPGFLTSSPELKPQSLPLPDQIRFGIFAPRASLLLLG S F V A G D T M T P R P N T G C Q H C Y S C MLKAVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYQ PDEPLTQFLEAAQQEFNLPVRYLQEFAPLGTGGGLYHFRDQILAGSPEAFFVLNADVCSD FPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHEVLHYVEKPSTFISDIIN CGIYLFSPEALKPLRDVFQRNQQDGQLEDSPGLWPGAGTIRLEQDVFSALAGQGQIYVHL TDGIWSQIKSAGSALYASRLYLSRYQDTHPERLAKHTPGGPWIRGNVYIHPTAKVAPSAV LGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEGTPSDP NPNDPRARMDSESLFKDGKLLPAITILGCRVRIPAEVLILNSIVLPHKELSRSFTNQIIL Q9BQI3 A8K2R2 Q549K6 Q8NBW3 Q9HC02 Q9NYE0 Q9P0V6 Q9P1J5 Q9P2H8 Q9UHG4 E2AK1_HUMAN Eukaryotic translation initiation factor 2-alpha kinase 1 2.7.11.1 Heme-controlled repressor HCR Heme-regulated eukaryotic initiation factor eIF-2-alpha kinase Heme-regulated inhibitor Hemin-sensitive initiation factor 2-alpha kinase EIF2AK1 HRI KIAA1369 PRO1362 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning of hHRI, human heme-regulated eukaryotic initiation factor 2alpha kinase: down-regulated in epithelial ovarian cancers. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Hair follicle dermal papilla Cloning and sequencing of a novel human cDNA homologous to rat hemin-sensitive initiation factor 2a kinase mRNA. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Cloning of the human heme-regulated eukaryotic initiation factor 2-alpha kinase from TNF-alpha stimulated dermal microvascular endothelial cells. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Skin Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Hypothalamus Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Amygdala Molecular cloning and sequencing of the human heme-regulated eukaryotic initiation factor 2 alpha (eIF-2 alpha) kinase from bone marrow culture. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) Bone marrow Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT ARG-558 Placenta Tongue The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Amygdala Human chromosome 7: DNA sequence and biology. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Ovary Functional prediction of the coding sequences of 121 new genes deduced by analysis of cDNA clones from human fetal liver. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 450-630 VARIANT ARG-558 Fetal liver Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase. INTERACTION WITH CDC37 AND THE HSP90 COMPLEX Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Hepatic heme-regulated inhibitor (HRI) eukaryotic initiation factor 2alpha kinase: a protagonist of heme-mediated translational control of CYP2B enzymes and a modulator of basal endoplasmic reticulum stress tone. TISSUE SPECIFICITY Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Patterns of somatic mutation in human cancer genomes. VARIANTS [LARGE SCALE ANALYSIS] THR-117; THR-132; LYS-134; SER-139; HIS-145; SER-202; LEU-292; HIS-319 AND ARG-558 Inhibits protein synthesis at the translation initiation level, in response to various stress conditions, including oxidative stress, heme deficiency, osmotic shock and heat shock. Exerts its function through the phosphorylation of EIF2S1 at 'Ser-48' and 'Ser-51', thus preventing its recycling. Binds hemin forming a 1:1 complex through a cysteine thiolate and histidine nitrogenous coordination. This binding occurs with moderate affinity, allowing it to sense the heme concentration within the cell. Thanks to this unique heme-sensing capacity, plays a crucial role to shut off protein synthesis during acute heme-deficient conditions. In red blood cells (RBCs), controls hemoglobin synthesis ensuring a coordinated regulation of the synthesis of its heme and globin moieties. Thus plays an essential protective role for RBC survival in anemias of iron deficiency. Similarly, in hepatocytes, involved in heme-mediated translational control of CYP2B and CYP3A and possibly other hepatic P450 cytochromes. May also contain ER stress during acute heme-deficient conditions (By similarity). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Induced by acute heme depletion, that not only increases EIF2AK1 protein levels, but also stimulates kinase activity by autophosphorylation. Inhibited by the heme-degradation products biliverdin and bilirubin. Induced by oxidative stress generated by arsenite treatment. Binding of nitric oxide (NO) to the heme iron in the N-terminal heme-binding domain activates the kinase activity, while binding of carbon monoxide (CO) suppresses kinase activity (By similarity). Synthesized in an inactive form that binds to the N-terminal domain of CDC37. Has to be associated with a multiprotein complex containing Hsp90, CDC37 and PPP5C for maturation and activation by autophosphorylation. The phosphatase PPP5C modulates this activation. Forms oligomers. Has been reported as a non-covalently bound homodimer, as well as a hexamer in the absence of hemin. Converted to an inactive disulfide linked homodimer in the presence of hemin (By similarity). Cytoplasm Q9BQI3-1 1 Q9BQI3-2 2 Expressed predominantly in erythroid cells. At much lower levels, expressed in hepatocytes (at protein level). Activated by autophosphorylation; phosphorylated predominantly on serine and threonine residues, but also on tyrosine residues. Autophosphorylation at Thr-488 is required for kinase activation. The active autophosphorylated form apparently is largely refractory to cellular heme fluctuations (By similarity). Can bind 1 molecules of heme per polypeptide chain. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. Translation N-terminally extended. Translation N-terminally shortened. Alternative splicing ATP-binding Complete proteome Cytoplasm Disulfide bond Kinase Nucleotide-binding Phosphoprotein Polymorphism Protein synthesis inhibitor Reference proteome Repeat Serine/threonine-protein kinase Transferase R T K T R K P S R H G S F L L H K R Q L G D PPAIDFPAE RRHRLSRR Q R I T A V T P MQGGNSGVRKREEEGDGAGAVAAPPAIDFPAEGPDPEYDESDVPAEIQVLKEPLQQPTFP FAVANQLLLVSLLEHLSHVHEPNPLRSRQVFKLLCQTFIKMGLLSSFTCSDEFSSLRLHH NRAITHLMRSAKERVRQDPCEDISRIQKIRSREVALEAQTSRYLNEFEELAILGKGGYGR VYKVRNKLDGQYYAIKKILIKGATKTVCMKVLREVKVLAGLQHPNIVGYHTAWIEHVHVI QPRADRAAIELPSLEVLSDQEEDREQCGVKNDESSSSSIIFAEPTPEKEKRFGESDTENQ NNKSVKYTTNLVIRESGELESTLELQENGLAGLSASSIVEQQLPLRRNSHLEESFTSTEE SSEENVNFLGQTEAQYHLMLHIQMQLCELSLWDWIVERNKRGREYVDESACPYVMANVAT KIFQELVEGVFYIHNMGIVHRDLKPRNIFLHGPDQQVKIGDFGLACTDILQKNTDWTNRN GKRTPTHTSRVGTCLYASPEQLEGSEYDAKSDMYSLGVVLLELFQPFGTEMERAEVLTGL RTGQLPESLRKRCPVQAKYIQHLTRRNSSQRPSAIQLLQSELFQNSGNVNLTLQMKIIEQ EKEIAELKKQLNLLSQDKGVRDDGKDGGVG H7C350 CC188_HUMAN Coiled-coil domain-containing protein 188 CCDC188 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence of human chromosome 22. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Membrane Single-pass membrane protein Coiled coil Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MEGLKTLGPCGHPHPQCPPTPASSSHGGGLDQPCQGFVGWPCLGPISSAHSVQSQRPFPV PGAGGSGPTVEGEAPGLFLSSQEQRARDTEGPRQGDLEAGLGWGWPLHPGSNQGAPRQGG SIGSGTRPCPCPPLSREGGALASPRVALSQLQCGLLGSAEQSFLQLEQENHSLKRQNQEL REQLGALLGPGQQFLPLCPEHSSCTALAWPPDPAGTQPLGNRAPLQLLRRELCQGQEAFV QQSQNELQQIRLCFERKKMVITEVWDNVAEMHMALNNQATGLLNLKKDIRGVLDQMEDIQ LEILRERAQCRTRARKEKQMASMSKGRPKLGSSKGLAGQLWLLTLRLLLGALLVWTAAYV YVVNPTPFEGLVPPLLSRATVWKLRALLDPFLRLKVDGFLPF Q15517 B0S7V2 B0UYZ7 O43509 Q5SQ85 Q5STD2 Q7LA70 Q7LA71 Q86Z04 Q8IZU4 Q8IZU5 Q8IZU6 Q8N5P3 Q95IF9 Q9NP52 Q9NPE0 Q9NPG5 Q9NRH4 Q9NRH5 Q9NRH6 Q9NRH7 Q9NRH8 Q9UBH8 Q9UIN6 Q9UIN7 Q9UIN8 Q9UIN9 Q9UIP0 CDSN_HUMAN Corneodesmosin S protein CDSN Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification in the HLA class I region of a gene expressed late in keratinocyte differentiation. NUCLEOTIDE SEQUENCE [MRNA] VARIANTS LEU-18 AND SER-143 Foreskin Expression cloning of human corneodesmosin proves its identity with the product of the S gene and allows improved characterization of its processing during keratinocyte differentiation. NUCLEOTIDE SEQUENCE [MRNA] VARIANTS SER-143 AND ALA-408 Epidermis Corneodesmosin DNA polymorphisms in MHC haplotypes and Japanese patients with psoriasis. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS LEU-18; SER-143; SER-153 DEL; PHE-202 AND LEU-410 Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANT SER-143 Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANT SER-143 The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANTS LEU-18; SER-143; SER-153 DEL; PHE-202; ALA-408; LEU-410 AND ASN-527 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANTS SER-143 AND PHE-202 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANTS LEU-18; SER-143; SER-153 DEL; PHE-202 AND LEU-410 Skin Identification of six novel polymorphisms in the human corneodesmosin gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-529 (ALLELES 1.11; 1.21; 1.31; 1.32; 1.41; 1.42; 1.43; 1.51; 1.52; 2.11; 2.21; 2.22 AND 2.23) VARIANTS PHE-56; ASN-143 DEL; ASN-150; PHE-202; GLY-401; ALA-408; LEU-410 AND ASN-527 Corneodesmosin gene polymorphism demonstrates strong linkage disequilibrium with HLA and association with psoriasis vulgaris. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-529 VARIANTS SER-143; PHE-202; GLY-401; ALA-408 AND LEU-410 ASSOCIATION WITH PSORIASIS Characterization and purification of human corneodesmosin, an epidermal basic glycoprotein associated with corneocyte-specific modified desmosomes. PARTIAL PROTEIN SEQUENCE CHARACTERIZATION VARIANT SER-143 Hypotrichosis simplex of the scalp is associated with nonsense mutations in CDSN encoding corneodesmosin. INVOLVEMENT IN HYPT2 Loss of corneodesmosin leads to severe skin barrier defect, pruritus, and atopy: unraveling the peeling skin disease. FUNCTION INVOLVEMENT IN PSS1 S gene (Corneodesmosin) diversity and its relationship to psoriasis; high content of cSNP in the HLA-linked S gene. VARIANTS PHE-202 AND LEU-410 ASSOCIATION WITH PSORIASIS Psoriasis is associated with a SNP haplotype of the corneodesmosin gene (CDSN). VARIANTS PHE-202; GLY-401; ALA-408; LEU-410 AND ASN-527 ASSOCIATION WITH PSORIASIS Important for the epidermal barrier integrity. Secreted Found in corneodesmosomes, the intercellular structures that are involved in desquamation. Exclusively expressed in skin. Genetic variation in CDSN may be associated with susceptibility to psoriasis [MIM:177900] (PubMed:10599883, PubMed:12472658,PubMed:10844560). Various CDSN alleles are known including alleles 1.11, 1.21, 1.31, 1.32, 1.41, 1.42, 1.43, 1.51, 1.52, 2.11, 2.21, 2.22 and 2.23 (PubMed:11169256). Hypotrichosis 2 HYPT2 A condition characterized by the presence of less than the normal amount of hair. Affected individuals have normal hair in early childhood but experience progressive hair loss limited to the scalp beginning in the middle of the first decade and almost complete baldness by the third decade. Body hair, beard, eyebrows, axillary hair, teeth, and nails develop normally. The disease is caused by mutations affecting the gene represented in this entry. Peeling skin syndrome 1 PSS1 A genodermatosis characterized by generalized, continuous shedding of the outer layers of the epidermis. Two main PSS subtypes have been suggested. Patients with non-inflammatory PSS (type A) manifest white scaling, with painless and easy removal of the skin, irritation when in contact with water, dust and sand, and no history of erythema, pruritis or atopy. Inflammatory PSS (type B) is associated with generalized erythema, pruritus and atopy. It is an ichthyosiform erythroderma characterized by lifelong patchy peeling of the entire skin with onset at birth or shortly after. Several patients have been reported with high IgE levels. The disease is caused by mutations affecting the gene represented in this entry. CDNS mutations are responsible for generalized, inflammatory peeling skin syndrome type B (PubMed:20691404). Translation N-terminally extended. Translation N-terminally extended. Complete proteome Direct protein sequencing Glycoprotein Hypotrichosis Polymorphism Reference proteome Secreted Signal M L L F N S G S S N S F S G S A S L D N S G S N MGSSRAPWMGRVGGHGMMALLLAGLLLPGTLAKSIGTFSDPCKDPTRITSPNDPCLTGKG DSSGFSSYSGSSSSGSSISSARSSGGGSSGSSSGSSIAQGGSAGSFKPGTGYSQVSYSSG SGSSLQGASGSSQLGSSSSHSGNSGSHSGSSSSHSSSSSSFQFSSSSFQVGNGSALPTND NSYRGILNPSQPGQSSSSSQTSGVSSSGQSVSSNQRPCSSDIPDSPCSGGPIVSHSGPYI PSSHSVSGGQRPVVVVVDQHGSGAPGVVQGPPCSNGGLPGKPCPPITSVDKSYGGYEVVG GSSDSYLVPGMTYSKGKIYPVGYFTKENPVKGSPGVPSFAAGPPISEGKYFSSNPIIPSQ SAASSAIAFQPVGTGGVQLCGGGSTGSKGPCSPSSSRVPSSSSISSSSGSPYHPCGSASQ SPCSPPGTGSFSSSSSSQSSGKIILQPCGSKSSSSGHPCMSVSSLTLTGGPDGSPHPDPS AGAKPCGSSSAGKIPCRSIRDILAQVKPLGPQLADPEVFLPQGELLDSP O95573 Q60I92 Q8IUM9 ACSL3_HUMAN Long-chain-fatty-acid--CoA ligase 3 6.2.1.3 Arachidonate--CoA ligase 6.2.1.15 Long-chain acyl-CoA synthetase 3 LACS 3 ACSL3 ACS3 FACL3 LACS3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Human acyl-coenzyme A synthetase 3 cDNA and localization of its gene (ACS3) to chromosome band 2q34-q35. NUCLEOTIDE SEQUENCE [MRNA] VARIANT SER-551 Placenta Genomic organization and transcription units of the human acyl-CoA synthetase 3 gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] VARIANT SER-551 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Pancreas Long chain acyl-CoA synthetase 3-mediated phosphatidylcholine synthesis is required for assembly of very low density lipoproteins in human hepatoma Huh7 cells. FUNCTION Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] The Sjogren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway. CATALYTIC ACTIVITY FUNCTION Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:22633490). Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) (PubMed:18003621). Has mainly an anabolic role in energy metabolism. Mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Both isoforms exhibit the same level of activity (By similarity). a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate (5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate (E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphate 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + ATP + CoA = 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoyl-CoA + AMP + diphosphate 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + ATP + CoA = 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate Mg(2+) Mitochondrion outer membrane Single-pass type III membrane protein Peroxisome membrane Single-pass type III membrane protein Microsome membrane Single-pass type III membrane protein Endoplasmic reticulum membrane Single-pass type III membrane protein Belongs to the ATP-dependent AMP-binding enzyme family. ATP-binding Complete proteome Endoplasmic reticulum Fatty acid metabolism Ligase Lipid metabolism Magnesium Membrane Microsome Mitochondrion Mitochondrion outer membrane Nucleotide-binding Peroxisome Phosphoprotein Polymorphism Reference proteome Signal-anchor Transmembrane Transmembrane helix F S E D MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPV NSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPN GKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACF MYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGK PPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMIS HSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQ SSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQI SKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTES AGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYY KNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAA LKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLK VLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK P20039 Q30006 Q9GIX8 2B1B_HUMAN HLA class II histocompatibility antigen, DRB1-11 beta chain DR-5 DR5 DRw11 MHC class II antigen DRB1*11 HLA-DRB1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete characterization and sequence of an HLA class II DR beta chain cDNA from the DR5 haplotype. NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*11:01) A novel HLA-DR beta I sequence from the DRw11 haplotype. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*11:03) Complete cDNA sequences of the HLA-DRB1*0402 and DRB1*11041 alleles. NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*11:04) HLA-DR beta-chain polymorphism. Second domain polymorphism reflects evolutionary relatedness of alleles and may explain public serologic epitopes. NUCLEOTIDE SEQUENCE [MRNA] OF 124-217 Influence of MHC class II genotype on outcome of infection with hepatitis C virus. ASSOCIATION WITH SUSCEPTIBILITY TO HEPATITIS C VIRUS Invariant chain structure and MHC class II function. REVIEW Presentation of antigens by MHC class II molecules: getting the most out of them. REVIEW Autophagy in MHC class II presentation: sampling from within. REVIEW MHC class II molecules on the move for successful antigen presentation. REVIEW MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation. UBIQUITINATION BY MARCH1 SUBCELLULAR LOCATION MHC class II transport at a glance. REVIEW CD74 in antigen presentation, inflammation, and cancers of the gastrointestinal tract. REVIEW Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading. Heterodimer of an alpha and a beta subunit; also referred as MHC class II molecule. In the endoplasmic reticulum (ER) it forms a heterononamer; 3 MHC class II molecules bind to a CD74 homotrimer (also known as invariant chain or HLA class II histocompatibility antigen gamma chain). In the endosomal/lysosomal system; CD74 undergoes sequential degradation by various proteases; leaving a small fragment termed CLIP on each MHC class II molecule. MHC class II molecule interacts with HLA_DM, and HLA_DO in B-cells, in order to release CLIP and facilitate the binding of antigenic peptides. Cell membrane Single-pass type I membrane protein Endoplasmic reticulum membrane Single-pass type I membrane protein Golgi apparatus trans-Golgi network membrane Single-pass type I membrane protein Endosome membrane Single-pass type I membrane protein Lysosome membrane Single-pass type I membrane protein Late endosome membrane Single-pass type I membrane protein The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation. Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to sorting into the endosome system and down-regulation of MHC class II. The following alleles of DRB1-11 are known: DRB1*11:01, DRB1*11:03, DRB1*11:04, DRB1*11:05, DRB1*11:06, DRB1*11:07, DRB1*11:08, DRB1*11:09, DRB1*11:10, DRB1*11:11, DRB1*11:12, DRB1*11:13, DRB1*11:14, DRB1*11:15, DRB1*11:16, DRB1*11:17, DRB1*11:18, DRB1*11:19, DRB1*11:20, DRB1*11:21, DRB1*11:22, DRB1*11:23, DRB1*11:24, DRB1*11:25, DRB1*11:26, DRB1*11:27, DRB1*11:28, DRB1*11:29, DRB1*11:30, DRB1*11:31, DRB1*11:32, DRB1*11:33, DRB1*11:34, DRB1*11:35, DRB1*11:36, DRB1*11:37, DRB1*11:38, DRB1*11:39, DRB1*11:40, DRB1*11:41, DRB1*11:42, DRB1*11:43, DRB1*11:44, DRB1*11:45, DRB1*11:46, DRB1*11:47, DRB1*11:48, DRB1*11:49, DRB1*11:50, DRB1*11:51, DRB1*11:52, DRB1*11:53, DRB1*11:54, DRB1*11:55, DRB1*11:56, DRB1*11:57, DRB1*11:58, DRB1*11:59, DRB1*11:60, DRB1*11:61, DRB1*11:62, DRB1*11:63, DRB1*11:64, DRB1*11:65, DRB1*11:66, DRB1*11:67, DRB1*11:68, DRB1*11:69, DRB1*11:70 and DRB1*11:72. The sequence shown is that of DRB1*11:01. Allele DRB1*11:01 is associated with self-limiting hepatitis C virus (HCV) infections [MIM:609532]. Belongs to the MHC class II family. 3D-structure Adaptive immunity Cell membrane Complete proteome Disulfide bond Endoplasmic reticulum Endosome Glycoprotein Golgi apparatus Immunity Isopeptide bond Lysosome Membrane MHC II Polymorphism Reference proteome Signal Transmembrane Transmembrane helix Ubl conjugation F Y R E G V MVCLRLPGGSCMAVLTVTLMVLSSPLALAGDTRPRFLEYSTSECHFFNGTERVRFLDRYF YNQEEYVRFDSDVGEFRAVTELGRPDEEYWNSQKDFLEDRRAAVDTYCRHNYGVGESFTV QRRVHPKVTVYPSKTQPLQHHNLLVCSVSGFYPGSIEVRWFRNGQEEKTGVVSTGLIHNG DWTFQTLVMLETVPRSGEVYTCQVEHPSVTSPLTVEWRARSESAQSKMLSGVGGFVLGLL FLGAGLFIYFRNQKGHSGLQPRGFLS Q9H246 B2R551 CA021_HUMAN Uncharacterized protein C1orf21 Cell proliferation-inducing gene 13 protein C1orf21 PIG13 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and characterization of 13 novel transcripts and the human RGS8 gene from the 1q25 region encompassing the hereditary prostate cancer (HPC1) locus. NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY Identification of a human cell proliferation gene 13. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Trachea The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-115 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-115 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Q8N682 DRAM1 false 3 Expressed in spleen, prostate, testis and uterus. Complete proteome Phosphoprotein Reference proteome MGCASAKHVATVQNEEEAQKGKNYQNGDVFGDEYRIKPVEEVKYMKNGAEEEQKIAARNQ ENLEKSASSNVRLKTNKEVPGLVHQPRANMHISESQQEFFRMLDEKIEKGRDYCSEEEDI T Q8WXQ8 G3V0G8 Q6ZNI6 Q86SE2 Q86XM3 Q8NA08 CBPA5_HUMAN Carboxypeptidase A5 3.4.17.- CPA5 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Mutation screening and imprinting analysis of four candidate genes for autism in the 7q32 region. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANTS SER-79; SER-336 AND ASP-338 The imprinted region on human chromosome 7q32 extends to the carboxypeptidase A gene cluster: an imprinted candidate for Silver-Russell syndrome. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Medulla oblongata Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) Testis The DNA sequence of human chromosome 7. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANTS SER-336 AND ASP-338 Testis Identification and characterization of three members of the human metallocarboxypeptidase gene family. GENE STRUCTURE Zn(2+) Binds 1 zinc ion per subunit. Secreted Q8WXQ8-1 1 Q8WXQ8-2 2 No experimental confirmation available. Q8WXQ8-3 3 No experimental confirmation available. Expression is very low or not detectable. Belongs to the peptidase M14 family. Alternative splicing Carboxypeptidase Cleavage on pair of basic residues Complete proteome Disulfide bond Hydrolase Metal-binding Metalloprotease Polymorphism Protease Reference proteome Secreted Signal Zinc Zymogen YDLAKDAVEALYKVHGIEYIFGSISTTLYVASGITVDWAYDSGIKYAFSFELRDTGQYGFLLPATQIIPTAQETWMALRTIMEHTLNHPY MWPVGSPSTGPMTVASSTPSALSSGTLGSMASCCRPHRSSPRPRRRGWRFGPSWSTP YDLAK VRLAA P S L S E D S G K R E G H R MQGTPGGGTRPGPSPVDRRTLLVFSFILAAALGQMNFTGDQVLRVLAKDEKQLSLLGDLE GLKPQKVDFWRGPARPSLPVDMRVPFSELKDIKAYLESHGLAYSIMIKDIQVLLDEERQA MAKSRRLERSTNSFSYSSYHTLEEIYSWIDNFVMEHSDIVSKIQIGNSFENQSILVLKFS TGGSRHPAIWIDTGIHSREWITHATGIWTANKIVSDYGKDRVLTDILNAMDIFIELVTNP DGFAFTHSMNRLWRKNKSIRPGIFCIGVDLNRNWKSGFGGNGSNSNPCSETYHGPSPQSE PEVAAIVNFITAHGNFKALISIHSYSQMLMYPYGRLLEPVSNQRELYDLAKDAVEALYKV HGIEYIFGSISTTLYVASGITVDWAYDSGIKYAFSFELRDTGQYGFLLPATQIIPTAQET WMALRTIMEHTLNHPY Q8IYE0 A8K8X6 Q9P223 CC146_HUMAN Coiled-coil domain-containing protein 146 CCDC146 KIAA1505 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) VARIANT SER-345 Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANT GLN-263 Testis A strategy for precise and large scale identification of core fucosylated glycoproteins. IDENTIFICATION Proteomic analysis of mammalian sperm cells identifies new components of the centrosome. SUBCELLULAR LOCATION Q96JN2-2 CCDC136 false 3 O95273 CCNDBP1 false 3 Q96L14 CEP170P1 false 3 Q9C0F1 CEP44 false 3 Q96EV8 DTNBP1 false 3 O75496 GMNN false 3 Q08379 GOLGA2 false 3 P05783 KRT18 false 3 P08727 KRT19 false 3 O76015 KRT38 false 4 Q6A162 KRT40 false 3 P43364-2 MAGEA11 false 3 P43360 MAGEA6 false 3 Q9NPJ6 MED4 false 3 Q5JR59 MTUS2 false 3 Q7Z6G3-2 NECAB2 false 3 Q9Y2I6 NINL false 3 P37198 NUP62 false 3 Q8ND90 PNMA1 false 3 P62333 PSMC6 false 3 Q6NUQ1 RINT1 false 3 O75150 RNF40 false 3 Q96KN7 RPGRIP1 false 3 Q8NA61 SPERT false 3 Q9UBB9 TFIP11 false 3 A1L306 TNR false 3 Q5VU62 TPM3 false 3 Q13077 TRAF1 false 3 P36406 TRIM23 false 3 Q9BYV2 TRIM54 false 3 Q9Y3Q8 TSC22D4 false 3 Q8N6Y0 USHBP1 false 3 Q8N1B4 VPS52 false 3 Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Centriole Localized to only one centriole identified as the mother centriole by co-staining with CEP164. Q8IYE0-1 1 Q8IYE0-2 2 No experimental confirmation available. A report observed N-glycosylation at Asn-815 (PubMed:19139490). However, as the protein is not predicted to localize in an extracellular compartment of the cell, additional evidence is required to confirm this result. Alternative splicing Coiled coil Complete proteome Cytoplasm Cytoskeleton Polymorphism Reference proteome E Q N S I T Y H M I MEDSSTDTEKEEEEEKDEKDQEPIYAIVPTINIQDERFVDLSETPAFIFLHELHAMGKLP GTRMAALKAKYTLLHDAVMSTQESEVQLLQNAKRFTEQIQQQQFHLQQADNFPEAFSTEV SKMREQLLKYQNEYNAVKEREFHNQYRLNSLKEEKIIIVKEFEKITKPGEMEKKMKILRE STEELRKEIMQKKLEIKNLREDLASKQKQLLKEQKELEELLGHQVVLKDEVAHHQTIPVQ IGKEIEKITRKKVEMEKKKIVLEQEVKTLNDSLKKVENKVSAIVDEKENVIKEVEGKRAL LEIKEREHNQLVKLLELARENEATSLTERGILDLNLRNSLIDKQNYHDELSRKQREKERD FRNLRKMELLLKVSWDALRQTQALHQRLLLEMEAIPKDDSTLSERRRELHKEVEVAKRNL AQQKIISEMESKLVEQQLAEENKLLKEQENMKELVVNLLRMTQIKIDEKEQKSKDFLKAQ QKYTNIVKEMKAKDLEIRIHKKKKCEIYRRLREFAKLYDTIRNERNKFVNLLHKAHQKVN EIKERHKMSLNELEILRNSAVSQERKLQNSMLKHANNVTIRESMQNDVRKIVSKLQEMKE KKEAQLNNIDRLANTITMIEEEMVQLRKRYEKAVQHRNESGVQLIEREEEICIFYEKINI QEKMKLNGEIEIHLLEEKIQFLKMKIAEKQRQICVTQKLLPAKRSLDADLAVLQIQFSQC TDRIKDLEKQFVKPDGENRARFLPGKDLTEKEMIQKLDKLELQLAKKEEKLLEKDFIYEQ VSRLTDRLCSKTQGCKQDTLLLAKKMNGYQRRIKNATEKMMALVAELSMKQALTIELQKE VREKEDFIFTCNSRIEKGLPLNKEIEKEWLKVLRDEEMHALAIAEKSQEFLEADNRQLPN GVYTTAEQRPNAYIPEADATLPLPKPYGALAPFKPSEPGANMRHIRKPVIKPVEI Q96PE2 B2RP20 Q86XU2 Q8N2S0 Q9Y4G3 ARHGH_HUMAN Rho guanine nucleotide exchange factor 17 164 kDa Rho-specific guanine-nucleotide exchange factor p164-RhoGEF p164RhoGEF Tumor endothelial marker 4 ARHGEF17 KIAA0337 TEM4 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cell surface tumor endothelial markers are conserved in mice and humans. NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Colon Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-401 Embryo Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 455-2063 Brain A mammalian Rho-specific guanine-nucleotide exchange factor (p164-RhoGEF) without a pleckstrin homology domain. FUNCTION TISSUE SPECIFICITY A quantitative atlas of mitotic phosphorylation. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410; SER-420; SER-735 AND SER-914 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND SER-546 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. Highly expressed in the heart. ARHGEF17 Complete proteome Guanine-nucleotide releasing factor Phosphoprotein Polymorphism Reference proteome G E A D L F MADGAPRPQLYRSVSFKLLERWSGGPGLREEDTDTPGLRRRASCRPTTAARGQPSRRVSK LASGPLAAPAQPRPLRSLSPSVRQLSRRFDAPRLDDGSAGTRDGGVLPAAAEEAAEGPAR GAWPSVTEMRKLFGGPGSRRPSADSESPGTPSPDGAAWEPPARESRQPPTPPPRTCFPLA GLRSARPLTGPETEGRLRRPQQQQERAQRPADGLHSWHIFSQPQAGARASCSSSSIAASY PVSRSRAASSSEEEEEGPPQLPGAQSPAYHGGHSSGSDDDRDGEGGHRWGGRPGLRPGSS LLDQDCRPDSDGLNLSSMNSAGVSGSPEPPTSPRAPREEGLREWGSGSPPCVPGPQEGLR PMSDSVGGAFRVAKVSFPSYLASPAGSRGSSRYSSTETLKDDDLWSSRGSGGWGVYRSPS FGAGEGLLRSQARTRAKGPGGTSRALRDGGFEPEKSRQRKSLSNPDIASETLTLLSFLRS DLSELRVRKPGGSSGDRGSNPLDGRDSPSAGGPVGQLEPIPIPAPASPGTRPTLKDLTAT LRRAKSFTCSEKPMARRLPRTSALKSSSSELLLTGPGAEEDPLPLIVQDQYVQEARQVFE KIQRMGAQQDDGSDAPPGSPDWAGDVTRGQRSQEELSGPESSLTDEGIGADPEPPVAAFC GLGTTGMWRPLSSSSAQTNHHGPGTEDSLGGWALVSPETPPTPGALRRRRKVPPSGSGGS ELSNGEAGEAYRSLSDPIPQRHRAATSEEPTGFSVDSNLLGSLSPKTGLPATSAMDEGLT SGHSDWSVGSEESKGYQEVIQSIVQGPGTLGRVVDDRIAGKAPKKKSLSDPSRRGELAGP GFEGPGGEPIREVEPMLPPSSSEPILVEQRAEPEEPGATRSRAQSERALPEALPPPATAH RNFHLDPKLADILSPRLIRRGSKKRPARSSHQELRRDEGSQDQTGSLSRARPSSRHVRHA SVPATFMPIVVPEPPTSVGPPVAVPEPIGFPTRAHPTLQAPSLEDVTKQYMLNLHSGEVP APVPVDMPCLPLAAPPSAEAKPPEAARPADEPTPASKCCSKPQVDMRKHVAMTLLDTEQS YVESLRTLMQGYMQPLKQPENSVLCDPSLVDEIFDQIPELLEHHEQFLEQVRHCMQTWHA QQKVGALLVQSFSKDVLVNIYSAYIDNFLNAKDAVRVAKEARPAFLKFLEQSMRENKEKQ ALSDLMIKPVQRIPRYELLVKDLLKHTPEDHPDHPLLLEAQRNIKQVAERINKGVRSAEE AERHARVLQEIEAHIEGMEDLQAPLRRFLRQEMVIEVKAIGGKKDRSLFLFTDLIVCTTL KRKSGSLRRSSMSLYTAASVIDTASKYKMLWKLPLEDADIIKGASQATNRENIQKAISRL DEDLTTLGQMSKLSESLGFPHQSLDDALRDLSAAMHRDLSEKQALCYALSFPPTKLELCA TRPEGTDSYIFEFPHPDARLGFEQAFDEAKRKLASSKSCLDPEFLKAIPIMKTRSGMQFS CAAPTLNSCPEPSPEVWVCNSDGYVGQVCLLSLRAEPDVEACIAVCSARILCIGAVPGLQ PRCHREPPPSLRSPPETAPEPAGPELDVEAAADEEAATLAEPGPQPCLHISIAGSGLEMT PGLGEGDPRPELVPFDSDSDDESSPSPSGTLQSQASRSTISSSFGNEETPSSKEATAETT SSEEEQEPGFLPLSGSFGPGGPCGTSPMDGRALRRSSHGSFTRGSLEDLLSVDPEAYQSS VWLGTEDGCVHVYQSSDSIRDRRNSMKLQHAASVTCILYLNNQVFVSLANGELVVYQREA GHFWDPQNFKSVTLGTQGSPITKMVSVGGRLWCGCQNRVLVLSPDTLQLEHMFYVGQDSS RCVACMVDSSLGVWVTLKGSAHVCLYHPDTFEQLAEVDVTPPVHRMLAGSDAIIRQHKAA CLRITALLVCEELLWVGTSAGVVLTMPTSPGTVSCPRAPLSPTGLGQGHTGHVRFLAAVQ LPDGFNLLCPTPPPPPDTGPEKLPSLEHRDSPWHRGPAPARPKMLVISGGDGYEDFRLSS GGGSSSETVGRDDSTNHLLLWRV O95841 Q5T5Z5 ANGL1_HUMAN Angiopoietin-related protein 1 Angiopoietin-3 ANG-3 Angiopoietin-like protein 1 ANGPTL1 ANG3 ANGPT3 ARP1 PSEC0154 UNQ162/PRO188 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning and characterization of a novel angiopoietin family protein, angiopoietin-3. NUCLEOTIDE SEQUENCE [MRNA] SUBCELLULAR LOCATION TISSUE SPECIFICITY Heart The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Ovary Secreted Highly expressed in adrenal gland, placenta, thyroid gland, heart, skeletal muscle and small intestine. Weakly expressed in testis, ovary, colon, pancreas, kidney and stomach. Coiled coil Complete proteome Disulfide bond Glycoprotein Reference proteome Secreted Signal MKTFTWTLGVLFFLLVDTGHCRGGQFKIKKINQRRYPRATDGKEEAKKCAYTFLVPEQRI TGPICVNTKGQDASTIKDMITRMDLENLKDVLSRQKREIDVLQLVVDVDGNIVNEVKLLR KESRNMNSRVTQLYMQLLHEIIRKRDNSLELSQLENKILNVTTEMLKMATRYRELEVKYA SLTDLVNNQSVMITLLEEQCLRIFSRQDTHVSPPLVQVVPQHIPNSQQYTPGLLGGNEIQ RDPGYPRDLMPPPDLATSPTKSPFKIPPVTFINEGPFKDCQQAKEAGHSVSGIYMIKPEN SNGPMQLWCENSLDPGGWTVIQKRTDGSVNFFRNWENYKKGFGNIDGEYWLGLENIYMLS NQDNYKLLIELEDWSDKKVYAEYSSFRLEPESEFYRLRLGTYQGNAGDSMMWHNGKQFTT LDRDKDMYAGNCAHFHKGGWWYNACAHSNLNGVWYRGGHYRSKHQDGIFWAEYRGGSYSL RAVQMMIKPID Q8WZB0 CI130_HUMAN Putative uncharacterized protein encoded by LINC00476 Nasopharyngeal carcinoma-associated gene 12 protein LINC00476 C9orf130 NAG12 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo NUCLEOTIDE SEQUENCE [MRNA] DNA sequence and analysis of human chromosome 9. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Product of a dubious CDS prediction. May be a non-coding RNA. Complete proteome Reference proteome MAANATSGRPPSIALRQPEATGWRRGIPAKVATKGTQAEREGDVRSGGRARGRCVRLAKR CSPSSLGLRRRRRRTGGRQGDPQIFLGSDFRLLTPANSNPVLENPARTGSRIVIGISRER NLPFCGRSNLPDVSSL Q96F63 Q658N6 Q96IF3 CCD97_HUMAN Coiled-coil domain-containing protein 97 CCDC97 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-343 Stomach A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-337 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-275 AND SER-337 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Acetylation Coiled coil Complete proteome Phosphoprotein Reference proteome MEAVATATAAKEPDKGCIEPGPGHWGELSRTPVPSKPQDKVEAAEATPVALDSDTSGAEN AAVSAMLHAVAASRLPVCSQQQGEPDLTEHEKVAILAQLYHEKPLVFLERFRTGLREEHL ACFGHVRGDHRADFYCAEVARQGTARPRTLRTRLRNRRYAALRELIQGGEYFSDEQMRFR APLLYEQYIGQYLTQEELSARTPTHQPPKPGSPGRPACPLSNLLLQSYEERELQQRLLQQ QEEEEACLEEEEEEEDSDEEDQRSGKDSEAWVPDSEERLILREEFTSRMHQRFLDGKDGD FDYSTVDDNPDFDNLDIVARDEEERYFDEEEPEDAPSPELDGD Q6E213 Q6IEE3 Q6P437 AWAT2_HUMAN Acyl-CoA wax alcohol acyltransferase 2 2.3.1.75 11-cis-specific retinyl-ester synthase 11-cis-RE-synthase Acyl-CoA retinol O-fatty-acyltransferase ARAT Retinol O-fatty-acyltransferase 2.3.1.76 Diacylglycerol O-acyltransferase 2-like protein 4 Diacylglycerol O-acyltransferase candidate 4 hDC4 Long-chain-alcohol O-fatty-acyltransferase 2 Multifunctional O-acyltransferase Wax synthase hWS AWAT2 DC4 DGAT2L4 MFAT WS Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family. NUCLEOTIDE SEQUENCE [MRNA] FUNCTION CATALYTIC ACTIVITY TISSUE SPECIFICITY The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-333 Skin Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. IDENTIFICATION Identification of two novel human Acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily. FUNCTION CATALYTIC ACTIVITY TISSUE SPECIFICITY A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters. CATALYTIC ACTIVITY FUNCTION TISSUE SPECIFICITY Identification of the 11-cis-specific retinyl-ester synthase in retinal Mueller cells as multifunctional O-acyltransferase (MFAT). FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases. FUNCTION CATALYTIC ACTIVITY Acyltransferase that catalyzes the formation of ester bonds between fatty alcohols and fatty acyl-CoAs to form wax monoesters (PubMed:15220349, PubMed:15671038, PubMed:16106050, PubMed:28420705). Shows a preference for medium chain acyl-CoAs from C12 to C16 in length and fatty alcohols shorter than C20, as the acyl donors and acceptors, respectively (PubMed:15220349, PubMed:15671038). Also possesses acyl-CoA retinol acyltransferase (ARAT) activity that catalyzes 11-cis-specific retinyl ester synthesis (PubMed:16106050, PubMed:24799687). Shows higher catalytic efficiency toward 11-cis-retinol versus 9-cis-retinol, 13-cis-retinol, and all-trans-retinol substrates (PubMed:24799687). a long chain fatty alcohol + an acyl-CoA = a wax ester + CoA all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CoA 2-(9Z-octadecenoyl)-glycerol + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CoA 1,2-di-(9Z-octadecenoyl)-sn-glycerol + hexadecanoyl-CoA = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + CoA hexadecan-1-ol + hexadecanoyl-CoA = CoA + hexadecanyl hexadecanoate hexadecane-1,2-diol + hexadecanoyl-CoA = 2-hydroxyhexadecyl hexadecanoate + CoA all-trans-retinol + hexadecanoyl-CoA = all-trans-retinyl hexadecanoate + CoA (9Z)-octadecenoyl-CoA + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + CoA (9Z)-octadecenoyl-CoA + hexadecan-1-ol = CoA + hexadecanyl (9Z)-octadecenoate (9Z)-hexadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-hexadecenyl (9Z)-octadecenoate + CoA (9Z)-octadecenoyl-CoA + octadecan-1-ol = 1-O-octadecyl (9Z)-octadecenoate + CoA (9Z)-octadecen-1-ol + (9Z)-octadecenoyl-CoA = 1-O-(9Z)-octadecenyl (9Z)-octadecenoate + CoA (9Z)-hexadecenoyl-CoA + hexadecan-1-ol = 1-O-hexadecyl (9Z)-hexadecenoate + CoA hexadecan-1-ol + octadecanoyl-CoA = CoA + hexadecanyl octadecanoate 11-cis-retinol + hexadecanoyl-CoA = 11-cis-retinyl hexadecanoate + CoA (9Z)-octadecenoyl-CoA + 1-O-(9Z-octadecenyl)-glycerol = 1-O-(9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol + CoA (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoA 11-cis-retinol + tetradecanoyl-CoA = 11-cis-retinyl tetradecanoate + CoA 9-cis-retinol + tetradecanoyl-CoA = 9-cis-retinyl tetradecanoate + CoA 13-cis-retinol + tetradecanoyl-CoA = 13-cis-retinyl tetradecanoate + CoA all-trans-retinol + tetradecanoyl-CoA = all-trans-retinyl tetradecanoate + CoA tetradecan-1-ol + tetradecanoyl-CoA = CoA + tetradecanyl tetradecanoate 11-cis retinoids act as allosteric modulators of acyl-CoA retinol O-fatty-acyltransferase (ARAT) activity by suppressing esterification of 9-cis, 13-cis, or all-trans retinols concurrently increasing the enzyme specificity toward 11-cis isomer. 5.8 uM for 11-cis-retinol 19.8 uM for 9-cis-retinol 27.4 uM for 13-cis-retinol 24.8 uM for all-trans-retinol 980 pmol/min/mg enzyme for 11-cis-retinol 1010 pmol/min/mg enzyme for 9-cis-retinol 6.4 pmol/min/mg enzyme for 13-cis-retinol 148 pmol/min/mg enzyme for all-trans-retinol Monomer. Endoplasmic reticulum membrane Multi-pass membrane protein Highly expressed in skin, where it is primarily restricted to undifferentiated peripheral sebocytes. Also expressed at lower level in other tissues except pancreas. Belongs to the diacylglycerol acyltransferase family. Acyltransferase Complete proteome Endoplasmic reticulum Lipid biosynthesis Lipid metabolism Membrane Reference proteome Transferase Transmembrane Transmembrane helix MLLPSKKDLKTALDVFAVFQWSFSALLITTTVIAVNLYLVVFTPYWPVTVLILTWLAFDW KTPQRGGRRFTCVRHWRLWKHYSDYFPLKLLKTHDICPSRNYILVCHPHGLFAHGWFGHF ATEASGFSKIFPGITPYILTLGAFFWMPFLREYVMSTGACSVSRSSIDFLLTHKGTGNMV IVVIGGLAECRYSLPGSSTLVLKNRSGFVRMALQHGVPLIPAYAFGETDLYDQHIFTPGG FVNRFQKWFQSMVHIYPCAFYGRGFTKNSWGLLPYSRPVTTIVGEPLPMPKIENPSQEIV AKYHTLYIDALRKLFDQHKTKFGISETQELEII P04222 O62883 O78060 O78068 O78069 P30503 Q29743 Q29992 Q29993 Q9GIK8 Q9TQB4 1C03_HUMAN HLA class I histocompatibility antigen, Cw-3 alpha chain MHC class I antigen Cw*3 HLA-C HLAC Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete nucleotide sequence of a gene encoding a functional human class I histocompatibility antigen (HLA-CW3). NUCLEOTIDE SEQUENCE (ALLELE CW*03:04) The molecular basis for reactivity of anti-Cw1 and anti-Cw3 alloantisera with HLA-B46 haplotypes. NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*03:02) NUCLEOTIDE SEQUENCE (ALLELES CW*03:03 AND CW*03:04) DNA typing of HLA-C locus alleles in Japanese. NUCLEOTIDE SEQUENCE (ALLELE CW*03:03) Peripheral blood Correction of the HLA-Cw3 genomic sequence tentatively identifies it as HLA-Cw*0304. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-206 (ALLELE CW*03:04) Sequencing based typing for HLA-C. Identification of three new alleles: Cw*0307, Cw*0502 and Cw*0504. NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE CW*03:07) Sequence-based typing provides a new look at HLA-C diversity. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES CW*03:05; CW*03:06; CW*03:08 AND CW*03:09) Sequence of two new HLA-Cw alleles: HLA-Cw*0313 and HLA-Cw*1208. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CW*03:13) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand. X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-302 IN COMPLEX WITH KIR2DL2 DISULFIDE BONDS N-terminome analysis of the human mitochondrial proteome. VARIANT [LARGE SCALE ANALYSIS] MET-272 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in the presentation of foreign antigens to the immune system. Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). P43628 KIR2DL3 false 3 Membrane Single-pass type I membrane protein Polyubiquitinated in a post ER compartment by interaction with human herpesvirus 8 MIR1 protein. This targets the protein for rapid degradation via the ubiquitin system (By similarity). The following alleles of Cw-3 are known: Cw*03:02 (Cw3.2), Cw*03:03, Cw*03:04 (Cw3.1), Cw*03:05, Cw*03:06, Cw*03:07, Cw*03:08, Cw*03:09 and Cw*03:13. The sequence shown is that of Cw*03:04. Belongs to the MHC class I family. 3D-structure Complete proteome Disulfide bond Glycoprotein Immunity Membrane MHC I Polymorphism Reference proteome Signal Transmembrane Transmembrane helix Ubl conjugation A E V M K N S N N K G R I T I L R S V L D V Y S V M Y C AA DE QE RK R P Y H D N R G MRVMAPRTLILLLSGALALTETWAGSHSMRYFYTAVSRPGRGEPHFIAVGYVDDTQFVRF DSDAASPRGEPRAPWVEQEGPEYWDRETQKYKRQAQTDRVSLRNLRGYYNQSEAGSHIIQ RMYGCDVGPDGRLLRGYDQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQL RAYLEGLCVEWLRRYLKNGKETLQRAEHPKTHVTHHPVSDHEATLRCWALGFYPAEITLT WQWDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWEP SSQPTIPIVGIVAGLAVLAVLAVLGAVVAVVMCRRKSSGGKGGSCSQAASSNSAQGSDES LIACKA P16152 B2RBZ7 B4DFK7 Q3LHW8 CBR1_HUMAN Carbonyl reductase [NADPH] 1 1.1.1.184 15-hydroxyprostaglandin dehydrogenase [NADP(+)] 1.1.1.197 NADPH-dependent carbonyl reductase 1 Prostaglandin 9-ketoreductase Prostaglandin-E(2) 9-reductase 1.1.1.189 Short chain dehydrogenase/reductase family 21C member 1 CBR1 CBR CRN SDR21C1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Human carbonyl reductase. Nucleotide sequence analysis of a cDNA and amino acid sequence of the encoded protein. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) PARTIAL PROTEIN SEQUENCE Placenta Induction of a human carbonyl reductase gene located on chromosome 21. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) PARTIAL PROTEIN SEQUENCE Mammary gland Genomic sequence and expression of a cloned human carbonyl reductase gene with daunorubicin reductase activity. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1) Mapping of a novel human carbonyl reductase, CBR3, and ribosomal pseudogenes to human chromosome 21q22.2. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1) Human fetal brain carbonyl reductases. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Fetal brain Cloning of human full-length CDSs in BD Creator(TM) system donor vector. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Hippocampus NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1) VARIANT SER-131 The DNA sequence of human chromosome 21. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Skin Carboxyethyllysine in a protein: native carbonyl reductase/NADP(+)-dependent prostaglandin dehydrogenase. PARTIAL PROTEIN SEQUENCE POST-TRANSLATIONAL MODIFICATION AT LYS-239 Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER). ACTIVITY REGULATION FUNCTION Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] An unbiased cell morphology-based screen for new, biologically active small molecules. X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 2-276 IN COMPLEX WITH THE SYNTHETIC INHIBITOR HYDROXY-PP AND NADP IDENTIFICATION BY MASS SPECTROMETRY PARTIAL PROTEIN SEQUENCE FUNCTION Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct. X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP AND FORMALDEHYDE-GLUTATHIONE ADDUCT FUNCTION Human carbonyl reductase 1 is an S-nitrosoglutathione reductase. X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP SUBSTRATE ANALOGS FUNCTION BIOPHYSICOCHEMICAL PROPERTIES A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity. VARIANT ILE-88 CHARACTERIZATION OF VARIANT ILE-88 BIOPHYSICOCHEMICAL PROPERTIES ACTIVITY REGULATION NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione. a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH NADP(+) + prostaglandin F2alpha = H(+) + NADPH + prostaglandin E2 NADP(+) + prostaglandin E1 = 15-oxo-prostaglandin E1 + H(+) + NADPH Inhibited by quercetin, rutenin and its derivatives. 30 uM for S-nitrosoglutathione 22 uM for menadione 309 uM for prostaglandin E2 173 uM for daunorubicin 247 uM for NADPH Monomer. Cytoplasm P16152-1 1 P16152-2 2 No experimental confirmation available. Belongs to the short-chain dehydrogenases/reductases (SDR) family. 3D-structure Acetylation Alternative splicing Complete proteome Cytoplasm Direct protein sequencing NADP Oxidoreductase Phosphoprotein Polymorphism Reference proteome GRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMN ASCVLSAWSCLSQNPSGGKSKPLAWFTEMSIICRCLTLGPF V I P S MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFH QLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRD VCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTK KGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKA TKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW P07311 A6NDV8 B2R590 ACYP1_HUMAN Acylphosphatase-1 3.6.1.7 Acylphosphatase, erythrocyte isozyme Acylphosphatase, organ-common type isozyme Acylphosphate phosphohydrolase 1 ACYP1 ACYPE Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Placenta Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis The DNA sequence and analysis of human chromosome 14. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Embryonic carcinoma Mammary gland A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure. PROTEIN SEQUENCE OF 2-99 CLEAVAGE OF INITIATOR METHIONINE ACETYLATION AT ALA-2 Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase. PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 10-86 Placenta Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase. X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) Rational stabilization of enzymes by computational redesign of surface charge-charge interactions. STRUCTURE BY NMR OF 2-99 Its physiological role is not yet clear. an acyl phosphate + H2O = a carboxylate + H(+) + phosphate P07311-1 1 P07311-2 2 No experimental confirmation available. Organ-common type isozyme is found in many different tissues. Belongs to the acylphosphatase family. 3D-structure Acetylation Alternative splicing Complete proteome Direct protein sequencing Hydrolase Reference proteome AEGKKLGLVGWVQNTDRGTVQGQLQGPISKVRHMQEWLETRGSPKSHIDKANFNNEKVILKLDYSDFQIVK EMTVENRIAETHSKSCVPVSFATSYAG MAEGNTLISVDYEIFGKVQGVFFRKHTQAEGKKLGLVGWVQNTDRGTVQGQLQGPISKVR HMQEWLETRGSPKSHIDKANFNNEKVILKLDYSDFQIVK Q6L9W6 Q6ZNC1 Q8N7T6 B4GN3_HUMAN Beta-1,4-N-acetylgalactosaminyltransferase 3 B4GalNAcT3 Beta4GalNAc-T3 Beta4GalNAcT3 2.4.1.244 Beta-1,4-N-acetylgalactosaminyltransferase III N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 2 NGalNAc-T2 B4GALNT3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning and characterization of a novel human beta 1,4-N-acetylgalactosaminyltransferase, beta 4GalNAc-T3, responsible for the synthesis of N,N'-diacetyllactosediamine, galNAc beta 1-4GlcNAc. NUCLEOTIDE SEQUENCE [MRNA] CATALYTIC ACTIVITY TISSUE SPECIFICITY VARIANT ARG-411 Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 540-998 Testis Tongue The finished DNA sequence of human chromosome 12. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Apical Golgi localization of N,N'-diacetyllactosediamine synthase, beta4GalNAc-T3, is responsible for LacdiNAc expression on gastric mucosa. FUNCTION SUBCELLULAR LOCATION Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked glycans and probably O-linked glycans. Mediates the N,N'-diacetyllactosediamine formation on gastric mucosa. an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP Golgi apparatus Golgi stack membrane Single-pass type II membrane protein Localizes to apical Golgi. Highly expressed in testis, colon and stomach. Weakly expressed in other tissues. Belongs to the chondroitin N-acetylgalactosaminyltransferase family. Translation N-terminally extended. Probable intron retention. Complete proteome Golgi apparatus Membrane Polymorphism Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix G S R Q K R R Q R H MGSPRAARPPLLLRPVKLLRRRFRLLLALAVVSVGLWTLYLELVASAQVGGNPLNRRYGS WRELAKALASRNIPAVDPHLQFYHPQRLSLEDHDIDQGVSSNSSYLKWNKPVPWLSEFRG RANLHVFEDWCGSSIQQLRRNLHFPLYPHIRTTLRKLAVSPKWTNYGLRIFGYLHPFTDG KIQFAIAADDNAEFWLSLDDQVSGLQLLASVGKTGKEWTAPGEFGKFRSQISKPVSLSAS HRYYFEVLHKQNEEGTDHVEVAWRRNDPGAKFTIIDSLSLSLFTNETFLQMDEVGHIPQT AASHVDSSNALPRDEQPPADMLRPDPRDTLYRVPLIPKSHLRHVLPDCPYKPSYLVDGLP LQRYQGLRFVHLSFVYPNDYTRLSHMETHNKCFYQENAYYQDRFSFQEYIKIDQPEKQGL EQPGFEENLLEESQYGEVAEETPASNNQNARMLEGRQTPASTLEQDATDYRLRSLRKLLA QPREGLLAPFSKRNSTASFPGRTSHIPVQQPEKRKQKPSPEPSQDSPHSDKWPPGHPVKN LPQMRGPRPRPAGDSPRKTQWLNQVESYIAEQRRGDRMRPQAPGRGWHGEEEVVAAAGQE GQVEGEEEGEEEEEEEDMSEVFEYVPVFDPVVNWDQTFSARNLDFQALRTDWIDLSCNTS GNLLLPEQEALEVTRVFLKKLNQRSRGRYQLQRIVNVEKRQDQLRGGRYLLELELLEQGQ RVVRLSEYVSARGWQGIDPAGGEEVEARNLQGLVWDPHNRRRQVLNTRAQEPKLCWPQGF SWSHRAVVHFVVPVKNQARWVQQFIKDMENLFQVTGDPHFNIVITDYSSEDMDVEMALKR SKLRSYQYVKLSGNFERSAGLQAGIDLVKDPHSIIFLCDLHIHFPAGVIDAIRKHCVEGK MAFAPMVMRLHCGATPQWPEGYWEVNGFGLLGIYKSDLDRIGGMNTKEFRDRWGGEDWEL LDRILQAGLDVERLSLRNFFHHFHSKRGMWSRRQMKTL Q14CZ0 CP072_HUMAN UPF0472 protein C16orf72 C16orf72 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-212 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia Q8IZU0 FAM9B false 4 Belongs to the UPF0472 family. Complete proteome Phosphoprotein Polymorphism Reference proteome N S MEERKEEGEAEIQEHGPEHWFSKWERQCLAEAEQDEQLPPELQEEAAAAAQPEHKQQKLW HLFQNSATAVAQLYKDRVCQQPGLSLWVPFQNAATAVTNLYKESVDTHQRSFDIGIQIGY QRRNKDVLAWVKKRRRTIRREDLISFLCGKVPPPRNSRAPPRLTVVSPNRATSTETSSSV ETDLQPFREAIALHGLSGAMASISVRSSTPGSPTHVSSGSNASRRRNGLHDVDLNTFISE EMALHLDNGGTRKRTSAQCGDVITDSPTHKRNRMI Q8NE62 Q9NY17 CHDH_HUMAN Choline dehydrogenase, mitochondrial CDH CHD 1.1.99.1 CHDH Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence, annotation and analysis of human chromosome 3. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT ARG-78 Testis Analysis of a putative tumor suppressor gene region of 100 kb at chromosome 3p21.1 in conventional renal cell carcinoma. NUCLEOTIDE SEQUENCE [MRNA] OF 113-594 Kidney An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver A + choline = AH2 + betaine aldehyde FAD Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Q7Z3S9 NOTCH2NLA false 3 Mitochondrion inner membrane Belongs to the GMC oxidoreductase family. Acetylation Complete proteome FAD Flavoprotein Membrane Mitochondrion Mitochondrion inner membrane Oxidoreductase Polymorphism Reference proteome Transit peptide E A L R N S R A MWCLLRGLGRPGALARGALGQQQSLGARALASAGSESRDEYSYVVVGAGSAGCVLAGRLT EDPAERVLLLEAGPKDVLAGSKRLSWKIHMPAALVANLCDDRYNWCYHTEVQRGLDGRVL YWPRGRVWGGSSSLNAMVYVRGHAEDYERWQRQGARGWDYAHCLPYFRKAQGHELGASRY RGADGPLRVSRGKTNHPLHCAFLEATQQAGYPLTEDMNGFQQEGFGWMDMTIHEGKRWSA ACAYLHPALSRTNLKAEAETLVSRVLFEGTRAVGVEYVKNGQSHRAYASKEVILSGGAIN SPQLLMLSGIGNADDLKKLGIPVVCHLPGVGQNLQDHLEIYIQQACTRPITLHSAQKPLR KVCIGLEWLWKFTGEGATAHLETGGFIRSQPGVPHPDIQFHFLPSQVIDHGRVPTQQEAY QVHVGPMRGTSVGWLKLRSANPQDHPVIQPNYLSTETDIEDFRLCVKLTREIFAQEALAP FRGKELQPGSHIQSDKEIDAFVRAKADSAYHPSCTCKMGQPSDPTAVVDPQTRVLGVENL RVVDASIMPSMVSGNLNAPTIMIAEKAADIIKGQPALWDKDVPVYKPRTLATQR Q16678 Q5TZW8 Q93089 Q9H316 CP1B1_HUMAN Cytochrome P450 1B1 1.14.14.- CYPIB1 Hydroperoxy icosatetraenoate dehydratase 4.2.1.152 CYP1B1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2. NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY INDUCTION Isolation and characterization of the human cytochrome P450 CYP1B1 gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Physical/genetic map of the 2p22-2p21 region on chromosome 2. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Cloning of human full-length CDSs in BD Creator(TM) system donor vector. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT SER-453 NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS GLY-48; SER-119; ASN-206; LEU-266; VAL-432 AND SER-453 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Lung NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112 VARIANT GLY-48 Catalytic properties of polymorphic human cytochrome P450 1B1 variants. FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES CHARACTERIZATION OF VARIANTS SER-119 AND VAL-432 Biosynthesis of all-trans-retinoic acid from all-trans-retinol: catalysis of all-trans-retinol oxidation by human P-450 cytochromes. FUNCTION CATALYTIC ACTIVITY PATHWAY BIOPHYSICOCHEMICAL PROPERTIES Role of human cytochrome P450 1A1, 1A2, 1B1, and 3A4 in the 2-, 4-, and 16alpha-hydroxylation of 17beta-estradiol. FUNCTION CATALYTIC ACTIVITY PATHWAY Characterization of the oxidative metabolites of 17beta-estradiol and estrone formed by 15 selectively expressed human cytochrome p450 isoforms. FUNCTION CATALYTIC ACTIVITY PATHWAY Metabolism of retinoids and arachidonic acid by human and mouse cytochrome P450 1b1. FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES PATHWAY CYP1B1 expression promotes the proangiogenic phenotype of endothelium through decreased intracellular oxidative stress and thrombospondin-2 expression. FUNCTION IN VASCULAR DEVELOPMENT AND ANGIOGENESIS TISSUE SPECIFICITY Analysis of epoxyeicosatrienoic acids by chiral liquid chromatography/electron capture atmospheric pressure chemical ionization mass spectrometry using [13C]-analog internal standards. FUNCTION CATALYTIC ACTIVITY PATHWAY Human CYP2S1 metabolizes cyclooxygenase- and lipoxygenase-derived eicosanoids. FUNCTION CATALYTIC ACTIVITY Increase of human CYP1B1 activities by acidic phospholipids and kinetic deuterium isotope effects on CYP1B1 substrate oxidation. CATALYTIC ACTIVITY ACTIVITY REGULATION FUNCTION The citrus flavanone naringenin suppresses CYP1B1 transactivation through antagonising xenobiotic-responsive element binding. ACTIVITY REGULATION Specificity determinants of CYP1B1 estradiol hydroxylation. FUNCTION CATALYTIC ACTIVITY ACTIVITY REGULATION MUTAGENESIS OF VAL-395 Structural characterization of the complex between alpha-naphthoflavone and human cytochrome P450 1B1. X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 51-543 IN COMPLEX WITH HEME AND THE INHIBITOR ALPHA-NAPHTOFLAVONE COFACTOR Mutations in CYP1B1, the gene for cytochrome P4501B1, are the predominant cause of primary congenital glaucoma in Saudi Arabia. VARIANTS GLC3A GLU-61; ASN-374 AND TRP-469 Sequence analysis and homology modeling suggest that primary congenital glaucoma on 2p21 results from mutations disrupting either the hinge region or the conserved core structures of cytochrome P4501B1. VARIANT GLC3A TRP-365 VARIANTS CYS-57; GLU-61; TRP-365; LEU-379; LYS-387; HIS-390; VAL-432; LEU-437 AND TRP-469 Association of cytochrome P450 1B1 (CYP1B1) polymorphism with steroid receptor status in breast cancer. VARIANTS VAL-432 AND SER-453 ERRATUM Identification of a single ancestral CYP1B1 mutation in Slovak Gypsies (Roms) affected with primary congenital glaucoma. VARIANT GLC3A LYS-387 Multiple CYP1B1 mutations and incomplete penetrance in an inbred population segregating primary congenital glaucoma suggest frequent de novo events and a dominant modifier locus. VARIANTS GLC3A GLU-61; PRO-77; 269-SER--PHE-271 DEL; HIS-368; ASN-374; SER-390 AND TRP-469 VARIANTS GLY-48; SER-119; VAL-432 AND SER-453 ERRATUM Novel compound heterozygous mutations in the cytochrome P4501B1 gene (CYP1B1) in a Japanese patient with primary congenital glaucoma. VARIANT GLC3A MET-364 Association of CYP1B1 genetic polymorphism with incidence to breast and lung cancer. VARIANTS SER-119 AND VAL-432 ASSOCIATION WITH BREAST OR LUNG CANCER Novel cytochrome P4501B1 (CYP1B1) gene mutations in Japanese patients with primary congenital glaucoma. VARIANTS GLC3A VAL-192; ILE-198; LEU-320; PHE-330; MET-364; GLN-444 AND GLY-499 VARIANTS GLY-48; SER-119 AND VAL-432 ERRATUM Phenotypic heterogeneity of CYP1B1: mutations in a patient with Peters' anomaly. INVOLVEMENT IN ASGD6 Digenic inheritance of early-onset glaucoma: CYP1B1, a potential modifier gene. VARIANT GLC3A PHE-345 VARIANT GLC1A HIS-368 VARIANT VAL-432 Identification of novel mutations causing familial primary congenital glaucoma in Indian pedigrees. VARIANTS GLC3A GLU-61; LEU-193; LYS-229 AND HIS-368 VARIANTS GLY-48; SER-184 AND VAL-432 Molecular genetics of primary congenital glaucoma in Brazil. VARIANTS GLC3A HIS-368; LYS-387; LEU-437 AND GLY-443 VARIANTS GLY-48; SER-119; VAL-432 AND SER-453 Functional analysis of six different polymorphic CYP1B1 enzyme variants found in an Ethiopian population. VARIANTS GLY-48; SER-119; VAL-432; GLY-443 AND SER-453 Gene symbol: CYP1B1. Disease: glaucoma, primary congenital. VARIANTS GLC3A ARG-144 AND CYS-445 Novel cytochrome P450 1B1 (CYP1B1) mutations in patients with primary congenital glaucoma in France. VARIANTS GLC3A LYS-229; ARG-232; LYS-387; SER-390; SER-399 AND TYR-423 VARIANTS GLY-48; SER-119; VAL-432 AND SER-453 CYP1B1 gene analysis in primary congenital glaucoma in Indonesian and European patients. VARIANTS GLC3A ILE-215; 355-ARG--ALA-358 DEL AND MET-364 VARIANTS GLY-48; SER-119; VAL-432 AND SER-453 CYP1B1 mutations in French patients with early-onset primary open-angle glaucoma. VARIANTS GLC3A ASN-81; LYS-229; ARG-232; SER-269--PHE-271 DEL; LYS-387; HIS-390; TYR-423 AND GLY-443 VARIANTS GLY-48; SER-119; VAL-432 AND SER-453 Mutation spectrum of the CYP1B1 gene in Indian primary congenital glaucoma patients. VARIANTS GLC3A PRO-77; PRO-115; ARG-132; PRO-144; LEU-193; LYS-229; ARG-239; HIS-368; HIS-390; CYS-390; LEU-437 AND ASP-466 VARIANTS GLY-48; SER-119; VAL-432 AND SER-453 Cytochrome P4501B1 mutations cause only part of primary congenital glaucoma in Ecuador. VARIANT GLC3A CYS-390 Molecular and clinical evaluation of primary congenital glaucoma in Kuwait. VARIANTS GLC3A GLU-61; HIS-368 AND THR-388 VARIANT GLY-422 Primary role of CYP1B1 in Indian juvenile-onset POAG patients. VARIANTS GLC3A CYS-57; LYS-229; HIS-368; LEU-515; THR-523 AND GLY-530 VARIANTS GLY-48; SER-119; VAL-432; SER-453 AND ALA-518 Primary congenital glaucoma and Rieger's anomaly: extended haplotypes reveal founder effects for eight distinct CYP1B1 mutations. VARIANTS GLC3A GLU-61; ASN-81; LYS-229; LEU-343 DEL; HIS-368; LYS-387 AND TRP-469 Heterozygous CYP1B1 gene mutations in Spanish patients with primary open-angle glaucoma. VARIANTS GLC3A TRP-28; GLU-61; ASN-81; TRP-145; LYS-229; PHE-409 AND GLY-443 VARIANTS LEU-52; HIS-144; PRO-189 AND SER-330 Mutations in CYP1B1 cause primary congenital glaucoma by reduction of either activity or abundance of the enzyme. CHARACTERIZATION OF VARIANTS GLC3A GLU-61; ASN-81; SER-203; LYS-229 AND LEU-343 DEL A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:20972997, PubMed:11555828, PubMed:12865317, PubMed:10681376, PubMed:15258110). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:20972997, PubMed:11555828, PubMed:12865317, PubMed:10681376, PubMed:15258110). Exhibits catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2- and 4-hydroxy E1 and E2. Displays a predominant hydroxylase activity toward E2 at the C-4 position (PubMed:11555828, PubMed:12865317). Metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites (PubMed:10426814). May act as a major enzyme for all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376, PubMed:15258110). Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE, that function as lipid mediators in the vascular system (PubMed:20972997). Additionally, displays dehydratase activity toward oxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). This activity is independent of cytochrome P450 reductase, NADPH, and O2 (PubMed:21068195). Also involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products (PubMed:10426814). Plays an important role in retinal vascular development. Under hyperoxic O2 conditions, promotes retinal angiogenesis and capillary morphogenesis, likely by metabolizing the oxygenated products generated during the oxidative stress. Also, contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression (By similarity). 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] O2 + reduced [NADPH--hemoprotein reductase] + testosterone = 6beta,17beta-dihydroxyandrost-4-en-3-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] O2 + progesterone + reduced [NADPH--hemoprotein reductase] = 6beta-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] O2 + progesterone + reduced [NADPH--hemoprotein reductase] = 16alpha-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] all-trans-retinol + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] all-trans-retinal + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2O (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O (13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O heme Enzyme activity is increased by liposomes containing anionic phospholipids, phosphatidic acid and cardiolipin. Inhibited by naringenin with an IC(50) of 5 uM (PubMed:22888116, PubMed:22935222). Enzyme activity is increased by cytochrome b5. 6.9 uM for 17-beta-estradiol (2-hydroxylation) 5.1 uM for 17-beta-estradiol (4-hydroxylation) 17.0 uM for testosterone(6-beta-hydroxylation) 25.0 uM for progesterone (6-beta-hydroxylation) 23.0 uM for progesterone (16-alpha-hydroxylation) 18.5 uM for all-trans-retinol 11 uM for all-trans retinol 8.5 uM for all-trans-retinal 29.8 uM for arachidonic acid 212.8 uM for 7,12-dimethyltetraphene 0.42 nmol/min/nmol enzyme for 17-beta-estradiol (2-hydroxylation) 0.91 nmol/min/nmol enzyme for 17-beta-estradiol (4-hydroxylation) 2.2 nmol/min/nmol enzyme for testosterone (6-beta-hydroxylation) 0.6 nmol/min/nmol enzyme for progesterone (6-beta-hydroxylation) 2.3 nmol/min/nmol enzyme for progesterone (16-alpha-hydroxylation) 493 pmol/min/nmol enzyme toward all-trans retinol kcat is 0.15 min(-1) for retinol, 0.77 min(-1) for retinal, 2.86 min(-1) for 7,12-dimethyltetraphene, 0.48 min(-1) for arachidonic acid. Steroid hormone biosynthesis. Cofactor metabolism; retinol metabolism. Lipid metabolism; arachidonate metabolism. Endoplasmic reticulum membrane Peripheral membrane protein Microsome membrane Peripheral membrane protein Mitochondrion Located primarily in endoplasmic reticulum. Upon treatment with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), CYP1B1 is also targeted to mitochondria. Expressed in heart, brain, lung, skeletal muscle, kidney, spleen, thymus, prostate, testis, ovary, small intestine, colon, and peripheral blood leukocytes (PubMed:8175734). Expressed in retinal endothelial cells and umbilical vein endothelial cells (at protein level) (PubMed:19005183). By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Various CYP1B1 alleles are known. The sequence shown is that of allele CYP1B1*1. Anterior segment dysgenesis 6 ASGD6 A form of anterior segment dysgenesis, a group of defects affecting anterior structures of the eye including cornea, iris, lens, trabecular meshwork, and Schlemm canal. Anterior segment dysgeneses result from abnormal migration or differentiation of the neural crest derived mesenchymal cells that give rise to components of the anterior chamber during eye development. Different anterior segment anomalies may exist alone or in combination, including iris hypoplasia, enlarged or reduced corneal diameter, corneal vascularization and opacity, posterior embryotoxon, corectopia, polycoria, abnormal iridocorneal angle, ectopia lentis, and anterior synechiae between the iris and posterior corneal surface. Clinical conditions falling within the phenotypic spectrum of anterior segment dysgeneses include aniridia, Axenfeld anomaly, Reiger anomaly/syndrome, Peters anomaly, and iridogoniodysgenesis. ASGD6 patients predominantly manifest Peters anomaly. Peters anomaly consists of corneal leukoma, defects in the posterior structures of the cornea such as absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iridocorneal and/or keratolenticular adhesions. Over 50% of patients develop glaucoma in childhood. The disease is caused by mutations affecting the gene represented in this entry. Glaucoma 3, primary congenital, A GLC3A An autosomal recessive form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor. The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Glaucoma 1, open angle, A GLC1A A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. The gene represented in this entry acts as a disease modifier. Digenic mutations in CYP1B1 and MYOC have been found in a family segregating both primary adult-onset and juvenile forms of open angle glaucoma (PubMed:11774072). All affected family members with mutations in both MYOC and CYP1B1 had juvenile glaucoma, whereas those with only the MYOC mutation had the adult-onset form (PubMed:11774072). Belongs to the cytochrome P450 family. CYP1B1 alleles 3D-structure Complete proteome Disease mutation Endoplasmic reticulum Fatty acid metabolism Glaucoma Heme Iron Lipid metabolism Lyase Membrane Metal-binding Microsome Mitochondrion Monooxygenase Oxidoreductase Peters anomaly Polymorphism Reference proteome Steroid metabolism S W R G P L W C G E Q R L P Y N A P A S M R Q H Q P Q R R W G S A P D V P L V I N S S N S I E K G R S R R L V L A F A S L F V M G W R H D N P L E K A T R C R H R S I S V F V G N Y L V P L D H A G R Q F C D E N S G D R W E G S L V A R T D G V L MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLI GNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAF ASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVAL LVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSL VDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSA EKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAEL DQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVV FVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQL FLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKE TCQ Q562R1 B2RPJ1 Q562R2 Q562S9 Q562X8 ACTBL_HUMAN Beta-actin-like protein 2 Kappa-actin ACTBL2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Endometrial tumor NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Identification of a novel actin isoform in hepatocellular carcinoma. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-187 INTERACTION WITH PFN1 AND PFDN1 Hepatoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others (By similarity). Interacts with PFN1 and PFDN1. Q8IW35 CEP97 false 2 Cytoplasm Cytoskeleton Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization (By similarity). Monomethylation at Lys-85 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (By similarity). In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. Belongs to the actin family. ATP-binding Complete proteome Cytoplasm Cytoskeleton Nucleotide-binding Oxidation Reference proteome T I V A H L I T MTDNELSALVVDNGSGMCKAGFGGDDAPRAVFPSMIGRPRHQGVMVGMGQKDCYVGDEAQ SKRGVLTLKYPIEHGVVTNWDDMEKIWYHTFYNELRVAPDEHPILLTEAPLNPKINREKM TQIMFEAFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHIVPIYEGYALPHAILRLD LAGRDLTDYLMKILTERGYNFTTTAEREIVRDVKEKLCYVALDFEQEMVRAAASSSPERS YELPDGQVITIGNERFRCPEAIFQPSFLGIESSGIHETTFNSIMKCDVDIRKDLYANTVL SGGSTMYPGIADRMQKEIITLAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISK QEYDEAGPPIVHRKCF P31946 A8K9K2 E1P616 1433B_HUMAN 14-3-3 protein beta/alpha Protein 1054 Protein kinase C inhibitor protein 1 KCIP-1 14-3-3 protein beta/alpha, N-terminally processed YWHAB Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway. NUCLEOTIDE SEQUENCE [MRNA] Keratinocyte Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG) Thymus The DNA sequence and comparative analysis of human chromosome 20. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Skin ACBD3 interaction with TBC1 domain 22 protein is differentially affected by enteroviral and kobuviral 3A protein binding. PROTEIN SEQUENCE OF 1-11; 30-51; 63-73 AND 130-159 INTERACTION WITH PI4KB; TBC1D22A AND TBC1D22B IDENTIFICATION BY MASS SPECTROMETRY PROTEIN SEQUENCE OF 1-11; 14-57; 63-70; 106-117; 130-169 AND 215-246 CLEAVAGE OF INITIATOR METHIONINE ACETYLATION AT MET-1 AND THR-2 IDENTIFICATION BY MASS SPECTROMETRY Colon carcinoma Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. PROTEIN SEQUENCE OF 3-20 Platelet Mammalian 14-3-3beta associates with the Chlamydia trachomatis inclusion membrane via its interaction with IncG. INTERACTION WITH CHLAMYDIA INCG SUBUNIT (MICROBIAL INFECTION) SUBCELLULAR LOCATION (MICROBIAL INFECTION) Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis. INTERACTION WITH AANAT Proteomic characterization of the human centrosome by protein correlation profiling. IDENTIFICATION BY MASS SPECTROMETRY Lymphoblast The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. INTERACTION WITH CRTC2 The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by protein kinase B. INTERACTION WITH YWHAB A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia. INTERACTION WITH SSH1 JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage. INTERACTION WITH ABL1 Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] Melanoma Transgenic mouse proteomics identifies new 14-3-3-associated proteins involved in cytoskeletal rearrangements and cell signaling. INTERACTION WITH MARK2 AND MARK3 Inactivation of YAP oncoprotein by the Hippo pathway is involved in cell contact inhibition and tissue growth control. INTERACTION WITH YAP1 Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-3(beta) phosphorylation and promotes osteoblast differentiation and bone formation. INTERACTION WITH ROR2 FUNCTION PHOSPHORYLATION DIMERIZATION IDENTIFICATION BY MASS SPECTROMETRY Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53. INTERACTION WITH SIRT2 Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein. INTERACTION WITH GAB2 SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a phosphorylation-dependent manner. INTERACTION WITH SLITRK1 Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons. FUNCTION INTERACTION WITH SRPK2 Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Lysine acetylation targets protein complexes and co-regulates major cellular functions. ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-117 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling complex involved in alpha1-adrenergic receptor-induced p38 activation. FUNCTION INTERACTION WITH AKAP13 RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively regulating MAPK activation. INTERACTION WITH SOS1 N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM SHORT) CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia A proteomic perspective of inbuilt viral protein regulation: pUL46 tegument protein is targeted for degradation by ICP0 during herpes simplex virus type 1 infection. INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL46 (MICROBIAL INFECTION) Crystal structure of human myosin 1c - the motor in GLUT4 exocytosis: implications for Ca(2+)-regulation and 14-3-3 binding. INTERACTION WITH MYO1C An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Suppression of death-associated protein kinase 2 by interaction with 14-3-3 proteins. INTERACTION WITH DAPK2 Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at leading edges polarizes neutrophils. INTERACTION WITH RIPOR2 Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects. ACETYLATION AT THR-2 CLEAVAGE OF INITIATOR METHIONINE N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Structural basis for protein-protein interactions in the 14-3-3 protein family. X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239 IDENTIFICATION BY MASS SPECTROMETRY INTERACTION WITH PHOSPHOSERINE MOTIFS SUBUNIT Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma. VARIANT ILE-99 Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13. Homodimer (PubMed:17717073). Interacts with SAMSN1 and PRKCE (By similarity). Interacts with AKAP13 (PubMed:21224381). Interacts with SSH1 and TORC2/CRTC2 (PubMed:15454081, PubMed:15159416). Interacts with ABL1; the interaction results in cytoplasmic location of ABL1 and inhibition of cABL-mediated apoptosis (PubMed:15696159). Interacts with ROR2 (dimer); the interaction results in phosphorylation of YWHAB on tyrosine residues (PubMed:17717073). Interacts with GAB2 (PubMed:19172738). Interacts with YAP1 (phosphorylated form) (PubMed:17974916). Interacts with the phosphorylated (by AKT1) form of SRPK2 (PubMed:19592491). Interacts with PKA-phosphorylated AANAT (PubMed:11427721). Interacts with MYO1C (PubMed:24636949). Interacts with SIRT2 (PubMed:18249187). Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552). Interacts with the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1 (PubMed:22827337). Interacts (via phosphorylated form) with YWHAB; this interaction occurs in a protein kinase AKT1-dependent manner (PubMed:15538381). Interacts with SLITRK1 (PubMed:19640509). Interacts with SYNPO2 (phosphorylated form); YWHAB competes with ACTN2 for interaction with SYNPO2 (By similarity). Interacts with RIPOR2 (via phosphorylated form) isoform 2; this interaction occurs in a chemokine-dependent manner and does not compete for binding of RIPOR2 with RHOA nor blocks inhibition of RIPOR2-mediated RHOA activity (PubMed:25588844). Interacts with MARK2 and MARK3 (PubMed:16959763). (Microbial infection) Interacts with herpes simplex virus 1 protein UL46. (Microbial infection) Probably interacts with Chlamydia trachomatis protein IncG. false 3 Q76353 true 3 Q9P0K1-3 ADAM22 false 2 P15056 BRAF false 3 P22681 CBL false 3 O00257 CBX4 false 2 P30304 CDC25A false 10 P30305 CDC25B false 5 P30307 CDC25C false 4 O94921 CDK14 false 5 P67828 CSNK1A1 true 3 Q9NYF0 DACT1 false 4 Q13627-2 DYRK1A false 3 Q9UQC2 GAB2 false 4 P55040 GEM false 4 P55041 Gem true 3 P56524 HDAC4 false 3 Q11184 let-756 true 2 Q5S007 LRRK2 false 5 Q99759 MAP3K3 false 2 Q99683 MAP3K5 false 3 Q7KZI7 MARK2 false 3 P27448 MARK3 false 4 P26045 PTPN3 false 4 P04049 RAF1 false 18 Q96TC7 RMDN3 false 5 P61587 RND3 false 2 P61588 Rnd3 true 5 P78362 SRPK2 false 2 Q8WYL5 SSH1 false 3 Q91YE8 Synpo2 true 3 P49815 TSC2 false 4 P46937 YAP1 false 6 P62258 YWHAE false 4 P61981 YWHAG false 2 P27348 YWHAQ false 2 P22893 Zfp36 true 5 Cytoplasm Melanosome Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Vacuole membrane (Microbial infection) Upon infection with Chlamydia trachomatis, this protein is associated with the pathogen-containing vacuole membrane where it colocalizes with IncG. P31946-1 Long P31946-2 Short Contains a N-acetylmethionine at position 1. The alpha, brain-specific form differs from the beta form in being phosphorylated. Phosphorylated on Ser-60 by protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion. Belongs to the 14-3-3 family. 3D-structure Acetylation Alternative initiation Complete proteome Cytoplasm Direct protein sequencing Host-virus interaction Isopeptide bond Membrane Nitration Phosphoprotein Polymorphism Reference proteome Ubl conjugation Vacuole V I MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSS WRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFY LKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFY YEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGD AGEGEN Q9H6S1 A8K3M2 C9JB40 H7BXU6 Q86W99 Q9BQF1 AZI2_HUMAN 5-azacytidine-induced protein 2 NF-kappa-B-activating kinase-associated protein 1 Nak-associated protein 1 TILP AZI2 NAP1 TBKBP2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of NAP1, a regulatory subunit of IkappaB kinase-related kinases that potentiates NF-kappaB signaling. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) FUNCTION INTERACTION WITH TBK1 AND IKBKE SUBCELLULAR LOCATION TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [GENOMIC DNA] ALTERNATIVE SPLICING (ISOFORMS 1 AND 2) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Embryo Hepatoma The DNA sequence, annotation and analysis of human chromosome 3. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NF-kappaB-activating kinase-associated protein 1 participates in TLR3/Toll-IL-1 homology domain-containing adapter molecule-1-mediated IFN regulatory factor 3 activation. FUNCTION INTERACTION WITH TICAM1 SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK. INTERACTION WITH IKBKE Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Large-scale proteomics analysis of the human kinome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Functional dissection of the TBK1 molecular network. FUNCTION INTERACTION WITH TBK1 Vaccinia virus protein C6 is a virulence factor that binds TBK-1 adaptor proteins and inhibits activation of IRF3 and IRF7. INTERACTION WITH VACCINIA VIRUS PROTEIN C6 Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity. Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization. Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1. Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B. Participates in IFNB promoter activation via TICAM1. Homodimer. Interacts with IKBKE, TBK1 and TICAM1. (Microbial infection) Interacts with vaccinia virus protein C6 (PubMed:21931555). Q9E7P0 true 2 Q9UHD2 TBK1 false 6 P17362 VACWR022 true 2 Cytoplasm Q9H6S1-1 1 Long Q9H6S1-3 2 Short Q9H6S1-4 3 Gene prediction based on EST data. Q9H6S1-5 4 Gene prediction based on EST data. Widely expressed. Abundant expression seen in the pancreas and testis. 3D-structure Alternative splicing Coiled coil Complete proteome Cytoplasm Host-virus interaction Phosphoprotein Reference proteome SDNMQHAYWELKREMSNLHLVTQVQAEL RQSICSTAWSAVAQSWDSMNFEDCSLFA SDNMQHAYWELKREMSN RVSVAQPGVQWRNHGIA SDNMQHAYWELKR TQPGVQWRNHGIA MDALVEDDICILNHEKAHKRDTVTPVSIYSGDESVASHFALVTAYEDIKKRLKDSEKENS LLKKRIRFLEEKLIARFEEETSSVGREQVNKAYHAYREVCIDRDNLKSKLDKMNKDNSES LKVLNEQLQSKEVELLQLRTEVETQQVMRNLNPPSSNWEVEKLSCDLKIHGLEQELELMR KECSDLKIELQKAKQTDPYQEDNLKSRDLQKLSISSDNMQHAYWELKREMSNLHLVTQVQ AELLRKLKTSTAIKKACAPVGCSEDLGRDSTKLHLMNFTATYTRHPPLLPNGKALCHTTS SPLPGDVKVLSEKAILQSWTDNERSIPNDGTCFQEHSSYGRNSLEDNSWVFPSPPKSSET AFGETKTKTLPLPNLPPLHYLDQHNQNCLYKN P0DMU7 Q8N7B7 CT456_HUMAN Cancer/testis antigen family 45 member A6 Cancer/testis antigen 45-6 Cancer/testis antigen 45A6 CT45A6 CT45-6 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of cancer/testis-antigen genes by massively parallel signature sequencing. NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY IDENTIFICATION AS A CANCER/TESTIS ANTIGEN Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis The DNA sequence of the human X chromosome. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Testis specific. Expressed in cancer cell lines. Belongs to the CT45 family. Complete proteome Reference proteome E A G R R Q MTDKTEKVAVDPETVFKRPRECDSPSYQKRQRMALLARKQGAGDSLIAGSAMSKEKKLMT GHAIPPSQLDSQIDDFTGFSKDGMMQKPGSNAPVGGNVTSSFSGDDLECRETASSPKSQR EINADIKRKLVKELRCVGQKYEKIFEMLEGVQGPTAVRKRFFESIIKEAARCMRRDFVKH LKKKLKRMI P78410 B4DRT7 B4E103 F5H791 F8W6E0 O00477 O15338 O75658 Q76PA0 Q9BU81 Q9NR44 BT3A2_HUMAN Butyrophilin subfamily 3 member A2 BTN3A2 BT3.2 BTF3 BTF4 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A 1.1-Mb transcript map of the hereditary hemochromatosis locus. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Cloning, localization, and structure of new members of the butyrophilin gene family in the juxta-telomeric region of the major histocompatibility complex. NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1) The cluster of BTN genes in the extended major histocompatibility complex. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) VARIANTS ASP-181; THR-182 AND ASN-307 Thymus Tongue The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Placenta Skin Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-286 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Stimulation of human butyrophilin 3 molecules results in negative regulation of cellular immunity. GLYCOSYLATION Differential role for CD277 as a co-regulator of the immune signal in T and NK cells. FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY Key implication of CD277/butyrophilin-3 (BTN3A) in cellular stress sensing by a major human gammadelta T-cell subset. FUNCTION SUBCELLULAR LOCATION The molecular basis for modulation of human Vgamma9Vdelta2 T cell responses by CD277/butyrophilin-3 (BTN3A)-specific antibodies. X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 30-239 SUBUNIT DISULFIDE BONDS Plays a role in T-cell responses in the adaptive immune response. Inhibits the release of IFNG from activated T-cells. Homodimer. Cell membrane Single-pass type I membrane protein P78410-1 1 P78410-2 2 No experimental confirmation available. P78410-3 3 No experimental confirmation available. Detected in T-cells and natural killer cells. N-glycosylated. Belongs to the immunoglobulin superfamily. BTN/MOG family. 3D-structure Adaptive immunity Alternative splicing Cell membrane Coiled coil Complete proteome Disulfide bond Glycoprotein Immunity Immunoglobulin domain Membrane Phosphoprotein Polymorphism Reference proteome Signal Transmembrane Transmembrane helix MKMASSLAFLLLNFHVSLLLVQLLTPCS MGIPR R T N D A T R K S N M L S G RG KS S L MKMASSLAFLLLNFHVSLLLVQLLTPCSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSA ETMELKWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASD SGKYLCYFQDGDFYEKALVELKVAALGSNLHVEVKGYEDGGIHLECRSTGWYPQPQIQWS NAKGENIPAVEAPVVADGVGLYEVAASVIMRGGSGEGVSCIIRNSLLGLEKTASISIADP FFRSAQPWIAALAGTLPILLLLLAGASYFLWRQQKEITALSSEIESEQEMKEMGYAATER EISLRESLQEELKRKKIQYLTRGEESSSDTNKSA A6NH57 ARL5C_HUMAN Putative ADP-ribosylation factor-like protein 5C ADP-ribosylation factor-like protein 12 ARL5C ARL12 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Binds and exchanges GTP and GDP. Belongs to the small GTPase superfamily. Arf family. Complete proteome GTP-binding Lipoprotein Myristate Nucleotide-binding Reference proteome MGQLIAKLMSIFGNQEHTVIIVGLDNEGKTTILYRFLTNEVVHMCPTIGSNVEEIILPKT HFFMWDIVRPEALSFIWNTYYSNTEFIILVIDSTDRDRLLTTREELYKMLAHEALQDASV LIFANKQDVKDSMRMVEISHFLTLSTIKDHSWHIQGCCALTREGLPARLQWMESQAAAN Q8NHU2 A6NHA1 Q5JXV4 Q5TE18 Q8N5R9 Q96M59 Q9BQL2 Q9H127 Q9H128 Q9NQH4 Q9UFV8 Q9Y4V7 CFA61_HUMAN Cilia- and flagella-associated protein 61 CFAP61 C20orf26 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6) Testis The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) Testis The DNA sequence and comparative analysis of human chromosome 20. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5) VARIANTS ARG-74 AND ILE-369 Brain Testis The WashU-Merck EST project. NUCLEOTIDE SEQUENCE OF 287-409 (ISOFORM 4) Diagnostic exome sequencing in persons with severe intellectual disability. VARIANT PRO-790 May regulate cilium motility through its role in the assembly of the axonemal radial spokes. Cytoplasm Cytoskeleton Cilium axoneme Q8NHU2-1 1 Q8NHU2-3 3 Q8NHU2-4 4 Q8NHU2-5 5 Created from a fragment entry and may await further characterization. Q8NHU2-6 6 Ref.1 (BAB71452) sequence is in conflict in position: 123:L->P. Experimental confirmation may be lacking for some isoforms. Alternative splicing Cell projection Complete proteome Cytoplasm Cytoskeleton Polymorphism Reference proteome SINIRFAT NICLGRSS GNIIVYGNTI DGGRASVLFC MFFSFCEKNVDYETFKALNDACLVYDSRLVID GAFFLGLTIICILPSLPFQLPWRYKWHSLIMV P R H R V I P L D E P L V I T P N S MSVLTSPRGKVEVVHCRRTESQDVYCIKSLIRKFTCKLFGKLNIIYLLEKANLAVTLCND KEEIMAQATFLDYPNWNVAKQDDWVSVFRELDSDIPCTPLNTLFMHLFVAVDEYSVGCCK EILRTVYKAVPELHFIFLIVPSYMSLGSTLITVFDQVGNIPCLTYEEDFAVHICHRHSHY PQLHVRKARVEDHDDLMPIFMRYDTILKETYGEYFLAELIEAQDEENHAVVCEVEGTAVG FMSVCSRVNMQLLHECFDLGPFHGLCFPHPDDVLESPQDLSVRRSQDAELRSSSQGSQKI VEELQEPVSPDTMENIQGNIAREAASEEALTAVQSGNVSEPEDIEKLSDISTGYAQYHHV SSRSLASLVLPEEPVHFRPIYRGASAAFCIQLFCIDEKYEARSLDFMNFVFSLFSDKNFC VISLPHLTPEFFLIQNFVKMVPFNTCTLEQDLYVFHRAGLLKSINIRFATLLDTPGVENL VSTLMLNKSILEDLDRYNKARKDPDGTLLQAFVAEVAEQIVGIAVIRNEMDIEYIRSHYN IEDFIYFSHHQREEHGHMHHFALNPIFRHYTKFFLKEILRLGFKSCLYYRVYPKSREGKF QNPYAHSLTSALHYLVPVRPRRQIVYPLEKLGINAPSKAVSKDPMSYALNHTNRKLTLEP KITVNAKIIVVGASSVGISFLETLVFCSHMKFNNLTLISTHGLPGKKLLDTEQRKFLASD HCFNDKDYALMSLCSWVNVVVGRMTGIDRAAKHVVLSTDEIVPYDHLILCTGQQYQVPCP TEADISQHLTNREVPNSSQRRYTGKVPCNHFTLNEEEDCFKALIWIRNNSITTEGNIIVY GNTIDTYTTVETLLNLGVSGSRIHLVQPPPASTITCINNYSVESAVADALGAAGVTMYRD AILAQWNDGLHPDPIYSASFTTPTKPFRLQCSMFFSFCEKNVDYETFKALNDACLVYDSR LVIDTNFHTNDIAIRAAGSLTKFSNRYYSNEWTHSNFSSKEIGFQLAAAMLHLFDPTLEP VTEPPANLDRLIPMYKGAKIQGGILPGSYHYLHIAKPAIPTPLEVQMAQPNYGLELVTGS AKNGTYFRIHINKYKMVETITCLSREPFPASNYIRLFGQHEQLLNNLCARYDENLITDLY SYFTEPWCLALFHDRFIDLRKELRQILASKEEEDLPSIEQLAHQIEDEEINPTEKPRQYL KRVFEESIYKTLVERSTLDYLHYNRYHLPMYAWPGIV Q5T9A4 A8K3H1 Q6ZRB5 Q9BUK4 Q9ULE7 ATD3B_HUMAN ATPase family AAA domain-containing protein 3B AAA-TOB3 ATAD3B KIAA1273 TOB3 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) Brain Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Thymus The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3) Leiomyosarcoma Placenta Molecular characterization of the tumor-associated antigen AAA-TOB3. IDENTIFICATION OF ISOFORMS 1 AND 3 SUBCELLULAR LOCATION INDUCTION TISSUE SPECIFICITY The layered structure of human mitochondrial DNA nucleoids. SUBCELLULAR LOCATION TOPOLOGY Lysine acetylation targets protein complexes and co-regulates major cellular functions. ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-427 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ATAD3B is a human embryonic stem cell specific mitochondrial protein, re-expressed in cancer cells, that functions as dominant negative for the ubiquitous ATAD3A. FUNCTION INTERACTION WITH ATAD3A TISSUE SPECIFICITY DEVELOPMENTAL STAGE TOPOLOGY Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Mitochondrial nucleoid interacting proteins support mitochondrial protein synthesis. INTERACTION WITH PROTEINS INVOLVED IN MITOCHONDRIAL TRANSLATION; RNA METABOLISM; ATAD3A AND GADD45GIP1 May play a role in a mitochondrial network organization typical for stem cells, characterized by reduced mitochondrial metabolism, low mtDNA copies and fragmentated mitochondrial network. may act by suppressing ATAD3A function, interfering with ATAD3A interaction with matrix nucleoid complexes. Forms heterooligomers with ATAD3A. Interacts with components of the mitochondrial ribosome, including MRPL11 and MRPS18B, and with other proteins involved in mitochondrial RNA metabolism, possibly via interaction with ATAD3A. Interacts with GADD45GIP1. Mitochondrion inner membrane Peripheral membrane protein Has been found to co-purify with nucleoids (PubMed:22453275). Since it does not face the mitochondrial matrix, the association with nucleoids could be mediated by ATAD3A. Q5T9A4-1 1 AAA-TOB3l Q5T9A4-2 2 No experimental confirmation available. Q5T9A4-3 3 AAA-TOB3s Tends to be down-regulated in differentiated cells and re-expressed in pluripotent stem cells or cancer cells (at protein level). Expressed in proliferating embryonic stem cells and down-regulated during differentiation. Up-regulated by MYC. Belongs to the AAA ATPase family. Translation N-terminally shortened. Acetylation Alternative splicing ATP-binding Coiled coil Complete proteome Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Polymorphism Reference proteome WSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLK MQLEALNLLHTLVWARSLCRAGAVQTQERLSGSASPEQVPAGECCALQ LSEETRQHQA MCLCRPLLPQ AGLTLLAVGVYSAKNATAVTGRFIEARLGKPSL NIFIKQGWQVAERQHVGASWSPRSCPCRLCTAL V I Q R E V MSWLFGVNKGPKGEGAGPPPPLPPAQPGAEGGGDRGLGDRPAPKDKWSNFDPTGLERAAK AARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTLS EETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMEL RHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAF VTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHP IQVSRRLLSRPQDVLEGVVLSPSLEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTL FAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGLLLFMDEADAFLRKR ATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHFDLPQQEE RERLVRLHFDNCVLKPATEGKRRLKLAQFDYGRKCSEVARLTEGMSGREIAQLAVSWQAT AYASKDGVLTEAMMDACVQDAVQQYRQKMRWLKAEGPGRGVEHPLSGVQGETLTSWSLAT DPSYPCLAGPCTFRICSWMGTGLCPGPLSPRMSCGGGRPFCPPGHPLL Q99218 Q6RWT1 AMELY_HUMAN Amelogenin, Y isoform AMELY AMGL AMGY Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The human enamel protein gene amelogenin is expressed from both the X and the Y chromosomes. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Tooth bud NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) A human X-Y homologous region encodes 'amelogenin'. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-206 (ISOFORM 2) Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel. Secreted Extracellular space Extracellular matrix Q99218-2 2 Q99218-1 1 Transiently but abundantly expressed by ameloblasts during tooth development. Amelogenin is the predominant protein in developing dental enamel. Belongs to the amelogenin family. Alternative splicing Biomineralization Complete proteome Extracellular matrix Reference proteome Repeat Secreted Signal F L D VSTP MGTWILFACLVGAAFAMPLPPHPGHPGYINFSYENSHSQAINVDRIALVLTPLKWYQSMI RPPYSSYGYEPMGGWLHHQIIPVVSQQHPLTHTLQSHHHIPVVPAQQPRVRQQALMPVPG QQSMTPTQHHQPNLPLPAQQPFQPQPVQPQPHQPMQPQPPVQPMQPLLPQPPLPPMFPLR PLPPILPDLHLEAWPATDKTKQEEVD P30484 Q9TPR2 1B46_HUMAN HLA class I histocompatibility antigen, B-46 alpha chain Bw-46 MHC class I antigen B*46 HLA-B HLAB Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Diversity and diversification of HLA-A,B,C alleles. NUCLEOTIDE SEQUENCE (ALLELE B*46:01) Cloning and sequencing full-length HLA-B and -C genes. NUCLEOTIDE SEQUENCE (ALLELE B*46:01) Blood Identification of a novel HLA-B46 allele, B*4602, in Japanese. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*46:02) Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in the presentation of foreign antigens to the immune system. Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). P43628 KIR2DL3 false 2 Membrane Single-pass type I membrane protein Polyubiquitinated in a post ER compartment by interaction with human herpesvirus 8 MIR1 protein. This targets the protein for rapid degradation via the ubiquitin system (By similarity). The following alleles of B-46 are known: B*46:01 and B*46:02. The sequence shown is that of B*46:01. Belongs to the MHC class I family. 3D-structure Complete proteome Disulfide bond Glycoprotein Immunity Membrane MHC I Polymorphism Reference proteome Signal Transmembrane Transmembrane helix Ubl conjugation D G MRVTAPRTVLLLLSGALALTETWAGSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRF DSDAASPRMAPRAPWIEQEGPEYWDRETQKYKRQAQTDRVSLRNLRGYYNQSEAGSHTLQ RMYGCDVGPDGRLLRGHDQSAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQW RAYLEGLCVEWLRRYLENGKETLQRADPPKTHVTHHPISDHEATLRCWALGFYPAEITLT WQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP SSQSTIPIVGIVAGLAVLAVVVIGAVVATVMCRRKSSGGKGGSYSQAASSDSAQGSDVSL TA P30481 P10320 P30482 P79524 Q29850 Q5RIP1 Q860I4 Q861B5 Q9BCM7 Q9MYC3 Q9UQS8 1B44_HUMAN HLA class I histocompatibility antigen, B-44 alpha chain Bw-44 MHC class I antigen B*44 HLA-B HLAB Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Diversity and diversification of HLA-A,B,C alleles. NUCLEOTIDE SEQUENCE (ALLELE B*44:02) The two major subtypes of HLA-B44 differ for a single amino acid in codon 156. NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*44:03) Three new HLA-B alleles found in Mexican-Americans. NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*44:03) Molecular characterization of the new alleles HLA-B*8101 and B*4407. NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*44:07) A new HLA-B44 variant (B44BO [B*4408]) identified by serology. NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*44:08) Further diversity within the HLA-B44 group: two novel alleles identified in UK Caucasoid potential bone marrow donors. NUCLEOTIDE SEQUENCE (ALLELE B*44:12) HLA-B*4413 identified in a UK Caucasoid potential bone marrow donor. NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*44:13) Complete nucleotide sequencing of HLA class I genes. NUCLEOTIDE SEQUENCE (ALLELES B*44:02 AND B*44:09) Complete cDNA sequence of HLA-B*4405. NUCLEOTIDE SEQUENCE (ALLELE B*44:05) Confirmation of HLA-B*4404. NUCLEOTIDE SEQUENCE (ALLELE B*44:04) Blood The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] DNA sequence of the coding region of the HLA-B44 gene. NUCLEOTIDE SEQUENCE [MRNA] OF 4-362 (ALLELE B*44:02) Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] A naturally selected dimorphism within the HLA-B44 supertype alters class I structure, peptide repertoire, and T cell recognition. X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 25-300 DISULFIDE BONDS Involved in the presentation of foreign antigens to the immune system. Heterodimer of an alpha chain and a beta chain (beta-2-microglobulin). Membrane Single-pass type I membrane protein Polyubiquitinated in a post ER compartment by interaction with human herpesvirus 8 MIR1 protein. This targets the protein for rapid degradation via the ubiquitin system (By similarity). The following alleles of B-44 are known: B*44:02 (B-12; B44.2), B*44:04, B*44:05, B*44:07, B*44:08 (B44BO), B*44:09, B*44:12 and B*44:13. The sequence shown is that of B*44:02. Belongs to the MHC class I family. 3D-structure Complete proteome Disulfide bond Glycoprotein Immunity Membrane MHC I Polymorphism Reference proteome Signal Transmembrane Transmembrane helix Ubl conjugation T A KE MA D E E N N S TALR NLRG D Y D L D R L T V I A T C S L A V A A S MRVTAPRTLLLLLWGAVALTETWAGSHSMRYFYTAMSRPGRGEPRFITVGYVDDTLFVRF DSDATSPRKEPRAPWIEQEGPEYWDRETQISKTNTQTYRENLRTALRYYNQSEAGSHIIQ RMYGCDVGPDGRLLRGYDQDAYDGKDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQD RAYLEGLCVESLRRYLENGKETLQRADPPKTHVTHHPISDHEVTLRCWALGFYPAEITLT WQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP SSQSTVPIVGIVAGLAVLAVVVIGAVVAAVMCRRKSSGGKGGSYSQAACSDSAQGSDVSL TA P07741 G5E9J2 Q3KP55 Q68DF9 APT_HUMAN Adenine phosphoribosyltransferase APRT 2.4.2.7 APRT Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Nucleotide sequence of the human APRT gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Liver Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence divergence and conservation of a nonrandom CpG dinucleotide arrangement. NUCLEOTIDE SEQUENCE [GENOMIC DNA] The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Uterine endothelium NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT ARG-121 The sequence and analysis of duplication-rich human chromosome 16. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Astrocytoma Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. PROTEIN SEQUENCE OF 2-180 Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. PROTEIN SEQUENCE OF 2-12 ACETYLATION AT ALA-2 Platelet Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Large-scale proteomics analysis of the human kinome. ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-15; TYR-60; SER-66 AND THR-135 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Lysine acetylation targets protein complexes and co-regulates major cellular functions. ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-30 AND SER-66 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver N-terminome analysis of the human mitochondrial proteome. ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis. X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) Identification of a single missense mutation in the adenine phosphoribosyltransferase (APRT) gene from five Icelandic patients and a British patient. VARIANT APRTD VAL-65 Missense mutation in the adenine phosphoribosyltransferase gene causing 2,8-dihydroxyadenine urolithiasis. VARIANT APRTD PRO-110 Human adenine phosphoribosyltransferase. Identification of allelic mutations at the nucleotide level as a cause of complete deficiency of the enzyme. VARIANT APRTD THR-136 Human adenine phosphoribosyltransferase deficiency. Demonstration of a single mutant allele common to the Japanese. VARIANTS APRTD THR-136 AND PHE-173 DEL Only three mutations account for almost all defective alleles causing adenine phosphoribosyltransferase deficiency in Japanese patients. VARIANT APRTD THR-136 2,8-Dihydroxyadenine urolithiasis in a patient with considerable residual adenine phosphoribosyltransferase activity in cell extracts but with mutations in both copies of APRT. VARIANTS APRTD PHE-150 AND ARG-153 Identification of two novel mutations in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis. VARIANTS APRTD MET-84 AND ASP-133 A Japanese boy with adenine phosphoribosyltransferase (APRT) deficiency caused by compound heterozygosity including a novel missense mutation in APRT gene. VARIANTS APRTD PRO-33 AND THR-136 Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. Homodimer. Cytoplasm P07741-1 1 P07741-2 2 No experimental confirmation available. Adenine phosphoribosyltransferase deficiency APRTD An enzymatic deficiency that can lead to urolithiasis and renal failure. Patients have 2,8-dihydroxyadenine (DHA) urinary stones. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the purine/pyrimidine phosphoribosyltransferase family. Adenine phosphoribosyltransferase entry 3D-structure Acetylation Alternative splicing Complete proteome Cytoplasm Direct protein sequencing Disease mutation Glycosyltransferase Phosphoprotein Polymorphism Purine salvage Reference proteome Transferase GTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE V L P D V V M L P Q R G D M T V F C R MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDY IAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPG QRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE Q9BWP8 A1IGE4 A1IGE5 A1IGE6 A7VJJ2 A7VJJ3 A7VJJ4 A7VJJ5 B2R9M5 B4E1G0 J3KQY9 Q5CZ85 Q7Z6N1 COL11_HUMAN Collectin-11 Collectin kidney protein 1 CL-K1 COLEC11 UNQ596/PRO1182 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification and characterization of a novel human collectin CL-K1. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8) FUNCTION TISSUE SPECIFICITY Kidney The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 10) VARIANT ARG-219 Lung Ovary Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 9) Neuroblastoma The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-271 (ISOFORM 3) Endometrium A quantitative atlas of mitotic phosphorylation. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin with microbial-binding activity. FUNCTION DNA-BINDING SUBUNIT INTERACTION WITH MASP1 TISSUE SPECIFICITY Characterization of the interaction between collectin 11 (CL-11, CL-K1) and nucleic acids. FUNCTION DNA-BINDING An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Molecular basis of sugar recognition by collectin-K1 and the effects of mutations associated with 3MC syndrome. X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 116-270 OF HOMOTRIMER IN COMPLEX WITH CALCIUM AND CARBOHYDRATE FUNCTION SUBUNIT SUBCELLULAR LOCATION DISULFIDE BONDS CHARACTERIZATION OF VARIANTS 3MC2 PRO-169; SER-204 AND SER-217 DEL Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome. FUNCTION VARIANTS 3MC2 PRO-169; SER-204 AND SER-217 DEL COLEC10 is mutated in 3MC patients and regulates early craniofacial development. FUNCTION VARIANT 3MC2 THR-166 Lectin that plays a role in innate immunity, apoptosis and embryogenesis (PubMed:23954398, PubMed:25912189, PubMed:21258343). Calcium-dependent lectin that binds self and non-self glycoproteins presenting high mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope (PubMed:25912189). Primarily recognizes the terminal disaccharide of the glycan (PubMed:25912189). Also recognizes a subset of fucosylated glycans and lipopolysaccharides (PubMed:17179669, PubMed:25912189). Plays a role in innate immunity through its ability to bind non-self sugars presented by microorganisms and to activate the complement through the recruitment of MAPS1 (PubMed:20956340, PubMed:25912189). Also plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding (Probable). Finally, plays a role in development, probably serving as a guidance cue during the migration of neural crest cells and other cell types during embryogenesis (PubMed:21258343, PubMed:28301481). Homotrimer; disulfide-linked (PubMed:20956340, PubMed:25912189). Interacts with MASP1; probably triggers the lectin pathway of complement (PubMed:20956340). Secreted Q9BWP8-1 1 CL-K1-I Q9BWP8-2 2 CL-K1-Ia Q9BWP8-3 3 CL-K1-Ib Q9BWP8-4 4 CL-K1-II Q9BWP8-5 5 CL-K1-Ic Q9BWP8-6 6 CL-K1-IIa Q9BWP8-7 7 CL-K1-IIb Q9BWP8-8 8 CL-K1-IIc Q9BWP8-9 9 Q9BWP8-10 10 No experimental confirmation available. Ubiquitous (PubMed:17179669). Detected in adrenal gland, kidney, liver, ovaries and testis (at protein level) (PubMed:20956340). 3MC syndrome 2 3MC2 A form of 3MC syndrome, an autosomal recessive disorder characterized by facial dysmorphism, craniosynostosis, learning disability, and genital, limb and vesicorenal anomalies. Facial features include hypertelorism, blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip and/or palate. The term 3MC syndrome includes Carnevale, Mingarelli, Malpuech, and Michels syndromes. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the COLEC10/COLEC11 family. Collectin K1 3D-structure Alternative splicing Calcium Coiled coil Collagen Complete proteome Developmental protein Disease mutation Disulfide bond Immunity Innate immunity Lectin Mannose-binding Metal-binding Polymorphism Reference proteome Secreted Signal MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLKGDAGEKGDKGAPGRPGRVGPTGEK MTPALCRSSSLASKGMRERRETKAPPDGLEESAPREKKQSQPVVTASDISKRKCTSSFVEMGSQ MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLK MWWVPPSPYGCLPCALP M MKKQRGVGVLPALRM DKGAPGRPGRVGPTGEK MWWVPPSPYGCLPCALP QKGSVGRHGKIGPIGSK MWWVPPSPYGCLPCALP A T S P G S H R S T G D MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLKGDAGEKGDKGAPGRPGR VGPTGEKGDMGDKGQKGSVGRHGKIGPIGSKGEKGDSGDIGPPGPNGEPGLPCECSQLRK AIGEMDNQVSQLTSELKFIKNAVAGVRETESKIYLLVKEEKRYADAQLSCQGRGGTLSMP KDEAANGLMAAYLAQAGLARVFIGINDLEKEGAFVYSDHSPMRTFNKWRSGEPNNAYDEE DCVEMVASGGWNDVACHTTMYFMCEFDKENM Q9P1Z2 B3KVA8 Q6FI59 Q71RC3 Q86WF8 Q96JU3 Q9H090 CACO1_HUMAN Calcium-binding and coiled-coil domain-containing protein 1 Calphoglin Coiled-coil coactivator protein Sarcoma antigen NY-SAR-3 CALCOCO1 KIAA1536 PP13275 UNQ2436/PRO4996 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cellular signaling mediated by calphoglin-induced activation of IPP and PGM. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) FUNCTION INTERACTION WITH PHOSPHOGLUCOMUTASE AND PPA1 Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Brain Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4) VARIANT LYS-393 Spleen Thyroid Large-scale cDNA transfection screening for genes related to cancer development and progression. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Kidney Immunomic analysis of human sarcoma. NUCLEOTIDE SEQUENCE [MRNA] OF 147-455 Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel pathway for GATA1 function. FUNCTION Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions (By similarity). In association with CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781). Seems to enhance inorganic pyrphosphatase thus activating phosphogluomutase (PMG). Probably functions as component of the calphoglin complex, which is involved in linking cellular metabolism (phosphate and glucose metabolism) with other core functions including protein synthesis and degradation, calcium signaling and cell growth. Part of a calphoglin complex consisting of CALCOCO1, PPA1 and PGM (Ref.1). Interacts with the bHLH-PAS domains of GRIP1, AHR and ARNT. Interacts with CTNNB1 via both its N- and C-terminal regions. Interacts with EP300. Interacts with CCAR1 (via N-terminus) and GATA1 (By similarity). Q96LK0 CEP19 false 5 Q2TBE0 CWF19L2 false 5 Q9UII6 DUSP13 false 5 Q3B820 FAM161A false 3 P60520 GABARAPL2 false 3 Q96CN7 ISOC1 false 3 O14777 NDC80 false 4 Q8TC07 TBC1D15 false 3 Cytoplasm Nucleus Shuttles between nucleus and cytoplasm. Q9P1Z2-1 1 Q9P1Z2-2 2 Q9P1Z2-3 3 No experimental confirmation available. Q9P1Z2-4 4 No experimental confirmation available. The C-terminal activation region (AD) is used for downstream signaling. Seems to be essential for coactivator function with nuclear receptors and with the aryl hydrocarbon receptor (By similarity). The N-terminal activation region (AD) is necessary and sufficient for synergistic activation of LEF1-mediated transcription by CTNNB1. Contains a EP3000 binding region which is important for synergistic cooperation (By similarity). Recruitment by nuclear receptors is accomplished by the interaction of the coiled-coiled domain with p160 coactivators. Belongs to the CALCOCO family. Activator Alternative splicing Coiled coil Complete proteome Cytoplasm Nucleus Phosphoprotein Polymorphism Reference proteome Transcription Transcription regulation Wnt signaling pathway SGFTVGTLSETSTGGPATPTWKECPICKERFPAESDKDALEDHMDGHFFFSTQDPFTFE R R K H R K R K E MEESPLSRAPSRGGVNFLNVARTYIPNTKVECHYTLPPGTMPSASDWIGIFKVEAACVRD YHTFVWSSVPESTTDGSPIHTSVQFQASYLPKPGAQLYQFRYVNRQGQVCGQSPPFQFRE PRPMDELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSR VQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTI SEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDL KEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKAT LLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVE AEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALR VLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVGLSCPAALTDSE DESPEDMRLPPYGLCERGDPGSSPAGPREASPLVVISQPAPISPHLSGPAEDSSSDSEAE DEKSVLMAAVQSGGEEANLLLPELGSAFYDMASGFTVGTLSETSTGGPATPTWKECPICK ERFPAESDKDALEDHMDGHFFFSTQDPFTFE Q8N8A2 Q53SL9 Q6P480 Q86VL5 Q8IZ72 Q9UFA4 ANR44_HUMAN Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B PP6-ARS-B Serine/threonine-protein phosphatase 6 regulatory subunit ARS-B Ankyrin repeat domain-containing protein 44 ANKRD44 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4) Spleen Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 812-989 (ISOFORM 1) Duodenum Skin The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-993 (ISOFORM 2) Testis Protein phosphatase 6 regulatory subunits composed of ankyrin repeat domains. INTERACTION WITH PPP6R1 Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Protein phosphatase 6 (PP6) holoenzyme is proposed to be a heterotrimeric complex formed by the catalytic subunit, a SAPS domain-containing subunit (PP6R) and an ankyrin repeat-domain containing regulatory subunit (ARS). Interacts with PPP6R1. Q9UPN7 PPP6R1 false 4 P35125-3 USP6 false 4 O00308 WWP2 false 3 Q8N8A2-1 1 Q8N8A2-2 2 No experimental confirmation available. Q8N8A2-3 3 No experimental confirmation available. Q8N8A2-4 4 No experimental confirmation available. Q8N8A2-5 5 Alternative splicing ANK repeat Complete proteome Reference proteome Repeat G GQKYSIVSLFSNEHVLSAG LLERTNSGFEESDSGATKSPLHLAAYNGH VSCFVLFSLTHTHTHTPNHRGINCFFPEL ASRSNGPRSTPGTAVQKEE GC K R I R Q P H R MAVLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELL ILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV KCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWA AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN TALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVN IQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLIT SGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVEC IKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAA SDMDRNKTILGNAHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAA AYGHRQCLELLLERTNSGFEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKG RTALDLAAFKGHTECVEALINQGASIFVKDNVTKRTPLHASVINGHTLCLRLLLEIADNP EAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQ MLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEDCCFKDNQGYTPLHWAC YNGNENCIEVLLEQKCFRKFIGNPFTPLHCAIINDHGNCASLLLGAIDSSIVSCRDDKGR TPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLT VKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINEKNNALQTPLHVAARNGLKVVVEE LLAKGACVLAVDENASRSNGPRSTPGTAVQKEE Q0P5P2 CQ067_HUMAN Uncharacterized protein C17orf67 C17orf67 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain A2RRN7 CADPS false 3 Q9HD26 GOPC false 3 Secreted Complete proteome Reference proteome Secreted Signal MKTLPVLVLSLTLLTVFSETSPILTEKQAKQLLRSRRQDRPSKPGFPDEPMREYMHHLLA LEHRAEEQFLEHWLNPHCKPHCDRNRIHPV Q9BUF7 A8KA91 D6W643 Q8N0V8 Q8WVA0 CRUM3_HUMAN Protein crumbs homolog 3 CRB3 UNQ588/PRO1158 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Mammalian Crumbs3 is a small transmembrane protein linked to protein associated with Lin-7 (Pals1). NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) TISSUE SPECIFICITY INTERACTION WITH MPP5 AND PATJ MUTAGENESIS OF ASN-36 SUBCELLULAR LOCATION GLYCOSYLATION AT ASN-36 Retina NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Pancreas The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Trachea NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Ovary Pancreas The Crumbs3-Pals1 complex participates in the establishment of polarity in mammalian epithelial cells. FUNCTION MUTAGENESIS OF 117-GLU--ILE-120 INTERACTION WITH MPP5 CRB3 binds directly to Par6 and regulates the morphogenesis of the tight junctions in mammalian epithelial cells. SUBCELLULAR LOCATION TISSUE SPECIFICITY INTERACTION WITH PARD6A AND PATJ MUTAGENESIS OF 117-GLU--ILE-120 FUNCTION Involved in the establishment of cell polarity in mammalian epithelial cells. Regulates the morphogenesis of tight junctions. Interacts with MPP5, PARD6A and PATJ. P25788 PSMA3 false 3 Apical cell membrane Single-pass type I membrane protein Cell junction Tight junction Localizes primarily to the apical membrane with a small fraction in the upper part of tight junctions of epithelial cells. Q9BUF7-1 1 A Q9BUF7-2 2 B Preferentially expressed in epithelial tissues. Expressed at high levels in lung, kidney, retina, colon and mammary glands. Expressed at moderate levels in liver, spleen, pancreas, placenta and prostate. The PDZ-binding motif is involved in the interactions with PARD6A and MPP5. 3D-structure Alternative splicing Cell junction Cell membrane Complete proteome Glycoprotein Membrane Reference proteome Signal Tight junction Transmembrane Transmembrane helix VGARVPPTPNLKLPPEERLI FSHAAEARAPQDSKETVQGCLPI N D MANPGLGLLLALGLPFLLARWGRAWGQIQTTSANENSTVLPSSTSSSSDGNLRPEAITAI IVVFSLLAALLLAVGLALLVRKLREKRQTEGTYRPSSEEQVGARVPPTPNLKLPPEERLI O95452 B3KQN2 Q5Q1H9 Q5Q1I0 Q5Q1I1 Q5T5U0 Q8IUP0 CXB6_HUMAN Gap junction beta-6 protein Connexin-30 Cx30 GJB6 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Mutations in GJB6 cause nonsyndromic autosomal dominant deafness at DFNA3 locus. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT DFNA3B MET-5 Human connexin 30 (GJB6), a candidate gene for nonsyndromic hearing loss: molecular cloning, tissue-specific expression, and assignment to chromosome 13q12. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS GLY-139 AND THR-199 Human connexin30, updated ORF. NUCLEOTIDE SEQUENCE [MRNA] Corpus callosum Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain cortex Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Thyroid The DNA sequence and analysis of human chromosome 13. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Gene structure and promoter analysis of the human GJB6 gene encoding connexin 30. NUCLEOTIDE SEQUENCE [MRNA] OF 1-40 GENE STRUCTURE Hair follicle A deletion involving the connexin 30 gene in nonsyndromic hearing impairment. INVOLVEMENT IN DFNB1B A novel deletion involving the connexin-30 gene, del(GJB6-d13s1854), found in trans with mutations in the GJB2 gene (connexin-26) in subjects with DFNB1 non-syndromic hearing impairment. INVOLVEMENT IN DFNB1B Mutations in GJB6 cause hidrotic ectodermal dysplasia. VARIANTS ECTD2 ARG-11 AND VAL-88 A novel connexin 30 mutation in Clouston syndrome. VARIANT ECTD2 GLU-37 Novel mutation p.Gly59Arg in GJB6 encoding connexin 30 underlies palmoplantar keratoderma with pseudoainhum, knuckle pads and hearing loss. VARIANT ARG-59 One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. A connexon is composed of a hexamer of connexins. Interacts with CNST (By similarity). Cell membrane Multi-pass membrane protein Cell junction Gap junction Ectodermal dysplasia 2, Clouston type ECTD2 A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures such as hair, teeth, nails and sweat glands, with or without any additional clinical sign. Each combination of clinical features represents a different type of ectodermal dysplasia. ECTD2 is an autosomal dominant condition characterized by atrichosis, nail hypoplasia and deformities, hyperpigmentation of the skin, normal teeth, normal sweat and sebaceous gland function. Palmoplantar hyperkeratosis is a frequent feature. Hearing impairment has been detected in few cases. The disease is caused by mutations affecting the gene represented in this entry. Deafness, autosomal recessive, 1B DFNB1B A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. The disease is caused by mutations affecting the gene represented in this entry. Deafness, autosomal dominant, 3B DFNA3B A form of non-syndromic sensorineural hearing loss characterized by a variable phenotype, ranging from bilateral middle to high frequency hearing loss to profound sensorineural deafness. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the connexin family. Beta-type (group I) subfamily. Gene page Cell junction Cell membrane Complete proteome Deafness Disease mutation Ectodermal dysplasia Gap junction Hearing Membrane Non-syndromic deafness Palmoplantar keratoderma Polymorphism Reference proteome Transmembrane Transmembrane helix T M G R V E G R A V S G N S S T G E Q H MDWGTLHTFIGGVNKHSTSIGKVWITVIFIFRVMILVVAAQEVWGDEQEDFVCNTLQPGC KNVCYDHFFPVSHIRLWALQLIFVSTPALLVAMHVAYYRHETTRKFRRGEKRNDFKDIED IKKQKVRIEGSLWWTYTSSIFFRIIFEAAFMYVFYFLYNGYHLPWVLKCGIDPCPNLVDC FISRPTEKTVFTIFMISASVICMLLNVAELCYLLLKVCFRRSKRAQTQKNHPNHALKESK QNEMNELISDSGQNAITGFPS Q15021 D3DUR4 Q8N6U3 CND1_HUMAN Condensin complex subunit 1 Chromosome condensation-related SMC-associated protein 1 Chromosome-associated protein D2 hCAP-D2 Non-SMC condensin I complex subunit D2 XCAP-D2 homolog NCAPD2 CAPD2 CNAP1 KIAA0159 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT GLU-83 Bone marrow The finished DNA sequence of human chromosome 12. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] VARIANT GLU-83 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANTS GLU-83 AND SER-1321 Mammary gland A human condensin complex containing hCAP-C-hCAP-E and CNAP1, a homolog of Xenopus XCAP-D2, colocalizes with phosphorylated histone H3 during the early stage of mitotic chromosome condensation. PROTEIN SEQUENCE OF 359-365; 537-560; 698-709 AND 1324-1331 IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2 AND SMC4 SUBCELLULAR LOCATION Chromosome condensation by a human condensin complex in Xenopus egg extracts. IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPH AND NCAPG FUNCTION OF THE CONDENSIN COMPLEX Identification of a chromosome-targeting domain in the human condensin subunit CNAP1/hCAP-D2/Eg7. INTERACTION WITH HISTONE H1 AND HISTONE H3 MUTAGENESIS OF 1343-ARG--ARG-1348 AND 1358-LYS--LYS-1360 Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1310 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic kidney Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1339 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585; SER-1330; THR-1331; SER-1333; THR-1339; SER-1366; SER-1367; SER-1370 AND SER-1371 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333 AND THR-1339 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-1333 AND THR-1339 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1333 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585; SER-1310; SER-1315; SER-1330; THR-1331; SER-1333; THR-1339 AND SER-1395 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Initial characterization of the human central proteome. VARIANT [LARGE SCALE ANALYSIS] GLU-83 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Mutations in genes encoding condensin complex proteins cause microcephaly through decatenation failure at mitosis. INVOLVEMENT IN MCPH21 FUNCTION Diagnostic yield and novel candidate genes by exome sequencing in 152 consanguineous families with neurodevelopmental disorders. VARIANT MCPH21 SER-8 Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. May target the condensin complex to DNA via its C-terminal domain (PubMed:11136719). May promote the resolution of double-strand DNA catenanes (intertwines) between sister chromatids. Condensin-mediated compaction likely increases tension in catenated sister chromatids, providing directionality for type II topoisomerase-mediated strand exchanges toward chromatid decatenation. Required for decatenation of non-centromeric ultrafine DNA bridges during anaphase. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (PubMed:27737959). Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. Interacts with histones H1 and H3. Q15003 NCAPH false 7 Nucleus Cytoplasm Chromosome In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. The C-terminal domain interacts with histones H1 and H3, and may be responsible for condensin complex targeting to mitotic chromosomes. This domain is independent from the bipartite nuclear localization signal, although they are contained within the same region. Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPH and NCAPG subunits, activates the condensin complex and is required for chromosome condensation (By similarity). Microcephaly 21, primary, autosomal recessive MCPH21 A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH21 features include mild intellectual disability, intrauterine growth retardation, short stature, and microcephaly. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the CND1 (condensin subunit 1) family. Translation N-terminally shortened. Cell cycle Cell division Chromosome Complete proteome Cytoplasm Direct protein sequencing Disease mutation DNA condensation Mitosis Nucleus Phosphoprotein Polymorphism Primary microcephaly Reference proteome F S Q E K R V M T S RRTTRR AATTAA KKK AAA M I R L MAPQMYEFHLPLSPEELLKSGGVNQYVVQEVLSIKHLPPQLRAFQAAFRAQGPLAMLQHF DTIYSILHHFRSIDPGLKEDTLQFLIKVVSRHSQELPAILDDTTLSGSDRNAHLNALKMN CYALIRLLESFETMASQTNLVDLDLGGKGKKARTKAAHGFDWEEERQPILQLLTQLLQLD IRHLWNHSIIEEEFVSLVTGCCYRLLENPTINHQKNRPTREAITHLLGVALTRYNHMLSA TVKIIQMLQHFEHLAPVLVAAVSLWATDYGMKSIVGEIVREIGQKCPQELSRDPSGTKGF AAFLTELAERVPAILMSSMCILLDHLDGENYMMRNAVLAAMAEMVLQVLSGDQLEAAARD TRDQFLDTLQAHGHDVNSFVRSRVLQLFTRIVQQKALPLTRFQAVVALAVGRLADKSVLV CKNAIQLLASFLANNPFSCKLSDADLAGPLQKETQKLQEMRAQRRTAAASAVLDPEEEWE AMLPELKSTLQQLLQLPQGEEEIPEQIANTETTEDVKGRIYQLLAKASYKKAIILTREAT GHFQESEPFSHIDPEESEETRLLNILGLIFKGPAASTQEKNPRESTGNMVTGQTVCKNKP NMSDPEESRGNDELVKQEMLVQYLQDAYSFSRKITEAIGIISKMMYENTTTVVQEVIEFF VMVFQFGVPQALFGVRRMLPLIWSKEPGVREAVLNAYRQLYLNPKGDSARAKAQALIQNL SLLLVDASVGTIQCLEEILCEFVQKDELKPAVTQLLWERATEKVACCPLERCSSVMLLGM MARGKPEIVGSNLDTLVSIGLDEKFPQDYRLAQQVCHAIANISDRRKPSLGKRHPPFRLP QEHRLFERLRETVTKGFVHPDPLWIPFKEVAVTLIYQLAEGPEVICAQILQGCAKQALEK LEEKRTSQEDPKESPAMLPTFLLMNLLSLAGDVALQQLVHLEQAVSGELCRRRVLREEQE HKTKDPKEKNTSSETTMEEELGLVGATADDTEAELIRGICEMELLDGKQTLAAFVPLLLK VCNNPGLYSNPDLSAAASLALGKFCMISATFCDSQLRLLFTMLEKSPLPIVRSNLMVATG DLAIRFPNLVDPWTPHLYARLRDPAQQVRKTAGLVMTHLILKDMVKVKGQVSEMAVLLID PEPQIAALAKNFFNELSHKGNAIYNLLPDIISRLSDPELGVEEEPFHTIMKQLLSYITKD KQTESLVEKLCQRFRTSRTERQQRDLAYCVSQLPLTERGLRKMLDNFDCFGDKLSDESIF SAFLSVVGKLRRGAKPEGKAIIDEFEQKLRACHTRGLDGIKELEIGQAGSQRAPSAKKPS TGSRYQPLASTASDNDFVTPEPRRTTRRHPNTQQRASKKKPKVVFSSDESSEEDLSAEMT EDETPKKTTPILRASARRHRS P10589 COT1_HUMAN COUP transcription factor 1 COUP-TF1 COUP transcription factor I COUP-TF I Nuclear receptor subfamily 2 group F member 1 V-erbA-related protein 3 EAR-3 NR2F1 EAR3 ERBAL3 TFCOUP1 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo COUP transcription factor is a member of the steroid receptor superfamily. NUCLEOTIDE SEQUENCE [MRNA] OF 6-423 PARTIAL PROTEIN SEQUENCE Identification of two novel members of erbA superfamily by molecular cloning: the gene products of the two are highly related to each other. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Lung The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Lung Uterus Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II). INTERACTION WITH GTF2B Alien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamily. INTERACTION WITH COPS2 Nuclear orphan receptors regulate transcription of the gene for the human luteinizing hormone receptor. FUNCTION EAR2 and EAR3/COUP-TFI regulate transcription of the rat LH receptor. FUNCTION SUBUNIT INDUCTION BY GONADOTROPIN Solution structure of the zinc finger, C4-type domain of human COUP transcription factor 1. STRUCTURE BY NMR OF 84-162 NR2F1 mutations cause optic atrophy with intellectual disability. INVOLVEMENT IN BBSOAS VARIANTS BBSOAS LYS-112; ARG-113; PRO-115 AND PRO-252 CHARACTERIZATION OF VARIANTS BBSOAS LYS-112; ARG-113; PRO-115 AND PRO-252 Whole-exome sequencing improves the diagnosis yield in sporadic infantile spasm syndrome. VARIANT PHE-110 DEL Coup (chicken ovalbumin upstream promoter) transcription factor binds to the ovalbumin promoter and, in conjunction with another protein (S300-II) stimulates initiation of transcription. Binds to both direct repeats and palindromes of the 5'-AGGTCA-3' motif. Represses transcriptional activity of LHCG. Binds DNA as dimer; homodimer and probable heterodimer with NR2F6 (PubMed:11682620). Interacts with GTF2B; this interaction is direct (PubMed:1517211). Interacts with COPS2 (PubMed:10207062). Nucleus Inhibited by gonadotropin in granulosa cells. Bosch-Boonstra-Schaaf optic atrophy syndrome BBSOAS An autosomal dominant disorder characterized by optic atrophy associated with developmental delay and intellectual disability. Most patients also have evidence of cerebral visual impairment. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the nuclear hormone receptor family. NR2 subfamily. 3D-structure Activator Complete proteome Direct protein sequencing Disease mutation DNA-binding Metal-binding Nucleus Receptor Reference proteome Repressor Transcription Transcription regulation Zinc Zinc-finger R K S R R P L P MAMVVSSWRDPQDDVAGGNPGGPNPAAQAARGGGGGAGEQQQQAGSGAPHTPQTPGQPGA PATPGTAGDKGQGPPGSGQSQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTY TCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPNPGQYALTNGDPLN GHCYLSGYISLLLRAEPYPTSRYGSQCMQPNNIMGIENICELAARLLFSAVEWARNIPFF PDLQITDQVSLLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIR IFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDAAHIESLQEKSQCALEEYVRSQY PNQPSRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMSI QCS Q53ET0 Q6UUV8 Q7Z3X7 Q8N332 CRTC2_HUMAN CREB-regulated transcription coactivator 2 Transducer of regulated cAMP response element-binding protein 2 TORC-2 Transducer of CREB protein 2 CRTC2 TORC2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells. NUCLEOTIDE SEQUENCE [MRNA] VARIANT CYS-379 FUNCTION NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain The DNA sequence and biological annotation of human chromosome 1. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Brain The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] PNS Urinary bladder TORCs: transducers of regulated CREB activity. FUNCTION TISSUE SPECIFICITY The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive coincidence detector. INTERACTION WITH CREB1; SIK2; PPP3CA; YWHAB AND YWHAG TISSUE SPECIFICITY SUBCELLULAR LOCATION FUNCTION PHOSPHORYLATION AT SER-70; SER-90; SER-136; SER-171; SER-306; SER-368; SER-393; SER-433; SER-456; SER-489; SER-492 AND SER-613 IDENTIFICATION BY MASS SPECTROMETRY MUTAGENESIS OF SER-171 AND SER-368 Activation of cAMP response element-mediated gene expression by regulated nuclear transport of TORC proteins. SUBCELLULAR LOCATION PHOSPHORYLATION Silencing the constitutive active transcription factor CREB by the LKB1-SIK signaling cascade. FUNCTION SUBCELLULAR LOCATION PHOSPHORYLATION AT SER-171 MUTAGENESIS OF SER-171 TORC1 and TORC2 coactivators are required for tax activation of the human T-cell leukemia virus type 1 long terminal repeats. INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION) FUNCTION A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Transducer of regulated CREB-binding proteins (TORCs) induce PGC-1alpha transcription and mitochondrial biogenesis in muscle cells. FUNCTION TISSUE SPECIFICITY Dephosphorylation of TORC initiates expression of the StAR gene. FUNCTION PHOSPHORYLATION AT SER-171 Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Glucose controls CREB activity in islet cells via regulated phosphorylation of TORC2. PHOSPHORYLATION AT SER-171 AND SER-274 INTERACTION WITH 14-3-3 MUTAGENESIS OF SER-171; SER-274 AND SER-368 A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-86; SER-90; SER-136; SER-433; THR-501; SER-613 AND SER-624 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-86; SER-90; THR-192; SER-433; TYR-488; SER-490; SER-613 AND SER-624 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-501; SER-613 AND SER-624 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433; SER-613 AND SER-624 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-613 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-234 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A Recruitment. INTERACTION WITH YWHAE AND PPP3CA Single nucleotide polymorphisms in genes encoding LKB1 (STK11), TORC2 (CRTC2) and AMPK alpha2-subunit (PRKAA2) and risk of type 2 diabetes. VARIANT CYS-379 INVOLVEMENT IN SUSCEPTIBILITY TO NIDDM Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). Binds, as a tetramer, through its N-terminal region, with the bZIP domain of CREB1 (PubMed:15454081). 'Arg-314' in the bZIP domain of CREB1 is essential for this interaction (PubMed:15454081). Interaction, via its C-terminal, with TAF4, enhances recruitment of TAF4 to CREB1 (PubMed:15454081). Interacts with SIK2 (PubMed:15454081). Interacts with 14-3-3 proteins, YWHAB and YWHAG (PubMed:15454081, PubMed:18626018). Interacts (probably when phosphorylated at Ser-171) with YWHAE (PubMed:30611118). Interacts with calmodulin-dependent catalytic subunit PPP3CA/calcineurin A (PubMed:15454081, PubMed:30611118). Interaction with COP1 mediates nuclear export and degradation of CRTC2 (By similarity). (Microbial infection) Interaction with the human T-cell leukemia virus type 1 (HTLV-1) Tax protein is essential for optimal transcription activation by Tax. P18850 ATF6 false 3 P03206 BZLF1 true 3 Q15233 NONO false 2 Cytoplasm Nucleus Translocated from the nucleus to the cytoplasm on interaction of the phosphorylated form with 14-3-3 protein (PubMed:15454081). In response to cAMP levels and glucagon, relocated to the nucleus (PubMed:15454081). Most abundantly expressed in the thymus. Present in both B and T-lymphocytes. Highly expressed in HEK293T cells and in insulinomas. High levels also in spleen, ovary, muscle and lung, with highest levels in muscle. Lower levels found in brain, colon, heart, kidney, prostate, small intestine and stomach. Weak expression in liver and pancreas. Phosphorylation/dephosphorylation states of Ser-171 are required for regulating transduction of CREB activity (PubMed:15589160, PubMed:17210223). CRTCs/TORCs are inactive when phosphorylated, and active when dephosphorylated at this site (PubMed:17210223). This primary site of phosphorylation, is regulated by cAMP and calcium levels and is dependent on the phosphorylation of SIKs (SIK1 and SIK2) by LKB1 (PubMed:15454081, PubMed:16817901). Following adenylyl cyclase activation, dephosphorylated at Ser-171 by PPP3CA/calcineurin A resulting in CRTC2 dissociation from 14-3-3 proteins and PPP3CA (By similarity). Both insulin and AMPK increase this phosphorylation of CRTC2 while glucagon suppresses it (PubMed:15454081). Phosphorylation at Ser-274 by MARK2 is induced under low glucose conditions and dephosphorylated in response to glucose influx (PubMed:18626018). Phosphorylation at Ser-274 promotes interaction with 14-3-3 proteins and translocation to the cytoplasm (PubMed:18626018). Asymmetric dimethylation of arginine resisues by PRMT6 enhances the association of CRTC2 with CREB on the promoters of gluconeogenic genes. Variant Cys-379, under a dominant model, linked to a recessive mutation in LKB1, may be associated with susceptibility to type II or non-insulin-dependent diabetes mellitus (NIDDM). Belongs to the TORC family. 3D-structure Acetylation Activator Complete proteome Cytoplasm Host-virus interaction Isopeptide bond Methylation Nucleus Phosphoprotein Polymorphism Reference proteome Transcription Transcription regulation Ubl conjugation M V R C S A S A S A S A S A MGL HGP P S MATSGANGPGSATASASNPRKFSEKIALQKQRQAEETAAFEEVMMDIGSTRLQAQKLRLA YTRSSHYGGSLPNVNQIGSGLAEFQSPLHSPLDSSRSTRHHGLVERVQRDPRRMVSPLRR YTRHIDSSPYSPAYLSPPPESSWRRTMAWGNFPAEKGQLFRLPSALNRTSSDSALHTSVM NPSPQDTYPGPTPPSILPSRRGGILDGEMDPKVPAIEENLLDDKHLLKPWDAKKLSSSSS RPRSCEVPGINIFPSPDQPANVPVLPPAMNTGGSLPDLTNLHFPPPLPTPLDPEETAYPS LSGGNSTSNLTHTMTHLGISRGMGLGPGYDAPGLHSPLSHPSLQSSLSNPNLQASLSSPQ PQLQGSHSHPSLPASSLARHVLPTTSLGHPSLSAPALSSSSSSSSTSSPVLGAPSYPAST PGASPHHRRVPLSPLSLLAGPADARRSQQQLPKQFSPTMSPTLSSITQGVPLDTSKLSTD QRLPPYPYSSPSLVLPTQPHTPKSLQQPGLPSQSCSVQSSGGQPPGRQSHYGTPYPPGPS GHGQQSYHRPMSDFNLGNLEQFSMESPSASLVLDPPGFSEGPGFLGGEGPMGGPQDPHTF NHQNLTHCSRHGSGPNIILTGDSSPGFSKEIAAALAGVPGFEVSAAGLELGLGLEDELRM EPLGLEGLNMLSDPCALLPDPAVEESFRSDRLQ O43809 Q6IB85 Q6NE84 CPSF5_HUMAN Cleavage and polyadenylation specificity factor subunit 5 Cleavage and polyadenylation specificity factor 25 kDa subunit CPSF 25 kDa subunit Cleavage factor Im complex 25 kDa subunit CFIm25 Nucleoside diphosphate-linked moiety X motif 21 Nudix motif 21 Nudix hydrolase 21 Pre-mRNA cleavage factor Im 68 kDa subunit NUDT21 CFIM25 CPSF25 CPSF5 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits. NUCLEOTIDE SEQUENCE [MRNA] PROTEIN SEQUENCE OF 60-73 AND 183-189 FUNCTION IDENTIFICATION IN THE CLEAVAGE FACTOR IM COMPLEX SUBCELLULAR LOCATION Brain Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Retina The sequence and analysis of duplication-rich human chromosome 16. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Placenta PROTEIN SEQUENCE OF 2-15; 24-50 AND 79-131 CLEAVAGE OF INITIATOR METHIONINE ACETYLATION AT SER-2 IDENTIFICATION BY MASS SPECTROMETRY Ovarian carcinoma Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors. FUNCTION IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX RNA-BINDING A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im. FUNCTION RNA-BINDING Association of polyadenylation cleavage factor I with U1 snRNP. IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX INTERACTION WITH CPSF6 AND SNRNP70 IDENTIFICATION BY MASS SPECTROMETRY Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization. IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX INTERACTION WITH CPSF6; PAPOLA AND PABPN1 RNA-BINDING SUBCELLULAR LOCATION DOMAIN Analysis of a noncanonical poly(A) site reveals a tripartite mechanism for vertebrate poly(A) site recognition. FUNCTION INTERACTION WITH FIP1L1 Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] An interaction between U2AF 65 and CF I(m) links the splicing and 3' end processing machineries. FUNCTION Knock-down of 25 kDa subunit of cleavage factor Im in Hela cells alters alternative polyadenylation within 3'-UTRs. FUNCTION TISSUE SPECIFICITY Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processing. ACETYLATION AT LYS-23 INTERACTION WITH PAPOLA AND CPSF6 IDENTIFICATION BY MASS SPECTROMETRY MUTAGENESIS OF LYS-23 AND LYS-29 Mammalian pre-mRNA 3' end processing factor CF I m 68 functions in mRNA export. SUBCELLULAR LOCATION INTERACTION WITH CPSF6 Lysine acetylation targets protein complexes and co-regulates major cellular functions. ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-29 AND LYS-56 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation. FUNCTION IDENTIFICATION IN THE CLEAVAGE FACTOR IM COMPLEX SUBUNIT SUBSTRATE SPECIFICITY SUBCELLULAR LOCATION Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Genome-wide analysis of pre-mRNA 3' end processing reveals a decisive role of human cleavage factor I in the regulation of 3' UTR length. RNA-BINDING Cleavage factor Im is a key regulator of 3' UTR length. FUNCTION SUBUNIT An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. METHYLATION [LARGE SCALE ANALYSIS] AT ARG-15 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Colon carcinoma N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop codon and associates with alternative polyadenylation. INTERACTION WITH VIRMA Molecular mechanisms for CFIm-mediated regulation of mRNA alternative polyadenylation. FUNCTION INTERACTION WITH CPSF6 AND CPSF7 IDENTIFICATION IN THE MRNA 3'-PROCESSING COMPLEX MUTAGENESIS OF LEU-218 Crystal structure of the 25 kDa subunit of human cleavage factor Im. X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH BETA DIADENOSINE TETRAPHOSPHATE LACK OF METAL-BINDING HOMODIMERIZATION The crystal structure of human cleavage and polyadenylation specific factor-5 reveals a dimeric Nudix protein with a conserved catalytic site. X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH SULFATE Structural basis of UGUA recognition by the Nudix protein CFI(m)25 and implications for a regulatory role in mRNA 3' processing. X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEXES WITH RNA UGUAAA AND UUGUAU FUNCTION SUBUNIT MUTAGENESIS OF GLU-55; ARG-63; GLU-81 AND PHE-103 Crystal structure of the complex between the 25 kDA subunit and the 59 kDA subunit (RRM domain) of human cleavage factor Im. X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 21-227 IN COMPLEX WITH CPSF7 SUBUNIT Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping. X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-227 IN COMPLEX WITH CPSF6 AND RNA FUNCTION SUBUNIT MUTAGENESIS OF GLU-55; ARG-63; PHE-103; TYR-158 AND TYR-160 Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:9659921, PubMed:8626397, PubMed:14690600, PubMed:15937220, PubMed:17024186, PubMed:17098938, PubMed:29276085). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:9659921, PubMed:8626397, PubMed:14690600, PubMed:17024186). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:17098938, PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:17098938, PubMed:20695905, PubMed:29276085). NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7 (PubMed:29276085). Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing (PubMed:8626397, PubMed:14690600, PubMed:15169763, PubMed:17024186, PubMed:22813749, PubMed:20479262). The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (PubMed:20479262, PubMed:21295486). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function (By similarity). Binds to chromatin (By similarity). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (PubMed:18445629). Homodimer (via N- and C-terminus); binds RNA as homodimer (PubMed:20695905, PubMed:18445629, PubMed:20479262). Component of the cleavage factor Im (CFIm) complex which is a heterotetramer composed of two subunits of NUDT21/CPSF5 and two subunits of CPSF6 or CPSF7 or a heterodimer of CPSF6 and CPSF7 (PubMed:9659921, PubMed:8626397, PubMed:14561889, PubMed:20695905, PubMed:23187700, PubMed:21295486). The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery (PubMed:29276085). Interacts with CPSF6 (via the RRM domain); this interaction is direct and enhances binding to RNA (PubMed:14561889, PubMed:15169763, PubMed:17172643, PubMed:19864460, PubMed:29276085). Interacts with CPSF7 (PubMed:29276085, Ref.30). Interacts with FIP1L1; this interaction occurs in a RNA sequence-specific manner (PubMed:15937220). Interacts with PABPN1 (PubMed:15169763). Interacts (via N-terminus) with PAPOLA (via C-terminus); this interaction is direct and diminished by acetylation (PubMed:15169763, PubMed:17172643). Interacts with SNRNP70 (PubMed:14561889). Interacts with VIRMA (PubMed:29507755). false 5 P54253 ATXN1 false 2 Q86X55 CARM1 false 2 Q16630 CPSF6 false 5 Q16630-1 CPSF6 false 4 Q16630-2 CPSF6 false 3 Q8N684 CPSF7 false 5 Q08379 GOLGA2 false 5 P60660 MYL6 false 3 P14373 TRIM27 false 5 Nucleus Cytoplasm Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460). In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles (PubMed:15169763). Expressed in the heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Acetylated mainly by p300/CBP, recruited to the complex by CPSF6. Acetylation decreases interaction with PAPAO. Deacetylated by the class I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1 AND SIRT2. Belongs to the Nudix hydrolase family. CPSF5 subfamily. Lacks the conserved metal-binding residues in the NUDIX motif and does not have hydrolase activity. 3D-structure Acetylation Complete proteome Cytoplasm Differentiation Direct protein sequencing Methylation mRNA processing Nucleus Phosphoprotein Reference proteome RNA-binding K R K R E A R S E A F A F W E A Y A Y A L R D G N D L P MSVVPPNRSQTGWPRGVTQFGNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSV AARFQRMREEFDKIGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEG LKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQ EKALFAVPKNYKLVAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYN Q7Z5M8 Q3KNR9 Q3KNS0 Q7Z5M6 Q7Z5M7 Q8N4D2 AB12B_HUMAN Protein ABHD12B 3.-.-.- Abhydrolase domain-containing protein 12B Alpha/beta hydrolase domain-containing protein 12B ABHD12B C14orf29 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and characterization of C14orf29. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5) Kidney The DNA sequence and analysis of human chromosome 14. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-362 (ISOFORM 1) VARIANT LEU-334 Skin The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] VAL-282 Q7Z5M8-1 1 Variant 1 Q7Z5M8-2 2 Variant 3 Q7Z5M8-4 4 Variant 4 May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Q7Z5M8-5 5 No experimental confirmation available. Belongs to the serine esterase family. Translation N-terminally extended. Wrong choice of CDS. Wrong choice of CDS. Alternative splicing Complete proteome Hydrolase Polymorphism Reference proteome YFPHSCSMLGRKIAALYDSFTSKSL QSPISCGFKETRVKDSSHSELLPES IYRNIPGFLRTLMDALRKDKIIFPNDENVKFLSSPLLILHGEDDRTVPLEYG SLALSSRLECSGVISAHCKLRFPGSRHSPASASRVAGTTGARHHAWLIFLCF I V F L MDAQDCQAAASPEPPGPPARSCVAAWWDMVDRNLRYFPHSCSMLGRKIAALYDSFTSKSL KEHVFLPLIDMLIYFNFFKAPFLVDLKKPELKIPHTVNFYLRVEPGVMLGIWHTVPSCRG EDAKGKDCCWYEAALRDGNPIIVYLHGSAEHRAASHRLKLVKVLSDGGFHVLSVDYRGFG DSTGKPTEEGLTTDAICVYEWTKARSGITPVCLWGHSLGTGVATNAAKVLEEKGCPVDAI VLEAPFTNMWVASINYPLLKIYRNIPGFLRTLMDALRKDKIIFPNDENVKFLSSPLLILH GEDDRTVPLEYGKKLYEIARNAYRNKERVKMVIFPPGFQHNLLCKSPTLLITVRDFLSKQ WS P58335 Q4W5H6 Q59E98 Q5JPE9 Q86UI1 Q8N4J8 Q8NB13 Q96NC7 ANTR2_HUMAN Anthrax toxin receptor 2 Capillary morphogenesis gene 2 protein CMG-2 ANTXR2 CMG2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Differential gene expression during capillary morphogenesis in 3D collagen matrices: regulated expression of genes involved in basement membrane matrix assembly, cell cycle progression, cellular differentiation and G-protein signaling. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) FUNCTION VARIANT PRO-357 Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) INTERACTION WITH ANTHRAX TOXIN VARIANT PRO-357 Placenta Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-489 (ISOFORM 3) Synovial cell NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4) VARIANT PRO-357 Aortic endothelium Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-489 (ISOFORM 4) Lymph node The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-489 (ISOFORM 4) VARIANT PRO-357 Brain Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. INTERACTION WITH ANTHRAX TOXIN CLATHRIN-DEPENDENT INTERNALIZATION Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway. INTERNALIZATION Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Crystal structure of a complex between anthrax toxin and its host cell receptor. X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-212 OF COMPLEX WITH THE PROTECTIVE ANTIGEN OF BACILLUS ANTHRACIS Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor. X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-217 Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation. X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 38-218 OF COMPLEX WITH THE PROTECTIVE ANTIGEN OF BACILLUS ANTHRACIS Mutations in the gene encoding capillary morphogenesis protein 2 cause juvenile hyaline fibromatosis and infantile systemic hyalinosis. VARIANTS HFS PRO-45; THR-189; ARG-218; GLN-293 INS AND CYS-381 VARIANT PRO-357 TISSUE SPECIFICITY Mutations in capillary morphogenesis gene-2 result in the allelic disorders juvenile hyaline fibromatosis and infantile systemic hyalinosis. VARIANTS HFS ASP-105; THR-189 AND ARG-329 FUNCTION Capillary morphogenesis gene-2 mutation in infantile systemic hyalinosis: ultrastructural study and mutation analysis in a Taiwanese infant. INVOLVEMENT IN HFS Necessary for cellular interactions with laminin and the extracellular matrix. Binds laminin, and possibly also collagen type IV. Binds to the protective antigen (PA) of Bacillus anthracis in a divalent cation-dependent manner, with the following preference: calcium > manganese > magnesium > zinc. Binding of PA leads to heptamerization of the receptor-PA complex. P13423 pagA true 7 Isoform 1 Cell membrane Single-pass type I membrane protein Expressed at the cell surface. Isoform 2 Endoplasmic reticulum membrane Single-pass type I membrane protein Expressed predominantly within the endoplasmic reticulum and not at the plasma membrane. Isoform 3 Secreted P58335-1 1 P58335-2 2 P58335-3 3 May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. P58335-4 4 Expressed in prostate, thymus, ovary, testis, pancreas, colon, heart, kidney, lung, liver, peripheral blood leukocytes, placenta, skeletal muscle, small intestine and spleen. Binding to PA seems to be effected through the VWA domain. Hyaline fibromatosis syndrome HFS An autosomal recessive syndrome characterized by abnormal growth of hyalinized fibrous tissue usually affecting subcutaneous regions on the scalp, ears, neck, face, hands, and feet. The lesions appear as pearly papules or fleshy nodules. Additional features include gingival hypertrophy, progressive joint contractures resulting in severe limitation of mobility, osteopenia, and osteoporosis. Disease severity is variable. Some individuals manifest symptoms in infancy and have additional visceral or systemic involvement. Hyaline deposits in multiple organs, recurrent infections and intractable diarrhea often lead to early death. Surviving children may suffer from severely reduced mobility due to joint contractures. Other patients have later onset of a milder disorder affecting only the face and digits. The disease is caused by mutations affecting the gene represented in this entry. Upon binding of the protective antigen (PA) of Bacillus anthracis the complex moves to glycosphingolipid-rich lipid rafts, where it is internalized via a clathrin-dependent pathway. In the endosomal membrane, at pH under 7, the complex then rearranges and forms a pore allowing the other components of anthrax toxin to escape to the cytoplasm. Belongs to the ATR family. Translation N-terminally extended. Translation N-terminally shortened. 3D-structure Alternative splicing Cell membrane Complete proteome Disease mutation Disulfide bond Endoplasmic reticulum Glycoprotein Membrane Metal-binding Phosphoprotein Polymorphism Receptor Reference proteome Secreted Signal Transmembrane Transmembrane helix TLDVSVSFNGGKSVISGSLIVTATECSNGIAAI WGLTVTQAGVKWHDLTHCTFGLSGSGDPPTSAS VCIWECIEKELTA GRCINFSRVPSQ L P G D I T C R V VQ L R A P Y C MVAERSPARSPGSWLFPGLWLLVLSGPGGLLRAQEQPSCRRAFDLYFVLDKSGSVANNWI EIYNFVQQLAERFVSPEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGETYI HEGLKLANEQIQKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYCVGVLD FEQAQLERIADSKEQVFPVKGGFQALKGIINSILAQSCTEILELQPSSVCVGEEFQIVLS GRGFMLGSRNGSVLCTYTVNETYTTSVKPVSVQLNSMLCPAPILNKAGETLDVSVSFNGG KSVISGSLIVTATECSNGIAAIIVILVLLLLLGIGLMWWFWPLCCKVVIKDPPPPPAPAP KEEEEEPLPTKKWPTVDASYYGGRGVGGIKRMEVRWGDKGSTEEGARLEKAKNAVVKIPE ETEEPIRPRPPRPKPTHQPPQTKWYTPIKGRLDALWALLRRQYDRVSLMRPQEGDEVCIW ECIEKELTA Q15003 B4E189 Q8TB87 CND2_HUMAN Condensin complex subunit 2 Barren homolog protein 1 Chromosome-associated protein H hCAP-H Non-SMC condensin I complex subunit H XCAP-H homolog NCAPH BRRN BRRN1 CAPH KIAA0074 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Bone marrow Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Kidney Generation and annotation of the DNA sequences of human chromosomes 2 and 4. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT ALA-539 Placenta Cell cycle-dependent expression and nucleolar localization of hCAP-H. SUBCELLULAR LOCATION DURING THE CELL CYCLE TISSUE SPECIFICITY Chromosome condensation by a human condensin complex in Xenopus egg extracts. IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; NCAPD2 AND NCAPG FUNCTION OF THE COMPLEX Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma A quantitative atlas of mitotic phosphorylation. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-78; SER-81; SER-87; SER-92; SER-201; SER-432 AND THR-605 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Lysine acetylation targets protein complexes and co-regulates major cellular functions. ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-25; THR-49; SER-78; SER-81; SER-87; SER-92; SER-96; SER-201; SER-432 AND THR-598 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-70; SER-78; SER-81; SER-87; SER-89; SER-92; SER-201; SER-233; SER-496 AND THR-605 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-488 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Mutations in genes encoding condensin complex proteins cause microcephaly through decatenation failure at mitosis. INVOLVEMENT IN MCPH23 VARIANT MCPH23 LEU-243 CHARACTERIZATION OF VARIANT MCPH23 LEU-243 FUNCTION Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (PubMed:11136719). Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size (PubMed:27737959). Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG. O00571 DDX3X false 2 P04910 hta2 true 2 Q15021 NCAPD2 false 7 Q9BPX3 NCAPG false 7 O95347 SMC2 false 5 Q9NTJ3 SMC4 false 3 Nucleus Cytoplasm Chromosome In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. Q15003-1 1 Q15003-2 2 No experimental confirmation available. Widely expressed at low level. Expressed in proliferating cells. Phosphorylated by CDK1. Its phosphorylation, as well as that of NCAPD2 and NCAPG subunits, activates the condensin complex and is required for chromosome condensation (By similarity). Microcephaly 23, primary, autosomal recessive MCPH23 A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the CND2 (condensin subunit 2) family. Translation N-terminally shortened. 3D-structure Acetylation Alternative splicing Cell cycle Cell division Chromosome Complete proteome Cytoplasm Disease mutation DNA condensation Isopeptide bond Mitosis Nucleus Phosphoprotein Polymorphism Primary microcephaly Reference proteome Ubl conjugation P L V A MGPPGPALPATMNNSSSETRGHPHSASSPSERVFPMPLPRKAPLNIPGTPVLEDFPQNDD EKERLQRRRSRVFDLQFSTDSPRLLASPSSRSIDISATIPKFTNTQITEHYSTCIKLSTE NKITTKNAFGLHLIDFMSEILKQKDTEPTNFKVAAGTLDASTKIYAVRVDAVHADVYRVL GGLGKDAPSLEEVEGHVADGSATEMGTTKKAVKPKKKHLHRTIEQNINNLNVSEADRKCE IDPMFQKTAASFDECSTAGVFLSTLHCQDYRSELLFPSDVQTLSTGEPLELPELGCVEMT DLKAPLQQCAEDRQICPSLAGFQFTQWDSETHNESVSALVDKFKKNDQVFDINAEVDESD CGDFPDGSLGDDFDANDEPDHTAVGDHEEFRSWKEPCQVQSCQEEMISLGDGDIRTMCPL LSMKPGEYSYFSPRTMSMWAGPDHWRFRPRRKQDAPSQSENKKKSTKKDFEIDFEDDIDF DVYFRKTKAATILTKSTLENQNWRATTLPTDFNYNVDTLVQLHLKPGTRLLKMAQGHRVE TEHYEEIEDYDYNNPNDTSNFCPGLQAADSDDEDLDDLFVGPVGNSDLSPYPCHPPKTAQ QNGDTPEAQGLDITTYGESNLVAEPQKVNKIEIHYAKTAKKMDMKKLKQSMWSLLTALSG KEADAEANHREAGKEAALAEVADEKMLSGLTKDLQRSLPPVMAQNLSIPLAFACLLHLAN EKNLKLEGTEDLSDVLVRQGD Q6P656 Q8N906 CF161_HUMAN Cilia- and flagella-associated protein 161 CFAP161 C15orf26 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Heart The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis May play a role in motile cilia function, possibly by acting on dynein arm assembly. Q6P656-1 1 Q6P656-2 2 No experimental confirmation available. Alternative splicing Complete proteome Polymorphism Reference proteome QAAFPDPQLRLEYEGFPVPANAKILINHCHT NMKASPSRQMLKFSSITVTQIGDWQPTGIFS P S MAQNVYGPGVRIGNWNEDVYLEEELMKDFLEKRDKGKLLIQRSRRLKQNLLRPMQLSVTE DGYIHYGDKVMLVNPDDPDTEADVFLRGDLSLCMTPDEIQSHLKDELEVPCGLSAVQAKT PIGRNTFIILSVHRDATGQVLRYGQDFCLGITGGFDNKMLYLSSDHRTLLKSSKRSWLQE VYLTDEVSHVNCWQAAFPDPQLRLEYEGFPVPANAKILINHCHTNRGLAAHRHLFLSTYF GKEAEVVAHTYLDSHRVEKPRNHWMLVTGNPRDASSSMLDLPKPPTEDTRAMEQAMGLDT Q Q9Y5P2 O75605 Q0VDC3 Q96IU8 CSAG2_HUMAN Chondrosarcoma-associated gene 2/3 protein Cancer/testis antigen 24.2 CT24.2 Taxol-resistant-associated gene 3 protein TRAG-3 CSAG2 TRAG3 CSAG3 CSAG3A Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo TRAG-3, a novel gene, isolated from a taxol-resistant ovarian carcinoma cell line. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Ovary Identification a novel TRAG-3 variant gene, TRAG-3L, from a taxol-resistant ovarian cancer cell line SKOV-3. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) Ovary NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) Lung Drug-resistance related protein, its expression is associated with the chemotherapy resistant and neoplastic phenotype. May also be linked to the malignant phenotype. Q9Y5P2-1 1 Long TRAG-3L Q9Y5P2-2 2 Short TRAG-3S Q9Y5P2-3 3 Weakly expressed in kidney. Expressed in various tumor cell lines including carcinomas, myeloid and lymphoid malignancies, melanomas and prostate cancer. Overexpressed in taxol-resistant breast cancer line MDA 435TR and the doxorubicin-resistant multiple myelanoma lines RPMI-8226/Dox40 and RPMI-8226/MDR10V. Alternative splicing Complete proteome Reference proteome R H L H R I P L K E MWMGLIQLVEGVKRKDQGFLEKEFYHKTNIKMRCEFLACWPAFTVLGEAWRDQVDWSRLL RDAGLVKMSRKPRASSPLSNNHPPTPKRRGSGRHPLNPGPEALSKFPRQPGREKGPIKEV PGTKGSP Q9NW15 A8K8K3 A8MV74 B3KTZ1 B3KY93 B4DJ83 B4DNK2 B7WP12 C9JHS1 Q8IXX9 ANO10_HUMAN Anoctamin-10 Transmembrane protein 16K ANO10 TMEM16K Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5) VARIANT GLN-462 Substantia nigra Teratocarcinoma Testis Urinary bladder The DNA sequence, annotation and analysis of human chromosome 3. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) VARIANTS MET-561 AND ALA-583 Leukocyte Expression and function of epithelial anoctamins. FUNCTION SUBCELLULAR LOCATION Physiological roles and diseases of Tmem16/Anoctamin proteins: are they all chloride channels? REVIEW Anoctamins. REVIEW ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular proteins. SUBCELLULAR LOCATION The anoctamin (TMEM16) gene family: calcium-activated chloride channels come of age. REVIEW The anoctamin family: TMEM16A and TMEM16B as calcium-activated chloride channels. REVIEW ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY Anoctamins are a family of Ca2+ activated Cl- channels. FUNCTION SUBCELLULAR LOCATION Targeted next-generation sequencing of a 12.5 Mb homozygous region reveals ANO10 mutations in patients with autosomal-recessive cerebellar ataxia. VARIANT SCAR10 ARG-510 TISSUE SPECIFICITY Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1. Cell membrane Multi-pass membrane protein Shows predominantly an intracellular localization with a weak expression in the cell membrane. Q9NW15-1 1 Q9NW15-2 2 No experimental confirmation available. Q9NW15-3 3 No experimental confirmation available. Q9NW15-4 4 No experimental confirmation available. Q9NW15-5 5 No experimental confirmation available. Ref.1 (BAG60264) sequence is in conflict in position: 607:S->P. Highly expressed in the brain. Intermediate levels in the retina and heart and low levels in the placenta, liver, lung, duodenum, kidney, testis and spleen. In brain areas, highest expression in the frontal and occipital cortices and in the cerebellum. Lower expression in the fetal brain than in the adult brain. Spinocerebellar ataxia, autosomal recessive, 10 SCAR10 A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAR10 is characterized by onset in the teenage or young adult years of gait and limb ataxia, dysarthria, and nystagmus associated with marked cerebellar atrophy on brain imaging. The disease is caused by mutations affecting the gene represented in this entry. The term 'anoctamin' was coined because these channels are anion selective and have eight (OCT) transmembrane segments. There is some dissatisfaction in the field with the Ano nomenclature because it is not certain that all the members of this family are anion channels or have the 8-transmembrane topology. Belongs to the anoctamin family. Contaminating sequence. 3D-structure Alternative splicing Cell membrane Complete proteome Disease mutation Membrane Neurodegeneration Polymorphism Reference proteome Transmembrane Transmembrane helix GAQLLFRPLLNKYEQETLENQNLYLVGASKIRMLLGAEAVGLVKECNDNTMRAFTYRTRQNFKGFDDNNDDFLTMAECQFIIKHELENLRAKDEKMIPGYPQAKLYPGKSLL V HALLALKFILAFAIPDKPRHIQMKLARLEFESLEALKQQQMKLVTENLKEEPMESGKEKAT AASCKLVSLPRYSWSTNSVPGTVIGPGV R Q L R T M V A MKVTLSALDTSESSFTPLVVIELAQDVKEETKEWLKNRIIAKKKDGGAQLLFRPLLNKYE QETLENQNLYLVGASKIRMLLGAEAVGLVKECNDNTMRAFTYRTRQNFKGFDDNNDDFLT MAECQFIIKHELENLRAKDEKMIPGYPQAKLYPGKSLLRRLLTSGIVIQVFPLHDSEALK KLEDTWYTRFALKYQPIDSIRGYFGETIALYFGFLEYFTFALIPMAVIGLPYYLFVWEDY DKYVIFASFNLIWSTVILELWKRGCANMTYRWGTLLMKRKFEEPRPGFHGVLGINSITGK EEPLYPSYKRQLRIYLVSLPFVCLCLYFSLYVMMIYFDMEVWALGLHENSGSEWTSVLLY VPSIIYAIVIEIMNRLYRYAAEFLTSWENHRLESAYQNHLILKVLVFNFLNCFASLFYIA FVLKDMKLLRQSLATLLITSQILNQIMESFLPYWLQRKHGVRVKRKVQALKADIDATLYE QVILEKEMGTYLGTFDDYLELFLQFGYVSLFSCVYPLAAAFAVLNNFTEVNSDALKMCRV FKRPFSEPSANIGVWQLAFETMSVISVVTNCALIGMSPQVNAVFPESKADLILIVVAVEH ALLALKFILAFAIPDKPRHIQMKLARLEFESLEALKQQQMKLVTENLKEEPMESGKEKAT P24468 B4DQJ2 B6ZGU1 Q03754 Q3KQR7 COT2_HUMAN COUP transcription factor 2 COUP-TF2 Apolipoprotein A-I regulatory protein 1 ARP-1 COUP transcription factor II COUP-TF II Nuclear receptor subfamily 2 group F member 2 NR2F2 ARP1 TFCOUP2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Regulation of the apolipoprotein AI gene by ARP-1, a novel member of the steroid receptor superfamily. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) FUNCTION SUBUNIT NUCLEOTIDE SEQUENCE [GENOMIC DNA] DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) DNA-BINDING Characterisation of a new, DNA binding domain deficient chicken ovalbumin upstream promoter- transcription factor IIdelta isoform in the human brain. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) Liver Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) Mammary gland Isolation of cDNA coding for multiple human nuclear receptor clones. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) Kidney Analysis of the DNA sequence and duplication history of human chromosome 15. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) Brain Kidney Spleen The COUP-TFs compose a family of functionally related transcription factors. NUCLEOTIDE SEQUENCE [MRNA] OF 1-351 (ISOFORM 1) The nuclear orphan receptors COUP-TFII and Ear-2 act as silencers of the human oxytocin gene promoter. FUNCTION Heterodimeric interactions between chicken ovalbumin upstream promoter-transcription factor family members ARP1 and ear2. SUBUNIT INTERACTION WITH NR2F6 Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Identification of COUP-TFII orphan nuclear receptor as a retinoic acid-activated receptor. X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 175-414 FUNCTION SUBUNIT INTERACTION WITH NCOA1; NCOA2; NCOA3 AND PPARGC1A MUTAGENESIS OF ARG-228; TRP-249; SER-250; 253-PHE-VAL-254; 260-LEU-LEU-270; 364-LEU-LEU-365 AND ASP-398 Rare variants in NR2F2 cause congenital heart defects in humans. VARIANTS CHTD4 GLN-75 INS; VAL-170; ILE-205; ASP-251; TYR-341 AND SER-412 CHARACTERIZATION OF VARIANTS CHTD4 GLN-75 INS; ILE-205 AND TYR-341 Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A. Interacts with SQSTM1 (By similarity). Binds DNA as a dimer; homodimer or heterodimer with NR2F6. Interacts with NCOA1, NCOA2, NCOA3 and PPARGC1A. Interacts with ZFPM2 (By similarity). Q13485 SMAD4 false 4 Nucleus P24468-1 1 P24468-2 2 P24468-3 3 Ubiquitous. Congenital heart defects, multiple types, 4 CHTD4 A disorder characterized by congenital developmental abnormalities involving structures of the heart. Common defects include transposition of the great arteries, aortic stenosis, atrial septal defect, ventricular septal defect, pulmonic stenosis, and patent ductus arteriosus. Some patients also have cardiac arrhythmias, which may be due to the anatomic defect itself or to surgical interventions. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the nuclear hormone receptor family. NR2 subfamily. 3D-structure Activator Alternative splicing Complete proteome Disease mutation DNA-binding Metal-binding Nucleus Phosphoprotein Receptor Reference proteome Transcription Transcription regulation Zinc Zinc-finger MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGGQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRRE MQAVWDLEQGKYGF Q QQ D V N I E D S Y A S R E W A S A S W FV AA LL AA LL AA D R MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGGQ GGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRN CPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPTHGQFALTNGDPLNCHSYLSG YISLLLRAEPYPTSRFGSQCMQPNNIMGIENICELAARMLFSAVEWARNIPFFPDLQITD QVALLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVE KLKALHVDSAEYSCLKAIVLFTSDACGLSDVAHVESLQEKSQCALEEYVRSQYPNQPTRF GKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMAIQ Q8TE58 Q32MI6 ATS15_HUMAN A disintegrin and metalloproteinase with thrombospondin motifs 15 ADAM-TS 15 ADAM-TS15 ADAMTS-15 3.4.24.- ADAMTS15 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains. NUCLEOTIDE SEQUENCE [MRNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The consensus coding sequences of human breast and colorectal cancers. VARIANTS [LARGE SCALE ANALYSIS] ARG-770 AND GLY-878 Zn(2+) Binds 1 zinc ion per subunit. Secreted Extracellular space Extracellular matrix Expressed in fetal liver and kidney, but not in any of the adult tissues examined. The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. The precursor is cleaved by a furin endopeptidase. Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). Cleavage on pair of basic residues Complete proteome Disulfide bond Extracellular matrix Glycoprotein Hydrolase Metal-binding Metalloprotease Polymorphism Protease Reference proteome Repeat Secreted Signal Zinc Zymogen N S Q R C G MLLLGILTLAFAGRTAGGSEPEREVVVPIRLDPDINGRRYYWRGPEDSGDQGLIFQITAF QEDFYLHLTPDAQFLAPAFSTEHLGVPLQGLTGGSSDLRRCFYSGDVNAEPDSFAAVSLC GGLRGAFGYRGAEYVISPLPNASAPAAQRNSQGAHLLQRRGVPGGPSGDPTSRCGVASGW NPAILRALDPYKPRRAGFGESRSRRRSGRAKRFVSIPRYVETLVVADESMVKFHGADLEH YLLTLLATAARLYRHPSILNPINIVVVKVLLLRDRDSGPKVTGNAALTLRNFCAWQKKLN KVSDKHPEYWDTAILFTRQDLCGATTCDTLGMADVGTMCDPKRSCSVIEDDGLPSAFTTA HELGHVFNMPHDNVKVCEEVFGKLRANHMMSPTLIQIDRANPWSACSAAIITDFLDSGHG DCLLDQPSKPISLPEDLPGASYTLSQQCELAFGVGSKPCPYMQYCTKLWCTGKAKGQMVC QTRHFPWADGTSCGEGKLCLKGACVERHNLNKHRVDGSWAKWDPYGPCSRTCGGGVQLAR RQCTNPTPANGGKYCEGVRVKYRSCNLEPCPSSASGKSFREEQCEAFNGYNHSTNRLTLA VAWVPKYSGVSPRDKCKLICRANGTGYFYVLAPKVVDGTLCSPDSTSVCVQGKCIKAGCD GNLGSKKRFDKCGVCGGDNKSCKKVTGLFTKPMHGYNFVVAIPAGASSIDIRQRGYKGLI GDDNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSLLRYSGTGTAVESLQASRPILEPLT VEVLSVGKMTPPRVRYSFYLPKEPREDKSSHPKDPRGPSVLHNSVLSLSNQVEQPDDRPP ARWVAGSWGPCSASCGSGLQKRAVDCRGSAGQRTVPACDAAHRPVETQACGEPCPTWELS AWSPCSKSCGRGFQRRSLKCVGHGGRLLARDQCNLHRKPQELDFCVLRPC Q99798 O75809 Q5JZ41 Q6FHX0 Q8TAQ6 ACON_HUMAN Aconitate hydratase, mitochondrial Aconitase 4.2.1.3 Citrate hydro-lyase ACO2 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Cloning and structural characterization of human mitochondrial aconitase. NUCLEOTIDE SEQUENCE [MRNA] Skeletal muscle Characterization of the human mitochondrial aconitase gene (ACO2). NUCLEOTIDE SEQUENCE [GENOMIC DNA] A genome annotation-driven approach to cloning the human ORFeome. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] The DNA sequence of human chromosome 22. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Uterus PROTEIN SEQUENCE OF 69-84; 234-245; 313-323; 379-395; 412-424; 430-437; 507-520; 565-573; 608-628; 634-648 AND 657-671 IDENTIFICATION BY MASS SPECTROMETRY Brain Cajal-Retzius cell Fetal brain cortex Purification and partial amino acid sequence of human aconitase. PROTEIN SEQUENCE OF 69-83; 96-107; 371-396 AND 524-534 Lysine acetylation targets protein complexes and co-regulates major cellular functions. ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-605 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Erythroleukemia Mutations in the tricarboxylic acid cycle enzyme, aconitase 2, cause either isolated or syndromic optic neuropathy with encephalopathy and cerebellar atrophy. INVOLVEMENT IN OPA9 INVOLVEMENT IN ICRD VARIANTS OPA9 VAL-74 AND ARG-661 VARIANTS ICRD ASP-259 AND ASN-736 An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] The consensus coding sequences of human breast and colorectal cancers. VARIANT [LARGE SCALE ANALYSIS] ASN-697 Infantile cerebellar-retinal degeneration associated with a mutation in mitochondrial aconitase, ACO2. VARIANT ICRD ARG-112 CHARACTERIZATION OF VARIANT ICRD ARG-112 Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. citrate = isocitrate [4Fe-4S] cluster Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme. Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. Monomer. Mitochondrion Infantile cerebellar-retinal degeneration ICRD A severe autosomal recessive neurodegenerative disorder characterized by onset between ages 2 and 6 months of truncal hypotonia, athetosis, seizures, and ophthalmologic abnormalities, particularly optic atrophy and retinal degeneration. Affected individuals show profound psychomotor retardation, with only some achieving rolling, sitting, or recognition of family. Brain MRI shows progressive cerebral and cerebellar degeneration. The disease is caused by mutations affecting the gene represented in this entry. Optic atrophy 9 OPA9 A condition that features progressive visual loss in association with optic atrophy. Atrophy of the optic disk indicates a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the aconitase/IPM isomerase family. Aconitase entry 4Fe-4S Acetylation Complete proteome Direct protein sequencing Disease mutation Iron Iron-sulfur Lyase Metal-binding Mitochondrion Neurodegeneration Phosphoprotein Polymorphism Reference proteome Transit peptide Tricarboxylic acid cycle L V S R G D G R T N K N A S S T G D A D K S G D G R S T P H I M L P T K G R MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLN RPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAV PSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILEN YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSG WSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYN HRMKKYLSKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHP VAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGS EQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRN DANPETHAFVTSPEIVTALAIAGTLKFNPETDYLTGTDGKKFRLEAPDADELPKGEFDPG QDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAA GPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVI GDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHP VDKLTIQGLKDFTPGKPLKCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ Q9BZJ0 A8K9T4 Q5JY64 Q8WYI5 Q9BZI9 Q9BZJ1 Q9BZJ2 Q9GZW7 Q9H8F8 Q9NQH5 Q9NYD8 CRNL1_HUMAN Crooked neck-like protein 1 Crooked neck homolog hCrn CRNKL1 CRN CGI-201 MSTP021 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Identification of the human crooked neck gene by comparative gene identification. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5) TISSUE SPECIFICITY VARIANT ARG-35 Crooked neck is a component of the human spliceosome and implicated in the splicing process. NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2) FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY IDENTIFICATION IN SPLICEOSOMAL COMPLEX WITH HPRP8BP AND SNRPB2 T lymphoblast NUCLEOTIDE SEQUENCE (ISOFORM 2) Heart Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Placenta Trachea The DNA sequence and comparative analysis of human chromosome 20. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. IDENTIFICATION BY MASS SPECTROMETRY IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX FUNCTION SUBCELLULAR LOCATION SUBUNIT A novel rat orthologue and homologue for the Drosophila crooked neck gene in neural stem cells and their immediate descendants. SUBCELLULAR LOCATION Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones. INTERACTION WITH PPIL2 AND HSP90 An unappreciated role for RNA surveillance. SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S) Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2) CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2) IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma An Atomic Structure of the Human Spliceosome. STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) FUNCTION SUBUNIT SUBCELLULAR LOCATION Cryo-EM structure of a human spliceosome activated for step 2 of splicing. STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS) FUNCTION SUBUNIT SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY Involved in pre-mRNA splicing process. Identified in the spliceosome C complex (PubMed:11991638, PubMed:28502770, PubMed:28076346). Present in a spliceosome complex assembled in vitro containing CRNKL1, HPRP8BP and SNRPB2 (PubMed:12084575). Isoform 2 seems to be predominant in the spliceosome complex (PubMed:12084575). Interacts with PPIL2 (via the PPIase cyclophilin-type domain); they may form a trimeric complex with HSP90 (PubMed:15189447). Q8WUD4 CCDC12 false 2 Nucleus Nucleus speckle Colocalizes with core spliceosomal snRNP proteins (PubMed:12084575). Q9BZJ0-1 1 Type-II Q9BZJ0-2 2 Short Initiator Met-1 is removed. Contains a N-acetylalanine at position 2. Q9BZJ0-3 3 Q9BZJ0-4 4 Type-III May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Q9BZJ0-5 5 type-IV May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Widely expressed (PubMed:11342225). Highly expressed in testis (PubMed:12084575). Not detected in brain and lung (PubMed:12084575). Belongs to the crooked-neck family. Translation N-terminally extended. Translation N-terminally extended. 3D-structure Acetylation Alternative splicing Complete proteome mRNA processing mRNA splicing Nucleus Phosphoprotein Polymorphism Reference proteome Repeat Spliceosome TSRLELRSYSLAGRHGSTEPLVLAWSSQFRRLTWGCALDALHRSPCVAASQH ILASLLVSTALPTSSAAPGRRTPRAAARRTRSLVTMETVPPPSRLKREVKGQ G R F L Q H T A V I K R V A MTATVENLTFQKDTLGNAVDKNTSRLELRSYSLAGRHGSTEPLVLAWSSQFRRLTWGCAL DALHRSPCVAASQHGVTHLIRSSRTPHSTRCRKEDAQPGHHGNGAASVTAQARGQRSVLQ VPLPVPRSCLFSESFVVSVSSQSRFLASVPGTGVQRSTAADMAASTAAGKQRIPKVAKVK NKAPAEVQITAEQLLREAKERELELLPPPPQQKITDEEELNDYKLRKRKTFEDNIRKNRT VISNWIKYAQWEESLKEIQRARSIYERALDVDYRNITLWLKYAEMEMKNRQVNHARNIWD RAITTLPRVNQFWYKYTYMEEMLGNVAGARQVFERWMEWQPEEQAWHSYINFELRYKEVD RARTIYERFVLVHPDVKNWIKYARFEEKHAYFAHARKVYERAVEFFGDEHMDEHLYVAFA KFEENQKEFERVRVIYKYALDRISKQDAQELFKNYTIFEKKFGDRRGIEDIIVSKRRFQY EEEVKANPHNYDAWFDYLRLVESDAEAEAVREVYERAIANVPPIQEKRHWKRYIYLWINY ALYEELEAKDPERTRQVYQASLELIPHKKFTFAKMWILYAQFEIRQKNLSLARRALGTSI GKCPKNKLFKVYIELELQLREFDRCRKLYEKFLEFGPENCTSWIKFAELETILGDIDRAR AIYELAISQPRLDMPEVLWKSYIDFEIEQEETERTRNLYRRLLQRTQHVKVWISFAQFEL SSGKEGSLTKCRQIYEEANKTMRNCEEKEERLMLLESWRSFEEEFGTASDKERVDKLMPE KVKKRRKVQTDDGSDAGWEEYFDYIFPEDAANQPNLKLLAMAKLWKKQQQEKEDAEHHPD EDVDESES Q6PL45 C9J7K2 Q8IXU9 BRID5_HUMAN BRICHOS domain-containing protein 5 BRICD5 C16orf79 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANTS GLY-31 AND ILE-46 The sequence and analysis of duplication-rich human chromosome 16. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) VARIANTS GLY-31 AND ILE-46 Brain Q8N205 SYNE4 false 3 Membrane Multi-pass membrane protein Q6PL45-1 1 Q6PL45-2 2 Alternative splicing Complete proteome Disulfide bond Glycoprotein Membrane Polymorphism Reference proteome Transmembrane Transmembrane helix S G V I H Y F S MEPASCCAERPKPGPTGVKTKPSCGGWRAVSLLLLLLLLVLAAVGVVAGGLLGSAQGPPK PRLQTLRMTLPSPHMPRPNQTILVDVARNAATITVTPPQSNHSWAVLFDGQSGCICYRPE EHQVCFLRLMEDSDRETLRLLVDTSKVQEAWVPSQDTHHTQELLAVQGSLEVDPAQAGAL VQRLCMRTPIYWARRAEGESGPLWGKARPSGWFEELGAEPLEIHGTLATGPRRQRLIYLC IDICFPSNICVSVCFYYLPD P00846 Q34772 Q5S8W5 Q5S9E7 Q5S9I6 Q5SA31 Q6RPB7 Q6VHC0 Q6VHE0 Q6WQF4 Q7YCC1 Q7YCF8 Q7YCG1 Q85KU8 Q85KX1 Q85L05 Q8HNQ4 Q8HNQ8 Q8WCX6 Q9B2U5 Q9B2Z2 ATP6_HUMAN ATP synthase subunit a F-ATPase protein 6 MT-ATP6 ATP6 ATPASE6 MTATP6 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Sequence and organization of the human mitochondrial genome. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT VAL-14 Placenta Mitochondrial genome variation and the origin of modern humans. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS TYR-90; ALA-112 AND LEU-193 Major genomic mitochondrial lineages delineate early human expansions. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS TYR-90; ALA-112 AND THR-204 Mitochondrial genome diversity of native Americans supports a single early entry of founder populations into America. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS THR-80; TYR-90 AND ALA-112 Mitochondrial DNA transit between West Asia and North Africa inferred from U6 phylogeography. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS VAL-14 AND ALA-112 Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS ALA-112 AND LEU-193 Lineage-specific selection in human mtDNA: lack of polymorphisms in a segment of MTND5 gene in haplogroup J. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS THR-11; THR-60; ALA-112 AND ALA-133 Natural selection shaped regional mtDNA variation in humans. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS THR-60; TYR-90; ALA-112; LEU-117 AND THR-192 Phylogeny of east Asian mitochondrial DNA lineages inferred from complete sequences. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS SER-16; PRO-37; TYR-90; ALA-112; ALA-178; LEU-182 AND THR-204 The molecular dissection of mtDNA haplogroup H confirms that the Franco-Cantabrian glacial refuge was a major source for the European gene pool. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS THR-11 AND ALA-112 Phylogeny of mitochondrial DNA macrohaplogroup N in India, based on complete sequencing: implications for the peopling of South Asia. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS THR-7; THR-11; ILE-53; THR-60; ALA-112; VAL-121 AND ILE-213 Single nucleotide polymorphisms over the entire mtDNA genome that increase the power of forensic testing in Caucasians. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS THR-11; THR-60; ALA-112 AND VAL-192 Mitochondrial DNA diversity in indigenous populations of the southern extent of Siberia, and the origins of native american haplogroups. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS TYR-90 AND ALA-112 Late onset Leigh syndrome and ataxia due to a T to C mutation at bp 9,185 of mitochondrial DNA. INVOLVEMENT IN LS VARIANT LS PRO-220 Initial characterization of the human central proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Mitochondrial myopathy, lactic acidosis, and sideroblastic anemia (MLASA) plus associated with a novel de novo mutation (m.8969G>A) in the mitochondrial encoded ATP6 gene. INVOLVEMENT IN MLASA3 VARIANT MLASA3 ASN-148 N-terminome analysis of the human mitochondrial proteome. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] The 7q11.23 protein DNAJC30 interacts with ATP synthase and links mitochondria to brain development. INTERACTION WITH DNAJC30 Mitochondrial DNA mutation associated with Leber's hereditary optic neuropathy. VARIANTS ALA-59 AND ILE-213 A new mitochondrial disease associated with mitochondrial DNA heteroplasmy. VARIANT NARP ARG-156 Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. VARIANTS SER-33; ALA-59; TYR-61; TYR-90; ALA-112; THR-155; ILE-213 AND GLY-219 A second missense mutation in the mitochondrial ATPase 6 gene in Leigh's syndrome. VARIANT LS PRO-156 A mitochondrial mutation at nt 9101 in the ATP synthase 6 gene associated with deficient oxidative phosphorylation in a family with Leber hereditary optic neuroretinopathy. VARIANT LHON THR-192 A novel mitochondrial ATPase 6 point mutation in familial bilateral striatal necrosis. VARIANT MIBSN PRO-217 Leigh syndrome associated with the T9176C mutation in the ATPase 6 gene of mitochondrial DNA. VARIANT LS PRO-217 De novo mtDNA nt 8993 (T-G) mutation resulting in Leigh syndrome. VARIANT LS ARG-156 Fulminant Leigh syndrome and sudden unexpected death in a family with the T9176C mutation of the mitochondrial ATPase 6 gene. VARIANT LS PRO-217 Automating the identification of DNA variations using quality-based fluorescence re-sequencing: analysis of the human mitochondrial genome. VARIANT THR-155 Adult-onset ataxia and polyneuropathy caused by mitochondrial 8993T-->C mutation. VARIANT MC5DM1 PRO-156 INVOLVEMENT IN APAO VARIANT APAO PRO-156 Episodic ataxia and hemiplegia caused by the 8993T->C mitochondrial DNA mutation. VARIANT MC5DM1 PRO-156 VARIANT APAO PRO-156 Infantile cardiomyopathy caused by a mutation in the overlapping region of mitochondrial ATPase 6 and 8 genes. INVOLVEMENT IN CMHI Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MD and ATP5MPL (By similarity). Interacts with DNAJC30; interaction is direct (PubMed:30318146). Mitochondrion inner membrane Multi-pass membrane protein Neuropathy, ataxia, and retinitis pigmentosa NARP A syndrome characterized by variable combination of developmental delay, psychomotor retardation, hearing loss, optic atrophy and retinitis pigmentosa, dementia, seizures, ataxia, proximal neurogenic muscle weakness, and sensory neuropathy. The disease is caused by mutations affecting the gene represented in this entry. Leber hereditary optic neuropathy LHON A maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. Cardiac conduction defects and neurological defects have also been described in some patients. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. The disease is caused by mutations affecting the gene represented in this entry. Leigh syndrome LS An early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia. The disease is caused by mutations affecting the gene represented in this entry. Mitochondrial infantile bilateral striatal necrosis MIBSN Bilateral striatal necrosis is a neurological disorder resembling Leigh syndrome. The disease is caused by mutations affecting the gene represented in this entry. Mitochondrial complex V deficiency, mitochondrial 1 MC5DM1 A mitochondrial disorder with heterogeneous clinical manifestations including neuropathy, ataxia, hypertrophic cardiomyopathy. Hypertrophic cardiomyopathy can present with negligible to extreme hypertrophy, minimal to extensive fibrosis and myocyte disarray, absent to severe left ventricular outflow tract obstruction, and distinct septal contours/morphologies with extremely varying clinical course. The disease is caused by mutations affecting the gene represented in this entry. Myopathy, lactic acidosis, and sideroblastic anemia 3 MLASA3 A rare mitochondrial disorder characterized by sideroblastic anemia, muscle weakness, and exercise intolerance associated with persistent lactic acidemia. Additional MLASA3 features are failure to thrive, hearing loss, epilepsy, stroke-like episodes, and severe developmental delay. The disease is caused by mutations affecting the gene represented in this entry. Ataxia and polyneuropathy, adult-onset APAO A mitochondrial disease characterized by ataxia, axonal sensorimotor polyneuropathy, abnormal eye movements, and dysarthria. The disease is caused by mutations affecting the gene represented in this entry. Cardiomyopathy, infantile hypertrophic CMHI An infantile form of hypertrophic cardiomyopathy, a heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. The disease is caused by mutations affecting the gene represented in this entry. Belongs to the ATPase A chain family. ATP synthesis Cardiomyopathy CF(0) Complete proteome Disease mutation Hydrogen ion transport Ion transport Leber hereditary optic neuropathy Leigh syndrome Membrane Mitochondrion Mitochondrion inner membrane Neuropathy Polymorphism Primary mitochondrial disease Reference proteome Retinitis pigmentosa Transmembrane Transmembrane helix Transport A T A T I V G S T S L P T I T A M T H Y A T H Y T A F L I V T A S N A T L P L R A T T A S L I T I V F L I T V I L P S G L P MNENLFASFIAPTILGLPAAVLIILFPPLLIPTSKYLINNRLITTQQWLIKLTSKQMMTM HNTKGRTWSLMLVSLIIFIATTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGTVIMGFRSK IKNALAHFLPQGTPTPLIPMLVIIETISLLIQPMALAVRLTANITAGHLLMHLIGSATLA MSTINLPSTLIIFTILILLTILEIAVALIQAYVFTLLVSLYLHDNT Q5TEZ5 CF163_HUMAN Uncharacterized protein C6orf163 C6orf163 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo The DNA sequence and analysis of human chromosome 6. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] Coiled coil Complete proteome Reference proteome MIRNSDYKNFVCCAVCNKIIPPAPFGKTFKRIHEYKPLKTRFYTHKDILDIGANILKKEE QFQEDILREHIAKAEAEVWAQANERQKQAVEKALEEANDRHKIEIQILKEEHQKDLQEVT AKTKTEMYQNMDDEMKREHLAAEQRMVHRIQRIMMECHREKVEAVEKARAEERHIAQEAI QAQKSKAVEEIVNTGVTVIKDEKTSVARLMREKEHEMSILYGIAQRQRQEEVQEVLQEAE KTHQATLGNMMDKLANTQGELLSIAKQLGIMTNWKDFLEEELQETRMAFQKYINYTFPKL SPGHADFILPERKKTPSNLVIKENKTTLD O75752 D3DNM4 Q3Y531 Q6IAI5 Q8NFM8 Q8NFM9 Q9HA06 B3GL1_HUMAN UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1 Beta-1,3-GalNAc-T1 2.4.1.79 Beta-1,3-galactosyltransferase 3 Beta-1,3-GalTase 3 Beta3Gal-T3 Beta3GalT3 b3Gal-T3 Beta-3-Gx-T3 Galactosylgalactosylglucosylceramide beta-D-acetyl-galactosaminyltransferase Globoside synthase UDP-N-acetylgalactosamine:globotriaosylceramide beta-1,3-N-acetylgalactosaminyltransferase B3GALNT1 B3GALT3 UNQ531/PRO1074 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A family of human beta3-galactosyltransferases. Characterization of four members of a UDP-galactose:beta-N-acetyl-glucosamine/beta-N-acetyl-galactosamine beta-1,3-galactosyltransferase family. NUCLEOTIDE SEQUENCE [MRNA] COFACTOR TISSUE SPECIFICITY Expression cloning of human globoside synthase cDNAs. Identification of beta3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide beta1,3-N-acetylgalactosaminyltransferase. NUCLEOTIDE SEQUENCE [MRNA] FUNCTION CATALYTIC ACTIVITY COFACTOR TISSUE SPECIFICITY POLYMORPHISM Kidney NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] Molecular basis of the globoside-deficient P(k) blood group phenotype. Identification of four inactivating mutations in the UDP-N-acetylgalactosamine: globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS ALA-266 AND ARG-271 POLYMORPHISM The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANT ASN-126 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Transfers N-acetylgalactosamine onto globotriaosylceramide (PubMed:10993897). Plays a critical role in preimplantation stage embryonic development (By similarity). globoside Gb3Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = globoside Gb4Cer (d18:1(4E)) + H(+) + UDP Mg(2+) Protein modification; protein glycosylation. Golgi apparatus membrane Single-pass type II membrane protein Higher expression in heart and brain, and to a lesser extent in lung, placenta, kidney and testis. Lower expression in liver, spleen and stomach. No expression in skeletal muscle. Genetic variation in B3GALNT1 is responsible for the blood group P1PK system [MIM:111400]. Different combinations or absence of the P1PK antigens define 5 different phenotypes: P1, P2, P1(k), P2(k), and P. The P1(k) and P2(k) phenotypes are rare and characterized by lack of the P antigen. B3GALNT1 activity is responsible for the globoside blood group system (GLOB), which is defined by the P antigen [MIM:615021]. Belongs to the glycosyltransferase 31 family. Blood group antigen gene mutation database Beta-1,3-galactosyltransferase 3 Blood group antigen Complete proteome Glycoprotein Glycosyltransferase Golgi apparatus Magnesium Membrane Polymorphism Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix D N E A G R MASALWTVLPSRMSLRSLKWSLLLLSLLSFFVMWYLSLPHYNVIERVNWMYFYEYEPIYR QDFHFTLREHSNCSHQNPFLVILVTSHPSDVKARQAIRVTWGEKKSWWGYEVLTFFLLGQ EAEKEDKMLALSLEDEHLLYGDIIRQDFLDTYNNLTLKTIMAFRWVTEFCPNAKYVMKTD TDVFINTGNLVKYLLNLNHSEKFFTGYPLIDNYSYRGFYQKTHISYQEYPFKVFPPYCSG LGYIMSRDLVPRIYEMMGHVKPIKFEDVYVGICLNLLKVNIHIPEDTNLFFLYRIHLDVC QLRRVIAAHGFSSKEIITFWQVMLRNTTCHY Q01954 Q15840 BNC1_HUMAN Zinc finger protein basonuclin-1 BNC1 BNC Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Basonuclin: a keratinocyte protein with multiple paired zinc fingers. NUCLEOTIDE SEQUENCE [MRNA] Keratinocyte The human basonuclin gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Association of basonuclin with ability of keratinocytes to multiply and with absence of terminal differentiation. FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY Nuclear localization of basonuclin in human keratinocytes and the role of phosphorylation. SUBCELLULAR LOCATION NUCLEAR LOCALIZATION SIGNAL PHOSPHORYLATION AT SER-537 AND SER-541 MUTAGENESIS OF SER-537; SER-540 AND SER-541 Translocation of the zinc finger protein basonuclin from the mouse germ cell nucleus to the midpiece of the spermatozoon during spermiogenesis. TISSUE SPECIFICITY Basonuclins 1 and 2, whose genes share a common origin, are proteins with widely different properties and functions. SUBCELLULAR LOCATION TISSUE SPECIFICITY Transcriptional activator (By similarity). Likely specific for squamous epithelium and for the constituent keratinocytes at a stage either prior to or at the very beginning of terminal differentiation (PubMed:8034748). Required for the maintenance of spermatogenesis (By similarity). May also play a role in the differentiation of oocytes and the early development of embryos (By similarity). Interacts with HSF2BP (via C-terminus). Nucleus Cytoplasm Nucleus Nucleoplasm Relocates to the midpiece of the flagellum during late spermiogenesis in spermatids. In epidermis, primarily detected in cells of the basal or immediately suprabasal layers (at protein level) (PubMed:16891417). In hair follicles, mainly expressed in the outer root sheath (at protein level) (PubMed:8034748). Expressed in epidermis, testis and foreskin, and to a lower extent in thymus, spleen, mammary glands, placenta, brain and heart (PubMed:9687312). Phosphorylation on Ser-537 and Ser-541 leads to cytoplasmic localization. Complete proteome Cytoplasm Differentiation DNA-binding Metal-binding Nucleus Phosphoprotein Reference proteome Repeat Spermatogenesis Transcription Transcription regulation Zinc Zinc-finger S A S D S D S A S D PSRGGRGAA EPGRTRGG S C F N S T Q H MRRRPPSRGGRGAARARETRRQPRHRSGRRMAEAISCTLNCSCQSFKPGKINHRQCDQCK HGWVAHALSKLRIPPMYPTSQVEIVQSNVVFDISSLMLYGTQAIPVRLKILLDRLFSVLK QDEVLQILHALDWTLQDYIRGYVLQDASGKVLDHWSIMTSEEEVATLQQFLRFGETKSIV ELMAIQEKEEQSIIIPPSTANVDIRAFIESCSHRSSSLPTPVDKGNPSSIHPFENLISNM TFMLPFQFFNPLPPALIGSLPEQYMLEQGHDQSQDPKQEVHGPFPDSSFLTSSSTPFQVE KDQCLNCPDAITKKEDSTHLSDSSSYNIVTKFERTQLSPEAKVKPERNSLGTKKGRVFCT ACEKTFYDKGTLKIHYNAVHLKIKHKCTIEGCNMVFSSLRSRNRHSANPNPRLHMPMNRN NRDKDLRNSLNLASSENYKCPGFTVTSPDCRPPPSYPGSGEDSKGQPAFPNIGQNGVLFP NLKTVQPVLPFYRSPATPAEVANTPGILPSLPLLSSSIPEQLISNEMPFDALPKKKSRKS SMPIKIEKEAVEIANEKRHNLSSDEDMPLQVVSEDEQEACSPQSHRVSEEQHVQSGGLGK PFPEGERPCHRESVIESSGAISQTPEQATHNSERETEQTPALIMVPREVEDGGHEHYFTP GMEPQVPFSDYMELQQRLLAGGLFSALSNRGMAFPCLEDSKELEHVGQHALARQIEENRF QCDICKKTFKNACSVKIHHKNMHVKEMHTCTVEGCNATFPSRRSRDRHSSNLNLHQKALS QEALESSEDHFRAAYLLKDVAKEAYQDVAFTQQASQTSVIFKGTSRMGSLVYPITQVHSA SLESYNSGPLSEGTILDLSTTSSMKSESSSHSSWDSDGVSEEGTVLMEDSDGNCEGSSLV PGEDEYPICVLMEKADQSLASLPSGLPITCHLCQKTYSNKGTFRAHYKTVHLRQLHKCKV PGCNTMFSSVRSRNRHSQNPNLHKSLASSPSHLQ Q68CJ9 B2R7S6 B7ZL69 M0QYW7 Q6ZMC5 Q96TB9 CR3L3_HUMAN Cyclic AMP-responsive element-binding protein 3-like protein 3 cAMP-responsive element-binding protein 3-like protein 3 Transcription factor CREB-H Processed cyclic AMP-responsive element-binding protein 3-like protein 3 CREB3L3 CREBH HYST1481 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo CREB-H: a novel mammalian transcription factor belonging to the CREB/ATF family and functioning via the box-B element with a liver-specific expression. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) Complete sequencing and characterization of 21,243 full-length human cDNAs. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Ileal mucosa Thalamus The DNA sequence and biology of human chromosome 19. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4) Brain The liver-enriched transcription factor CREB-H is a growth suppressor protein underexpressed in hepatocellular carcinoma. FUNCTION TISSUE SPECIFICITY Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response. FUNCTION PROTEOLYTIC CLEAVAGE SELF-ASSOCIATION INTERACTION WITH ATF6 MUTAGENESIS OF ARG-361 N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H. GLYCOSYLATION AT ASN-413; ASN-420 AND ASN-427 Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD. GLYCOSYLATION AT SER-379 STRUCTURE OF CARBOHYDRATES IDENTIFICATION BY MASS SPECTROMETRY An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Transcription factor that may act during endoplasmic reticulum stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. In vitro, binds to the cAMP response element (CRE) and box-B element. Activates transcription through box-B element. Activates transcription through CRE (By similarity). Seems to function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes. May be involved in growth suppression. Binds DNA as a dimer (By similarity). Probably homodimerizes. Probably forms a heterodimer with ATF6. Interacts with ATF6. P18850 ATF6 false 2 O43889 CREB3 false 2 Q16649 NFIL3 false 2 Endoplasmic reticulum membrane Single-pass type II membrane protein Processed cyclic AMP-responsive element-binding protein 3-like protein 3 Nucleus Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus. Q68CJ9-1 1 Q68CJ9-2 2 Q68CJ9-4 3 No experimental confirmation available. Q68CJ9-5 4 Exclusively expressed in liver. Underexpressed in hepatocellular carcinoma tissues. Controlled by regulated intramembrane proteolysis (RIP). Following ER stress a fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 and site-2 proteases (PS1 and PS2). N- and O-glycosylated. N-glycosylation is required for optimal proteolytic activation. O-glycosylated with core 1 or possibly core 8 glycans. Belongs to the bZIP family. ATF subfamily. Aberrant splicing. Activator Alternative splicing Complete proteome DNA-binding Endoplasmic reticulum Glycoprotein Membrane Nucleus Phosphoprotein Reference proteome Signal-anchor Transcription Transcription regulation Transmembrane Transmembrane helix Unfolded protein response YEERVLKKIRRKIRNKQSAQESRKKKKEYIDGLETRMSACTAQNQELQRKVLHLEKQNLSLLEQLKKLQAIVVQSTSKSAQTGTCVAVLLLSFALIILP DVSLHCSESGVTEESLASREAKPVPLGATEETPGHCGAVHQQVSPDRHLCRSPVAVLCPHHPPLHQPFWPQQNREPWGLCACTSVLQNFAQRCCLPRGC R A L P MNTDLAAGKMASAACSMDPIDSFELLDLLFDRQDGILRHVELGEGWGHVKDQQVLPNPDS DDFLSSILGSGDSLPSSPLWSPEGSDSGISEDLPSDPQDTPPRSGPATSPAGCHPAQPGK GPCLSYHPGNSCSTTTPGPVIQVPEASVTIDLEMWSPGGRICAEKPADPVDLSPRCNLTV KDLLLSGSSGDLQQHHLGASYLLRPGAGHCQELVLTEDEKKLLAKEGITLPTQLPLTKYE ERVLKKIRRKIRNKQSAQESRKKKKEYIDGLETRMSACTAQNQELQRKVLHLEKQNLSLL EQLKKLQAIVVQSTSKSAQTGTCVAVLLLSFALIILPSISPFGPNKTESPGDFAPVRVFS RTLHNDAASRVAADAVPGSEAPGPRPEADTTREESPGSPGADWGFQDTANLTNSTEELDN ATLVLRNATEGLGQVALLDWVAPGPSTGSGRAGLEAAGDEL Q8IXJ9 B2RP59 Q5JWS9 Q8IYY7 Q9H466 Q9NQF8 Q9UFJ0 Q9UFP8 Q9Y2I4 ASXL1_HUMAN Putative Polycomb group protein ASXL1 Additional sex combs-like protein 1 ASXL1 KIAA0978 Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo A human homolog of Additional sex combs, additional sex combs-like 1, maps to chromosome 20q11. NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2) TISSUE SPECIFICITY The DNA sequence and comparative analysis of human chromosome 20. NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Prostate Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-1541 TISSUE SPECIFICITY Brain Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. SEQUENCE REVISION The full-ORF clone resource of the German cDNA consortium. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-1541 (ISOFORM 1) Testis Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor. FUNCTION INTERACTION WITH RARA; RXRA AND NCOA1 MUTAGENESIS OF VAL-1108 AND LEU-1111 A quantitative atlas of mitotic phosphorylation. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Mutations of polycomb-associated gene ASXL1 in myelodysplastic syndromes and chronic myelomonocytic leukaemia. INVOLVEMENT IN MDS Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Leukemic T-cell Frequent mutation of the polycomb-associated gene ASXL1 in the myelodysplastic syndromes and in acute myeloid leukemia. INVOLVEMENT IN MDS Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB. FUNCTION IDENTIFICATION IN THE PR-DUB COMPLEX INTERACTION WITH BAP1 ASXL1 represses retinoic acid receptor-mediated transcription through associating with HP1 and LSD1. RETRACTED PAPER Retraction: 'ASXL1 represses retinoic acid receptor-mediated transcription through associating with HP1 and LSD1'. RETRACTION NOTICE FOR PUBMED:19880879 De novo nonsense mutations in ASXL1 cause Bohring-Opitz syndrome. INVOLVEMENT IN BOPS Toward a comprehensive characterization of a human cancer cell phosphoproteome. PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501 AND SER-503 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cervix carcinoma Erythroleukemia Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator of RARA and RXRA through association with NCOA1. Acts as corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity (By similarity). Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Component of the PR-DUB complex, at least composed of BAP1 and ASXL1 (PubMed:20436459). Interacts with RARA, RXRA and NCOA1 (PubMed:16606617). Interacts with PPARA and PPARG (By similarity). P31749 AKT1 false 2 Q92560 BAP1 false 7 O75530 EED false 5 P03372 ESR1 false 2 Q15910 EZH2 false 6 P28700 Rxra true 2 P68306 THRB true 2 Nucleus Q8IXJ9-1 1 Q8IXJ9-2 2 Derived from EST data. No experimental confirmation available. Widely expressed at low level. Expressed in heart, brain, skeletal muscle, placenta, pancreas, spleen, prostate, small intestine, colon, peripheral blood, leukocytes, bone marrow and fetal liver. Highly expressed in testes. Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which may be required for an association with nuclear receptors. Bohring-Opitz syndrome BOPS A syndrome characterized by severe intrauterine growth retardation, poor feeding, profound mental retardation, trigonocephaly, prominent metopic suture, exophthalmos, nevus flammeus of the face, upslanting palpebral fissures, hirsutism, and flexion of the elbows and wrists with deviation of the wrists and metacarpophalangeal joints. The disease is caused by mutations affecting the gene represented in this entry. Myelodysplastic syndrome MDS A heterogeneous group of closely related clonal hematopoietic disorders. All are characterized by a hypercellular or hypocellular bone marrow with impaired morphology and maturation, dysplasia of the myeloid, megakaryocytic and/or erythroid lineages, and peripheral blood cytopenias resulting from ineffective blood cell production. Included diseases are: refractory anemia (RA), refractory anemia with ringed sideroblasts (RARS), refractory anemia with excess blasts (RAEB), refractory cytopenia with multilineage dysplasia and ringed sideroblasts (RCMD-RS); chronic myelomonocytic leukemia (CMML) is a myelodysplastic/myeloproliferative disease. MDS is considered a premalignant condition in a subgroup of patients that often progresses to acute myeloid leukemia (AML). The disease is caused by mutations affecting the gene represented in this entry. Belongs to the Asx family. Was previously reported to interact with KDM1A, CBX1, CBX3 and CBX5. However, this publication has been retracted.