Q8C5V8 CC187_MOUSE Coiled-coil domain-containing protein 187 Ccdc187 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis Coiled coil Complete proteome Reference proteome MTTPLMGVMPTSLRATLQNCSRGNQQEGLFSPKAMGRMAGQKDSTKPRDEVFHPHAAKDS LLATTLRWPVLSQQLSPPQTVPYVAWSGNIKDPSPYMKGCSLPMWSPCLDTKDVDSSVSS GRMSGSSGGHESCTLSHGPWKERPPLILGPQRQPRKSDPRLEQLRDKIRAQAQWQASCAS LGTSAPSSASCLYKTSTMLWRKTPKVTNALPVPAFPGSGVLRTAEHRGKDRASLSLRREL SKVPQHHTSVPRTNFKKVKNASCKREISKSSILRRTAKGRGSDRKAAAVKASPAHTWLCK PMSAHSDQQVSKHTPSLAFQDQSATIHGAMETLQDLRQQIQAGLELTRSPRVDRKLSLSK PKPQNLVGKRDRGLQSTQDMQGSSKTAWTVTEGKNSSLHRAGNLHSQQHRKKALAEHESC PRRTWTGQGQDSSFPRPGSTPEKPRFFSQRPWSALARQTYPQRTWDAQGQDISVQKSGSS LKKPSPFSQRPWSALAGRAYSACEDREVFEPSPWNSLSRPHSALQDPWSNSFVQRSSPSS KGKSAVPPPSKVKPAWPEPSQDLLQSKPAKEQDTPCPRPRGSLGQQHSSESLRDFMRQKA QARRQQALEQKALAAHTLELRNQRLQEVYRKQREAVLGKDIPVVSQRRPGIVTFVPMQSG GMEAPGSLGSPREQTWSKVTSGMVLGDQEAPDSFCLCLNKPWNRIETQDTGRPLEGYKQA RLQALETMAEALRQRVDILTTKLDKPTSPDTSGDLASDVLPLCPSTAPATPTLVPPSYLR TLMSKGGRESPRDLVDSQAEPLLLSTCFQDGEMLPWSPSWELPNPNLGTHIESQPQGPVS STPASVSQVIPHTQSCPAGSSSHGALSKEAIQGLEKKLQREMATLQALGACMKSSLGMPD APDPTRGSLWQEEMPEVKKEGLVTPWTTRSCGKGEPADRPWAGWSGGQGGLPWASSTA O35864 Q3UA70 Q8C1S1 CSN5_MOUSE COP9 signalosome complex subunit 5 SGN5 Signalosome subunit 5 3.4.-.- Jun activation domain-binding protein 1 Kip1 C-terminus-interacting protein 2 Cops5 Csn5 Jab1 Kic2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] INTERACTION WITH CDKN1B NIH Swiss NUCLEOTIDE SEQUENCE [MRNA] SUBCELLULAR LOCATION TISSUE SPECIFICITY BALB/cJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] BALB/cJ C57BL/6J Bone marrow Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain PROTEIN SEQUENCE OF 192-210 AND 220-230 IDENTIFICATION BY MASS SPECTROMETRY Brain Hippocampus IDENTIFICATION IN THE CSN COMPLEX C57BL/6J INTERACTION WITH HIF1A MUTAGENESIS OF ASP-151 INTERACTION WITH ID1 AND ID3 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Probable protease subunit 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 the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Promotes the proteasomal degradation of BRSK2. 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. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. a divalent metal cation Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9. In the complex, it probably interacts directly with COPS1, COPS2, COPS4, COPS6 and COPS7 (COPS7A or COPS7B) and COPS9. The CSN complex interacts with the BRISC complex. Also exists as monomeric form. Interacts with TP53, MIF, JUN, UCHL1, NCOA1, BCL3, GFER, PGR, LHCGR, SMAD4, SMAD7, ITGB2 and TOP2A. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5. Interacts with CDKN1B, HIF1A, ID1 and ID3. Interacts with IFIT3. Interacts with BRSK2 (By similarity). Interacts with ZDHHC16 (By similarity). Interacts with MINDY3 (By similarity). Interacts with FANK1; regulates the phosphorylation of JUN and the transcriptional activity of AP-1 (By similarity). Interacts with NUPR1; this interaction allows COPS5-dependent CDKN1B nuclear to cytoplasm translocation (By similarity). Cytoplasm Cytosol Nucleus Cytoplasm Perinuclear region Cytoplasmic vesicle Secretory vesicle Synaptic vesicle Nuclear localization is diminished in the presence of IFIT3. Widely expressed. The JAMM motif is essential for the protease activity of the CSN complex resulting in deneddylation of cullins. It constitutes the catalytic center of the complex. The CSN complex is associated with some 'Lys-63'-specific deubiquitination. Such activity is however not mediated by the core CSN complex but by the BRCC3/BRCC36 component of the BRISC complex (By similarity). Belongs to the peptidase M67A family. CSN5 subfamily. Acetylation Cell junction Complete proteome Cytoplasm Cytoplasmic vesicle Direct protein sequencing Hydrolase Metal-binding Metalloprotease Nucleus Protease Reference proteome Signalosome Synapse Zinc D N MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISAL ALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAY IENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGK VNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLEL LWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKL AKATRDSCKTTIEAIHGLMSQVIKDKLFNQINVA Q8BVN0 B2RSJ0 CC122_MOUSE Coiled-coil domain-containing protein 122 Ccdc122 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Coiled coil Complete proteome Reference proteome MSGDTERKNEVIPTKAAVKDTSALTDAVEQVAKQQQSQTSEIEKHKKILFQLQIELHELE KQIATIAEEAKETDRQMHRQDAAMENSKLQCGRLEAQIESLYSESLKLKFDTETAQEKFE EQMIKYNAYYVKIKAYKDNLGEIKSQCPFMTELYEKRDLIKNLKTMKEDLMENLQDSQGN CTIQIQEDISEIKNKIMTVKESITEKTSFVEEEKKTHEKLRKEIEVQHKRYDAILKRLHC QMNKIQLNRRKWQWNIQQLEKTAAELKKRIREKEASEIQSRPAAPWERIL Q8K4Q7 Q52KP2 CERK1_MOUSE Ceramide kinase mCERK 2.7.1.138 Acylsphingosine kinase Cerk Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY DEVELOPMENTAL STAGE Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Heart Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain FUNCTION CATALYTIC ACTIVITY TISSUE SPECIFICITY Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate (PubMed:16269826). Acts efficiently on natural and analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide), to a lesser extent on C2-ceramide and C6-dihydroceramide, but not on other lipids, such as various sphingosines (PubMed:16269826). Shows a greater preference for D-erythro isomer of ceramides (By similarity). Binds phosphoinositides (By similarity). an N-acylsphing-4-enine + ATP = ADP + H(+) + N-acylsphing-4-enine 1-phosphate ATP + N-(hexanoyl)sphing-4-enine = ADP + H(+) + N-hexanoylsphing-4-enine 1-phosphate ATP + N-(acetyl)-sphing-4-enine = ADP + H(+) + N-(acetyl)-sphing-4-enine-1-phosphate ATP + N-hexadecanoylsphing-4-enine = ADP + H(+) + N-(hexadecanoyl)-sphing-4-enine-1-phosphate ATP + N-(hexanoyl)-4-hydroxysphinganine = ADP + H(+) + N-(hexanoyl)-4-hydroxysphinganine-1-phosphate Ca(2+) Mg(2+) Cytoplasm Cell membrane Peripheral membrane protein High level expression in heart, brain, testis and pancreas; low expression in spleen, liver and lung; not detected in skeletal muscle. Highly expressed at 7 dpc and decreases rapidly thereafter. ATP-binding Calcium Cell membrane Complete proteome Cytoplasm Kinase Magnesium Membrane Nucleotide-binding Phosphoprotein Reference proteome Transferase M V D Y MGAMGAAEPLHSVLWVKRRRCAVSLEPARALLRWWRSPEPGPSAPGADARSVLVSEIIAV EEKDDCEKHASSGRWHKMENPFAFTVHRVKRVRHHRWKWARVTFWSADEQLCHLWLQTLR GLLESLTSRPKHLLVFINPFGGKGQGKRIYEKTVAPLFTLASITTEIIITEHANQAKETL YEINTDSYDGIVCVGGDGMFSEVLHGVIGRTQQSAGIDPNHPRAVLVPSTLRIGIIPAGS TDCVCYSTVGTNDAETSALHIIIGDSLAIDVSSVHYHNTLLRYSVSLLGYGFYGDLIKDS EKKRWMGLVRYDFSGLKTFLSHQYYEGTLSFLPAQHTVGSPRDNKPCRAGCFVCRQSKQQ LEEEEKKALYGLENAEEMEEWQVTCGKFLAINATNMSCACPRSPGGLSPFAHLGDGSSDL ILIRKCSRFNFLRFLIRHTNQEDQFDFTFVEVYRVKKFHFTSKHVEDEDNDSKEQEKQKF GKICKDRPSCTCSASRSSWNCDGEVMHSPAIEVRVHCQLVRLFARGIEEES Q6P5U8 A2APN1 Q8CDB5 CC148_MOUSE Coiled-coil domain-containing protein 148 Ccdc148 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) C57BL/6J Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Brain Q6P5U8-1 1 Q6P5U8-2 2 No experimental confirmation available. Alternative splicing Coiled coil Complete proteome Reference proteome IISDPRLRFELALREAGLHKTQYAKEMLPKIGPQKPPRKDTESTVFKV VLMGIALLVQSLG MLIKQHKQVWWQEQERLKGIRCKLESEIRSCLNEESIGSECFCELMNFEKELSEEWCAYL TAVIDPIQQLRTGLKRWYPTSQSAPCHEGSDATEVLEEVDFVKKQSKAAFERLHQEQWHL EEDLLDLSVKLLDHSSEEKPNLLSEQPMELVTLDCPYPDLKSSILNEFCNFTERYQEKLE DFDLQLEDIRSNFQLSAEEHWTYQAVLDQYPGNLLGRRALYLDMLQRYFPHKSRHHLVEH EKYCDQYHFAREQRRILIDNWSRSRKDFIQKAMLTLLEACAAHEMGSLLAKDRRRQQELC ADLKAKVSQWRAQQEELSRLEMEISARRREREEEKEKLWKKKELLRREETEIKIRKYWAM KQQKWQEMEKRDLRRLEELKKLMAEQSVKDRERVKYRQELLEKRLMERKKLALQEVQEEE ERERRLEALRKQVAVAVQSDPVRMMSETLAWKARTGSESEEEFILQKPLFTLTTYNEQQI ISDPRLRFELALREAGLHKTQYAKEMLPKIGPQKPPRKDTESTVFKV Q9D4V3 Q8CEQ7 Q9D4W3 CCD83_MOUSE Coiled-coil domain-containing protein 83 Ccdc83 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3) C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain Q9D4V3-1 1 Q9D4V3-2 2 No experimental confirmation available. Q9D4V3-3 3 No experimental confirmation available. Alternative splicing Coiled coil Complete proteome Reference proteome ENDW KMTG K Q S T E G MDSSAKGSKKDAPDGPPKDSKLPVSEALLDYHREIKENAVERFMFHIKKLREKNQKYQER NRRLKEEQNWHIKNLIKELKEKNLDEAPIVTREEVEEAMKEKWEFERQQEASLKEMRIQI NEAEKLFLEKLSEKEYWEEYKNVGSAQHAQLIVSLQNDIDTVKENAEKMSEQYKVTLEDE KKRISRETMIQLKQRKEWATQHAVRFIDKNNYREIWENDWLKKEGDTASFGNVLSLLDFL PPDLHTAEPCVSSGQSRGSLRILAPFALQLWSKLSGLLPTLVTPDPVCIIWSFGPGQTNS MAICP Q9ESW4 Q9D087 AGK_MOUSE Acylglycerol kinase, mitochondrial 2.7.1.107 2.7.1.138 2.7.1.94 Multiple substrate lipid kinase MuLK Multi-substrate lipid kinase Agk Mulk Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES TISSUE SPECIFICITY COFACTOR ACTIVITY REGULATION FVB/N Carcinoma NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J Head NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) FVB/N Liver Mammary tumor FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (PubMed:15252046). Phosphorylates ceramide but not sphingosine (PubMed:15252046). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (PubMed:18004883). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (By similarity). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (By similarity). In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23 (By similarity). Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth (By similarity). a monoacylglycerol + ATP = ADP + H(+) + monoacyl-sn-glycero-3-phosphate a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+) an N-acylsphing-4-enine + ATP = ADP + H(+) + N-acylsphing-4-enine 1-phosphate 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+) 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) a 1-acyl-sn-glycerol + ATP = a 1-acyl-sn-glycero-3-phosphate + ADP + H(+) 1-hexadecanoyl-sn-glycerol + ATP = 1-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+) 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + ATP = 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+) Mg(2+) Both the ceramide and diacylglycerol kinase activities are inhibited by sphingosine and stimulated by cardiolipin (PubMed:15252046). Both activities are stimulated by calcium when magnesium concentrations are low but inhibited by calcium when magnesium concentrations are high (PubMed:15252046). 45 uM for diacylglycerol 34 uM for ceramide 159 nmol/min/mg enzyme with dioeoylglycerol as substrate 37 nmol/min/mg enzyme with ceramide as substrate 23.6 nmol/min/mg enzyme with 1,2-dioleoylglycerol as substrate 10.21 nmol/min/mg enzyme with 2,3-dioleoylglycerol as substrate Lipid metabolism; glycerolipid metabolism. Component of the TIM22 complex, which core is composed of TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and TIMM29. Mitochondrion inner membrane Peripheral membrane protein Mitochondrion intermembrane space Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane. It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it. Q9ESW4-1 1 Q9ESW4-2 2 No experimental confirmation available. Ubiquitously expressed. Belongs to the AGK family. Was originally (PubMed:15252046) thought to have ceramide kinase activity. Such activity is however unlikely in vivo. Acetylation Alternative splicing ATP-binding Complete proteome Kinase Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Reference proteome Transferase MTAFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQV KKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTVVKTDYEGQAKKLLELMESTDVII VAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGQTSSLSHTLFAESGNKVQHITDATL AIVKGETVPLDVLQIKGEKEQPVYAMTGLRWGSFRDAGVKVSKYWYLGPLKTKAAHFFST LQEWPQTHQASISYTGPRERPPIEPEETPPRPSLYRRILRRLASFWAQPQDASSREVSPE VWKDVQLSTIELSITTRNTQLDLMSKEDFMNICIEPDTVSKGDFIIIGSKKVRDPGLRAA GTECLQASHCTLVLPEGTEGSFSIDSEEYEAMPVEVKLLPRKLRFFCDPRKREQMLPSTS Q Q8CDI7 E9QMC0 CC150_MOUSE Coiled-coil domain-containing protein 150 Ccdc150 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J Coiled coil Complete proteome Reference proteome V I METNLLPGGPSYGLLDESGVQMETTVCRPVLSPTHINGTASETFTVLQQKMRIVEEQTSS LRDDLIMLGYGDRRGQLETPNYLEDPASQKAISPIPNEVICPESPGNLWRNYEFLVNRMC YLENLIQSLKMNIFHLQTEKESNPQKTAFLNDQLNIIQGEHSKGLKLLQLEVMNLRQQLK VVKEEEDRAQDEMQRLTATLEIATETKKNAAVIEEELKTTKRKMNLKIQELRRQLAQEKL VRESLETSASSMLLKVQEMGSVVEAERQQVHALQEKCTALHSSMKTTQDLLAQEQRKNED LGMTISQLKSDLNSRDNLICKLVEENKATQISLKKEHEENIYLKSEILSLQDVSGKAQVL NDQLSKKCSELTSMLQVVKMENSRIIAEHQAILKVEQKMITETFQEQNLLLDAAHASITG ELQAVQNEKAQLQIHLDHLILEHNQCLQKSQEAEKRTVVQKELLESTIARLQGELKASLQ EKKSLLEKNEWFQREVNKTEKEVAKEKCNLEKELAESKEDINVLNQNLQTLMEENKHLTN KMASLEHHKATSDYQGKVEKALEKITDSKNMLAYEKGKLQTKVKQLEAQLHTFAETMLQK DHLHKLNKALEVKYTQANSELSASKAYLEQTEAHLKEMKSILGKNEEELAQAVKCRDAAL KESQKLKGDLKALEDRESKKVGNFQKQLAEAKEDNCKVTIMLENVLASHSKMQGALEKVQ IELGRRDSEIAGLKKERSLNQQRVQKLEAEVDQWQARMLIVEAQHGSEIEPLQKSLDITR EDNRKLAMSLEQALQTNGHLQSKLDHLQEKLESKERERQSLEAFKEQVAEESKVEAELHA ERIEALRKQFQTERETAKKASQREVSELKKALDEANFRSVEVSRANRELRHKATELEKVV NSNKEKLKNQRAQIKLHLSAKANNAQNMERMKQIEMELRQMEIIKDQYQKKNYEQSLSIQ RFVSEMNTLQKEMELLTKSQYETSARNKQQELRLVAERKMRLELENRCKELEETIRHLKR CKEATENKLKEASVESEQITANLEEAHRWFKCRFDGLQLELTKNRLQRLPREDRWLEENQ DMMHNVATSQSVLHRWETKQKYHSDTERKK Q7JJ13 O54795 O88411 Q3UGI0 Q5DTS6 Q794H7 Q794H9 Q99PC5 BRD2_MOUSE Bromodomain-containing protein 2 Female sterile homeotic-related protein 1 Fsrg-1 Protein RING3 Brd2 Fsrg1 Kiaa4005 Ring3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY SUBCELLULAR LOCATION FUNCTION Testis NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1) NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-549 (ISOFORM 2) TISSUE SPECIFICITY SUBCELLULAR LOCATION FUNCTION 129/SvJ CD-1 Testis NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Amnion Visual cortex NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Fetal brain NUCLEOTIDE SEQUENCE [MRNA] OF 1-503 C57BL/6J PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-300 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-300 AND SER-304 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Liver Pancreas Spleen Testis Binds hyperacetylated chromatin and plays a role in the regulation of transcription, probably by chromatin remodeling. Regulates transcription of the CCND1 gene. Plays a role in nucleosome assembly (By similarity). May play a role in spermatogenesis or folliculogenesis. Homodimer. Interacts with E2F1 and with histone H4 acetylated at 'Lys-13' (By similarity). Nucleus Detected on chromatin and nucleosomes. Q7JJ13-1 1 Q7JJ13-2 2 No experimental confirmation available. Predominantly expressed in the testis, followed by ovary, placenta, embryo and to a lower extent in somatic tissues. One bromodomain is sufficient for a partial interaction with histone H4 acetylated at 'Lys-13'. Acetylation Alternative splicing Bromodomain Chromatin regulator Complete proteome Nucleus Phosphoprotein Reference proteome Repeat Transcription Transcription regulation E K A G P L QVA LVP MLQNVTPHKLPGEGNAGLLGLGPEAAAPGKRIRKPSLLYEGFESPTMASVPALQLAPANP PPPEVSNPKKPGRVTNQLQYLHKVVMKALWKHQFAWPFRQPVDAVKLGLPDYHKIIKQPM DMGTIKRRLENNYYWAASECMQDFNTMFTNCYIYNKPTDDIVLMAQTLEKIFLQKVASMP QEEQELVVTIPKNSHKKGAKLAALQGSITSAHQVPAVSSVSHTALYTPPPEIPTTVLNIP HPSVISSPLLKSLHSAGPPLLAVSAAPPAQPLAKKKGVKRKADTTTPTPTAILAPGSPAS PPGSLEPKAARLPPMRRESGRPIKPPRKDLPDSQQQHQSSKKGKLSEQLKHCNGILKELL SKKHAAYAWPFYKPVDASALGLHDYHDIIKHPMDLSTVKRKMENRDYRDAQEFAADVRLM FSNCYKYNPPDHDVVAMARKLQDVFEFRYAKMPDEPLEPGPLPVSTALPPGLTKSSSESS SEESSSESSSEEEEEEEEDEDEEESESSDSEEERAHRLAELQEQLRAVHEQLAALSQGPI SKPKRKREKKEKKKKRKAEKHRGRIGIDEDDKGPRAPRPPQPKKSKKAGGGGSNATTLSH PGFGTSGGSSNKLPKKSQKTAPPVLPTGYDSEEEEESRPMSYDEKRQLSLDINKLPGEKL GRVVHIIQAREPSLRDSNPEEIEIDFETLKPSTLRELERYVLSCLRKKPRKPYTIRKPVG KTKEELALEKKRELEKRLQDVSGQLNSTKKPPKKASEKTESSAQQVAVSRLSASSSSSDS SSSSSSSSSSDTSDSDSG Q99PV5 BHE41_MOUSE Class E basic helix-loop-helix protein 41 bHLHe41 Class B basic helix-loop-helix protein 3 bHLHb3 Differentially expressed in chondrocytes protein 2 mDEC2 Bhlhe41 Bhlhb3 Dec2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION INTERACTION WITH ARNTL FUNCTION SUBUNIT HETERODIMERIZATION WITH BHLHE40 FUNCTION FUNCTION INDUCTION TRANSGENIC MICE FUNCTION INTERACTION WITH CIART FUNCTION INTERACTION WITH NR0B2 AND HNF1A Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA/B/G, NR1H3/LXRA, NR1H4 and VDR transactivation activity. Inhibits HNF1A-mediated transactivation of CYP1A2, CYP2E1 AND CYP3A11 (PubMed:30555544). Homodimer (PubMed:15560782). Heterodimer with BHLHE40/DEC1 (PubMed:15560782). Interacts with CIART (PubMed:24736997). Interacts with ARNTL/BMAL1 (PubMed:12397359). Interacts with RXRA (By similarity). Interacts with NR0B2 and HNF1A (PubMed:30555544). P28033 Cebpb false 5 Q3TQ03 Ciart false 2 Q16665 HIF1A true 3 P25789 PSMA4 true 2 Nucleus Expressed in skeletal muscle, brain and lung. Expressed in a circdadian manner in the liver with a peak at ZT10. Activity profiles and sleep recordings of transgenic mice carrying the mutation Arg-325 show increased vigilance time and less sleep time than control mice in a zeitgeber time- and sleep deprivation-dependent manner. Biological rhythms Complete proteome DNA-binding Isopeptide bond Nucleus Reference proteome Repressor Transcription Transcription regulation Ubl conjugation MDEGIPHLQERQLLEHRDFIGLDYSSLYMCKPKRSLKRDDTKDTYKLPHRLIEKKRRDRI NECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHLKALTALTEQQHQKIIALQNGERSL KSPVQADLDAFHSGFQTCAKEVLQYLARFESWTPREPRCAQLVSHLHAVATQLLTPQVPS GRGSGRAPCSAGAAAASGPERVARCVPVIQRTQPGTEPEHDTDTDSGYGGEAEQGRAAVK QEPPGDSSPAPKRPKLEARGALLGPEPALLGSLVALGGGAPFAQPAAAPFCLPFYLLSPS AAAYVQPWLDKSGLDKYLYPAAAAPFPLLYPGIPAAAAAAAAAAFPCLSSVLSPPPEKAG ATAGAPFLAHEVAPPGPLRPQHAHSRTHLPRAVNPESSQEDATQPAKDAP P0C7Q1 CC153_MOUSE Coiled-coil domain-containing protein 153 Ccdc153 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J Belongs to the UPF0610 family. Coiled coil Complete proteome Reference proteome MPPKTKGRGRKAEARKKKKNSSPGVEAEAKHRLVLLEKELLQDRLALQREEARRAKASED RLKQRLQGLEAELERTQSEGKAIYAEMSRQRQALKEELGTRSKQLEEEVRSLKEQLETCQ REAKTAKEEAERALRKQDGTLAQLHAHVADMEAKYEEILHDNLDCLLAKLRVVKPHWDAN VLRLHTRLKEQLRQFGLNPLDL Q8K1L0 Q3TCE1 Q3U228 Q8BWH8 CREB5_MOUSE Cyclic AMP-responsive element-binding protein 5 CREB-5 cAMP-responsive element-binding protein 5 CRE-BPa Creb5 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) NOD NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-357 (ISOFORM 1) Mammary gland Binds to the cAMP response element and activates transcription. Binds DNA as a homodimer or as a heterodimer with JUN or ATF2/CREBP1. Nucleus Q8K1L0-1 1 Q8K1L0-2 2 Belongs to the bZIP family. Activator Alternative splicing Complete proteome DNA-binding Nucleus Reference proteome Transcription Transcription regulation MSMR MNLEQERPFVCSAPGCSQRFPTEDHLMIHRHKHEMTLKFPSIKTDNMLSDQTPTPTRFLKNCEEVGLFSELDCSFEHEFRKAQEEENSKRNISMHNTVGGTMTGPGAHQLGSTRMPNHDSSVVIQQAMPSPQSSSVITQAPSTNRQIG RLKAALTHHPAAMS NLHRPSPLALCLHS H P MSMRPVPGSLSSLLHLHNRQRQPMPASMPGTLPNPTMPGSSAVLMPMERQMSVNSSIMGM QGPNLSNPCASPQVQPMHSEAKMRLKAALTHHPAAMSNGNMSTIGHMMEMMGSRQDQTPH HHLHSHPHQHQTLPPHHPYPHQHQHPAHHPHPQPHHQQNHPHHHSHSHLHAHPAHHQTSP HPPLHTGNQAQVSPATQQMQPTQTIQPPQPTGGRRRRVVDEDPDERRRKFLERNRAAATR CRQKRKVWVMSLEKKAEELTQTNMQLQNEVSMLKNEVAQLKQLLLTHKDCPITAMQKESQ GYLSPESSPPASPVPACSQQQVIQHNTITTSSSVSEVVGSSTLSQLTTHRTDLNPIL P28651 Q8CF58 Q91XF6 CAH8_MOUSE Carbonic anhydrase-related protein CARP Carbonic anhydrase VIII CA-VIII Ca8 Cals Cals1 Car8 Carp Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ Brain NUCLEOTIDE SEQUENCE [MRNA] PROTEIN SEQUENCE OF N-TERMINUS MUTAGENESIS NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Colon IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Liver Lung Does not have a carbonic anhydrase catalytic activity. Expressed only in Purkinje cells. Belongs to the alpha-carbonic anhydrase family. Although it belongs to the alpha-carbonic anhydrase family, Arg-117 is present instead of the conserved His which is a zinc-binding residue. It is therefore expected that this protein lacks carbonic anhydrase activity. Complete proteome Direct protein sequencing Metal-binding Phosphoprotein Reference proteome Zinc EVR QVH A V V I Q SSQRDREQTHLHQ MADLSFIEDAVAFPEKEEDEEEEEEEGVEWGYEEGVEWGLVFPDANGEYQSPINLNSREA RYDPSLLDVRLSPNYVVCRDCEVTNDGHTIQVILKSKSVLSGGPLPQGQEFELYEVRFHW GRENQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIAIIALFVQIGKEHVGL KAVTEILQDIQYKGKSKTIPCFNPNTLLPDPLLRDYWVYEGSLTIPPCSEGVTWILFRYP LTISQMQIEEFRRLRTHVKGAELVEGCDGILGDNFRPTQPLSDRVIRAAFQ Q8BI72 CARF_MOUSE CDKN2A-interacting protein Collaborator of ARF Cdkn2aip Carf Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Head IDENTIFICATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-234 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Heart Kidney Liver Lung Pancreas Spleen Testis Regulates DNA damage response and cell proliferation in a dose-dependent manner through a number of signaling pathways involved in cell proliferation, apoptosis and senescence. Interacts with CDKN2A/p14ARF, p53/TP53 and MDM2. Interacts with CHEK2 and MAPK3. Interacts with XRN2. Nucleus Nucleoplasm May be ubiquitinated. Belongs to the CARF family. Acetylation Complete proteome Isopeptide bond Nucleus Phosphoprotein Reference proteome RNA-binding Ubl conjugation MAQEVSEYLSQNPRVAAWVETLRCEGETDKHWRHRREFLLRNAGDLVPATDETADAESGA RTRQLQQLVSFSMAWANHVFLGCRYPQKVMDKILSMAEGIKVTDAPIHTTRDELVAKVKK RGISSSNEGVEEPSKKRAVEGKNNSSVERDHGKKSAKTDRSAAQQENSSPSRGSSTKSES GGTSARSSSSGSHQDSATSEGDRSVCSQSSSNSSQVTAGSGKALESEAPHKRGSASFVSS LLKSSMNSHMTQSTDNRQQSGSPKKGALEGSSGSASQSSSEIEVPLLGSSGSAEVELPLL SCKSSSETASSGLTSKSSSEANISSSVSKNSSSSGSSLLTPQSSSTNPSLLTSKSTAQVA ASLLATKSGASLGSVSQLAAKSGSQSSTSQLPSKSTSQASESSVKFACRKLTNEDIKQKQ PFFNRLYKTVAWKLVAVGGFSPTVNHGELLNAAIEALKATLDVFFVPLKELADLPQNKSS QESIVCELRCKSVYLGTGCGKSKENAKAVASREALKLFLKKKVVVKICKRKYRGSEIEDL VLLDEEARPVNLPPALKHPQELL Q9WUE3 Q3TRQ1 C56D2_MOUSE Cytochrome b561 domain-containing protein 2 7.2.1.3 Putative tumor suppressor protein 101F6 Transmembrane ascorbate ferrireductase Cyb561d2 101f6 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C57BL/6J NUCLEOTIDE SEQUENCE [MRNA] FUNCTION CATALYTIC ACTIVITY COFACTOR SUBCELLULAR LOCATION TISSUE SPECIFICITY MUTAGENESIS OF 111-LEU--PRO-222 AND 139-MET--PRO-222 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Cerebellum Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor FUNCTION COFACTOR BIOPHYSICOCHEMICAL PROPERTIES Two-heme-containing cytochrome that catalyzes ascorbate-dependent trans-membrane ferric-chelate reduction. Fe(3+)(out) + L-ascorbate(in) = Fe(2+)(out) + H(+) + monodehydro-L-ascorbate radical(in) heme Binds 2 heme groups non-covalently. E(0) is +141 +/-9 mV for the high potential heme and +43 +/-9 mV for the low potential heme. Cytoplasmic vesicle membrane Multi-pass membrane protein Endoplasmic reticulum membrane Multi-pass membrane protein Highly expressed in the brain, lung, liver, and kidney (PubMed:17938141). Moderately expressed in the heart, placenta, skeletal muscle, and pancreas (PubMed:17938141). Complete proteome Cytoplasmic vesicle Electron transport Endoplasmic reticulum Heme Iron Membrane Metal-binding Reference proteome Translocase Transmembrane Transmembrane helix Transport MALSVETESHIYRALRTASGAAAHLVALGFTIFVAVLARPGSSLFSWHPVLMSLAFSFLM TEALLMFSPESSLLRSLSRKVRARCHWVLQLLALLCALLGLGLVILHKEQLGKAHLTTRH GQAGLLAVLWAGLQCSGGMGLLYPKLLPRWPLAKLKLYHATSGLVGYLLGSASLLLGMFS LWFTATVTGGAWYLAVLCPILTSLVIMNQVSNAYLYRKRIQP Q9JI67 B3GT5_MOUSE Beta-1,3-galactosyltransferase 5 Beta-1,3-GalTase 5 Beta3Gal-T5 Beta3GalT5 b3Gal-T5 2.4.1.- Beta-3-Gx-T5 Stage-specific embryonic antigen 3 synthase SSEA-3 synthase UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 5 UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 5 B3galt5 B3gt5 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Colon Catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Can use glycolipid LC3Cer as an efficient acceptor. Also catalyzes the transfer of Gal to the terminal GalNAc unit of the globoside GB4, thereby synthesizing the glycolipid GB5, also known as the stage-specific embryonic antigen-3 (SSEA-3). Protein modification; protein glycosylation. Golgi apparatus membrane Single-pass type II membrane protein Expressed in brain and kidney. Belongs to the glycosyltransferase 31 family. b3GalT5 Complete proteome Glycoprotein Glycosyltransferase Golgi apparatus Membrane Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix MAHMKTRLVYASILMMGALCLYFSMDSFRELPFVFKKSHGKFLQIPDIDCKQKPPFLVLL VTSSHKQLAARMAIRKTWGRETSVQGQQVRTFFLLGTSDSTEEMDATTLESEQHRDIIQK DFKDAYFNLTLKTMMGMEWVYHFCPQTAYVMKTDSDMFVNVGYLTELLLKKNKTTRFFTG YIKPHDFPIRQKFNKWFVSKFEYPWDRYPPFCSGTGYVFSSDVAIQVYNVSESVPFIKLE DVFVGLCLAKLKIRPEELHTKQTFFPGGLRFSVCRFQKIVACHFMKPQDLLTYWQALENS KEQDCPAV Q9JJS6 Q6K1L5 Q8C6N5 Q9ERN9 BCDO1_MOUSE Beta,beta-carotene 15,15'-dioxygenase 1.13.11.63 Beta-carotene dioxygenase 1 Beta-carotene oxygenase 1 Bco1 Bcdo Bcdo1 Bcmo1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C57BL/6J Kidney NUCLEOTIDE SEQUENCE [MRNA] C57BL/6J Kidney NUCLEOTIDE SEQUENCE [MRNA] CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES TISSUE SPECIFICITY DEVELOPMENTAL STAGE C57BL/6J NUCLEOTIDE SEQUENCE [GENOMIC DNA] 129/Sv NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-483 C57BL/6J Oviduct Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism. all-trans-beta-carotene + O2 = 2 all-trans-retinal Fe(2+) Binds 1 Fe(2+) ion per subunit. Cofactor metabolism; retinol metabolism. Expressed in liver, kidney, small intestine and testis. Abundantly expressed at embryonic day 7 with lower levels at embryonic days 11, 13 and 15. Belongs to the carotenoid oxygenase family. Complete proteome Dioxygenase Iron Metal-binding Oxidoreductase Reference proteome I T MEIIFGQNKKEQLEPVQAKVTGSIPAWLQGTLLRNGPGMHTVGESKYNHWFDGLALLHSF SIRDGEVFYRSKYLQSDTYIANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDF TDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGN VLNMGTSVVDKGRTKYVIFKIPATVPDSKKKGKSPVKHAEVFCSISSRSLLSPSYYHSFG VTENYVVFLEQPFKLDILKMATAYMRGVSWASCMSFDREDKTYIHIIDQRTRKPVPTKFY TDPMVVFHHVNAYEEDGCVLFDVIAYEDSSLYQLFYLANLNKDFEEKSRLTSVPTLRRFA VPLHVDKDAEVGSNLVKVSSTTATALKEKDGHVYCQPEVLYEGLELPRINYAYNGKPYRY IFAAEVQWSPVPTKILKYDILTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIVS TDPQKLPFLLILDAKSFTELARASVDADMHLDLHGLFIPDADWNAVKQTPAETQEVENSD HPTDPTAPELSHSENDFTAGHGGSSL P98203 Q6PGJ6 Q8BQ36 Q8BRF2 Q8C3U7 Q924L2 Q924L3 Q924L4 Q924L5 ARVC_MOUSE Armadillo repeat protein deleted in velo-cardio-facial syndrome homolog Arvcf Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 5) C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5) C57BL/6J Embryonic ganglion Embryonic lung NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Brain NUCLEOTIDE SEQUENCE [MRNA] OF 8-927 (ISOFORM 2) PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-334; SER-337 AND THR-643 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis METHYLATION [LARGE SCALE ANALYSIS] AT ARG-171 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Involved in protein-protein interactions at adherens junctions. Interacts (via the extreme C-terminus) with FRMPD2 (via the PDZ 2 domain). P98203-1 1 A1 P98203-2 2 A2 P98203-4 4 B2 P98203-5 5 B1 Belongs to the beta-catenin family. Aberrant splicing. Alternative splicing Cell adhesion Coiled coil Complete proteome Methylation Phosphoprotein Reference proteome Repeat MEDCNVHSAASILASVKEQEARFERLTRALEQERRHVALQLERAQQPGMSSGGMVGSGQPLPMAWQQLVL MPAELR E G P T R L V E N K MEDCNVHSAASILASVKEQEARFERLTRALEQERRHVALQLERAQQPGMSSGGMVGSGQP LPMAWQQLVLQEQSPGSQASLATMPEAPEVLEETVTVEEDPGTPTSHVSIVTSEDGTTRR TETKVTKTVKTVTTRTVRQVPLGPDGLPLLDGGPPLGSFADGPLDRHYLLRGGGGPAATL SRTYHSSGGGFPDGPESRDIPSYGSLSRGLGVRPPRTGLLGPGPGDGCFTLPGRREAFPM GSESGPPSGRSLPEHFQAEPYGLEDDTRSLAADDEGGPDLEPDYSTATRRRPEYGRGLRA RAFEDTADDAGELIEERPPFPAATAPLAQPERGSLGSLDRVVRRSPSVDSTRKEPRWRDP ELPEVLAMLRHPVDPVKANAAAYLQHLCFENEGIKRRVRQLRGLPLLVALLDHPRAEVRR RACGALRNLSYGRDTDNKAAIRDCGGVPALVRLLRAARDNEVRELVTGTLWNLSSYEPLK MVIIDHGLQTLTHEVIVPHSGWEREPNEDSKPRDAEWTTVFKNTSGCLRNVSSDGAEARR RLRECEGLVDALLHALQSAVGRKDTDNKSVENCVCIMRNLSYHVHKEVPGADRYQEAEPG IPGSTTSQRRRKDDASCFGGKKAKEEWFHQGKKDAEMDRNFDTLDLPKRTEAAKGFELLY QPEVVRLYLSLLTESRNFNTLEAAAGALQNLSAGNWTWATYIRATVRKERGLPVLVELLQ SETDKVVRAVAIALRNLSLDQRNKDLIGSYAMTELVRNVRNAQAPAHPSAHLEEDTVVAV LNTIHEIVSDSLDNARSLLQARGVPALVALVASSQSVREAKAASHVLQTVWSYKELRGAL QRDGWTKSRFQSASTAKGPKGTPSSGGFDDSTLPLVDKSLDGEKSNTRDVIPMDTLGPDG YATVDRRERRTLGSDSTGDTSEKELLRPDPGRKAPPPGPSRPSVRLVDAVGDTKPQPVDS WV Q62210 A6H6S7 O08864 BIRC2_MOUSE Baculoviral IAP repeat-containing protein 2 2.3.2.27 Cellular inhibitor of apoptosis 1 C-IAP1 Inhibitor of apoptosis protein 2 mIAP2 RING-type E3 ubiquitin transferase BIRC2 Birc2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] PARTIAL PROTEIN SEQUENCE NUCLEOTIDE SEQUENCE [MRNA] Skeletal muscle NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE CATALYTIC ACTIVITY PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Spleen Testis METHYLATION [LARGE SCALE ANALYSIS] AT ARG-143 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle. S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. The CARD domain inhibits the activation of E3 ubiquitin ligase activity by preventing RING domain dimerization and E2 ubiquitin donor binding and activation. The CARD domain-mediated autoinhibition of the E3 ubiquitin-protein ligase activity suppresses cell proliferation and migration. USP19 regulates the stability of BIRC2/c-IAP1 by preventing its ubiquitination (By similarity). Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with CASP9. Interacts (via BIR domains) with TRAF2; the interaction is required for IKBKE ubiquitination. Interacts with E2F1, RIPK1, RIPK2, RIPK3, RIPK4, BIRC5/survivin and USP19 (By similarity). Interacts with HSP90AB1 (By similarity). Cytoplasm Nucleus Agents that induce either the extrinsic or intrinsic apoptotic pathways promote its redistribution from the nuclear compartment to the cytoplasmic compartment. Associated with the midbody in telophase cells, and found diffusely in the nucleus of interphase cells (By similarity). Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. The BIR domains mediate nuclear localization. The CARD domain is necessary to stabilize the protein and inhibit the activation of E3 ubiquitin-protein ligase activity of BIRC2/c-IAP1 by preventing RING domain dimerization and E2 ubiquitin donor binding and activation. Auto-ubiquitinated and degraded by the proteasome in apoptotic cells. Belongs to the IAP family. Activator Apoptosis Complete proteome Cytoplasm Direct protein sequencing Metal-binding Methylation Nucleus Phosphoprotein Reference proteome Repeat Transcription Transcription regulation Transferase Ubl conjugation Ubl conjugation pathway Zinc Zinc-finger E K MDKTVSQRLGQGTLHQKLKRIMEKSTILSNWTKESEEKMKFDFSCELYRMSTYSAFPRGV PVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKQGDSPVEKHRQFYPSCSFVQTLLSAS LQSPSKNMSPVKSRFAHSSPLERGGIHSNLCSSPLNSRAVEDFSSRMDPCSYAMSTEEAR FLTYSMWPLSFLSPAELARAGFYYIGPGDRVACFACGGKLSNWEPKDDAMSEHRRHFPHC PFLENTSETQRFSISNLSMQTHSARLRTFLYWPPSVPVQPEQLASAGFYYVDRNDDVKCF CCDGGLRCWEPGDDPWIEHAKWFPRCEFLIRMKGQEFVDEIQARYPHLLEQLLSTSDTPG EENADPTETVVHFGPGESSEDVVMMSTPVVKAALEMGFSRSLVRQTVQRQILATGENYRT VNDIVSVLLNAEDERREEEKERQTEEMASGDLSLIRKNRMALFQQLTHVLPILDNLLEAS VITKQEHDIIRQKTQIPLQARELIDTVLVKGNAAANIFKNSLKEIDSTLYENLFVEKNMK YIPTEDVSGLSLEEQLRRLQEERTCKVCMDREVSIVFIPCGHLVVCQECAPSLRKCPICR GTIKGTVRTFLS O08707 Q8CEG1 ACKR2_MOUSE Atypical chemokine receptor 2 C-C chemokine receptor D6 Chemokine-binding protein 2 Chemokine-binding protein D6 Ackr2 Ccbp2 D6 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C3H/HeJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FUNCTION TISSUE SPECIFICITY REVIEW Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1)-dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs. Early endosome Recycling endosome Cell membrane Multi-pass membrane protein Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). Expressed on apoptotic neutrophils (at protein level). The C-terminal cytoplasmic tail controls its phosphorylation, stability, intracellular trafficking itinerary, and chemokine scavenging properties. Phosphorylated on serine residues in the C-terminal cytoplasmic tail. Belongs to the G-protein coupled receptor 1 family. Atypical chemokine receptor subfamily. Cell membrane Complete proteome Disulfide bond Endosome G-protein coupled receptor Glycoprotein Inflammatory response Membrane Phosphoprotein Receptor Reference proteome Transducer Transmembrane Transmembrane helix N Y MPTVASPLPLTTVGSENSSSIYDYDYLDDMTILVCRKDEVLSFGRVFLPVVYSLIFVLGL AGNLLLLVVLLHSAPRRRTMELYLLNLAVSNLLFVVTMPFWAISVAWHWVFGSFLCKVIS TLYSINFYCGIFFITCMSLDKYLEIVHAQPLHRPKAQFRNLLLIVMVWITSLAISVPEMV FVQIHQTLDGVWHCYADFGGHATIWKLYLRFQLNLLGFLLPLLAMIFFYSRIGCVLVRLR PPGQGRALRMAAALVIVFFMLWFPYNLTLFLHSLLDLHVFGNCEISHRLDYTLQVTESLA FSHCCFTPVLYAFCSHRFRRYLKAFLSVMLRWHQAPGTPSSNHSESSRVTAQEDVVSMND LGERQSEDSLNKGEMGNT Q9WVM8 AADAT_MOUSE Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial KAT/AadAT 2-aminoadipate aminotransferase 2-aminoadipate transaminase 2.6.1.39 Alpha-aminoadipate aminotransferase AadAT Kynurenine aminotransferase II Kynurenine--oxoglutarate aminotransferase II Kynurenine--oxoglutarate transaminase 2 2.6.1.7 Kynurenine--oxoglutarate transaminase II Aadat Kat2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Kidney NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Liver SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-263; LYS-339 AND LYS-367 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69; LYS-179; LYS-263; LYS-339; LYS-351; LYS-367 AND LYS-422 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) (By similarity). 2-oxoglutarate + L-kynurenine = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate 2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-glutamate pyridoxal 5'-phosphate Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6. Homodimer. Mitochondrion Expressed mainly in kidney and to a lesser amount in liver and brain. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Acetylation Aminotransferase Complete proteome Mitochondrion Phosphoprotein Pyridoxal phosphate Reference proteome Transferase Transit peptide MNYSRFLTATSLARKPSPIRTTADILSKAPKTLISLAPGSPNPSMFPFKSAAFTVENGST IRFEDDLIKRALQYSPSYGIPELLSWLKQFQVKLHNPPTVNYPPNQGQMDLCITSGCQDG LCKAFEMLINPGDTILVNEPLFPGTLYAMKPLGCNIINVPSDEHGIIPEGLKKILSQWKP EDSKDPTKKTPKFLYTVPNGNNPTGNSLTGDRKKEIYELARKYDFLIIEDDPYYFLQFSK PWEPTFLSMDVDGRVIRADTFSKTVSSGLRVGFMTGPKTLIQNIVLHTQVSSVHACTLSQ LMILQLLHQWGEEGFLAHIDRTIDFYKNQRDSILAAADKWLRGLAEWHVPKAGMFLWIKV KGISDTKQLIEEKAIEREVLLVPGNGFFIDGSAPTSFFRASFSLATPAQMDTAFQRLAQL IKESL Q91XE4 Q3UP59 Q9DD17 ACY3_MOUSE N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming) 3.5.1.114 Acylase III Aminoacylase III AAIII Aminoacylase-3 ACY-3 Aspartoacylase-2 Hepatitis C virus core-binding protein 1 HCBP1 Acy3 Aspa2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ Kidney NUCLEOTIDE SEQUENCE [GENOMIC DNA] BALB/cJ NUCLEOTIDE SEQUENCE [MRNA] FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES SUBUNIT SUBCELLULAR LOCATION TISSUE SPECIFICITY C57BL/6J NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Kidney Spleen NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Kidney FUNCTION CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Spleen Testis STRUCTURE BY ELECTRON MICROSCOPY (16 ANGSTROMS) SUBUNIT X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATES ZINC-BINDING SITES SUBUNIT COFACTOR MUTAGENESIS OF ARG-63 AND TYR-287 Plays an important role in deacetylating mercapturic acids in kidney proximal tubules. Also acts on N-acetyl-aromatic amino acids. an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate + an aromatic L-alpha-amino acid an N-acetyl-L-cysteine-S-conjugate + H2O = acetate + an S-substituted L-cysteine Zn(2+) Binds 1 zinc ion per subunit. 1.1 mM for S-benzyl-N-acetyl-L-cysteine 1.8 mM for N-acetyl-L-histidine 1.4 mM for N-acetyl-L-tyrosine 1.6 mM for N-acetyl-L-phenylalanine 11.7 umol/min/mg enzyme with S-benzyl-N-acetyl-L-cysteine as substrate 5.9 umol/min/mg enzyme with N-acetyl-L-histidine as substrate 7.5 umol/min/mg enzyme with N-acetyl-L-tyrosine as substrate 7.9 umol/min/mg enzyme with N-acetyl-L-phenylalanine as substrate Optimum pH is 7.5 with S-benzyl-N-acetyl-L-cysteine as substrate, 7.6 with N-acetyl-L-histidine as substrate, 7.6 with N-acetyl-L-tyrosine as substrate, and 7.7 with N-acetyl-L-phenylalanine as substrate. Exists as a mixture of homodimers and homotetramer, both catalytically active. false 4 P26664 true 6 Apical cell membrane Peripheral membrane protein Cytoplasm Predominantly localized in the apical membrane of cells in the S1 segment. In the proximal straight tubules (S2 and S3 segments) is expressed diffusely throughout the cytoplasm. Expressed predominantly in kidney and to a lesser extent in liver. Weakly expressed in heart, small intestine, brain, lung, testis, and stomach. Belongs to the AspA/AstE family. Aspartoacylase subfamily. 3D-structure Cell membrane Complete proteome Cytoplasm Hydrolase Membrane Metal-binding Phosphoprotein Reference proteome Zinc R A Y A D G MSSLPGSREPLLRVAVTGGTHGNEMCGVYLARYWLQNPGELQRPSFSAMPVLANPAATAA CCRYLDRDLNRSCTLTFLGSTATPDDPYEVKRARELNQLLGPKGTGQAFDFTLDLHNTTA NTGVCLISESNISFNLHLCHYLQRQNPGMPCRLFLYEPAGTETFSVESISKNGICLEMGP QPQGVLRADLFSRMRALVASILDFIELFNQGMDLPAFEMDIYRNLGSVDFPRTADGDLAG TVHPQLQDHDFEPLRPGEPIFKLFSGEDVLYEGDSIVYPVFINEAAYYEKHVAFLKSEKI RVTVPALLRLTPRSTQTP O35126 P70200 Q80YQ0 ATN1_MOUSE Atrophin-1 Dentatorubral-pallidoluysian atrophy protein homolog Atn1 Drpla Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY DEVELOPMENTAL STAGE POLYMORPHISM OF POLY-GLN REGION NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain INTERACTION WITH NR2E1 FUNCTION CHARACTERISTICS OF THE MOUSE MODEL OF DRPLA INTERACTION WITH FAT1 INDUCTION FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-79; SER-101 AND SER-107 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Kidney Liver Lung Spleen Testis METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1100 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryo Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of the poly-Q repeats (By similarity). Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation. Interacts with BAIAP2, WWP1, WWP2, WWP3 and RERE. Interacts (via its N-terminus) with MTG8; the interaction enhances transcriptional repression of MTG8. Interacts with PQBP1 (By similarity). Interacts with NR2E1; the interaction represses the transcriptional activity of NR2E1. Interacts with FAT1 (via a C-terminal domain). Cytoplasm Perinuclear region Cell junction Nucleus Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells. Colocalizes with MTG8 in discrete nuclear dots (By similarity). Widely expressed. Most abundant in the brain. Expressed as early as 5 days and thereafter shows little variation throughout 17 days. In vascular smooth muscle, induced by angiotensin II, FGF; PGF and IL1B. Phosphorylated in vitro by MAPK8/JNK1 on Ser-724. The poly-Gln region of Atn1 is polymorphic (3 to 8 repeats). The mouse model of DRPLA with 129 CAG repeats (Q129) exhibited severe neurological defects similar to those of juvenile-onset DRPLA patients including age-dependent and region-specific presynaptic dysfunction in the globus pallidus and cerebellum. Progressive shrinkage of distal dendrites of Purkinje cells and decreased currents through alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid and gamma-aminobutyrate type A receptors in CA1 neurons was observed. There is progressive brain atrophy. Acetylation Cell junction Complete proteome Cytoplasm Isopeptide bond Methylation Nucleus Phosphoprotein Polymorphism Reference proteome Transcription Transcription regulation Triplet repeat expansion Ubl conjugation A G P A P A S L P A D T D N MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARIE EPSAPKASKQGRSEEISESESEETSAPKKTKTEQELPRPQSPSDLDSLDGRSINDDGSSD PRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPPPPDSTPRQPE SGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHPQLYPGNASGGVLSGPPMGPKGG AAASSVGAPSGGKQHPPPTTPIPISSSGASGAPPAKPPSAPVGGGSLPSAPPPASFPHVT PNLPPPPALRPLNNASASPPGMGAQPIPGHLPSPHAMGQGMSGLPPGPEKGPTLAPSPHP LPPASSSAPGPPMRYPYSSSSSSAAASSSSSSSSASQYPASQALPSYPHSFPPPTSMSVS NQPPKYTQPSLPSQAVWSQGPPPPPPYGRLLANNNTHPGPFPPTGGQSTAHPAAPTHHHH QQQPQQQHHHGNSGPPPPGAYPHPLESSNSHHAHPYNMSPSLGSLRPYPPGPAHLPPPHG QVSYNQAGPNGPPVSSSNSSGSSSQASYSCSHPSSSQGPQGASYPFPPVPPVTTSSATLS TVIATVASSPAGYKTASPPGPPQYSKRAPSPGSYKTATPPGYKPGSPPSFRTGTPPGYRG TSPPAGPGTFKPGSPTVGPGPLPPAGPSSLSSLPPPPAAPTTGPPLTATQIKQEPAEEYE PPESPVPPARSPSPPPKVVDVPSHASQSARFNKHLDRGFNSCARSDLYFVPLEGSKLAKK RADLVEKVRREAEQRAREEKEREREREREKEREREKERELERSVKLAQEGRAPVECPSLG PVPHRPPFEPGSAVATVPPYLGPDTPALRTLSEYARPHVMSPGNRNHPFYVPLGAVDPGL LGYNVPALYSSDPAAREREREARERDLRDRLKPGFEVKPSELEPLHGVPGPGLDPFPRHG GLALQPGPPGLHPFPFHPSLGPLERERLALAAGPALRPDMSYAERLAAERQHAERVAALG NDPLARLQMLNVTPHHHQHSHIHSHLHLHQQDAIHAASASVHPLIDPLASGSHLTRIPYP AGTLPNPLLPHPLHENEVLRHQLFAAPYRDLPASLSAPMSAAHQLQAMHAQSAELQRLAL EQQQWLHAHHPLHSVPLPAQEDYYSHLKKESDKPL Q61458 Q9CVJ0 Q9JHV7 CCNH_MOUSE Cyclin-H Ccnh Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] Spermatocyte NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Medulla oblongata Pancreas NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Thymus NUCLEOTIDE SEQUENCE [MRNA] OF 92-109 CD-1 Testis IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Spleen Regulates CDK7, the catalytic subunit of the CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (POLR2A), allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle. Associates primarily with CDK7 and MAT1 to form the CAK complex. CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor. Nucleus Expressed in both the germinal and somatic cells of the testis. Higher expression during spermatogenesis from the mitotic stages to the meiotic stages. Belongs to the cyclin family. Cyclin C subfamily. Cell cycle Complete proteome Cyclin Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation MYHSSSQKRHWTFASEEQLARLRADANRKFKCKAVANGKVLPNDPVFLEPHEELTLCKYY EKRLLEFCSVFKPAMPRSVVGTACMYFKRFYLNNSVMEYHPRIIMLTCAFLACKVDEFNV SSPQFVGNLRESPLGQERALEQILEYELLLIQQLNFHLIVHNPYRPFEGFLIDIKTRYPM LENPEILRKTADDFLSRIALTDAYLLYTPSQIALTAILSSASRAGITMESYLSESLMLKE NRTCLSQLLDIMKSMRNLVKKYEPPRSDEVAVLKQKLERCHSSDLALNAVTKKRKGYEDD DYVSKKPKQEEEEWTDDDLVDSL Q9JJA7 A2AD95 A2RSY2 Q5XK66 Q60995 Q8C136 Q8CIJ8 Q99L73 Q9QXH5 CCNL2_MOUSE Cyclin-L2 Cyclin Ania-6b Paneth cell-enhanced expression protein PCEE Ccnl2 Ania6b MNCb-5160 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) C57BL/6J NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) C57BL/6J NOD Head Pancreas Skin Spleen NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) FVB/N Brain Mammary gland NUCLEOTIDE SEQUENCE [MRNA] OF 321-518 BALB/cJ Jejunal epithelium INTERACTION CDK13 TISSUE SPECIFICITY PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Involved in pre-mRNA splicing. May induce cell death, possibly by acting on the transcription and RNA processing of apoptosis-related factors. Interacts with CDK11A, CDK11B, CDK12, CDK13 and POLR2A, the hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II. May form a ternary complex with CDK11B and casein kinase II (CKII). Interacts with pre-mRNA-splicing factors, including at least SRSF1, SRSF2 AND SRSF7/SLU7. Nucleus speckle Nucleus Nucleoplasm Q9JJA7-1 1 Q9JJA7-2 2 May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. Q9JJA7-3 3 No experimental confirmation available. Widely expressed (at protein level). Contains a RS region (arginine-serine dipeptide repeat) within the C-terminal domain which is the hallmark of the SR family of splicing factors. This region probably plays a role in protein-protein interactions (By similarity). Belongs to the cyclin family. Cyclin L subfamily. Translation N-terminally extended. Translated as stop. Alternative splicing Complete proteome Cyclin Nucleus Phosphoprotein Reference proteome Repeat Transcription Transcription regulation NYMNDS VASEGK S A K R Y F T S E VE MAAAAAGAAGLMAPASAACSSGSAGAAPGSQGVLIGDRLYSGVLITLENCLLPDDKLRFT PSMSSGLDVDTETGLRVVGCELIQAAGILLRLPQVAMATGQVLFQRFFYTKSFVKHSMEH VSMACVHLASKIEEAPRRIRDVINVFHRLRHLREKKKPVPLVLDQEYVNLKNQIIKAERR VLKELGFCVHVKHPHKIIVMYLQVLECERNQHLVQTAWNYMNDSLRTDVFVRFQPESIAC ACIYLAARTLEIPLPNRPHWFLLFGATEEEIQEICFKILQLYTRKKVDLTHLESEVEKRK HAIEEAKARAKGLLPGTAPGLDSAAGFSPAPKLESPKEGKGGKPSPPSGKSAKRKMEGPK KAQGHSPVNGLLKGQESRSQSRSREQSYSRSPSRSASPKRRKSDSGSTSGGSKSQSRSRS RSDSPPRQVHRGAPYKGSEVRGSRKSKDCKYLTQKPHKSRSRSSSRSRSRSRERTDNSGK YKKKSHYYRDQRRERSRSYERTGHRYERDHPGHSRHRR P53762 Q60661 Q921F3 ARNT_MOUSE Aryl hydrocarbon receptor nuclear translocator ARNT protein Dioxin receptor, nuclear translocator Hypoxia-inducible factor 1-beta HIF-1-beta HIF1-beta Arnt Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG) C57BL/6J Liver NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT) C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor INTERACTION WITH AHRR INTERACTION WITH TACC3 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Spleen INTERACTION WITH AHR MUTAGENESIS OF LEU-167; ILE-168 AND ALA-171 REGION X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 81-464 IN COMPLEXES WITH EPAS1; HIF1A; INHIBITOR AND DNA MUTAGENESIS OF HIS-94; GLU-98; ARG-102; LEU-112; LEU-132; VAL-136; LEU-167; ILE-168; ALA-171; ILE-264; ARG-266; VAL-305; HIS-307; ARG-366; ASN-448 AND TYR-456 REGION INTERACTION WITH EPAS1 AND HIF1A FUNCTION X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 81-464 IN COMPLEXES WITH NPAS1; NPAS3 AND DNA MUTAGENESIS OF LEU-112; LEU-132; VAL-136; LEU-167; ILE-168; ALA-171; ILE-264; ARG-266; VAL-305; HIS-307; ARG-366; ASN-448 AND TYR-456 INTERACTION WITH NPAS1; NPAS3; SIM1; NPAS4 AND AHR FUNCTION X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 84-345 IN COMPLEXES WITH AHR AND DNA SUBUNIT INTERACTION WITH AHR MUTAGENESIS OF ARG-102; LEU-112; MET-139 AND LEU-164 FUNCTION REGION Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens (By similarity). The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (PubMed:26245371, PubMed:27782878). The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820). Monomer (PubMed:28602820). Homodimer only upon binding to a DNA (PubMed:26245371, PubMed:28602820). Efficient DNA binding requires dimerization with another bHLH protein (By similarity). Interacts with TACC3 (PubMed:11025203). Interacts with HIF1A, EPAS1, NPAS1 and NPAS3; forms a heterodimer that binds core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (PubMed:26245371, PubMed:27782878). Forms a heterodimer with AHRR, as well as with other bHLH proteins (PubMed:9887096). Interacts with NOCA7 (By similarity). Interacts with AHR; the heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820, PubMed:24001774, PubMed:27782878). Interacts with SIM1 and NPAS4 (PubMed:27782878). P97481 Epas1 false 5 Q61221-1 Hif1a false 5 Q61045 Sim1 false 2 Nucleus P53762-1 Long P53762-2 Short Ubiquitous. 3D-structure Acetylation Activator Alternative splicing Complete proteome DNA-binding Isopeptide bond Nucleus Phosphoprotein Reference proteome Repeat Transcription Transcription regulation Ubl conjugation SDDEQSSADKERLARENHSEIERR TKFL H A E A R E L D L E L E V D M D L D L E I D A D I D R A V D H A R A N A Y D S T A R S T A C MAATTANPEMTSDVPSLGPTIASGNPGPGIQGGGAVVQRAIKRRSGLDFDDEVEVNTKFL RCDDDQMCNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCS ALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVS CETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRVLDLK TGTVKKEGQQSSMRMCMGSRRSFICRMRCGTSSVDPVSMNRLSFLRNRCRNGLGSVKEGE PHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNICQP TEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKG QVLSVMFRFRSKTREWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPTLSNTIP RSQLGPTANLSLEMGTGQLPSRQQQQQHTELDMVPGRDGLASYNHSQVSVQPVASAGSEH SKPLEKSEGLFAQDRDPRFPEIYPSITADQSKGISSSTVPATQQLFSQGSSFPPNPRPAE NFRNSGLTPPVTIVQPSSSAGQILAQISRHSNPAQGSAPTWTSSSRPGFAAQQVPTQATA KTRSSQFGVNNFQTSSSFSAMSLPGAPTASSGTAAYPALPNRGSNFPPETGQTTGQFQAR TAEGVGVWPQWQGQQPHHRSSSSEQHVQQTQAQAPSQPEVFQEMLSMLGDQSNTYNNEEF PDLTMFPPFSE Q8R464 CADM4_MOUSE Cell adhesion molecule 4 Immunoglobulin superfamily member 4C IgSF4C Nectin-like protein 4 NECL-4 TSLC1-like protein 2 Cadm4 Igsf4c Necl4 Tsll2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION TISSUE SPECIFICITY 129/SvJ GLYCOSYLATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Spleen Involved in the cell-cell adhesion. Has calcium- and magnesium-independent cell-cell adhesion activity. May have tumor-suppressor activity. Monomer and homodimer. Membrane Single-pass type I membrane protein Expressed in the brain and several organs including the kidney and liver. N-glycosylated. Belongs to the nectin family. 3D-structure Cell adhesion Complete proteome Disulfide bond Glycoprotein Immunoglobulin domain Membrane Phosphoprotein Reference proteome Repeat Signal Transmembrane Transmembrane helix Tumor suppressor MGRARRFQWPLLLLWAAAAGPGTGQEVQTENVTVAEGGVAEITCRLHQYDGSIVVIQNPA RQTLFFNGTRALKDERFQLEEFSPRRVRIRLSDARLEDEGGYFCQLYTEDTHHQIATLTV LVAPENPVVEVREQAVEGGEVELSCLVPRSRPAAVLRWYRDRKELKGVSSGQENGKVWSV ASTVRFRVDRKDDGGIVICEAQNQALPSGHSKQTQYVLDVQYSPTARIHASQAVVREGDT LVLTCAVTGNPRPNQIRWNRGNESLPERAEAVGETLTLPGLVSADNGTYTCEAANKHGHA RALYVLVVYDPGAVVEAQTSVPYAIVGGILALLVFLIICVLVGMVWCSVRQKGSYLTHEA SGLDEQGEAREAFLNGGDGHKRKEEFFI P06909 Q6NZK3 CFAH_MOUSE Complement factor H Protein beta-1-H Cfh Hf1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain NUCLEOTIDE SEQUENCE [MRNA] OF 1-19 BALB/cJ NUCLEOTIDE SEQUENCE [MRNA] OF 1-18 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-773 AND ASN-1061 C57BL/6J Plasma GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-773; ASN-801; ASN-1030; ASN-1061 AND ASN-1225 C57BL/6J Plasma PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1198 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis DISRUPTION PHENOTYPE X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 321-444 Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces. Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop. As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b. In addition, mediates several cellular responses through interaction with specific receptors. For example, interacts with CR3/ITGAM receptor and thereby mediates the adhesion of human neutrophils to different pathogens. In turn, these pathogens are phagocytosed and destroyed. Homodimer. Forms also homooligomers. Interacts with complement protein C3b; this interaction inhibits complement activation. Interacts with complement protein C3d. Interacts with CR3/ITGAM; this interaction mediates adhesion of neutrophils to pathogens leading to pathogen clearance. Secreted CFH is one of the most abundant complement components in blood where the liver is the major source of CFH protein in vivo. in addition, CFH is secreted by additional cell types including monocytes, fibroblasts, or endothelial cells. Sushi 1-3 domain represents the minimal unit capable of cofactor activity. The property to discriminate self surfaces from non-self surfaces depends on the C-terminal region made of Sushis 19-20. Two codominant alleles of factor H are present in mice. The lack of CFH alters the microarchitecture of bone and affects osteoblast and osteoclast dynamics. 3D-structure Complement alternate pathway Complete proteome Disulfide bond Glycoprotein Immunity Innate immunity Phosphoprotein Reference proteome Repeat Secreted Signal Sushi R T MRLSARIIWLILWTVCAAEDCKGPPPRENSEILSGSWSEQLYPEGTQATYKCRPGYRTLG TIVKVCKNGKWVASNPSRICRKKPCGHPGDTPFGSFRLAVGSQFEFGAKVVYTCDDGYQL LGEIDYRECGADGWINDIPLCEVVKCLPVTELENGRIVSGAAETDQEYYFGQVVRFECNS GFKIEGHKEIHCSENGLWSNEKPRCVEILCTPPRVENGDGINVKPVYKENERYHYKCKHG YVPKERGDAVCTGSGWSSQPFCEEKRCSPPYILNGIYTPHRIIHRSDDEIRYECNYGFYP VTGSTVSKCTPTGWIPVPRCTLKPCEFPQFKYGRLYYEESLRPNFPVSIGNKYSYKCDNG FSPPSGYSWDYLRCTAQGWEPEVPCVRKCVFHYVENGDSAYWEKVYVQGQSLKVQCYNGY SLQNGQDTMTCTENGWSPPPKCIRIKTCSASDIHIDNGFLSESSSIYALNRETSYRCKQG YVTNTGEISGSITCLQNGWSPQPSCIKSCDMPVFENSITKNTRTWFKLNDKLDYECLVGF ENEYKHTKGSITCTYYGWSDTPSCYERECSVPTLDRKLVVSPRKEKYRVGDLLEFSCHSG HRVGPDSVQCYHFGWSPGFPTCKGQVASCAPPLEILNGEINGAKKVEYSHGEVVKYDCKP RFLLKGPNKIQCVDGNWTTLPVCIEEERTCGDIPELEHGSAKCSVPPYHHGDSVEFICEE NFTMIGHGSVSCISGKWTQLPKCVATDQLEKCRVLKSTGIEAIKPKLTEFTHNSTMDYKC RDKQEYERSICINGKWDPEPNCTSKTSCPPPPQIPNTQVIETTVKYLDGEKLSVLCQDNY LTQDSEEMVCKDGRWQSLPRCIEKIPCSQPPTIEHGSINLPRSSEERRDSIESSSHEHGT TFSYVCDDGFRIPEENRITCYMGKWSTPPRCVGLPCGPPPSIPLGTVSLELESYQHGEEV TYHCSTGFGIDGPAFIICEGGKWSDPPKCIKTDCDVLPTVKNAIIRGKSKKSYRTGEQVT FRCQSPYQMNGSDTVTCVNSRWIGQPVCKDNSCVDPPHVPNATIVTRTKNKYLHGDRVRY ECNKPLELFGQVEVMCENGIWTEKPKCRDSTGKCGPPPPIDNGDITSLSLPVYEPLSSVE YQCQKYYLLKGKKTITCRNGKWSEPPTCLHACVIPENIMESHNIILKWRHTEKIYSHSGE DIEFGCKYGYYKARDSPPFRTKCINGTINYPTCV O35457 O70171 Q3UKM6 Q4FK04 Q91YD7 CCRL2_MOUSE C-C chemokine receptor-like 2 Chemokine receptor CCR11 G-protein coupled beta chemokine receptor Lipopolysaccharide-inducible C-C chemokine receptor L-CCR Ccrl2 Ccr11 Lccr Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [MRNA] INDUCTION TISSUE SPECIFICITY CD-1 NUCLEOTIDE SEQUENCE [MRNA] 129/Sv C57BL/10 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Placenta NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Mammary gland FUNCTION TISSUE SPECIFICITY TISSUE SPECIFICITY LIGAND-BINDING DISRUPTION PHENOTYPE FUNCTION LACK OF RESPOND TO CCL2; CCL5; CCL7 AND CCL8 TISSUE SPECIFICITY DISRUPTION PHENOTYPE FUNCTION Receptor for CCL19 and chemerin/RARRES2. Does not appear to be a signaling receptor, but may have a role in modulating chemokine-triggered immune responses by capturing and internalizing CCL19 or by presenting RARRES2 ligand to CMKLR1, a functional signaling receptor. Plays a critical role for the development of Th2 responses (By similarity). Cell membrane Multi-pass membrane protein Expressed in macrophages, astrocytes, in glial cells. Constitutively expressed by mast cells. Detected in bronchial epithelium in OVA-induced airway inflammation. Up-regulated during dendritic cell (DC) maturation. By bacterial lipopolysaccharide in astrocytes. Lacks the conserved DRYLAIV motif in the second intracellular loop that is required for signaling of functional chemokine receptors. No visible phenotype. Deficient-mice have normal numbers of mast cells in all tissues analyzed. Wild-type and deficient mice develop marked local inflammation when sensitized with a high dose of DNP-specific IgE, however deficient mice have significantly reduced IgE-dependent passive cutaneous anaphylaxis (PCA) reactions when lower sensitizing dose is used. Deficient-mice show normal recruitment of circulating DC into the lung, but a defective trafficking of antigen-loaded lung DC to mediastinal lymph nodes. This defect was associated to a reduction in lymph node cellularity and reduced priming of T-helper cell 2 response. It was initially reported that CCRL2 responds functionally to CCL2, CCL5, CCL7, and CCL8 via intracellular calcium mobilization and transwell chemotaxis although no evidence for a direct ligand-receptor interaction was provided in this report (PubMed:14999816). These results are now controversial and other studies failed to confirm CCRL2 recognition and transwell chemotaxis of these chemokines or a series of other CC- and CXC-chemokines using CCRL2-transfected cells (PubMed:18794339). Belongs to the G-protein coupled receptor 1 family. Cell membrane Complete proteome Disulfide bond G-protein coupled receptor Glycoprotein Membrane Receptor Reference proteome Transducer Transmembrane Transmembrane helix P S Q R I V F L V A Y S E K I K MDNYTVAPDDEYDVLILDDYLDNSGPDQVPAPEFLSPQQVLQFCCAVFAVGLLDNVLAVF ILVKYKGLKNLGNIYFLNLALSNLCFLLPLPFWAHTAAHGESPGNGTCKVLVGLHSSGLY SEVFSNILLLVQGYRVFSQGRLASIFTTVSCGIVACILAWAMATALSLPESVFYEPRMER QKHKCAFGKPHFLPIEAPLWKYVLTSKMIILVLAFPLLVFIICCRQLRRRQSFRERQYDL HKPALVITGVFLLMWAPYNTVLFLSAFQEHLSLQDEKSSYHLDASVQVTQLVATTHCCVN PLLYLLLDRKAFMRYLRSLFPRCNDIPYQSSGGYQQAPPREGHGRPIELYSNLHQRQDII Q9D518 A2AR82 F227B_MOUSE Protein FAM227B Fam227b Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-393 C57BL/6J Testis Belongs to the FAM227 family. Intron retention. The sequence differs at its 3' end due to intron retention. Coiled coil Complete proteome Reference proteome L F MELPVPQKLPDPPRSFDEFLKSQNWDYWPRDVHFRDSDIWEDTLKKLEEAISYTSIYSYL WTNVPRLYDIVDSLESKLKESSHLLQHHASRLFESDKMISKKRSYTNLERYKAFVKEHYR PKKIALSDRMETEKNIEGCTFLFNQNEVTQLPRHLDAKQIYLYVLKTHNFEEKVFKVWKT HVLSDCSIALLHDSFWWWFLHKFKPDKRDEDFLFDRIAESYVTLFIKIPLRRKDAFFKMY PDCLTQAVYTTFQESFPESCSLFNDKFKEDLGNTIFLWLSGLKPETGFWTHWKLQDLCTT TIHGSRRVPVKLRRSVIPSQEHIPGIRDLKIEDILKNPRAYAMPKLMKESVASKAATKPS HYRSLGPEFHKVLFDFGGQSPLILYYLKMHELGGISVTHNPKGTKFTKILREPSPAPTYC DIIRDAKRKFADNKKDFKRVKQRIKDDIKFLREQQELIDKELDRIQAKASKNLQEVKNEF ENFLHKQRVEAKLKEEYGGSTSASESPQSMQSPQSSSSFPTISEDFNNVEEG Q03059 CLAT_MOUSE Choline O-acetyltransferase CHOACTase ChAT Choline acetylase 2.3.1.6 Chat Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE Spinal cord NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-219 Spinal cord Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. acetyl-CoA + choline = acetylcholine + CoA Belongs to the carnitine/choline acetyltransferase family. Acyltransferase Complete proteome Neurotransmitter biosynthesis Phosphoprotein Reference proteome Transferase MPILEKVPPKMPVQASSCEEVLDLPKLPVPPLQQTLATYLQCMQHLVPEEQFRKSQAIVK RFGAPGGLGETLQEKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFQD TNDQLRFAASLISGVLSYKALLDSQSIPTDWAKGQLSGQPLCMKQYYRLFSSYRLPGHTQ DTLVAQKSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERL PPIGLLTSDGRSEWAKARTVLLKDSTNRDSLDMIERCICLVCLDGPGTGDLSDTHRALQL LHGGGCSLNGANRWYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHMMTGNKK LVRVDSVSELPAPRRLRWKCSPETQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQ KCSPDGFIQVALQLAYYRLYQRLVPTYESASIRRFQEGRVDNIRSATPEALAFVQAMTDH KAAVLASEKLQLLQRAIQAQTEYTVMAITGMAIDNHLLALRELARDLCKEPPEMFMDETY LMSNRFILSTSQVPTTMEMFCCYGPVVPNGYGACYNPHAEAITFCISSFHGCKETSSVEF AEAVGASLVDMRDLCSSRQPADSKPPTAKERARGPSQAKQS Q91Z58 Q8K108 CF132_MOUSE Uncharacterized protein C6orf132 homolog Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1010-1206 (ISOFORM 1) FVB/N Liver Mammary tumor PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Lung METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1051 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryo Q91Z58-1 1 Q91Z58-2 2 No experimental confirmation available. Alternative splicing Complete proteome Methylation Phosphoprotein Reference proteome EPPPPPSTAPPPPP GGRTRYYRSQLRHS MKKNQTMQGTFSKLFGKKHAHPSTTSLYATNPPWIFTHEAQEEGTRDFDGIYYGDNRFNT VSESGTATLKARPRVRPLLTFIPLNAQENHGLAVPTPSVPEDFADKEVGGTSTLVNGNLR LYSSVGDLRPACYDLDSSIPPPPPGPAPGPPQDISQPPGESPPPPPPSVPPPPPPPLLVE PPPPPSTAPPPPPPLDILSPPSTPTPPDFIPPAPPSAFLSPPPPSLPAPGPPAPVSLHTP GTHLFPPGAITKWKSEVALNGRHPEDPRTSPPKSPAELKRSPLGPSPEPHLTFPRSPKVP PPTPVRTSSIPVQEAPGASPEEEEATQKTSAPSPLPPSFNIRPASQIYPDRALEPEQPRE PRPETPGSPRLRQSEPQTNGQAGAPPPAPPLPPPAPPLPPPAPSLPPAAPPLPSTELAAP PSSGFMKTSKSNSPALKPKPKPPSVEDTASSEPVDWRDPRQMEKLRSELSAYLCGTRKED RSLSHRPGPTVALKDKENNKGTSLSEEAAPPSLPEKVHPCIPEKSPSSSSLPEREATSSL VLPPVDYIAQDTPAPSVRQIRSELEARFASSAEKEAKPSLASLPPKPRLEGGRTFENGTD NGRFHKPATKNPPQPSTTPLPTTILQPKVVPGPATSPKVTPGPATPFKPTPGQAILPKAT PGLTLPLKPTPEQTTSPKNTPGKATPLKDTPGQATTPKDTPGQDTPPKDTPGQAAVLKNA PELSTPSSQLMAEKDLASVRQREKPETQEDPVATQLSTNGTLSPPALPPKMSTSGEEAPF LYRPHRSQNSHSRGVAVVTPTRARGEAPDSGDVVDEKELQNHPAKSLTPGQPADQLLRHP VTGEVVERGSPMALLLAARQRAQKTRTGGTAIGRSSLPGSLRDHSNQPEASSDSIFYRGS RPNSFIVVPKVPSETEDSHLTSARPTGPSHWKPQQGPDTQGSEPTYRHGWTKAETPAPVA RERPAPSSLPQSRALPKSFSSPPSPSYKREEEEEEFSFDIIPPPPEFSNDPEPPAPGQQH QGRRGSPPRNNFSDLGQSWGPNPTPGFSRFRGTQYPESGGLDRFSGSGRSLIKKRLYVGE SHRNPGMPRGSTGRSLSSPNCFGPQPGGPEMRRVNSAGRAAPGGLHARRLSLEGARGATE VKFKAPGGGGGSSSKAGDYGFVPAKGSRSPHGNTHYGSPINTFTVRPGTRHPISYAYPGT HRKATS G3X982 B2RSI5 Q8VI15 AOXC_MOUSE Aldehyde oxidase 3 1.2.3.1 Aldehyde oxidase homolog 1 Azaheterocycle hydroxylase 3 1.17.3.- Aox3 Aoh1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] IDENTIFICATION BY MASS SPECTROMETRY FUNCTION AS OXIDASE ACTIVITY REGULATION KINETIC PARAMETERS SUBCELLULAR LOCATION TISSUE SPECIFICITY 129/Sv NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] TISSUE SPECIFICITY SUBCELLULAR LOCATION CD-1 Olfactory epithelium FUNCTION TISSUE SPECIFICITY INDUCTION BY TESTOSTERONE IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Lung CRYSTALLIZATION FUNCTION AS OXIDASE SUBSTRATE SPECIFICITY KINETIC PARAMETERS COFACTOR HOMODIMER IDENTIFICATION OF PARALOGS X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) IN COMPLEX WITH FE-S CLUSTERS; FAD AND MO-MPT FUNCTION AS OXIDASE SUBSTRATE SPECIFICITY COFACTOR KINETIC PARAMETERS HOMODIMER ACTIVITY REGULATION REACTION MECHANISM ACTIVE SITE MUTAGENESIS OF ALA-807; TYR-885; LYS-889 AND GLU-1266 Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and phthalazine, as well as aldehydes, such as benzaldehyde, retinal and pyridoxal. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 [2Fe-2S] cluster Binds 2 [2Fe-2S] clusters per subunit. FAD Binds 1 FAD per subunit. Mo-molybdopterin Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. Inhibited by potassium cyanide, menadione, benzamidine, raloxifene and norharmane. 2.3 uM for phthalazine 1.4 uM for phthalazine (at 37 degrees Celsius and pH 8) 2.5 uM for benzaldehyde (at 37 degrees Celsius and pH 8) 128.5 uM for N1-methylnicotinamide (at 37 degrees Celsius and pH 8) 32.3 uM for phenanthridine (at 37 degrees Celsius and pH 8) 13 uM for benzaldehyde (at 37 degrees Celsius and pH 7.4) 29 uM for butyraldehyde (at 37 degrees Celsius and pH 8) 173 uM for 2-OH-pyrimidine (at 37 degrees Celsius and pH 8) kcat is 4 sec(-1) for phthalazine oxidation (PubMed:11562361). kcat is 130 min(-1) for benzaldehyde oxidation, 384 min(-1) for butyraldehyde oxidation and 1279 min(-1) for 2-OH-pyrimidine oxidation (PubMed:21705476). kcat is 41.1 min(-1) for phthalazine oxidation, 41.9 min(-1) for benzaldehyde oxidation, 14.7 min(-1) for N1-methylnicotinamide oxidation and 51.7 min(-1) for phenanthridine oxidation (PubMed:23019336). Homodimer. Cytoplasm Highly expressed in liver (at protein level). In liver, the expression is greater in males than females. Induced by testosterone. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. 2Fe-2S 3D-structure Complete proteome Cytoplasm FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum Oxidoreductase Phosphoprotein Reference proteome A V Y M K H E Q A T K R MSPSKESDELIFFVNGKKVTERNADPEVNLLFYLRKVIRLTGTKYGCGGGDCGACTVMIS RYDPISKRISHFSATACLVPICSLHGAAVTTVEGIGSTKTRIHPVQERIAKGHGTQCGFC TPGMVMSIYTLLRNHPEPSTEQIMETLGGNLCRCTGYRPIVESAKSFCPSSTCCQMNGEG KCCLDEEKNEPERKNSVCTKLYEKKEFQPLDPTQELIFPPELMRMAEESQNTVLTFRGER TTWIAPGTLNDLLELKMKHPSAPLVIGNTYLGLHMKFTDVSYPIIISPARILELFVVTNT KQGLTLGAGLSLTQVKNVLSDVVSRLPKEKTQIYCALLKQLKTLAGQQIRNVASLGGHII SRLPTSDLNPILGIGNCILNVASTEGIQQIPLNDHFLAGVPDAILKPEQVLISVFVPRSS KWEFVSAFRQAPRQQNAFATVNAGMKVVFKEDTNTITDLGILYGGIGATVISADKSCRQL IGRCWDEEMLDDAGKMICEEVSLLMAAPGGMEEYRKTLAISFLFMFYLDVLKQLKTRDPH KYPDISQKLLHILEDFPLTMPYGMQSFQDVDFQQPLQDPIGRPIMHQSGIKHATGEAVFC DDMSVLPGELFLAVVTSSKSHAKIISLDASEALASLGVVDVVTARDVPGDNGREEESLYA QDEVICVGQIVCAVAADSYAHAQQAAKKVKIVYQDIEPMIVTVQDALQYESFIGPERKLE QGNVEEAFQCADQILEGEVHLGGQEHFYMETQSVRVVPKGEDKEMDIYVSSQDAAFTQEM VARTLGIPKNRINCHVKRVGGAFGGKASKPGLLASVAAVAAQKTGRPIRFILERRDDMLI TGGRHPLLGKYKIGFMNNGKIKAADIQLYINGGCTPDDSELVIEYALLKLENAYKIPNLR VRGRVCKTNLPSNTAFRGFGFPQGAFVTETCMSAVAAKCRLPPEKVRELNMYRTIDRTIH NQEFDPTNLLQCWEACVENSSYYNRKKAVDEFNQQRFWKKRGIAIIPMKFSVGFPKTFYY QAAALVQIYTDGSVLVAHGGVELGQGINTKMIQVASRELKIPMSYIHLDEMSTVTVPNTV TTGASTGADVNGRAVQNACQILMKRLEPIIKQNPSGTWEEWVKEAFVQSISLSATGYFRG YQADMDWEKGEGDIFPYFVFGAACSEVEIDCLTGAHKNIRTDIVMDGSFSINPAVDIGQI EGAFVQGLGLYTLEELKYSPEGVLYTRGPHQYKIASVTDIPEEFHVSLLTPTPNPKAIYS SKGLGEAGTFLGCSVFFAIAAAVAAAREERGLSPIWAINSPATAEVIRMACEDQFTNLVP QTDSKCCKPWSIPVA P30677 Q8R2X9 GNA14_MOUSE Guanine nucleotide-binding protein subunit alpha-14 G alpha-14 G-protein subunit alpha-14 Gna14 Gna-14 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Head Stomach NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N-3 Mammary tumor PROTEIN SEQUENCE OF 57-69; 74-88; 163-177 AND 199-206 IDENTIFICATION BY MASS SPECTROMETRY C57BL/6J Brain NUCLEOTIDE SEQUENCE [MRNA] OF 217-267 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Testis Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Belongs to the G-alpha family. G(q) subfamily. Complete proteome Direct protein sequencing GTP-binding Magnesium Metal-binding Nucleotide-binding Reference proteome Transducer QL HV MAGCCCLSAEEKESQRISAEIERQLRRDKKDARRELKLLLLGTGESGKSTFIKQMRIIHG SGYSDEDRKGFTKLVYQNIFTAMQAMIRAMDTLRIQYMCEQNKENAQIIREVEVDKVTAL SRDQVAAIKQLWLDPGIQECYDRRREYQLSDSAKYYLTDIERIAMPSFVPTQQDVLRVRV PTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFESVTSIIFLVALSEYDQVLAECDN ENRMEESKALFRTIITYPWFLNSSVILFLNKKDLLEEKIMYSHLISYFPEYTGPKQDVKA ARDFILKLYQDQNPDKEKVIYSHFTCATDTENIRFVFAAVKDTILQLNLREFNLV Q9WVF9 Q1AFZ2 Q7TSP6 Q7TSP7 Q8BFR3 Q924B1 CLC2I_MOUSE C-type lectin domain family 2 member I C-type lectin-related protein DCL1 C-type lectin-related protein G Clr-g Lymphoid-derived C-type lectin-1 LCL-1 Osteoclast inhibitory lectin-related protein 2 Ocil-related protein 2 Clec2i Clrg Dcl1 Ocilrp2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) TISSUE SPECIFICITY C57BL/6J Natural killer cell NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2) FUNCTION INDUCTION TISSUE SPECIFICITY 129/Sv C57BL/6J NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4) FUNCTION SUBCELLULAR LOCATION INDUCTION TISSUE SPECIFICITY C57BL/6J Spleen NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) BALB/cJ Dendritic cell NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-171 BALB/cByJ Inhibits osteoclast formation. Receptor for KLRB1F. Enhances T-cell activation. Plays a role in splenocyte activation, T-cell responses and IL-2 production. Cell membrane Single-pass type II membrane protein Q9WVF9-1 1 Q9WVF9-2 2 Lymphoid-derived C-type lectin-1b LCL-1b Q9WVF9-3 3 Lymphoid-derived C-type lectin-1a LCL-1a Q9WVF9-4 4 Lymphoid-derived C-type lectin-1c LCL-1c Detected in osteoblasts, growth plate chondrocytes and skeletal muscle overlying the bone (at protein level). Detected in spleen, B-cells, dendritic cells, thymus, and in IL2-activated natural killer cells. Up-regulated in CD4(+) T-cells upon stimulation with CD3-ligands. Up-regulated in cultured calvarial osteoblasts by 1,25-dihydroxyvitamin D3. Constitutively expressed in cultured bone marrow cells during osteoclast formation. 3D-structure Alternative splicing Cell membrane Complete proteome Disulfide bond Glycoprotein Lectin Membrane Receptor Reference proteome Signal-anchor Transmembrane Transmembrane helix G GVQCC MPDCLETGEKLFVHNMNAQCVQKPEEGNGPLGTGGKIVQGKCFRIISTVSPVKLYCCYGV IMVLTVAVIALSVALSTKKTEQIIINKTYAACSKNWTGVGNKCFYFSGYPRNWTFAQAFC MAQEAQLARFDNEEELIFLKRFKGDFDCWIGLHRESSEHPWKWTNNTEYNNMNPILGVGR YAYLSSDRISSSRSYINRMWICSKLNNYNLHCQTPPV P10287 Q61465 Q8BSL6 CADH3_MOUSE Cadherin-3 Placental cadherin P-cadherin Cdh3 Cdhp Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Forelimb NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Embryo PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] C57BL/6J Embryo NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55 NUCLEOTIDE SEQUENCE OF 1-55 C57BL/6J DEVELOPMENTAL STAGE C57BL/6J Testis Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Interacts with CDCP1 and CTNNB1. Cell membrane Single-pass type I membrane protein Expression is high in both fetal and newborn testis but minimal in testis of 7-day-old animals. Not detected in testis of 21-day-old or adult. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. 3D-structure Calcium Cell adhesion Cell membrane Cleavage on pair of basic residues Complete proteome Glycoprotein Membrane Metal-binding Reference proteome Repeat Signal Transmembrane Transmembrane helix S W A P L M MELLSGPHAFLLLLLQVCWLRSVVSEPYRAGFIGEAGVTLEVEGTDLEPSQVLGKVALAG QGMHHADNGDIIMLTRGTVQGGKDAMHSPPTRILRRRKREWVMPPIFVPENGKGPFPQRL NQLKSNKDRGTKIFYSITGPGADSPPEGVFTIEKESGWLLLHMPLDREKIVKYELYGHAV SENGASVEEPMNISIIVTDQNDNKPKFTQDTFRGSVLEGVMPGTSVMQVTATDEDDAVNT YNGVVAYSIHSQEPKEPHDLMFTIHKSTGTISVISSGLDREKVPEYRLTVQATDMDGEGS TTTAEAVVQILDANDNAPEFEPQKYEAWVPENEVGHEVQRLTVTDLDVPNSPAWRATYHI VGGDDGDHFTITTHPETNQGVLTTKKGLDFEAQDQHTLYVEVTNEAPFAVKLPTATATVV VHVKDVNEAPVFVPPSKVIEAQEGISIGELVCIYTAQDPDKEDQKISYTISRDPANWLAV DPDSGQITAAGILDREDEQFVKNNVYEVMVLATDSGNPPTTGTGTLLLTLTDINDHGPIP EPRQIIICNQSPVPQVLNITDKDLSPNSSPFQAQLTHDSDIYWMAEVSEKGDTVALSLKK FLKQDTYDLHLSLSDHGNREQLTMIRATVCDCHGQVFNDCPRPWKGGFILPILGAVLALL TLLLALLLLVRKKRKVKEPLLLPEDDTRDNVFYYGEEGGGEEDQDYDITQLHRGLEARPE VVLRNDVVPTFIPTPMYRPRPANPDEIGNFIIENLKAANTDPTAPPYDSLLVFDYEGSGS DAASLSSLTTSASDQDQDYNYLNEWGSRFKKLADMYGGGEDD P59384 Q504Z2 Q91Z56 ATS15_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 15 ADAM-TS 15 ADAM-TS15 ADAMTS-15 3.4.24.- Adamts15 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J FVB/N Brain Kidney Zn(2+) Binds 1 zinc ion per subunit. Secreted Extracellular space Extracellular matrix 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 Protease Reference proteome Repeat Secreted Signal Zinc Zymogen MMSPTLIQ AIPAGASS SPRD PRVR P L MLLLGISILALAWRPAGSSEPEWEVVVPIRRDPDINGRHYYRRGTEDSGDQGLIFQITAF QQDFYLHLTPDAQFLAPAFATEYLGVPLQRLTGSSLDLRRCFYSGYVNAEPDSFAAVSLC GGLRGAFGYRGAEYVISPLPNTSAPEAQRHSQGAHLLQRRGAPVGPSGDPTSRCGVASGW NPAILRALDPYKPRRTGAGESHNRRRSGRAKRFVSIPRYVETLVVADESMVKFHGADLEH YLLTLLATAARLYRHPSILNPINIVVVKVLLLGDRDTGPKVTGNAALTLRNFCAWQKKLN KVSDKHPEYWDTAILFTRQDLCGATTCDTLGMADVGTMCDPKRSCSVIEDDGLPSAFTTA HELGHVFNMPHDNVKVCEEVFGKLRANHMMSPTLIQIDRANPWSACSAAIITDFLDSGHG DCLLDQPSKPITLPEDLPGTSYSLSQQCELAFGVGSKPCPYMQYCTKLWCTGKAKGQMVC QTRHFPWADGTSCGEGKFCLKGACVERHNPNKYRVDGSWAKWEPYGSCSRTCGGGVQLAR RQCSNPTPANGGKYCEGVRVKYRSCNLEPCPSSASGKSFREEQCEAFNGYNHSTNRLTLA VAWVPKYSGVSPRDKCKLICRANGTGYFYVLAPKVVDGTLCTPDSTSVCVQGKCIKAGCD GNLGSKKKFDKCGVCGGDNKSCKRVTGLFTKPMHGYNFVVAIPAGASSIDIRQRGYKGLI GDDNYLALKNSQGKYLLNGHFVVSAVERDLVVKGSVLRYSGTGTAVESLQASRPILEPLT VEVLSVGKMTPPRVRYSFYLPKEPREDKSTRPKDPRGSPVLRNSVLSLSNQVEQPDNRPP ARWVAGSWGPCSVSCGSGLQKRAVDCRDSPGQQGASACDVDHRPLEKRACGEPCPTWELG NWSPCSKSCGRGFKRRPLKCVGHGGRLLARDQCDLRRKPQELDFCVLRPC Q3UMW8 Q8C054 Q8R152 CLN5_MOUSE Ceroid-lipofuscinosis neuronal protein 5 homolog Protein CLN5 Ceroid-lipofuscinosis neuronal protein 5 homolog, secreted form Cln5 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Lung Olfactory bulb NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-341 FVB/N Mammary tumor INTERACTION WITH PPT1; TPP1; CLN3; CLN6; CLN8; ATP5F1A AND ATP5F1B SUBCELLULAR LOCATION (SECRETED FORM) PROTEOLYTIC CLEAVAGE AT C-TERMINUS TISSUE SPECIFICITY Plays a role in influencing the retrograde trafficking of lysosomal sorting receptors SORT1 and IGF2R from the endosomes to the trans-Golgi network by controlling the recruitment of retromer complex to the endosomal membrane. Regulates the localization and activation of RAB7A which is required to recruit the retromer complex to the endosomal membrane. Interacts with PPT1, TPP1, CLN3, CLN6, CLN8, ATP5F1A and ATP5F1B (PubMed:19941651). Interacts with SORT1, RAB5A and RAB7A (By similarity). Ceroid-lipofuscinosis neuronal protein 5 homolog, secreted form Lysosome Ceroid-lipofuscinosis neuronal protein 5 homolog Membrane Single-pass type II membrane protein An amphipathic anchor region facilitates its association with the membrane. Heart, kidney, liver, spleen, muscle and rectum (at protein level). N-glycosylated with both high mannose and complex type sugars. Glycosylation is important for proper folding and trafficking to the lysosomes. Ceroid-lipofuscinosis neuronal protein 5 homolog: The type II membrane signal anchor is proteolytically cleaved to produce a mature form that is transported to the lysosomes (Ceroid-lipofuscinosis neuronal protein 5 homolog, secreted form). Can undergo proteolytic cleavage at the C-terminus, probably by a cysteine protease and may involve the removal of approximately 10-15 residues from the C-terminal end (PubMed:26342652). Belongs to the CLN5 family. Complete proteome Glycoprotein Lysosome Membrane Neurodegeneration Neuronal ceroid lipofuscinosis Reference proteome Signal-anchor Transmembrane Transmembrane helix PCG TRP R H MLRGGPCGAHWRPALALALLGLATILGASPTSGQRWPVPYKRFSFRPKTDPYCQAKYTFC PTGSPIPVMKDNDVIEVLRLQAPIWEFKYGDLLGHFKLMHDAVGFRSTLTGKNYTIEWYE LFQLGNCTFPHLRPDKSAPFWCNQGAACFFEGIDDKHWKENGTLSVVATISGNTFNKVAE WVKQDNETGIYYETWTVRAGPGQGAQTWFESYDCSNFVLRTYKKLAEFGTEFKKIETNYT KIFLYSGEPIYLGNETSIFGPKGNKTLALAIKKFYGPFRPYLSTKDFLMNFLKIFDTVII HRQFYLFYNFEYWFLPMKPPFVKITYEETPLPTRHTTFTDL P60824 O09069 O09148 Q3V1A6 Q61413 CIRBP_MOUSE Cold-inducible RNA-binding protein A18 hnRNP Glycine-rich RNA-binding protein CIRP Cirbp Cirp Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION INDUCTION BY COLD-SHOCK DDY/STD Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Head NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Eye FUNCTION METHYLATION SUBCELLULAR LOCATION MUTAGENESIS OF ARG-91; ARG-94; ARG-101; ARG-105; ARG-108; ARG-110; ARG-112; ARG-116; ARG-121; ARG-127 AND ARG-131 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Liver Lung Pancreas Spleen Testis Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Promotes assembly of stress granules (SGs), when overexpressed. Seems to play an essential role in cold-induced suppression of cell proliferation. Acts as a translational repressor. Acts as a translational activator. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Interacts with EIF4G1. Associates with ribosomes (By similarity). Nucleus Nucleoplasm Cytoplasm Translocates from the nucleus to the cytoplasm after exposure to UV radiation (By similarity). Translocates from the nucleus to the cytoplasm into stress granules upon various cytoplasmic stresses, such as osmotic and heat shocks. Its recruitment into stress granules occurs in the absence of TIAR proteins. Ubiquitous. Up-regulated upon mild cold-shock and hypoxia. Both the RRM domain and the arginine, glycine (RGG) rich domain are necessary for binding to the TXN 3'-untranslated region (By similarity). Both the RRM domain and the arginine, glycine (RGG) rich domain (RGG repeats) are necessary for optimal recruitment into SGs upon cellular stress. The C-terminal domain containing RGG repeats is necessary for translational repression. Methylated on arginine residues. Methylation of the RGG motifs is a prerequisite for recruitment into SGs. Phosphorylated by CK2, GSK3A and GSK3B. Phosphorylation by GSK3B increases RNA-binding activity to the TXN 3'-UTR transcript upon exposure to UV radiation (By similarity). Activator Complete proteome Cytoplasm Methylation Nucleus Phosphoprotein Reference proteome Repressor RNA-binding Stress response R K R K R K R K R K R K R K R K R K R K R K MASDEGKLFVGGLSFDTNEQALEQVFSKYGQISEVVVVKDRETQRSRGFGFVTFENIDDA KDAMMAMNGKSVDGRQIRVDQAGKSSDNRSRGYRGGSAGGRGFFRGGRSRGRGFSRGGGD RGYGGGRFESRSGGYGGSRDYYASRSQGGSYGYRSSGGSYRDSYDSYATHNE P00184 Q61455 CP1A1_MOUSE Cytochrome P450 1A1 1.14.14.- CYPIA1 Cytochrome P450 form 6 Cytochrome P450-C Cytochrome P450-P1 Hydroperoxy icosatetraenoate dehydratase 4.2.1.152 Cyp1a1 Cyp1a-1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] C57BL/6J Liver NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [MRNA] C57BL/6J NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Liver PROTEIN SEQUENCE OF 2-25 C57BL/6J NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 280-321 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Lung A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. Catalyzes the epoxidation of double bonds of certain PUFA. Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system. Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer. May play an important role in 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. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent). 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] estrone + O2 + reduced [NADPH--hemoprotein reductase] = 6alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] estrone + O2 + reduced [NADPH--hemoprotein reductase] = 15alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] estrone + O2 + reduced [NADPH--hemoprotein reductase] = 16alpha-hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 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] 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 6alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase] = 15alpha-hydroxy-17beta-estradiol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 16-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 17-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + 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] = (14S,15R)-epoxy-(5Z,8Z,11Z)-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] (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (19S,20R)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + 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] (13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-(6E,8Z,11Z,14Z)-eicosatetraenoate + H2O heme Steroid hormone biosynthesis. Lipid metabolism; fatty acid metabolism. Cofactor metabolism; retinol metabolism. Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria. Interacts (via mitochondrial targeting signal) with TOMM40 (via N-terminus); this interaction is required for translocation across the mitochondrial outer membrane. Endoplasmic reticulum membrane Peripheral membrane protein Mitochondrion inner membrane Peripheral membrane protein Microsome membrane Peripheral membrane protein Cytoplasm By 3-methylcholanthrene (3MC). Belongs to the cytochrome P450 family. Complete proteome Cytoplasm Direct protein sequencing Endoplasmic reticulum Glycoprotein Heme Iron Lipid biosynthesis Lipid metabolism Lyase Membrane Metal-binding Microsome Mitochondrion Mitochondrion inner membrane Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis MPSMYGLPAFVSATELLLAVTVFCLGFWVVRATRTWVPKGLKTPPGPWGLPFIGHMLTVG KNPHLSLTRLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVRQGDDFKGRPDLYSFTLIT NGKSMTFNPDSGPVWAARRRLAQNALKSFSIASDPTSASSCYLEEHVSKEANYLVSKLQK VMAEVGHFDPYKYLVVSVANVICAICFGQRYDHDDQELLSIVNLSNEFGEVTGSGYPADF IPVLRYLPNSSLDAFKDLNDKFYSFMKKLIKEHYRTFEKGHIRDITDSLIEHCQDRKLDE NANVQLSDDKVITIVLDLFGAGFDTVTTAISWSLMYLVTNPRVQRKIQEELDTVIGRDRQ PRLSDRPQLPYLEAFILETFRHSSFVPFTIPHSTTRDTSLNGFYIPKGCCVFVNQWQVNH DRELWGDPNEFRPERFLTPSGTLDKRLSEKVTLFGLGKRKCIGETIGRSEVFLFLAILLQ QIEFKVSPGEKVDMTPTYGLTLKHARCEHFQVQMRSSGPQHLQA Q60649 CLPB_MOUSE Caseinolytic peptidase B protein homolog 3.6.1.3 Suppressor of potassium transport defect 3 Clpb Skd3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain PROTEIN SEQUENCE OF 574-590 IDENTIFICATION BY MASS SPECTROMETRY OF1 Hippocampus IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Pancreas May function as a regulatory ATPase and be related to secretion/protein trafficking process. ATP + H2O = ADP + H(+) + phosphate Mitochondrion Widely expressed, with highest levels in testis. Also expressed in heart, skeletal muscle and kidney. Belongs to the ClpA/ClpB family. Acetylation ANK repeat ATP-binding Complete proteome Direct protein sequencing Hydrolase Mitochondrion Nucleotide-binding Reference proteome Repeat Transit peptide MMLSAVLRRTTPAPRLFLGLIKSPSLQSRGGAYGRGVVTGDRGEPQRLRAAAWVRPGASS TFVPGRGAATWGRRGERTEIPYLTAASSERGPSPEETLPGQDSWNGVPNKTGLGMWALAM ALVVQCYSKNPSNKDAALMEAARANNVQEVRRLLSEGADVNARHKLGWTALMVASISHNE SVVQVLLAAGADPNLGDEFSSVYKTANEQGVHSLEVLVTREDDFNNRLNHRASFKGCTAL HYAVLADDYSIVKELLDRGANPLQRNEMGHTPLDYAREGEVMKLLKTSETKYMEKQRKRE AEERRRFPLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLVFLFLGSSGIGKTEL AKQTAKYMHKDAKKGFIRLDMSEFQERHEVAKFIGSPPGYIGHEEGGQLTKKLKQCPNAV VLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALQLR QEALEMSRNRIAENLGDVQMSDKITISKNFKENVIRPILKAHFRRDEFLGRINEIVYFLP FCHSELIQLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYNVHYGARSIKHEVERRV VNQLAAAYEQDLLPGGCTLRITVEDSDKHLLKSPELPSPQAEKRPPTLRLEIIDKDSKTR KLDIQAPLHPEKVCYTI Q8WTY4 Q3UJW5 Q8VC24 Q91W83 CPIN1_MOUSE Anamorsin Cytokine-induced apoptosis inhibitor 1 Fe-S cluster assembly protein DRE2 homolog Ciapin1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION SUBCELLULAR LOCATION INDUCTION DISRUPTION PHENOTYPE NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J DBA/2J NOD Cerebellum Diencephalon Spinal cord Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Liver Salivary gland SUBCELLULAR LOCATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (PubMed:14970183). [2Fe-2S] cluster [4Fe-4S] cluster Monomer. Interacts with NDOR1. Interacts with CHCHD4. Q9CQM9 Glrx3 false 4 Cytoplasm Nucleus Mitochondrion intermembrane space Expressed from early embryogenesis. By cytokines such as IL3 and THPO. The twin Cx2C motifs are involved in the recognition by the mitochondrial CHCHD4/MIA40-GFER/ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space. The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation. The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters. Death in late gestation due to defective definitive hematopoiesis in the fetal liver, possibly due to initiated apoptosis in erythroid cells during terminal maturation. 'Ana-mors-in' means 'anti-death molecule' in Latin. Belongs to the anamorsin family. 2Fe-2S 4Fe-4S Apoptosis Complete proteome Cytoplasm Iron Iron-sulfur Metal-binding Mitochondrion Nucleus Phosphoprotein Reference proteome MEEFGISPGQLVAVFWDKSSPEEALKKLVARLQELTGSEGQVFMENVTQLLQSSHKESSF DVILSGVVPGSTSLHSAEVLAEMARILRPGGCLFLKEPVETAEVNNDKMKTASKLCSALT LSGLVEIKELQREALSPEEVQSVQEHLGYHSDSLRSVRVTGKKPNFEVGSSSQLKLPNKK SSSVKPVVDPAAAKLWTLSANDMEDDSVDLIDSDELLDPEDLKRPDPASLKAPSCGEGKK RKACKNCTCGLAEELEREQSKAQSSQPKSACGNCYLGDAFRCANCPYLGMPAFKPGEQVL LSNSNLQDA Q8R1B5 Q96AW7 CPLX3_MOUSE Complexin-3 Complexin III CPX III Cplx3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION SUBUNIT SUBCELLULAR LOCATION TISSUE SPECIFICITY DEVELOPMENTAL STAGE ISOPRENYLATION AT CYS-155 METHYLATION AT CYS-155 BALB/cJ Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Retina NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Eye FUNCTION TISSUE SPECIFICITY DISRUPTION PHENOTYPE IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY DISRUPTION PHENOTYPE FUNCTION DISRUPTION PHENOTYPE Complexin that regulates SNARE protein complex-mediated synaptic vesicle fusion (PubMed:19386896). Required for the maintenance of synaptic ultrastructure in the adult retina (PubMed:19386896). Positively regulates synaptic transmission through synaptic vesicle availability and exocytosis of neurotransmitters at photoreceptor ribbon synapses in the retina (PubMed:15911881, PubMed:19386896, PubMed:27335398). Suppresses tonic photoreceptor activity and baseline 'noise' by suppression of Ca(2+) vesicle tonic release and the facilitation of evoked synchronous and asynchronous Ca(2+) vesicle release (PubMed:22694764, PubMed:27335398). Binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A. Cell junction Synapse Cell membrane Lipid-anchor Enriched at the synaptic terminal (PubMed:15911881). Localized at glycinergic synaptic contacts of AII amacrine cells with OFF cone bipolar cells in the OFF sublamina of the retina inner nuclear layer (PubMed:22694764). Present in many brain regions, including hippocampus and cerebellum (at protein level) (PubMed:15911881). Expressed in the retina (at protein level) (PubMed:15911881, PubMed:19386896). Expressed in retinal amacrine cells (at protein level) (PubMed:19386896, PubMed:22694764). Expressed in retinal photoreceptor ribbon synapses (PubMed:19386896). Expressed in the retinal inner nuclear layer, at bipolar cells (at protein level) (PubMed:22694764). Expressed in cone photoreceptor synaptic terminals (at protein level) (PubMed:22694764). In the brain, expression starts at P6 and increases to reach a plateau at P20. Farnesylation mediates presynaptic targeting. Knockout mice are generally phenotypically normal, viable, and fertile (PubMed:19386896). Normal overall retina structure and morphology of the outer plexiform layer (OPL) and inner plexiform layer (IPL) (PubMed:19386896). Abundance and distribution of synaptic proteins remain consistent (PubMed:19386896). Reduced retinal synaptic transmission and inner retinal processing (PubMed:19386896). Cplx3 and Cplx4 double knockout mice are generally phenotypically normal, viable, and fertile, however show disordered morphology of the OPL and vision perturbation when compared to single knockout mice (PubMed:19386896). Cplx3 and Cplx4 double knockout mice show evidence of mild vision perturbation, with a reduction in the number of morphologically normal anchored presynaptic ribbon synapses and a decrease in controlled neurotransmitter release at photoreceptor ribbon synapses (PubMed:19386896). Cplx3 and Cplx4 double knockout mice show reduced response and sensitivity of ON and OFF ganglion cell response as a result of disrupted synaptic transmission (PubMed:22694764). Cplx3 and Cplx4 double knockout mice show a greater variance in photoreceptor activity response and a decrease in sustained response, this is caused by an increase in release and fusion of synaptic vesicles in an asynchronous manner, this is particularly evident following multiple stimuli (PubMed:27335398). Belongs to the complexin/synaphin family. Cell junction Cell membrane Coiled coil Complete proteome Exocytosis Lipoprotein Membrane Methylation Neurotransmitter transport Prenylation Reference proteome Sensory transduction Synapse Transport Vision MAFMVKSMVGGQLKNLTGSLGGGEDKGDGDKSAAEAQGMSREEYEEYQKQLVEEKMERDA QFTQRKAERATLRSHFRDKYRLPKNETDESQIQLAGGDVELPRELAKMIEEDTEEEEDKA SVLGQLASLPGLDLSSLKDKAQTTLGDLKQSAEKCHIM P70194 Q8BLZ8 CLC4F_MOUSE C-type lectin domain family 4 member F C-type lectin superfamily member 13 C-type lectin 13 Kupffer cell receptor Clec4f Clecsf13 Kclr Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Aorta NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Liver IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Receptor with an affinity for galactose and fucose. Could be involved in endocytosis. Membrane Single-pass type II membrane protein Kupffer cells. Kupffer cell receptor Complete proteome Disulfide bond Endocytosis Glycoprotein Lectin Membrane Receptor Reference proteome Signal-anchor Transmembrane Transmembrane helix T S MKEAELNRDMARYCTDNQCVSLQPQGLGPKSAALMAPRTLRHVQVILALMVVTVIFSLLA LFVVASQPWRPEWNKEPPSLLLRGSNNSGHDNHSQFVRETEMQVAIQRLRDYEENSSSCH KEVQILKYQMDNVSSLVQLLGSHLEDVNADILQTKDVLKESGALALETQALRSSLEVASA DIHSLRGDLEKANAMTSQTRGLLKSSTENTSAELHVLGRGLEEAQSEIQALRGSLQSAND LSSQTQGFLQHSMDNISAQIQTVRDGMERAGEKMNSLKKELETLTAQTQKANGHLEQTDA QIQGLKAELKSTSSLNSRIEVVNGQMKDASRELQTLRRDLSDVSALKSNVQMLQSNLQRA KTEMQTLKADLQATKALTAKIQGEQNRLGALQEAVAAQKQEQKTQNQVLQLIAQNWKYFN GNFYYFSRDKKPWREAEKFCTSQGAHLASVTSQEEQAFLVQTTSSGDHWIGLTDQGTEGI WRWVDGTPFNNAQSKGFWGKNQPDNWRHRNGEREDCVHVRQQWNDMACGSSYPWVCKKST GWSAARVG O35298 AOAH_MOUSE Acyloxyacyl hydrolase 3.1.1.77 Acyloxyacyl hydrolase small subunit Acyloxyacyl hydrolase large subunit Aoah Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C57B1/6 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Eye FUNCTION CATALYTIC ACTIVITY TISSUE SPECIFICITY DISRUPTION PHENOTYPE FUNCTION CATALYTIC ACTIVITY SUBUNIT SUBCELLULAR LOCATION TISSUE SPECIFICITY FUNCTION CATALYTIC ACTIVITY TISSUE SPECIFICITY DISRUPTION PHENOTYPE FUNCTION CATALYTIC ACTIVITY DISRUPTION PHENOTYPE FUNCTION CATALYTIC ACTIVITY FUNCTION TISSUE SPECIFICITY INDUCTION DISRUPTION PHENOTYPE X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 23-574 OF MUTANT ALA-262 IN COMPLEX WITH CALCIUM AND THE LIPID A MOIETY OF BACTERIAL LIPOPOLYSACCHARIDE COFACTOR SUBUNIT DISULFIDE BONDS MUTAGENESIS OF SER-262 ACTIVE SITE GLYCOSYLATION AT ASN-206; ASN-408 AND ASN-465 Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS) (PubMed:12810692, PubMed:15155618, PubMed:17322564, PubMed:19860560). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses (PubMed:17322564, PubMed:19860560, PubMed:28622363). In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria (PubMed:18779055). a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+) Ca(2+) Binds 3 Ca(2+) ions per subunit. The calcium ions probably have a structural role. Heterodimer of the large and small subunits; disulfide-linked. Secreted Cytoplasmic vesicle Detected in urine. Detected in peritoneal macrophages (at protein level) (PubMed:17322564, PubMed:28622363). Strongly expressed in kidney cortex, where it may be produced by proximal tubule cells (PubMed:15155618). In liver, expressed at high levels in Kupffer cells (PubMed:17322564). Expressed by dendritic cells (PubMed:12810692). Detected at low levels in alveolar macrophages (PubMed:28622363). Strongly up-regulated in alveolar macrophages in response to bacterial lipopolysaccharides (LPS). Cleaved into a large and a small subunit. The small subunit is N-glycosylated. Animals develop significant and prolonged hepatosplenomegaly in response to bacterial lipopolysaccharide (LPS) challenge (PubMed:17322564). Both liver and spleen show increased accumulation of leukocytes (PubMed:17322564). Significantly reduced deacylation of LPS in liver and spleen, in peritoneal macrophages, and in bone marrow-derived dendritic cells (PubMed:12810692, PubMed:17322564, PubMed:18779055). Increased lung injury, delayed neutrophil clearance, and prolonged recovery time in response to intranasal LPS administration (PubMed:28622363). Alveolar macrophages show persistent activation and cytokine levels in lung remain elevated 4-7 days after LPS administration (PubMed:28622363). Impaired response to a second infection challenge, with reduced production of the pro-inflammatory chemokines CCL5/RANTES, TNF and IL6 by peritoneal macrophages and reduced survival rates, indicating a prolonged state of immune tolerance (PubMed:18779055). This immune tolerant state can perisist for two months or longer (PubMed:18779055). 3D-structure Calcium Complete proteome Cytoplasmic vesicle Disulfide bond Glycoprotein Hydrolase Lipid metabolism Metal-binding Reference proteome Secreted Signal Zymogen S A MKFPWKVFKTTLLLLLLSHSLASVPSEDQPGDSYSHGQSCLGCVVLVSVIEQLAEVHNSS VQVAMERLCSYLPEKLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFCKRGAVQP QCHLYPLPQEAWESALEKARQVLRRSSTMKYPRSGRNICSLPFLTKICQKIELSIKKAVP FKDIDSDKHSVFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDIHQDSNCNGIWGIDPKDG IPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVNSFLNLPSALTDELNWPQL SGVTGFLDSTSGIEEKSIYHRLRKRNHCNHRDYQSISKNGASSRNLKNFIESLSRNQASD HPAIVLYAMIGNDVCNSKADTVPEMTTPEQMYANVMQTLTHLNSHLPNGSHVILYGLPDG TFLWDSLHNRYHPLGQLNKDVTYAQFFSFLRCLQLNPCNGWMSSNKTLRTLTSERAEQLS NTLKKIATTETFANFDLFYVDFAFHEIIEDWQKRGGQPWQLIEPVDGFHPNEVASLLQAN RVWEKIQLQWPHVLGKENPFNSQIEEVFGDQGGH P33622 Q8VC58 Q9CPP9 APOC3_MOUSE Apolipoprotein C-III Apo-CIII ApoC-III Apolipoprotein C3 Apoc3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Kidney Small intestine NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Liver PROTEIN SEQUENCE OF 42-68 MASS SPECTROMETRY OXIDATION AT MET-63 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners. Secreted The most abundant glycoforms are characterized by an O-linked disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc), further modified with up to 3 sialic acid residues. Less abundant glycoforms are characterized by more complex and fucosylated glycan moieties. O-glycosylated on Thr-94 with a core 1 or possibly core 8 glycan. Strain C57BL/6. Without methionine sulfoxide. Strain BALB/c. Without methionine sulfoxide. Belongs to the apolipoprotein C3 family. Chylomicron Complete proteome Direct protein sequencing Glycoprotein Lipid degradation Lipid metabolism Lipid transport Oxidation Reference proteome Secreted Sialic acid Signal Transport VLDL V A F S MQPRTLLTVALLALLASARAEEVEGSLLLGSVQGYMEQASKTVQDALSSVQESDIAVVAR GWMDNHFRFLKGYWSKFTDKFTGFWDSNPEDQPTPAIES Q8VEG6 Q3U9M0 Q8C0P4 CNO6L_MOUSE CCR4-NOT transcription complex subunit 6-like 3.1.13.4 Cnot6l Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3) C57BL/6J Bone marrow Testis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) FVB/N Mammary tumor PROTEIN SEQUENCE OF 269-277 IDENTIFICATION BY MASS SPECTROMETRY OF1 Hippocampus INTERACTION WITH NANOS2 INTERACTION WITH ZFP36 DEVELOPMENTAL STAGE Poly(A) nuclease with 3'-5' RNase activity. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Involved in mRNA decay mediated by the major-protein-coding determinant of instability (mCRD) of the FOS gene in the cytoplasm. Involved in deadenylation-dependent degradation of CDKN1B mRNA. Its mRNA deadenylase activity can be inhibited by TOB1. Mediates cell proliferation and cell survival and prevents cellular senescence (By similarity). Exonucleolytic cleavage of poly(A) to 5'-AMP. Mg(2+) Binds 2 magnesium ions, but the ions interact each with only 1 or 2 residues. Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits; the complex contains two deadenylase subunits, CNOT6 or CNOT6L, and CNOT7 or CNOT8 (By similarity). Interacts with CNOT1, CNOT3, CNOT7, CNOT8 and CNOT9 (By similarity). Interacts with TOB1 (By similarity). Interacts with NANOS2 (PubMed:20133598). Interacts with ZFP36 (PubMed:21078877). Q60809 Cnot7 false 2 Cytoplasm Nucleus Predominantly cytoplasmic. Q8VEG6-1 1 Q8VEG6-2 2 Q8VEG6-3 3 Expressed in embryonic stem (ES) cells. Belongs to the CCR4/nocturin family. Alternative splicing Complete proteome Cytoplasm Direct protein sequencing Exonuclease Hydrolase Leucine-rich repeat Magnesium Metal-binding mRNA processing Nuclease Nucleus Reference proteome Repeat RNA-mediated gene silencing Transcription Transcription regulation Translation regulation MRLIGM M Y V L F MRLIGMPKEKYDPPDPRRIYTIMSAEEVANGKKSHWAELEISGRVRSLSTSLWSLTHLTA LHLNDNNLARIPPDIAKLHNLVYLDLSSNKLRSLPAELGNMVSLRELLLNDNYLRVLPYE LGRLFQLQTLGLTGNPLSQDIMSLYQDPDGTRKLLNFMLDNLAVHPEQLPPRPWITLKER DQILPSASFTVMCYNVLCDKYATRQLYGYCPSWALNWEYRKKGIMEEIVNWDADIISLQE VETEQYFTLFLPALKDRGYDGFFSPKSRAKIMSEQERKHVDGCAIFFKTEKFTLVQKHTV EFNQVAMANSDGSEAMLNRVMTKDNIGVAVVLEVHKELFGTGMKPIHAADKQLLIVANAH MHWDPEYSDVKLIQTMMFVSEVKNILEKASSRPGSPTADPNSIPLVLCADLNSLPDSGVV EYLSNGGVADNHKDFKELRYNECLMNFSCSGKNGSSEGRITHGFQLKSAYENNLMPYTNY TFDFKGVIDYIFYSKTHMNVLGVLGPLDPQWLVENNITGCPHPHIPSDHFSLLTQLELHP PLLPLVNGVHLPNRR Q8N9S3 Q0P626 Q6P3F2 Q7TMW7 Q8CBI4 AHSA2_MOUSE Activator of 90 kDa heat shock protein ATPase homolog 2 Ahsa2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J NOD Cerebellum Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3) C57BL/6NCr Czech II Hematopoietic stem cell Jaw Limb Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Lung Spleen Co-chaperone that stimulates HSP90 ATPase activity. Q8N9S3-1 1 Q8N9S3-2 2 Q8N9S3-3 3 Belongs to the AHA1 family. Translation N-terminally extended. Alternative splicing Chaperone Complete proteome Reference proteome Stress response EHYATVELNFVPAPGQTELQLDCKGVPVCKEENMKFCWQKQHFEEIKGLLELTAQNA ALGFFPRTLCNS E A E A E G T A MAKWGQGDPRWIVEEREDGTNVNNWHWTERDATIWSKGKLRELLVGIAMENEAGRCEISE LKQVEGEASCNSRKGKLIFFYEWNIKLAWKGTVKESGAKHKGLIEIPSLSEENEINDTEV NVSKKKGDGEILKDLMRTTGTAKVREALGEYLKALKTEFTTGMILPTKAVATQELTLQRK LNENKLQASPVALGVRIPTVALHLTELFDTTVEQLYSIFTVKELVQKFSKSPAVLEAERG GKFQMFDGNISGEYVELVTNRKIIMKWRCRNWPEEHYATVELNFVPAPGQTELQLDCKGV PVCKEENMKFCWQKQHFEEIKGLLELTAQNA Q922Q9 Q3TVF7 Q6P8U4 Q8C7C5 Q9CXR7 CHID1_MOUSE Chitinase domain-containing protein 1 Chid1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J Head Pancreas Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) FVB/N Brain Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Spleen Testis Saccharide- and LPS-binding protein with possible roles in pathogen sensing and endotoxin neutralization. Ligand-binding specificity relates to the length of the oligosaccharides, with preference for chitotetraose (in vitro) (By similarity). Interacts with STAB1. Secreted Lysosome Q922Q9-1 1 Q922Q9-2 2 Belongs to the glycosyl hydrolase 18 family. Translated as Tyr. Alternative splicing Complete proteome Immunity Innate immunity Lysosome Reference proteome Secreted Signal W R MWPLLHVLWLALVCGSVHTTLSKSDAKKAASKMLLEKTQFSDKPVQDRGLVVTDIKAEDV VLEHRSYCSSRARERNFAGEVLGYVTPWNSHGYDVAKVFGSKFTQISPVWLQLKRRGREM FEITGLHDVDQGWMRAVKKHAKGVRIVPRLLFEDWTYDDFRNVLDSEDEIEELSKTVAQV AKNQHFDGFVVEVWSQLLSQKHVGLIHMLTHLAEALHQARLLVILVIPPAVTPGTDQLGM FTHKEFEQLAPILDGFSLMTYDYSTSQQPGPNAPLSWIRACVQVLDPKSQWRSKILLGLN FYGMDYAASKDAREPVIGARYVQTLKDHRPRVVWDSQAAEHFFEYKKNRGGRHVVFYPTL KSLQVRLELARELGVGVSIWELGQGLDYFYDLL Q3UX43 B2RST2 Q6P1G4 AN13C_MOUSE Ankyrin repeat domain-containing protein 13C Ankrd13c Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Egg NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J Brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Acts as a molecular chaperone for G protein-coupled receptors, regulating their biogenesis and exit from the ER. Endoplasmic reticulum membrane Associated with the cytosolic side. Q3UX43-1 1 Q3UX43-2 2 No experimental confirmation available. Alternative splicing ANK repeat Chaperone Complete proteome Endoplasmic reticulum Membrane Phosphoprotein Reference proteome Repeat VPLLSRILPSDAC GKSVLRFIIKVQL APAVPGPGVPAPPQHNAVTATCPAPACLGGSNPALVADGGGCP VSSEALARGAGERWLRRVFPSEEEAAAAAPGVVRSWSLELRLS MTGEKIRSLRRDHKPSKEDGDVLEPCEEEATAALGGAFTGGRSGPGGSGKGGKACHKIFS HHHRLQLKAPAVPGPGVPAPPQHNAVTATCPAPACLGGSNPALVADGGGCPSLYPVHECV FKGDVRRLSSLIRTHNIGQKDNHGNTPLHLAVMLGNKECAHLLLAHNAPVKVKNAQGWSP LAEAISYGDRQMITALLRKLKQQSRESVGEKRPRLLKALKELGDFYLELHWDFQSWVPLL SRILPSDACKIYKQGINIRLDTTLIDFTDMKCQRGDLSFIFNGDAAPSESFVVLDNEQKV YQRIHHEESEMETEEEVDILMSSDIYSATLSTKSISFTRAQTGWLFREDKTERVGNFLAD FYLVNGLVLESRKRREHLSEEDILRNKAIMESLSKGGSLAEQSFEPVRRQSLTPPPQNTI TWEEYISAENGKAPHLGRELVCKESKKTFKATVAMSQEFPLGIESLLNVLEVIAPFKHFN KLREFVQMKLPPGFPVKLDIPVFPTITATVTFQEFRCDEFDGSIFAIPEDYKEDPSRFPD L Q80U30 A6X932 B2RSL3 Q3TCF2 Q3U0F5 Q3U2F6 Q8CEQ8 CL16A_MOUSE Protein CLEC16A Clec16a Kiaa0350 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5) C57BL/6J NOD Spleen Testis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain TISSUE SPECIFICITY IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Heart Liver Lung Pancreas FUNCTION SUBCELLULAR LOCATION INTERACTION WITH RNF41 DISRUPTION PHENOTYPE TISSUE SPECIFICITY Regulator of mitophagy through the upstream regulation of the RNF41/NRDP1-PRKN pathway. Mitophagy is a selective form of autophagy necessary for mitochondrial quality control. The RNF41/NRDP1-PRKN pathway regulates autophagosome-lysosome fusion during late mitophagy. May protect RNF41/NRDP1 from proteosomal degradation, RNF41/NRDP1 which regulates proteosomal degradation of PRKN. Plays a key role in beta cells functions by regulating mitophagy/autophagy and mitochondrial health. Interacts with RNF41/NRDP1. Q8BH75 Rnf41 false 3 Endosome membrane Peripheral membrane protein Lysosome membrane Peripheral membrane protein Associates with the endolysosome membrane. Q80U30-1 1 Q80U30-2 2 Q80U30-3 3 Q80U30-4 4 Q80U30-5 5 Ubiquitously expressed. Expressed in pancreatic islets. Mice with pancreatic specific deletion of Clec16a are significantly hyperglycemic and have reduced basal and blunted insulin release after glucose administration. Mutant mice have normal islet architecture and beta cell mass, but beta cells show accumulation of vacuolated structures and unhealthy mitochondria (rounded mitochondria with disordered and amorphous structure). Not associated with immune infiltration and insulitis. Belongs to the CLEC16A/gop-1 family. Translation N-terminally shortened. Alternative splicing Autophagy Complete proteome Endosome Lysosome Membrane Reference proteome K KGTEGGSKSMKTSGERE FAVAQCINQHSSPSLSSPSPPFASGSPGGSGS KPHLLLGTQAAFLLSPLEAFLSESRLLAALAS AV HV DAPTTPEQPQPHLDQSVIGNEMDVN VRSGRKGRRRVFSLSEADSHGGHWV E G MFGRSRSWVGGGHSKSSRNIHSLDHLKYLYHVLTKNTTVTEQNRNLLVETIRSITEILIW GDQNDSSVFDFFLEKNMFVFFLNILRQKSGRYVCVQLLQTLNILFENISHETSLYYLLSN NYVNSIIVHKFDFSDEEIMAYYISFLKTLSLKLNNHTVHFFYNEHTNDFALYTEAIKFFN HPESMVRIAVRTITLNVYKVSLDNQAMLHYIRDKTAVPYFSNLVWFIGSHVIELDNCVQT DEEHRNRGKLSDLVAEHLDHLHYLNDILIINCEFLNDVLTDHLLNRLFLPLYVYSLENPD KGGERPKISLPVSLYLLSQVFLIIHHAPLVNSLAEVILNGDLSETYTKPAQDVPRSSAKP SIRCFIKPTETLERSLEMNKHKGKKRMQKRPNYKNVGEEEDEERGSAEDAQEDAEKTKEI EMVIMKLGKLSEVAAAGTSVQEQNTTDEEKSAATNSENAQWSRPFLDMVYHALDSPDDDY HALFVLCLLYAMSHNKGMDPEKLKRIQLPVPSEAEKTTYNHLLAERLIRIMNNAAQPDGR IRLATLELSCLLLKQQVLTSSGCVIKDVHLACLEGAREESVHLVRHFYKGEEIFLDMFED EYRSMTIKPMNVEYLMMDASILLPPTGTPLTGIDFVKRLPCGDVEKTRRAIRVFFMLRSL SLQLRGEPETQLPLTREEDLIKTDDVLDLNNSDLIACTVITKDGGMVQRFLAVDIYQMSL VEPDVSRLGWGVVKFAGLLQDMQVTGVEDDSRALNITIHKPASSPHSKPFPILQATFVFS DHIRCIIAKQRLAKGRIQARRMKMQRIAALLDLPIQPTTEVLGFGLCSSSSSSQHLPFRF YEQCRRGSSDPTVQRSVFASVDKVPGFAVAQCINQHSSPSLSSPSPPFASGSPGGSGSTS HCDSGGSSSAPSATQSPADAPTTPEQPQPHLDQSVIGNEMDVNSKPSKNSSARSSEGETM HLSPSLLPAQQPTISLLYEDTADTLSVESLTIVPPVDPHSLRALSGISQLPTLPAADTET PAEGAVNPEPAEPTEH Q9D6Y4 BORC8_MOUSE BLOC-1-related complex subunit 8 Borcs8 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Tongue IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor. Component of the BLOC-one-related complex (BORC) which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN. Lysosome membrane Belongs to the BORCS8 family. Complete proteome Lysosome Membrane Phosphoprotein Reference proteome MEEPEMQLKGKKVTDKFTESVYVLANEPSVALYRLQEHVRRSLPELAQHKADMQRWEEQS QGAIYTVEYACSAVKSLVDSSVYFRSVEGLLKQAISIRDHMNTSAQGHSQEKLSPPPSLA Q64462 CP4B1_MOUSE Cytochrome P450 4B1 1.14.14.1 CYPIVB1 Cyp4b1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] PARTIAL PROTEIN SEQUENCE BALB/cJ Kidney NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Heart Kidney Lung Responsible for mutagenic activation of 3-methoxy-4-aminoazobenzene (3-MeO-AAB); a potent procarcinogen. Also active on 2-aminofluorene and 2-aminoanthracene. an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] heme Endoplasmic reticulum membrane Peripheral membrane protein Microsome membrane Peripheral membrane protein Present abundantly in renal microsomes of male mice but not in those of female mice. Also present in pulmonary microsomes of male and female mice. Not found in liver. P450 can be induced to high levels in liver and other tissues by various foreign compounds, including drugs, pesticides, and carcinogens. Belongs to the cytochrome P450 family. Complete proteome Direct protein sequencing Endoplasmic reticulum Heme Iron Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome MALSFLSPSLSRLGLWASVVILMVTVLKLLSLLFRRQKLARALDSFPGPPKHWLFGHALE IQKTGGLDKVVTWTEQFPYAHPLWLGQFIVFLNIYEPDYAKAVYSRGDPKAAYVYDFFLQ WIGKGLLVLEGPKWFQHRKLLTPGFHYDVLKPYVAIFAESTRVMLDKWEKKASENKSFDI FCDVGHMALDTLMKCTFGKGDSGLSHSDNSYYLAVSDLTLLMQQRIDSFQYHNDFIYWLT PHGRRFLRACQIAHDHTDHVIRQRKAALQDEKEQKKLQERRHLDFLDILLGARDESGIKL SDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPMHQQRCREEVREILGDRDSFQWDDL AQMTYLTMCMKECFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISLHIYALHRNSAVWP DPEVFDPLRFSPENMTGRHPFAFMPFSAGPRNCIGQQFAMNEMKVVTALCLLRFEFSPDP SKIPIKVPQLILRSKNGIHLYLKPLGPGSGK Q91W53 Q8BN18 Q9JJE0 GOGA7_MOUSE Golgin subfamily A member 7 Golga7 MNCb-1213 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J NOD Bone marrow Embryo Head Inner ear Spleen NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J FVB/N Brain Colon Limb Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Liver Lung Testis May be involved in protein transport from Golgi to cell surface. The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for HRAS and NRAS (By similarity). Interacts with GOLGA3. Interacts with ZDHHC9 (By similarity). Golgi apparatus membrane Lipid-anchor Q91W53-1 1 Q91W53-2 2 No experimental confirmation available. Palmitoylated on Cys-69 and Cys-72; which is required for Golgi localization and interaction with GOLGA3. Belongs to the ERF4 family. Alternative splicing Complete proteome Golgi apparatus Lipoprotein Membrane Palmitate Reference proteome LKKVSKYIQEQNEKIYAPQGLLLTDPIERGLRVIEITIYEDRGVSSGR WLHLCSVKSLNTMKEDKSLHINSSFKLEKPLYNSDFVIALTVQSTQKWVLSVCEIGQHVQVCLG MRPQQAPVSGKVFIQRDYSSGTRCQFQTKFPAELENRIDRQQFEETVRTLNNLYAEAEKL GGQSYLEGCLACLTAYTIFLCMETHYEKVLKKVSKYIQEQNEKIYAPQGLLLTDPIERGL RVIEITIYEDRGVSSGR Q9DBC3 Q3U3G5 Q3U7Y9 Q6A0D5 Q8C7V0 CMTR1_MOUSE Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 2.1.1.57 Cap methyltransferase 1 Cap1 2'O-ribose methyltransferase 1 MTr1 FtsJ methyltransferase domain-containing protein 2 Cmtr1 Ftsjd2 Kiaa0082 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Brain cortex Dendritic cell Embryonic stem cell Liver Macrophage Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Mammary tumor NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-837 Embryonic tail PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-30 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-30 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1). Displays a preference for cap0 transcripts. Cap1 modification is linked to higher levels of translation. May be involved in the interferon response pathway. a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide) in mRNA + S-adenosyl-L-methionine = a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide) in mRNA + H(+) + S-adenosyl-L-homocysteine Interacts with POLR2A (via C-terminus). Nucleus Acetylation Complete proteome Methyltransferase mRNA capping mRNA processing Nucleus Phosphoprotein Reference proteome S-adenosyl-L-methionine Transferase C W L F L I E V V I MKRRTDPECTAPLKKQKRIGELARHLSSTSDDEPLSSVNHAAKASATSLSGSDSETEGKQ PCSDDFKDAFKADSLVEGTSSRYSMYNSVSQRLMAKMGFREGEGLGKYSQGRKDIVETSN QKGRRGLGLTLQGFDQELNVDWRDEPEPNACEQVSWFPECTTEIPDSREMSDWMVVGKRK MVIEDETEFCGEELLHSMLKCKSVFDILDGEEMRRARTRANPYEMIRGVFFLNRAAMKMA NMDFVFDRMFTNPLDSSGKPLLKESDIDLLYFADVCAGPGGFSEYVLWRKKWHAKGFGMT LKGPNDFKLEDFYSASSELFEPYYGEGGVDGDGDITRPENINAFRNFVLDNTDRKGVHFV MADGGFSVEGQENLQEILSKQLLLCQFLMALSVVRTGGHFVCKTFDLFTPFSVGLIYLLY CCFERVCLFKPITSRPANSERYVVCKGLKVGIDDVREYLFSVNIKLNQLRNTESDVNLVV PLMVIKGDHEFNDYMIRSNESYCSLQIKALAKIHAFVQDTTLSEPRQAEIRKECLQLWKI PDQARVAPSSSDPKFKFFELIKDTDINIFSYKPTLLTAKTLEKIRPVLEYRCMVSGSEQK FLLGLGKSQIYTWDGRQSDRWVKLDLKTELPRDTLLCVEIVHELKGEGKAQRKISAIHIL DVLVLNGSDVREQHFNQRIQLAEKFVKAVSKPSRPDMNPIRVKEVYRLEEMEKIFVRLEM KLIKGSGGTPKLSYTGRDDRHFVPTGVYIVRTVNEPWTMGFSKSNNRKFFYNKKTQKSVY ALPTESIAPFHTCYYSRLFWEWGDGFHMRDSQKPQDPDKLSKEDVLSFIQSHNPLGP Q80ZF8 G3XA05 AGRB3_MOUSE Adhesion G protein-coupled receptor B3 Brain-specific angiogenesis inhibitor 3 Adgrb3 Bai3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] ICR Brain NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] TISSUE SPECIFICITY DEVELOPMENTAL STAGE IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220 AND SER-1411 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain INTERACTION WITH ELMO1 FUNCTION Receptor that plays a role in the regulation of synaptogenesis and dendritic spine formation at least partly via interaction with ELMO1 and RAC1 activity (PubMed:23628982). Promotes myoblast fusion through ELMO/DOCK1 (By similarity). Forms a heterodimer, consisting of a large extracellular region non-covalently linked to a seven-transmembrane moiety. Interacts (via its TSRs) with C1QL1, C1QL2, C1QL3 and C1QL4. Interacts via (C-terminus) with ELMO1 (PubMed:23628982), ELMO2 and ELMO3. Cell membrane Multi-pass membrane protein Brain-specific expression. Limited to the central nervous system (CNS) at all developmental stages. Peaks 1 day after birth. The endogenous protein is proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily. Cell membrane Complete proteome Disulfide bond G-protein coupled receptor Glycoprotein Membrane Phosphoprotein Receptor Reference proteome Repeat Signal Transducer Transmembrane Transmembrane helix L V H Y V I MKAVRNLLIYIFSTYLLVMFGFNAAQDFWCSTLVKGVIYGSYSVSEMFPKNFTNCTWTLE NPDPTKYSIYLKFSKKDLSCSNFSLLAYQFDHFSHEKIKDLLRKNHSIMQLCSSKNAFVF LQYDKNFIQIRRVFPTDFPGLQKKVEEDQKSFFEFLVLNKVSPSQFGCHVLCTWLESCLK SENGRTESCGIMYTKCTCPQHLGEWGIDDQSLVLLNNVVLPLNEQTEGCLTQELQTTQVC NLTREAKRPPKEEFGMMGDHTIKSQRPRSVHEKRVPQEQADAAKFMAQTGESGVEEWSQW SACSVTCGQGSQVRTRTCVSPYGTHCSGPLRESRVCNNTALCPVHGVWEEWSPWSLCSFT CGRGQRTRTRSCTPPQYGGRPCEGPETHHKPCNIALCPVDGQWQEWSSWSHCSVTCSNGT QQRSRQCTAAAHGGSECRGPWAESRECYNPECTANGQWNQWGHWSGCSKSCDGGWERRMR TCQGAAVTGQQCEGTGEEVRRCSEQRCPAPYEICPEDYLISMVWKRTPAGDLAFNQCPLN ATGTTSRRCSLSLHGVASWEQPSFARCISNEYRHLQHSIKEHLAKGQRMLAGDGMSQVTK TLLDLTQRKNFYAGDLLVSVEILRNVTDTFKRASYIPASDGVQNFFQIVSNLLDEENKEK WEDAQQIYPGSIELMQVIEDFIHIVGMGMMDFQNSYLMTGNVVASIQKLPAASVLTDINF PMKGRKGMVDWARNSEDRVVIPKSIFTPVSSKELDESSVFVLGAVLYKNLDLILPTLRNY TVVNSKVIVVTIRPEPKTTDSFLEIELAHLANGTLNPYCVLWDDSKSNESLGTWSTQGCK TVLTDASHTKCLCDRLSTFAILAQQPREIVMESSGTPSVTLIVGSGLSCLALITLAVVYA ALWRYIRSERSIILINFCLSIISSNILILVGQTQTHNKSICTTTTAFLHFFFLASFCWVL TEAWQSYMAVTGKIRTRLIRKRFLCLGWGLPALVVATSVGFTRTKGYGTDHYCWLSLEGG LLYAFVGPAAAVVLVNMVIGILVFNKLVSRDGILDKKLKHRAGQMSEPHSGLTLKCAKCG VVSTTALSATTASNAMASLWSSCVVLPLLALTWMSAVLAMTDKRSILFQILFAVFDSLQG FVIVMVHCILRREVQDAFRCRLRNCQDPINADSSSSFPNGHAQIMTDFEKDVDIACRSVL HKDIGPCRAATITGTLSRISLNDDEEEKGTNPEGLSYSTLPGNVISKVIIQQPTGLHMPM SMNELSNPCLKKENTELRRTVYLCTDDNLRGADMDIVHPQERMMESDYIVMPRSSVSTQP SMKEESKMNIGMETLPHERLLHYKVNPEFNMNPPVMDQFNMNLDQHLAPQEHMQNLPFEP RTAVKNFMASELDDNVGLSRSETGSTISMSSLERRKSRYSDLDFEKVMHTRKRHMELFQE LNQKFQTLDRFRDIPNTSSMENPAPNKNPWDTFKPPSEYQHYTTINVLDTEAKDTLELRP AEWEKCLNLPLDVQEGDFQTEV P22518 A6H6K2 Q3UXB6 CLK1_MOUSE Dual specificity protein kinase CLK1 2.7.12.1 CDC-like kinase 1 Protein kinase STY Clk1 Clk Sty Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG) MUTAGENESIS OF LYS-190 NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT) NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG) C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT) Brain CHARACTERIZATION FUNCTION PHOSPHORYLATION SUBCELLULAR LOCATION FUNCTION ACTIVITY REGULATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Liver Lung Pancreas Spleen Testis ACTIVITY REGULATION Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Regulates splicing of its own pre-mRNA according to its kinase activity; increased expression of the catalytically active form influences splicing to generate the catalytically inactive splicing variant lacking the kinase domain. Leucettine L41 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins. Interacts with PPIG and UBL5. Q5ZRQ0 lubX true 3 Nucleus P22518-1 Long P22518-2 Short Clk1T Lacks the kinase domain. Autophosphorylates on all three types of residues. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. Alternative splicing ATP-binding Complete proteome Kinase Nucleotide-binding Nucleus Phosphoprotein Reference proteome Serine/threonine-protein kinase Transferase Tyrosine-protein kinase KSHRRK MKLLIL K R P S L F I V M I MRHSKRTYCPDWDERDWDYGTWRSSSSHKRKKRSHSSAREQKRCRYDHSKTTDSYYLESR SINEKAYHSRRYVDEYRNDYMGYEPGHPYGEPGSRYQMHSSKSSGRSGRSSYKSKHRSRH HTSQHHSHGKSHRRKRSRSVEDDEEGHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDH KVGGRRVAVKIVKNVDRYCEAAQSEIQVLEHLNTTDPHSTFRCVQMLEWFEHRGHICIVF ELLGLSTYDFIKENSFLPFRMDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVKSDY TEAYNPKMKRDERTIVNPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCD VWSIGCILIEYYLGFTVFPTHDSREHLAMMERILGPLPKHMIQKTRKRRYFHHDRLDWDE HSSAGRYVSRRCKPLKEFMLSQDAEHELLFDLIGKMLEYDPAKRITLKEALKHPFFYPLK KHT O35492 Q3TJU0 Q3UIF5 Q3V463 Q5U4I1 Q8C1V1 CLK3_MOUSE Dual specificity protein kinase CLK3 2.7.12.1 CDC-like kinase 3 Clk3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Brain Kidney Placenta Thymus Tongue NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-638 Olfactory epithelium NUCLEOTIDE SEQUENCE [MRNA] OF 141-638 FUNCTION PHOSPHORYLATION SUBCELLULAR LOCATION TISSUE SPECIFICITY CATALYTIC ACTIVITY SUBCELLULAR LOCATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-224 AND SER-226 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Kidney Liver Lung Pancreas Spleen Testis ACTIVITY REGULATION Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Leucettine L41 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins. Nucleus Cytoplasm Cytoplasmic vesicle Secretory vesicle Acrosome Present at high levels in testis and ovary. In testis, expression is restricted to elongated, maturing spermatozoa. Also present in spleen, brain, lung and liver (at protein level). Autophosphorylates on all three types of residues. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. ATP-binding Complete proteome Cytoplasm Cytoplasmic vesicle Kinase Nucleotide-binding Nucleus Phosphoprotein Reference proteome Serine/threonine-protein kinase Transferase Tyrosine-protein kinase P T S T T L T A MPVLSARRKRLASTAGPRRGSGPSLAVRWVPPLGPEPSSDRGRAPMRPRGPTCSTTRRGA GRGPRLLPGPPGRDLHRCRPDPGGAGQSPRVCEFGARAVRPLGRVEPGPPTAASREGAVL PRAEARAGSGRGARSGEWGLAAAGAWETMHHCKRYRSPEPDPYLSYRWKRRRSYSREHEG RLRYPSRREPPPRRSRSRSHDRIPYQRRYREHRDSDTYRCEERSPSFGEDCYGSSRSRHR RRSRERAPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWL QERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKD KENKFLCVLMSDWFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHVRHMAYQLCHALR FLHENQLTHTDLKPENILFVNSEFETLYNEHKSCEEKSVKNTSIRVADFGSATFDHEHHT TIVATRHYRPPEVILELGWAQPCDVWSIGCILFEYYRGFTLFQTHENREHLVMMEKILGP IPSHMIHRTRKQKYFYKGGLVWDENSSDGRYVKENCKPLKSYMLQDSLEHVQLFDLMRRM LEFDPAQRITLAEALLHPFFAGLTPEERSFHSSRNPSR Q99LL3 Q3TCX9 Q9JJS3 CHSTC_MOUSE Carbohydrate sulfotransferase 12 2.8.2.5 Chondroitin 4-O-sulfotransferase 2 Chondroitin 4-sulfotransferase 2 C4ST-2 C4ST2 Chst12 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Heart NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Czech II Mammary tumor Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor (By similarity). n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate = n adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate + n H(+) Golgi apparatus membrane Single-pass type II membrane protein Belongs to the sulfotransferase 2 family. Carbohydrate metabolism Complete proteome Glycoprotein Golgi apparatus Membrane Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix V A MTKPRLFRLWLVLGSALMILLIIVYWDNVGTAHFYLHTSLSRPHILEPLPTQGLVEENVF TSDVDEFLDTLLSSDAKHNDLSRRKTEQPPVPAPSKPVLSHMEENVRGYDWSTHDAHQNP DRDRQQAERRSLLRDFCANASLAFPTKDRSFDDIPNYELNHLIVDDRHGVIYCYVPKVAC TNWKRVMIVLSESLLDRGSPYRDPLDIPREHVHNTSTHLTFNKFWRRYGKFSRHLMKVKL KKYTKFLFVRDPFVRLISAFRSKFELENEEFYRKFAVPMLRLYANHTSLPASVSEAFSAG LKVSFANFIQYLLDPHTEKLAPFNEHWRQVYRLCHPCQIDYDFVGKLETLDEDAAQLLRF LKVDSQLHFPPSYRNRTASSWEEDWFANIPLAWRQQLYKLYEADFVLFGYPKPENLLRD O88573 AFF1_MOUSE AF4/FMR2 family member 1 Proto-oncogene AF4 Protein AF-4 Aff1 Mllt2 Mllt2h Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-191; SER-197; SER-755 AND SER-760 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Kidney Liver Lung Pancreas Spleen Testis Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Nucleus Belongs to the AF4 family. Acetylation Complete proteome Nucleus Phosphoprotein Proto-oncogene Reference proteome P L G R K R R KT MAAHSSLYNEDRNLLRIREKERRNQEAHQEKEAFPEKAPLFPEPYKTAKGDELSSRIQTM LGDYEEMKEFLSSKSHPHRLDGSEDRPGKPRYPLGHDRGNGAASSSLRTHVYHQPIHTSA PGSRPVGNISHSPKMAQPRMEPSLHTKIYDGPRLTQDHLSQGHCSRKCDRRAEGDSAPER KLSPLISSLPSPVPPLSPVHSRLQGTSKAHSSGVSSKSCCVAKSSKDLVAKAQDKETPHD GLVAVTSLGSAPPQPPCQTFPPPPLPSKSAAMQQKPTAYVRPMDGQDQAPSESPELKLPL EDYGQQSFEKPDLKVPAKAKLTRLRMPSQSVEQPYSNEVHCVEEILKEMTHSWPPPLTAI HTPSTAEPSRFPFPTKDPLHVSPATQSQKQYDTPSKTHPNPQQGTSMLEDDLQLSDSEDS DTEQATEKPPSPPAPPSAPQTLPEPVASAHSSSGESESSESDSSSDSESESSSSDSEEEE ENEPLETRAPEPEPPTTNKWQLDNWLTKVNQPSVPLDGRGSTESPQWRQESKGVAEGSSD QQHPDSKDPLPKSSSKTLRGPSEGPSLGRGAVRNPPLNRNPHLGKPWAANNPGNPPRLRP GRAQASSQAESEVGPLPYGSKEQTSKDRPKVKTKGRPRAVGSREPKPEVPAPTPQAAVPR PKPPVPTPSEKRKHKSSTAPSKAPSAPQPPKDSAGDRNPEHSALVSLTQSQGPSHSSRGS SGSVRTSGCRQAVIAQGDGCKDKLLLPLRDTKLLSPLRDSPPPTSLVVKITLDLLTRIPQ PLGKGSRPRKAEDKQLSAGKKQDSETKSCDSSSRVTKKRKVTQKKSTVTRDTNWISRRAS SSSSHTESSRTKAPRSSSENSRKEMLPPASASSVSSSSSSQKPSRPAQKRPRPDEDTCSQ EPPRSASSTKSSSTDPPAPKHRKVQARGSEHKGSSGDAANAANPFPVPSLPNGNAKPGKP QVKSDRQQADFHMKEAKKLKCKAETMVDKAGKAFKYLEAVLSFIECGMASESESSAKSAY AVYSETIDLIRYVMSLKCFSDNTMPAQEKIFAVLCLRCQSLLNMAMFRCKKDTVMKYSRT LSEHFKSTSKVAQAPSPCTARSTGVPSPLSPMPSPASSVGSQSSAGSSMGSVGVTATVST PVSIQNMTSSYVTITSHVLTAFSLWEQAEALTRKNKEFFAQLSTKVRVLALNSSLVDLVH YTRQGLQRLKQSPKGP Q8C138 D3Z6U0 Q3UXS3 Q8K180 ADTRP_MOUSE Androgen-dependent TFPI-regulating protein Fatty acid esters of hydroxy fatty acids hydrolase ADTRP FAHFA hydrolase ADTRP 3.1.-.- Adtrp Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Skin Wolffian duct NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Liver Hydrolyzes bioactive fatty-acid esters of hydroxy-fatty acids (FAHFAs), but not other major classes of lipids (By similarity). Show a preference for FAHFAs with branching distal from the carboxylate head group of the lipids (By similarity). Regulates the expression and the cell-associated anticoagulant activity of the inhibitor TFPI in endothelial cells (in vitro) (By similarity). 9-hexadecanoyloxy-octadecanoate + H2O = 9-hydroxy-octadecanoate + H(+) + hexadecanoate 12-hexadecanoyloxy-octadecanoate + H2O = 12-hydroxyoctadecanoate + H(+) + hexadecanoate 9-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 9-hydroxy-octadecanoate + H(+) 12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 12-hydroxyoctadecanoate + H(+) 13-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-hexadecenoate + 13-hydroxy-octadecanoate + H(+) 9-octadecanoyloxy-octadecanoate + H2O = 9-hydroxy-octadecanoate + H(+) + octadecanoate 12-octadecanoyloxy-octadecanoate + H2O = 12-hydroxyoctadecanoate + H(+) + octadecanoate 13-octadecanoyloxy-octadecanoate + H2O = 13-hydroxy-octadecanoate + H(+) + octadecanoate 9-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 9-hydroxy-octadecanoate + H(+) 12-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 12-hydroxyoctadecanoate + H(+) 13-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 13-hydroxy-octadecanoate + H(+) 5-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-octadecenoate + 5-hydroxy-octadecanoate + H(+) Cell membrane Multi-pass membrane protein Colocalized with TFPI and CAV1 in lipid rafts. Belongs to the AIG1 family. Translation N-terminally shortened. Cell membrane Complete proteome Hydrolase Lipid metabolism Membrane Reference proteome Transmembrane Transmembrane helix MTKTTTCVYHFLVLNWYIFLNYHIPQIGRNEEKLREFHDGGRSKYLTLLNLLLQAIFFGV ACLDDVLKRVIGRKDIKFVTSFRDLLFTTMAFPISTFVFLVFWTLFHYDRSLVYPKGLDD FFPAWVNHAMHTSIFPFSLFETILRPHNYPSKKLGLTLLGAFNFAYIIRILWRYVQTGNW VYPVFDSLSPLGIIIFFSAAYILVAGIYLFGEKINHWKWGAIAKPQMKKN Q9Z1T6 E9QL40 Q3TNE4 Q3UTT6 Q69ZU1 Q9CU94 FYV1_MOUSE 1-phosphatidylinositol 3-phosphate 5-kinase Phosphatidylinositol 3-phosphate 5-kinase 2.7.1.150 FYVE finger-containing phosphoinositide kinase PIKfyve Phosphatidylinositol 3-phosphate 5-kinase type III PIPkin-III Type III PIP kinase p235 Pikfyve Kiaa0981 Pip5k3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2) CHARACTERIZATION Adipose tissue NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Pancreatic islet NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) C57BL/6J Cerebellum Ovary Spleen Uterus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J CATALYTIC ACTIVITY IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver TISSUE SPECIFICITY IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX FUNCTION SUBCELLULAR LOCATION PHOSPHORYLATION AT SER-318 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-312; SER-475 AND SER-1753 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Liver Lung Pancreas Spleen Testis The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. The product of the reaction it catalyzes functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole. a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 3-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + ADP + H(+) Component of the PI(3,5)P2 regulatory complex/PAS complex, at least composed of PIKFYVE, FIG4 and VAC14. VAC14 nucleates the assembly of the complex and serves as a scaffold. Cytoplasmic vesicle membrane Peripheral membrane protein Endosome membrane Associated with vesicle structures. Displays a peripheral vesicular punctate pattern. Mainly associated with membranes of the late endocytic pathway (By similarity). Q9Z1T6-2 1 p235S Q9Z1T6-1 2 p235L Q9Z1T6-3 3 Ubiquitous. Phosphorylated in response to insulin at Ser-318 in a protein kinase B (PKB)-dependent manner. Translation N-terminally extended. Translation N-terminally shortened. Acetylation Alternative splicing ATP-binding Complete proteome Cytoplasmic vesicle Endosome Kinase Membrane Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Transferase Zinc Zinc-finger L LENTLPHPQEST NSASPSKR SKFGFLML E K K Q QP HR R T L V S Y V E MATDDKSSPTLDSANDLPRSPASPSHLTHFKPLTPDQDEPPFKSAYSSFVNLFRFNKERG EGGQGEQQSPSSSWASPQIPSRTQSVRSPVPYKKQLNEELHRRSSVLDSRRKAEPACGGH DPRTAVQLRSLSTVLKRLKEIMEGKSQDSDLKQYWMPDSQCKECYDCSEKFTTFRRRHHC RLCGQIFCSRCCNQEIPGKFMGYTGDLRACTYCRKIALSYAHSTDSNSIGEDLNALSDST CSVSILDPSEPRTPVGSRKASRNIFLEDDLAWQSLIHPDSSNSALSTRLVSVQEDAGKSP ARNRSASITNLSLDRSGSPMVPSYETSVSPQANRNYIRTETTEDERKILLDSAQLKDLWK KICHHTSGMEFQDHRYWLRTHPNCIVGKELVNWLIRNGHIATRAQAIAIGQAMVDGRWLD CVSHHDQLFRDEYALYRPLQSTEFSETPSPDSDSVNSVEGHSEPSWFKDIKFDDSDTEQI AEEGDDNLANSASPSKRTSVSSFQSTVDSDSAASISLNVELDNVNFHIKKPSKYPHVPPH PADQKEYLVSDTGGQQLSISDAFIKESLFNRRVEEKSKELPFTPLGWHHNNLELLREENE EKQAMERLLSANHNHMMALLQQLLQNESLSSSWRDIIVSLVCQVVQTVRPDVKHQDDDMD IRQFVHIKKIPGGKKFDSVVVNGFVCTKNIAHKKMNSCIKNPKILLLKCSIEYLYREETK FTCIDPIVLQEREFLKNYVQRIVDVRPTLVLVEKTVSRIAQDMLLEHGITLVINVKSQVL ERISRMTQGDLVVSMDQLLTKPHLGTCHKFYMQIFQLPNEQTKTLMFFEGCPQHLGCTIK LRGGSDYELARVKEILIFMICVAYHSQLEISFLMDEFAMPPTLMQSPSFHLLTEGRGEEG ASQEQVSGSSLPQDPECPREALSSEDSTLLESRTVLEKGELDNKSIPQAVASLKHQDYTT PTCPAGIPCALFALVPESLLPLHMDQQDAVGNEQPETSQQTDEQQDPKSQMKAFRDPLQD DTGMYVTEEVTSSEDQRKTYALTFKQELKDVILCISPVITFREPFLLTEKGMRCSTRDYF PEQIYWSPLLNKEVKEMESRRKKQLLRDLSGLQGMNGSVQAKSIQVLPSHELVSTRIAEH LGDSQTLGRMLADYRARGGRIQSKHLDPFVHSKDASCTSGGKSGNKTESDEERGLIPSDV IWPTKVDCLNPANHQRLCVLFSSSSAQSSNAPSACVSPWIVTMEFYGKNDLTLGIFLERY CFRSSYQCPSMFCDTPMVHHIRRFVHGQGCVQIILKELDSPVPGYQHTILTYSWCRICKQ VTPVVALSNESWSMSFAKYLELRFYGHQYTRRANAEPCGHSIHHDYHQYFSYNQMVASFS YSPIRLLEVCVPLPKIFIKRQAPLKVSLLQDLKDFFQKVSQVYLAVDERLASLKTDTFSK TREEKMEDIFAQKEMEEGEFKNWTEKMQARLMSSSVDTPQQLQSIFESLIAKKQSLCEVL QAWNSRLQDLFQQEKGRKRPSVPPSPGRLRQGEESKINAMDTSPRNISPGLHNGEKEDRF LTTLSSQSSTSSTHLQLPTPPEALAEQVVGGPTDLDSASGSEDVFDGHLLGSTDSQVKEK STMKAIFANLLPGNSYNPIPFPFDPDKHYLMYEHERVPIAVCEKEPSSIIAFALSCKEYR NALEELSKATLRNSAEEGLPANSALDNRPKSSSPIRLPEISGGQTNRTVEAEPQPTKKAS GMLSFFRGTAGKSPDLSSQKRETLRGADSAYYQVGQAGKEGLESQGLEPQDEVDGGDTQK KQLTNPHVELQFSDANAKFYCRLYYAGEFHKMREVILGSSEEEFIRSLSHSSPWQARGGK SGAAFYATEDDRFILKQMPRLEVQSFLDFAPHYFNYITNAVQQKRPTALAKILGVYRIGY KNSQNNTEKKLDLLVMENLFYGRKMAQVFDLKGSLRNRNVKTDTGKESCDVVLLDENLLK MVRDNPLYIRSHSKSVLRTSIHSDAHFLSSHLIIDYSLLVGRDDTSNELVVGIIDYIRTF TWDKKLEMVVKSTGILGGQGKMPTVVSPELYRTRFCEAMDKYFLMVPDHWTGLDLNC Q8BQN5 A2RSM0 Q8CC61 FA78B_MOUSE Protein FAM78B Fam78b Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Corpus striatum Epididymis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Belongs to the FAM78 family. Complete proteome Reference proteome MGCIQSITCKARIRRENIVVYDVCATIDQCPTRIEETSPIVLRYKTPYFKASARVVMPPI PRHETWVVGWIQACNQMEFFNTYSDLGMSSWELPDLREGRVKAISDSDGVSYPWYGNTTE TVTLVGPTNKISRFSVSMNDNFYPSVTWAVPVSDSNVPLLTRIKRDQSFTTWLVAMNTTT KEKIILQTIKWRMRVDIEVDPLQLLGQRARLVGRTQQEQPRILSRMEPIPPNALVKPNAN DAQVLMWRPKRGPPLVVIPPK Q9QUH0 GLRX1_MOUSE Glutaredoxin-1 Thioltransferase-1 TTase-1 Glrx Glrx1 Grx Grx1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] MUTAGENESIS Spleen NUCLEOTIDE SEQUENCE [MRNA] Liver NUCLEOTIDE SEQUENCE [MRNA] CFW Lens NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Colon IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-9 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. Cytoplasm Belongs to the glutaredoxin family. Acetylation Complete proteome Cytoplasm Disulfide bond Electron transport Redox-active center Reference proteome Transport C S C S MAQEFVNCKIQSGKVVVFIKPTCPYCRKTQEILSQLPFKQGLLEFVDITATNNTSAIQDY LQQLTGARTVPRVFIGKDCIGGCSDLISMQQTGELMTRLKQIGALQL Q9JMF7 Q8BN02 Q8R0P7 Q9CRF2 DOPP1_MOUSE Dolichyldiphosphatase 1 3.6.1.43 Dolichyl pyrophosphate phosphatase 1 Protein 2-23 Dolpp1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain cortex Embryonic stem cell Kidney Oviduct NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Kidney FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides. Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl monophosphate at a much lower rate. Does not act on phosphatidate. dolichyl diphosphate + H2O = dolichyl phosphate + H(+) + phosphate Protein modification; protein glycosylation. Endoplasmic reticulum membrane Multi-pass membrane protein Widely expressed with highest levels in brain, kidney, lung and intestine. Belongs to the dolichyldiphosphatase family. Complete proteome Endoplasmic reticulum Hydrolase Membrane Reference proteome Transmembrane Transmembrane helix V A L S MAADGQCSLPASWRPVTLTHVEYPAGDLSGHLLAYLSLSPIFVVVGFLTLIIFKRELHTI SFLGGLALNQGVNWLIKHVIQEPRPCGGPHTAVGTKYGMPSSHSQFMWFFSVYSFLFLYL RMHQTNNARFLDLLWRHVLSLGLLTAAFLVSYSRVYLLYHTWSQVFYGGVAGSLMAVAWF IITQEILTPLFPRIAAWPISEFFLIRDTSLIPNVLWFEYTVTRAEARNRQRKLGTKLQ Q810D6 G3UVT6 Q922H3 GRWD1_MOUSE Glutamate-rich WD repeat-containing protein 1 Protein A301 Grwd1 A301 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] ICR Forebrain NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-446 FVB/N Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Pancreas Spleen Testis Histone binding-protein that regulates chromatin dynamics and minichromosome maintenance (MCM) loading at replication origins, possibly by promoting chromatin openness. Interacts with METTL18. Interacts with CDT1; origin binding of GRWD1 is dependent on CDT1. Interacts with CDC6; origin binding of GRWD1 is dependent on CDC6. Binds to histone H2A-H2B and H3-H4 complexes. Nucleus Nucleolus Nucleus Chromosome Present in the nucleus throughout interphase and is detached from chromatin at the onset of mitosis and rebinds at telophase when the pre-replication complexes (pre-RC) is formed (By similarity). Chromosome Complete proteome Nucleus Phosphoprotein Reference proteome Repeat WD repeat S P MAARKGRSRTCETGEPMEAETCDPGTEGPSQVYLPGRGPPLSEGEELVMDEEAYVLYHRA QTGAPCLSFDIVRDHLGDNRTELPLSLYLCAGTQAESAQSNRLMMLRMHNLHGTRPSPSE GSDDDEEDEDEEDEEEQKPQLELAMVPHYGGINRVRVSWLGEEPVAGVWSEKGQVEVFAL RRLLQVVDDPQALAIFLRDEQARIKPIFSFAGHMGEGFALDWSPRVPGRLLTGDCQKNVH LWTPTEGGSWNVDQRPFVGHTRSVEDLQWSPTEDTVFASCSADASIRIWDIRAAPGKACM LTTATAHDGDVNVISWSRREPFLLSGGDDGALKVWDLRQFKSGSPVATFKQHMAPVTSVE WHPQDSGVFAASGADNQITQWDLAVERDPESGETETDPGLAALPQQLLFVHQGETDLKEL HWHPQCPGVLISTALSGFTVFRTISV Q8BLD9 Q61439 Q80UB7 DRD5_MOUSE D(1B) dopamine receptor D(5) dopamine receptor Dopamine D5 receptor Drd5 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-252 NUCLEOTIDE SEQUENCE [MRNA] OF 138-298 Testis Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase. Cell membrane Multi-pass membrane protein Belongs to the G-protein coupled receptor 1 family. Cell membrane Complete proteome Disulfide bond G-protein coupled receptor Glycoprotein Lipoprotein Membrane Palmitate Receptor Reference proteome Transducer Transmembrane Transmembrane helix P L MLPPGRNGTAHRARLGLQRQLAQVDAPGGSAAPLGPAQVVTAGLLTLLIVWTLLGNVLVC AAIVRSRHLRAKMTNIFIVSLAVSDLFVALLVMPWKAVAEVAGYWPFGAFCDIWVAFDIM CSTASILNLCIISVDRYWAISRPFRYERKMTQRVALVMVALAWTLSILISFIPVQLNWHR DKAGSQGREGLLSNETPWEEGWELDGRTENCDSSLNRTYAISSSLISFYIPVAIMIVTYT RIYRIAQVQIRRISSLERAAEHAQSCRSRGACEPDPSLRASIKKETKVFKTLSVIMGVFV CCWLPFFILNCMVPFCSSGDAQGPRTGFPCVSETTFDIFVWFGWANSSLNPIIYAFNADF RKVFAQLLGCSHLCFRTPVQTVNISNELISYNQDTVFHREIAAAYVHMIPNAVSSGDREV GEEEEAEEEGPFDHMSQISPTTPDGDLAAESVWELDCEEEVSLGKISPLTPNCFHKTA Q8VIH7 Q499D9 CYYR1_MOUSE Cysteine and tyrosine-rich protein 1 Proline-rich domain-containing protein Cyyr1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ Brain NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Pancreas IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Lung Membrane Single-pass type I membrane protein Belongs to the CYYR1 family. Complete proteome Membrane Reference proteome Signal Transmembrane Transmembrane helix H R MDALRLPRRPGVLLPKLILLFVYAGDCLAQCGKECHSYCCDGSTPYCCSYYAYIGNILSG TAIAGIVFGIVFIMGVIAGIAICICMCMKNNRGTRVGVIRAAHINAISYPMAPPPYTYDH EMEYRTDLPPPYSAAPQASAQRSPPPPYPGNPRKYSSSQNRIRDN Q64317 DLX1_MOUSE Homeobox protein DLX-1 Dlx1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] 129 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-255 POSSIBLE FUNCTION TISSUE SPECIFICITY DEVELOPMENTAL STAGE Brain FUNCTION INTERACTION WITH POU4F2 DEVELOPMENTAL STAGE Plays a role as a transcriptional activator or repressor (PubMed:21875655). Inhibits several cytokine signaling pathways, such as TGFB1, activin-A/INHBA and BMP4 by interfering with the transcriptional stimulatory activity of transcription factors, such as MSX2, FAST2, SMAD2 and SMAD3 during hematopoietic cell differentiation (By similarity). Plays a role in terminal differentiation of interneurons, such as amacrine and bipolar cells in the developing retina (PubMed:21875655). Likely to play a regulatory role in the development of the ventral forebrain (PubMed:1676488). May play a role in craniofacial patterning and morphogenesis and may be involved in the early development of diencephalic subdivisions (PubMed:1676488). Interacts with SMAD4 (via homeobox DNA-binding domain) (By similarity). Interacts (via homeobox DNA-binding domain) with POU4F2; this interaction suppresses DLX1-mediated transcriptional activity in postnatal retina and enhances retinal ganglion cell (RGC) differentiation (PubMed:21875655). Nucleus Expressed in a restricted region of the developing brain, within the diencephalon and the adjacent telencephalic regions. Expressed in developing retinal progenitor cells at 12 dpc (PubMed:21875655). Has a segmental expression in the developing forebrain (PubMed:1676488). The homeobox DNA-binding domain is necessary for its nuclear localization, transcriptional and erythroid differentiation activities. Belongs to the distal-less homeobox family. Activator Complete proteome Developmental protein Differentiation DNA-binding Homeobox Nucleus Reference proteome Repressor Transcription Transcription regulation QSRLED PEPPGG G GQ MTMTTMPESLNSPVSGKAVFMEFGPPNQQMSPSPMSHGHYSMHCLHSAGHSQPDGAYSSA SSFSRPLGYPYVNSVSSHASSPYISSVQSYPGSASLAQSRLEDPGADSEKSTVVEGGEVR FNGKGKKIRKPRTIYSSLQLQALNRRFQQTQYLALPERAELAASLGLTQTQVKIWFQNKR SKFKKLMKQGGAALEGSALANGRALSAGSPPVPPGWNPNSSSGKGSGSSAGSYVPSYTSW YPSAHQEAMQQPQLM P61202 O88950 Q15647 Q3V1W6 Q8R5B0 Q9CWU1 Q9R249 Q9UNQ5 CSN2_MOUSE COP9 signalosome complex subunit 2 SGN2 Signalosome subunit 2 Alien homolog JAB1-containing signalosome subunit 2 Thyroid receptor-interacting protein 15 TR-interacting protein 15 TRIP-15 Cops2 Csn2 Trip15 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1) SUBCELLULAR LOCATION TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J Eye NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-443 (ISOFORM 1) Czech II Mammary tumor NUCLEOTIDE SEQUENCE [MRNA] OF 4-443 (ISOFORM 1) IDENTIFICATION IN THE CSN COMPLEX C57BL/6J FUNCTION INTERACTION WITH CUL1 AND CUL2 FUNCTION INTERACTION WITH NIF3L1 FUNCTION DISRUPTION PHENOTYPE IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Essential 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/ICSBP, 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. Involved in early stage of neuronal differentiation via its interaction with NIF3L1. Component of the CSN complex, composed of COPS1/GPS1, COPS2, COPS3, COPS4, COPS5, COPS6, COPS7 (COPS7A or COPS7B), COPS8 and COPS9 (PubMed:9707402). In the complex, it probably interacts directly with COPS1, COPS4, COPS5, COPS6 and COPS7 (COPS7A or COPS7B) (PubMed:9707402). Specifically interacts with the ligand binding domain of the thyroid receptor (TR). Does not require the presence of thyroid hormone for its interaction. Interacts with CUL1 and CUL2 (PubMed:11967155). Interacts with IRF8/ICSBP1 and with nuclear receptors NR2F1 and NR0B1 (By similarity). Interacts with NIF3L1 (PubMed:12522100). Cytoplasm Nucleus P61202-1 1 P61202-2 2 Widely expressed in embryonic, fetal and adult tissues, except cartilage and smooth muscle. Phosphorylated by CK2 and PKD kinases. Its absence causes arrest of embryo development at the peri-implantation stage. Blastocysts without Cops2 fail to outgrow in culture and exhibit a cell proliferation defect in inner cell mass, accompanied by a slight decrease in Oct4. In addition, lack of Cops2 disrupts the CSN complex and results in a drastic increase in cyclin E. It also induces elevated levels of p53 and p21, which may contribute to premature cell cycle arrest of the mutant. Belongs to the CSN2 family. Alternative splicing Complete proteome Cytoplasm Nucleus Phosphoprotein Reference proteome Signalosome Q QNSDFLCQ K Y S T R K MSDMEDDFMCDDEEDYDLEYSEDSNSEPNVDLENQYYNSKALKEDDPKAALSSFQKVLEL EGEKGEWGFKALKQMIKINFKLTNFPEMMNRYKQLLTYIRSAVTRNYSEKSINSILDYIS TSKQMDLLQEFYETTLEALKDAKNDRLWFKTNTKLGKLYLEREEYGKLQKILRQLHQSCQ TDDGEDDLKKGTQLLEIYALEIQMYTAQKNNKKLKALYEQSLHIKSAIPHPLIMGVIREC GGKMHLREGEFEKAHTDFFEAFKNYDESGSPRRTTCLKYLVLANMLMKSGINPFDSQEAK PYKNDPEILAMTNLVSAYQNNDITEFEKILKTNHSNIMDDPFIREHIEELLRNIRTQVLI KLIKPYTRIHIPFISKELNIDVADVESLLVQCILDNTIHGRIDQVNQLLELDHQKRGGAR YTALDKWTNQLNSLNQAVVSKLA Q8K0L0 Q9CTH4 Q9WV73 ASB2_MOUSE Ankyrin repeat and SOCS box protein 2 ASB-2 Asb2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2) TISSUE SPECIFICITY C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) FVB/N Colon NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-634 C57BL/6J Embryo IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Heart Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. Component of a probable ECS E3 ubiquitin-protein ligase complex which contains CUL5, either RBX1 or RNF7/RBX2, Elongin BC complex (ELOB and ELOC) and ASB2. Q8K0L0-1 1 Q8K0L0-2 2 Highest expression in muscle, heart and spleen. The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family. Translation N-terminally extended. Alternative splicing ANK repeat Complete proteome Reference proteome Repeat Ubl conjugation pathway AEASASSQTNHQPGHFHPWT MTRFSYAEYFALFHSGSAPS SS LF MATEISTRGRQRAIGHEEYSLYSSLSEEELLQMAIEQSLADKTRGPTPAEASASSQTNHQ PGHFHPWTRSPSSPENPPARAPLGLFQGVMQKYSSNLFKTSQMAAMDPVLKAIKEGDEEA LKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLAT CREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWT ALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQ ASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPVT SRTRVRRSGISPLHLAAERNHDAVLEALLAARFDVNAPLAPERARLYEDRRSSALYFAVV NNNVYATELLLLAGADPNRDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPA TIMFAMKCLSLLKFLMDLGCDGEPCFSCLYGNGPHPPAPRPGRFHDAPVDDKAPSVVQFC EFLSAPEVSRWAGPIIDVLLDYVGNVQLCSRLKEHIDSFEDWAVIKEKAEPPRPLAHLCR LRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ P15089 CBPA3_MOUSE Mast cell carboxypeptidase A MC-CPA 3.4.17.1 Carboxypeptidase A3 Cpa3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. Zn(2+) Binds 1 zinc ion per subunit. Cytoplasmic vesicle Secretory vesicle Secretory granules. Belongs to the peptidase M14 family. Carboxypeptidase Complete proteome Cytoplasmic vesicle Disulfide bond Hydrolase Metal-binding Metalloprotease Protease Reference proteome Signal Zinc Zymogen MRFFLLMAVIYTTLAIAPVHFDREKVFRVKLQNEKHASVLKNLTQSIELDFWYPDAIHDI AVNMTVDFRVSEKESQTIQSTLEQHKIHYEILIHDLQEEIEKQFDVKDEIAGRHSYAKYN DWDKIVSWTEKMLEKHPEMVSRIKIGSTVEDNPLYVLKIGKKDGERKAIFMDCGIHAREW ISPAFCQWFVYQATKSYGKNKIMTKLLDRMNFYVLPVFNVDGYIWSWTQDRMWRKNRSRN QNSTCIGTDLNRNFDVSWDSSPNTNKPCLNVYRGPAPESEKETKAVTNFIRSHLNSIKAY ITFHSYSQMLLIPYGYTFKLPPNHQDLLKVARIATDALSTRYETRYIYGPIASTIYKTSG SSLDWVYDLGIKHTFAFELRDKGKSGFLLPESRIKPTCKETMLSVKFIAKYILKNTS Q921C5 Q80TU1 Q8BTE3 Q9DCL3 BICD2_MOUSE Protein bicaudal D homolog 2 Bic-D 2 Bicd2 Kiaa0699 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) FUNCTION INTERACTION WITH DCTN2 SUBCELLULAR LOCATION DOMAIN NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Mammary tumor PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3) C57BL/6J Embryo Kidney FUNCTION INTERACTION WITH RAB6A SUBCELLULAR LOCATION INTERACTION WITH CPNE4 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Heart Kidney Lung Spleen Testis FUNCTION INTERACTION WITH RANBP2; RAB6A AND KIF5A FUNCTION INTERACTION WITH DYNLL1; DYNC1H1; DYNC1I2; DCTN1 AND DCTN2 TISSUE SPECIFICITY FUNCTION COMPLEX FORMATION WITH DYNEIN AND DYNACTIN FUNCTION FUNCTION INTERACTION WITH RAB6A SUBCELLULAR LOCATION ASSOCIATION WITH MICROTUBULES Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates and stabilizes the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (PubMed:11483508, PubMed:25035494, PubMed:24986880, PubMed:22956769). Facilitates the binding of RAB6A to the Golgi by stabilizing its GTP-bound form (PubMed:25962623). Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport via its interaction with RAB6A and recruitment of the dynein-dynactin motor complex (PubMed:12447383, PubMed:25962623). Contributes to nuclear and centrosomal positioning prior to mitotic entry through regulation of both dynein and kinesin-1. During G2 phase of the cell cycle, associates with RANBP2 at the nuclear pores and recruits dynein and dynactin to the nuclear envelope to ensure proper positioning of the nucleus relative to centrosomes prior to the onset of mitosis (PubMed:20386726). Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with NEK9 (By similarity). Interacts with DCTN2 (PubMed:11483508, PubMed:22956769). Interacts with RAB6A (PubMed:12447383, PubMed:25962623). Interacts with DNAI1 (By similarity). Interacts with DYNLL1, DYNC1H1, DYNC1I2 and DCTN1 (PubMed:22956769). Forms a complex with dynein and dynactin (PubMed:24986880). The dynein-dynactin-BICD2 ternary complex (DDB) binds preferentially to tyrosinated microtubules than to detyrosinated microtubules (PubMed:26968983). Interacts with RANBP2, RAB6A and KIF5A (PubMed:20386726). Interacts with KIF1C (By similarity). P35279 Rab6a false 3 P49792 RANBP2 true 4 Golgi apparatus Cytoplasm Cytoskeleton Cytoplasm Nucleus Nuclear pore complex Nucleus envelope In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends (PubMed:11483508). Localizes to the nuclear envelope and cytoplasmic stacks of nuclear pore complex known as annulate lamellae in a RANBP2-dependent manner during G2 phase of the cell cycle (By similarity). Q921C5-1 1 Q921C5-2 2 No experimental confirmation available. Q921C5-3 3 Ref.4 (BAB22282) sequence differs from that shown due to a frameshift in position 70. No experimental confirmation available. Ubiquitously expressed with high expression in the spinal cord. The fourth coiled coil region is involved in Golgi targeting and in the interaction with DCTN2. Phosphorylated by NEK9 in vitro. Belongs to the BicD family. Translation N-terminally shortened. Acetylation Alternative splicing Coiled coil Complete proteome Cytoplasm Cytoskeleton Golgi apparatus mRNA transport Nuclear pore complex Nucleus Phosphoprotein Protein transport Reference proteome Translocation Transport APPSPSLVSDL VHPLHALCLTV L VSHTCACASERAEGAGLANQVFCSEKHSIYCD MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQ FEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLE LQTELKQLRNVLTNTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQD YSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL EEALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDDTVTAEPNNDAEA LVNGFEHSGLVKSSLDNKTSTPRKDGLAPPSPSLVSDLLSELHISEIQKLKQQLVQMERE KVGLLATLQDTQKQLEQARGTLSEQHEKVNRLTENLSALRRLQAGKERQTSLDNEKDRDS HEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEG QALTEKISLLEKASHQDRELLAHLEKELKKVSDVAGETQGSLNVAQDELVTFSEELANLY HHVCMCNNETPNRVMLDYYREGQGKAGRTSPEGRGRRSPVLLPKGLLATEVGRADGGTGD NSPSPSSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRTTELSRQRIASQELGPA VDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTE TMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRM AIQQKLALTQRLELLELDHEQTRRGRSKAASKAKPASPSL Q9EQ32 Q2KHL6 Q3TBW6 Q3TC39 Q3U5J3 Q8BN25 Q8C2Y4 BCAP_MOUSE Phosphoinositide 3-kinase adapter protein 1 B-cell adapter for phosphoinositide 3-kinase B-cell phosphoinositide 3-kinase adapter protein 1 Pik3ap1 Bcap Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) TISSUE SPECIFICITY INTERACTION WITH PIK3R1 PHOSPHORYLATION AT TYR-264; TYR-420; TYR-445 AND TYR-460 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3) C57BL/6J NOD Bone marrow Ovary Spleen NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) FUNCTION TYROSINE PHOSPHORYLATION (ISOFORMS 1 AND 2) FUNCTION DISRUPTION PHENOTYPE HOMOOLIGOMERIZATION DBB DOMAIN FUNCTION FUNCTION INTERACTION WITH PIK3R1 PHOSPHORYLATION AT TYR-264; TYR-420; TYR-445 AND TYR-460 MUTAGENESIS OF TYR-264; TYR-420; TYR-445 AND TYR-460 DISRUPTION PHENOTYPE FUNCTION TISSUE SPECIFICITY DISRUPTION PHENOTYPE FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING (ISOFORMS 1 AND 2) PHOSPHORYLATION AT TYR-420; TYR-445 AND TYR-460 BY SYK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Lung Pancreas Spleen FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING DISRUPTION PHENOTYPE PHOSPHORYLATION SUBCELLULAR LOCATION FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING INTERACTION WITH MYD88 AND TIRAP PHOSPHORYLATION Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. Homooligomer (Probable). Interacts (phosphorylated on tyrosine residues within YXXM motifs) with PIK3R1 (via SH2 domain); required for BCR- and TLR-mediated activation of phosphoinositide 3-kinase. Interacts (via polyproline C-terminal region) with ABI1 (via SH3 domain); the interaction promotes phosphorylation of PIK3AP1 by ABL1 (By similarity). May interact with MYD88 and TIRAP. false 3 P22366 Myd88 false 2 Q99JY1 Tirap false 2 Cytoplasm Cell membrane Peripheral membrane protein Q9EQ32-1 1 BCAP-L Q9EQ32-2 2 BCAP-S Q9EQ32-3 3 Predominantly expressed in spleen (at protein level). Expressed at lower levels in thymus, liver and lung. Expressed in B-cells, macrophages and natural killer (NK) cells. The DBB domain is required for dimerization. Constitutively phosphorylated. Phosphorylated on tyrosine residues in C-terminal region by ABL1 (By similarity). Phosphorylated on tyrosine residues within the YXXM motifs by BTK and SYK. Isoform 1 and isoform 2 are phosphorylated on tyrosine residues, most likely within the YXXM motifs, via CD19 activation. Toll-like receptor activation induces appearance of a phosphorylated form associated with membranes. Mice lacking Pik3ap1 display altered B-cell maturation and impaired immune function. Pik3ap1 depletion has an opposite effect in NK cells by promoting their maturation. Mice lacking Pik3ap1 and Cd19 have severe defects in generation of immature and mature B-cells. Moreover, mice lacking Pik3ap1 display increased IL-10, Il-12 and TNF proinflammatory cytokine secretion upon activation of the Toll-like receptors TLR4, TLR7 and TLR9. Alternative splicing Cell membrane Complete proteome Cytoplasm Membrane Phosphoprotein Reference proteome NSVKPASWEREQHHPYGEELYHIVD KLSLIREAETLVFKGQVATDMACDD Y F Y F Y F Y F K N E G G GE A AP MAASGWGRGCDILIFYSPDAEEWCQYLQDLFVSCRQVRSQKTQTYRLVPDASFSAQDLWV FRDARCVLVLLSAGLVGCFGQPGLLPMLQRACHPPQRVVRLLCGVQPGDEDFQAFFPDWA HWQEMTCDDEPETYLAAVRKAISEDSGCDSVTDTEPEDERELPFSKQTNLPPEISPGNLM VVQPDRIRCGAETTVYIIVRCKLDEKVSTEAEFSPEDSPSIRVEGTLENEYTVSVKAPDL SSGNVSLKVYSGDLVVCETTVSYYTDMEEIGNLLSSAANPVEFMCQAFKIVPYNTETLDK LLTESLKNNIPASGLHLFGINQLEEDDMMTNQRDEELPTLLHFAAKYGLKNLTALLLTCP GALQAYSVANKHGHYPNTIAEKHGFRDLRQFIDEYVETVDMLKTHIKEELMQGEEADDVY ESMAHLSTDLLMKCSLNPGCDDELYESMAAFAPAATEDLYVEMLQASAGNPVSGESFSRP TKDSMIRKFLEGNSVKPASWEREQHHPYGEELYHIVDEDETFSVDLANRPPVPVPRPEAS APGPPPPPDNEPYISKVFAEKSQERLGNFYVSSESIRKEPLVRPWRDRPPSSIYDPFAGM KTPGQRQLITLQEQVKLGIVNVDEAVLHFKEWQLNQKKRSESFRFQQENLKRLRESITRR RKEKPKSGKHTDLEITVPIRHSQHLPEKVEFGVYESGPRKSVLPARTELRRGDWKTDSMS STASSTSNRSSTRSLLSVSSGMEGDNEDNEIPEITRSRGPGPTQVDGAPVVTGTPVGTLE RPPRVPPRAASQRPLTRESFHPPPPVPPRGR B1AXD8 Q641L8 Q9DAH4 AKIR2_MOUSE Akirin-2 Akirin2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-21 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver FUNCTION DISRUPTION PHENOTYPE ERRATUM PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-21 AND SER-55 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Lung Spleen Testis Forms a complex with YWHAB that acts to repress transcription of DUSP1 (By similarity). Required for embryonic development and the innate immune response. Downstream effector of the Toll-like receptor (TLR), TNF and IL-1 beta signaling pathways leading to the production of IL-6. Interacts with YWHAB. Q9BYH8 NFKBIZ true 3 Q9EST8 Nfkbiz false 3 Q61466 Smarcd1 false 2 Nucleus Mice are embryonic lethal. Null mutant embryos could not be detected even on embryonic day 9.5. 'Akiraka ni suru' means 'making things clear' in Japanese. The name is given based on the presence of the clear nuclear localization signal. Belongs to the akirin family. Complete proteome Developmental protein Immunity Innate immunity Nucleus Phosphoprotein Reference proteome Repressor Transcription Transcription regulation A V V G MACGATLKRTLDFDPLLSPASPKRRRCAPLSAPASAAASPAAATAAAAASAAAASPQKYL RMEPSPFGDVSSRLTTEQILYNIKQEYKRMQKRRHLEASFQQADPGCTSDSQPHAFLISG PASPGTSSATSSPLKKEQPLFTLRQVGMICERLLKEREEKVREEYEEILNTKLAEQYDAF VKFTHDQIMRRYGEQPASYVS P15530 Q4FJP4 CD79B_MOUSE B-cell antigen receptor complex-associated protein beta chain B-cell-specific glycoprotein B29 Ig-beta Immunoglobulin-associated B29 protein CD79b Cd79b Igb Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] B-cell NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Spleen NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Salivary gland NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17 INTERACTION WITH BLK INTERACTION WITH LYN PHOSPHORYLATION FUNCTION INTERACTION WITH BLK PHOSPHORYLATION AT TYR-195 AND TYR-206 SUBCELLULAR LOCATION FUNCTION SUBCELLULAR LOCATION FUNCTION FUNCTION SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Lung Spleen X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 27-159 SUBUNIT DISULFIDE BONDS 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. false 3 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. B-cells. Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-kinases such as BLK, LYN and SYK. 3D-structure Adaptive immunity Cell membrane Complete proteome Disulfide bond Glycoprotein Immunity Immunoglobulin domain Membrane Phosphoprotein Reference proteome Signal Transmembrane Transmembrane helix MATLVLSSMPCHWLLFLLLLFSGEPVPAMTSSDLPLNFQGSPCSQIWQHPRFAAKKRSSM VKFHCYTNHSGALTWFRKRGSQQPQELVSEEGRIVQTQNGSVYTLTIQNIQYEDNGIYFC KQKCDSANHNVTDSCGTELLVLGFSTLDQLKRRNTLKDGIILIQTLLIILFIIVPIFLLL DKDDGKAGMEEDHTYEGLNIDQTATYEDIVTLRTGEVKWSVGEHPGQE P10605 Q3UDW7 CATB_MOUSE Cathepsin B 3.4.22.1 Cathepsin B1 Cathepsin B light chain Cathepsin B heavy chain Ctsb Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE NUCLEOTIDE SEQUENCE NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Placenta Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary gland NUCLEOTIDE SEQUENCE [MRNA] OF 314-339 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Has also been implicated in tumor invasion and metastasis. Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. Dimer of a heavy chain and a light chain cross-linked by a disulfide bond. Interacts with SRPX2. Directly interacts with SHKBP1. Lysosome Melanosome Secreted Extracellular space Belongs to the peptidase C1 family. Acetylation Complete proteome Disulfide bond Glycoprotein Hydrolase Lysosome Protease Reference proteome Secreted Signal Thiol protease Zymogen S N N D V I G V MWWSLILLSCLLALTSAHDKPSFHPLSDDLINYINKQNTTWQAGRNFYNVDISYLKKLCG TVLGGPKLPGRVAFGEDIDLPETFDAREQWSNCPTIGQIRDQGSCGSCWAFGAVEAISDR TCIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGGYPSGAWSFWTKKGLVSGGVYNSHVGCL PYTIPPCEHHVNGSRPPCTGEGDTPRCNKSCEAGYSPSYKEDKHFGYTSYSVSNSVKEIM AEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDMMGGHAIRILGWGVENGVPYWLAANSW NLDWGDNGFFKILRGENHCGIESEIVAGIPRTDQYWGRF Q9DAR0 CE049_MOUSE Uncharacterized protein C5orf49 homolog Y regulated sperm protein Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Hypothalamus Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] IDENTIFICATION BY MASS SPECTROMETRY TISSUE SPECIFICITY RIII Sperm IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis Expressed in sperm (at protein level). On the 2D-gel the determined pI of this protein is: 7.7, its MW is: 22 kDa. Complete proteome Reference proteome MEELAKKERRAMDPGGLKKEGKVEEEAGKEEGREEEGGEEEEVTSETLRGKPRPLPISAL PAFSYIPPRHQGPKERSYFSREGQTGIVSLYDCVFKRRLDYNQKLHRDDREHAKNLGLHI NEEEQERTVPVLMSSVYGKRINQPIEPLNRDYGHVSHVKTDFYRKNEIPSIKGPGFGHIN PA P00186 Q9QWJ4 CP1A2_MOUSE Cytochrome P450 1A2 1.14.14.- CYPIA2 Cholesterol 25-hydroxylase Cytochrome P450-P2 Cytochrome P450-P3 Hydroperoxy icosatetraenoate dehydratase 4.2.1.152 Cyp1a2 Cyp1a-2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3) C57BL/6N NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3) C57BL/6N NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3) ERRATUM NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3) NUCLEOTIDE SEQUENCE [MRNA] (P2) DBA/2N Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (P3) Liver PROTEIN SEQUENCE OF 2-26 DBA/2J NUCLEOTIDE SEQUENCE [MRNA] OF 277-315 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation. 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] cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 25-hydroxycholesterol + 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] = (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + 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 (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-(5Z,8Z,11Z,13E)-eicosatetraenoate + H2O (13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-octadecadienoate + H2O (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] heme Cofactor metabolism; retinol metabolism. Steroid metabolism; cholesterol metabolism. Lipid metabolism; arachidonate metabolism. Endoplasmic reticulum membrane Peripheral membrane protein Microsome membrane Peripheral membrane protein By 3-methylcholanthrene (3MC). Belongs to the cytochrome P450 family. Complete proteome Direct protein sequencing Endoplasmic reticulum Fatty acid metabolism Glycoprotein Heme Iron Lipid metabolism Lyase Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Polymorphism Reference proteome Steroid metabolism Sterol metabolism I M MAFSQYISLAPELLLATAIFCLVFWMVRASRTQVPKGLKNPPGPWGLPFIGHMLTVGKNP HLSLTRLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVRQGDDFKGRPDLYSFTLITNGK SMTFNPDSGPVWAARRRLAQDALKSFSIASDPTSASSCYLEEHVSKEANHLVSKLQKAMA EVGHFEPVSQVVESVANVIGAMCFGKNFPRKSEEMLNIVNNSKDFVENVTSGNAVDFFPV LRYLPNPALKRFKTFNDNFVLFLQKTVQEHYQDFNKNSIQDITSALFKHSENYKDNGGLI PEEKIVNIVNDIFGAGFDTVTTAITWSILLLVTWPNVQRKIHEELDTVVGRDRQPRLSDR PQLPYLEAFILEIYRYTSFVPFTIPHSTTRDTSLNGFHIPKERCIYINQWQVNHDEKQWK DPFVFRPERFLTNNNSAIDKTQSEKVMLFGLGKRRCIGEIPAKWEVFLFLAILLQHLEFS VPPGVKVDLTPNYGLTMKPGTCEHVQAWPRFSK P0DP27 P02593 P62204 P70667 P99014 Q3TEH7 Q3THK5 Q3U6Z5 Q3U7C7 Q498A3 Q61379 Q61380 Q8BNC9 Q91VQ9 Q9D6G4 CALM2_MOUSE Calmodulin-2 Calm2 Cam2 CamC Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] CAST/EiJ Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J DBA/2J NOD Amnion Bone marrow Colon Hippocampus Kidney Liver Lung Mammary gland Ovary Placenta Stomach Testis Thymus Tongue NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] 129 C57BL/6J Czech II Brain Mammary tumor Placenta Spinal ganglion NUCLEOTIDE SEQUENCE [MRNA] OF 1-131 PROTEIN SEQUENCE OF 2-14 CLEAVAGE OF INITIATOR METHIONINE ACETYLATION AT ALA-2 IDENTIFICATION BY MASS SPECTROMETRY C57BL/6J Liver PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107 IDENTIFICATION BY MASS SPECTROMETRY C57BL/6J Brain Hippocampus INTERACTION WITH RYR1 AND RYR2 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND SER-102 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast INTERACTION WITH IQCF1 INTERACTION WITH SYT7 Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY. Interacts with MYO10. Interacts with RRAD (By similarity). Interacts with USP6; the interaction is calcium dependent (By similarity). Interacts with CDK5RAP2. Interacts with SCN5A (By similarity). Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure. Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with RYR1 (PubMed:18650434). Interacts with MYO5A (By similarity). Interacts with IQCF1 (PubMed:25380116). Interacts with SYT7 (PubMed:24569478). Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (By similarity). Interacts with RYR2; regulates RYR2 calcium-release channel activity (PubMed:18650434). Interacts with PCP4; regulates calmodulin calcium-binding (By similarity). Interacts with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-independent, constitutive and participates to the proper assembly of a functional heterotetrameric M channel (By similarity). Cytoplasm Cytoskeleton Spindle Cytoplasm Cytoskeleton Spindle pole Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. Ubiquitination results in a strongly decreased activity. Phosphorylation results in a decreased activity. This protein has four functional calcium-binding sites. Belongs to the calmodulin family. Acetylation Calcium Complete proteome Cytoplasm Cytoskeleton Direct protein sequencing Isopeptide bond Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK P61213 P41275 Q3TGR5 ARL4A_MOUSE ADP-ribosylation factor-like protein 4A Arl4a Arl4 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Amnion Head Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor SUBCELLULAR LOCATION TISSUE SPECIFICITY DEVELOPMENTAL STAGE Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane in GDP-bound form (By similarity). Interacts with CYTH2. Interacts with KPNA2; the interaction is direct. Does not interacts with ARL4A (By similarity). Cell membrane Cytoplasm Nucleus Nucleolus Localization in the nucleolus is dependent by nucleotide binding. Expressed strongly in testis and liver. Expressed slightly in heart, spleen, lung and kidney. Expressed strongly in embryo at 7 dpc. Expressed slightly in embryo at 11, 15 and 17 dpc. Myristoylated. Belongs to the small GTPase superfamily. Arf family. Cell membrane Complete proteome Cytoplasm GTP-binding Lipoprotein Membrane Myristate Nucleotide-binding Nucleus Reference proteome MGNGLSDQTSILSSLPSFQSFHIVILGLDCAGKTTVLYRLQFNEFVNTVPTKGFNTEKIK VTLGNSKTVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVDSVDVERMEEAKTELHKITR ISENQGVPVLIVANKQDLRNSLSLSEIEKLLAMGELSSSTPWHLQPTCAIIGDGLKEGLE KLHDMIIKRRKMLRQQKKKR Q65CL1 Q3UQ61 Q8C0N3 CTNA3_MOUSE Catenin alpha-3 Alpha T-catenin Cadherin-associated protein Ctnna3 Catna3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] Heart NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Heart Testis INTERACTION WITH CTNNB1 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; THR-361; SER-637; SER-647 AND THR-649 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Heart Lung Spleen Testis May be involved in formation of stretch-resistant cell-cell adhesion complexes. Interacts with CTNNB1. Cytoplasm Cytoskeleton Localizes to intercalated disks of cardiomyocytes and in peritubular myoid cells of testis, and colocalizes with CTNNA1 and CTNNA2. Belongs to the vinculin/alpha-catenin family. Cell adhesion Coiled coil Complete proteome Cytoplasm Cytoskeleton Phosphoprotein Reference proteome E K S C A V V A MSAETPITLNMDTQDLQIQTFTVEKLLEPLIIQVTTLVNCPQNPSNRKKGRSKRARVLLA SVEEATWNLLDKGEMIAKEATVLKEELAAALQEVRKESKALKVSAERFTDDPCYLPKREA VVQAARALLAAVTRLLVLADMIDVMCLLQHVSSFQRTFESLKNVSNKSDLQRTYQKLGKE LESLDYLAFKRQQDLKSPSQRDEIAGARATLKENSPLLHSICSACLEHSDVASLKASKDT VCEEIQNALDVISNASQGIQNAPAPPEPQAATLGSAFDELENLIVLNPLTVTEEDVRPSL EKRLEAIISGAALLADSSCTRDLHRERIIAECNAIRQALQDLLTEYMSNTGKTERSNTLN TAIVNMSKKTRDLRRQLRKAIIDHISDSFLDTTVPLLVLIEAAKNGRVKEIKDYAAIFHE HTGRLVEVANLACSMSTNEDGIKIVRIAANHLETLCPQIINAALALASRPKSQVVKNTME MYKRTWEHYIHVLTEAVDDITSIDDFLAVSESHILEDVNKCIIALRDQDADNLDRAAGAI RGRAARVAHIVAGEMDSYEPGAYTEGVMRNVNFLTSTVIPEFVTQVNVALDALSKNSLTA LDDNQFVDISKKIYDTIHDIRCSVMMIRTPEELEDVSDLEDDHEVRSHTSIQTEGKTDRA KMTQLPEAEKEKIAEQVADFKKVKSKLDAEIEIWDDTSNDIIVLAKKMCMIMMEMTDFTR GKGPLKHTTDVIYAAKMISESGSRMDVLARQIANQCPDPPCKQDLLAYLEQIKFYSHQLK ICSQVKAEIQNLGGELIVSALDSVTSLIQAAKNLMNAVVQTVKMSYIASTKIIRIQSSAG PRHPVVMWRMKAPAKKPLIKREKPEETWAAVRRGSAKKKIHPVQVMSEFRGRQVY Q8BJ64 Q3TPY4 Q8CHT7 CHDH_MOUSE Choline dehydrogenase, mitochondrial CDH CHD 1.1.99.1 Chdh Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Kidney Liver Pancreas Testis SUBCELLULAR LOCATION DISRUPTION PHENOTYPE SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-438; LYS-486 AND LYS-498 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486; LYS-498 AND LYS-582 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. Mitochondrion inner membrane Acetylation of Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice. Decreased testicular betaine and increased choline and phosphatidylcholine concentrations. Only one of eleven males was able to reproduce, impaired fertility was due to diminished sperm motility. Belongs to the GMC oxidoreductase family. Acetylation Complete proteome FAD Flavoprotein Membrane Mitochondrion Mitochondrion inner membrane Oxidoreductase Reference proteome Transit peptide V A W C Q R G A MWQVLRGWRKGWQSPRGALAWAVQGQPCPPCSRAVASVGKDEYTFVVVGAGSAGCVLASR LTEDPNHRVLLLEAGPKDLLMGSKRLQWKIHMPAALVSNLCDDKYNWYYHTEPQPGMDSR VLYWPRGRVWGGSSSLNAMVYIRGHAEDYNRWHREGAEGWDYAHCLPYFRKAQRHELGAN MYRGGDGPLHVSRGKTNHPLHQAFLQAARQAGYPFTEDMNGFQQEGFGWMDMTVHQGKRW STACAYLHPVLSRPNLRAEVQTLVSRVLFEGTRAVGVEYIKDGQRHKAYVSREVILSGGA INSPQLLMLSGVGNADDLRKLDIPVVCHLPGVGQNLQDHLEVYVQQACTQPITLHSAQKP LRKVCIGLEWLWSYTGDGATAHLETGGFIRSRPGVPHPDIQFHFLPSQVIDHGRKPTQQE AYQVHVGTMRATSVGWLKLRSANPRDHPVIHPNYLSTETDVEDFRQCVRLSREIFAQEAL APFRGKELQPGSHVQSDKEIDAFVRAKADSAYHPSCTCKMGRSSDPTAVVDAQTKVIGVE NLRVVDASIMPSVVSGNLNAPTVMIAEKAADIIKGHPALEDKNVPVYKPQTLDTQR Q9D7B6 Q8BK36 Q8BKQ8 Q8CFY9 Q9D2L8 ACAD8_MOUSE Isobutyryl-CoA dehydrogenase, mitochondrial 1.3.8.- Acyl-CoA dehydrogenase family member 8 ACAD-8 Acad8 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Embryo Pituitary Skin Testis Tongue NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Liver IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-211 AND LYS-269 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-229 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Isobutyryl-CoA dehydrogenase which catalyzes one of the steps of the valine catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of (2S)-2-methylbutanoyl-CoA. 2-methylpropanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-2-methylpropenoyl-CoA + reduced [electron-transfer flavoprotein] (2S)-2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-2-methylbutenoyl-CoA + reduced [electron-transfer flavoprotein] H(+) + oxidized [electron-transfer flavoprotein] + propanoyl-CoA = acryloyl-CoA + reduced [electron-transfer flavoprotein] FAD Amino-acid degradation; L-valine degradation. Homotetramer, formed by a dimer of dimers. Mitochondrion Belongs to the acyl-CoA dehydrogenase family. Acetylation Branched-chain amino acid catabolism Complete proteome FAD Flavoprotein Mitochondrion Oxidoreductase Reference proteome Transit peptide G E A P D RLAPKLESLAWSLCAAGISLDAPMGCSVQVNHEVDQRAELF MAMLRSGYRRFGCLRAALKSLAQTHHRSITFCIDPSLGLNEEQKGFQKVAFDFAAREMAP NMAEWDQKELFPVDVMRKAAQLGFGGVYVRTDVGGSGLSRLDTSVIFEALATGCTSTTAY ISIHNMCAWMIDSFGNEEQRHKFCPPLCTMEKFASYCLTEPGSGSDAASLLTSAKQQGDH YILNGSKAFISGGGESDIYVVMCRTGGSGAKGISCIVVEKGTPGLSFGKKEKKVGWNSQP TRAVIFEDCAVPVANRIGTEGQGFLIAMKGLNGGRINVASCSLGAAHASVILTQEHLKVR KQFGAPLARSQYLQFQLADMATKLVASRLMIRTAAVALQEEREDAVALCSMAKLFATEEC FAICNQALQMHGGYGYLKDYAVQQYMRDSRVHQILEGSNEVMRMLISRNLLQD O55102 Q9DC96 BL1S1_MOUSE Biogenesis of lysosome-related organelles complex 1 subunit 1 BLOC-1 subunit 1 GCN5-like protein 1 Bloc1s1 Gcn5l1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Eye IDENTIFICATION IN THE BLOC-1 COMPLEX FUNCTION IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Liver Pancreas Testis FUNCTION FUNCTION ASSOCIATION WITH THE AP-3 COMPLEX SUBCELLULAR LOCATION INTERACTION WITH KXD1 Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension (PubMed:16760431, PubMed:19546860, PubMed:21998198). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. The BORC complex is most probably associated with the cytosolic face of lysosomes, may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity). May negatively regulate aerobic respiration through mitochondrial protein lysine-acetylation. May counteract the action of the deacetylase SIRT3 by acetylating and regulating proteins of the mitochondrial respiratory chain including ATP5F1A and NDUFA9. Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8 (PubMed:15102850). The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos (PubMed:21998198). Interacts with ATP5F1A and NDUFA9; involved in their acetylation on lysine residues (By similarity). Interacts with KXD1 (PubMed:22554196). Mitochondrion intermembrane space Mitochondrion matrix Cytoplasm Cytosol Lysosome membrane Belongs to the BLOC1S1 family. Coiled coil Complete proteome Cytoplasm Lysosome Membrane Mitochondrion Reference proteome E Y T I D V MLSRLLKEHQAKQNERKELQEKRRREAIAAATCLTEALVDHLNVGVAQAYMNQRKLDHEV KTLQVQAAQFAKQTGQWIGMVENFNQALKEIGDVENWARSIELDMRTIATALEYVYKGQL QSAPS O55137 Q549A9 ACOT1_MOUSE Acyl-coenzyme A thioesterase 1 Acyl-CoA thioesterase 1 3.1.2.- CTE-I Inducible cytosolic acyl-coenzyme A thioester hydrolase Long chain acyl-CoA thioester hydrolase Long chain acyl-CoA hydrolase Palmitoyl-coenzyme A thioesterase 3.1.2.2 Acot1 Cte1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] TISSUE SPECIFICITY C57BL/6J NUCLEOTIDE SEQUENCE [MRNA] CHARACTERIZATION INDUCTION TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [MRNA] C57BL/6J Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Liver FUNCTION CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY BIOPHYSICOCHEMICAL PROPERTIES PATHWAY ACTIVE SITES MUTAGENESIS OF SER-232; ASP-324 AND HIS-358 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Heart Kidney Liver Lung Spleen Testis Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating intracellular levels of acyl-CoAs, free fatty acids and CoASH. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20). H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate decanoyl-CoA + H2O = CoA + decanoate + H(+) dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+) H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+) (9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+) (9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+) (9E)-octadecenoyl-CoA + H2O = (9E)-octadecenoate + CoA + H(+) 2.6 uM for C16:0-acyl-CoA 15.2 uM for C10:0-acyl-CoA 2.6 uM for C12:0-acyl-CoA 3.5 uM for C14:0-acyl-CoA 0.5 uM for C20:0-acyl-CoA 1.5 uM for C14:1-acyl-CoA 1.1 uM for C16:1-acyl-CoA 2.4 uM for C18:1(cis)-acyl-CoA 1.8 uM for C18:1(trans)-acyl-CoA 4.5 uM for C18:2-acyl-CoA 3.0 uM for C20:4-acyl-CoA 1.2 umol/min/mg enzyme with C16:0-acyl-CoA as substrate 0.192 umol/min/mg enzyme with C10:0-acyl-CoA as substrate 0.780 umol/min/mg enzyme with C12:0-acyl-CoA as substrate 1.68 umol/min/mg enzyme with C14:0-acyl-CoA as substrate 0.692 umol/min/mg enzyme with C18:0-acyl-CoA as substrate 0.245 umol/min/mg enzyme with C20:0-acyl-CoA as substrate 0.745 umol/min/mg enzyme with C14:1-acyl-CoA as substrate 0.621 umol/min/mg enzyme with C16:1-acyl-CoA as substrate 0.176 umol/min/mg enzyme with C18:1(cis)-acyl-CoA as substrate 0.188 umol/min/mg enzyme with C18:1(trans)-acyl-CoA as substrate 0.316 umol/min/mg enzyme with C18:2-acyl-CoA as substrate 0.007 umol/min/mg enzyme with C20:4-acyl-CoA as substrate Lipid metabolism; fatty acid metabolism. Monomer. Cytoplasm Cytosol Expressed in heart, kidney, brown adipose tissue, white adipose tissue, adrenal gland and muscle. In the liver, by peroxisome proliferator (Clofibrate) treatment, via the peroxisome proliferator-activated receptors (PPARs) or fasting for 24 hours. Belongs to the C/M/P thioester hydrolase family. Complete proteome Cytoplasm Fatty acid metabolism Hydrolase Lipid metabolism Phosphoprotein Reference proteome Serine esterase S A S C D A H Q MEATLNLEPSGRSCWDEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGEL DLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLVKRDVQTPFVVELEVLDGHEPDGGQRL AHAVHERHFLAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAG KGFAVMALAYYNYDDLPKNMETMHMEYFEEAVNYLRSHPEVKGPGIGLLGISKGGELGLA MASFLKGITAAVVINGSVAAVGNTISYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPL VDKKSFIPVERSDTTFLFLVGQDDHNWKSEFYADEISKRLQAHGKEKPQIICYPAAGHYI EPPYFPLCSAGMHLLVGANITFGGEPKPHAMAQLDAWQQLQTFFHKQLGSECLHVSPKI Q9D504 Q810N2 Q8BVP4 ANKR7_MOUSE Ankyrin repeat domain-containing protein 7 Ankrd7 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis ANK repeat Complete proteome Reference proteome Repeat S N H R D G K KQ MKKFFPFRGKRKTDDSHSHSSEVPISLAKTAPPSLSIGGGYHLRDKHLKKLHKAATIGNE QKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIK AVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDG HTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLA HKDIYGFTAEEYASFNGFTMYHHITANNENKKKTEQTAY Q3SXB8 Q3SXB7 Q9DC75 COL11_MOUSE Collectin-11 Collectin kidney protein 1 CL-K1 Colec11 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Heart NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) TISSUE SPECIFICITY Lectin that plays a role in innate immunity, apoptosis and embryogenesis. 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. Primarily recognizes the terminal disaccharide of the glycan. Also recognizes a subset of fucosylated glycans and lipopolysaccharides. 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. 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. 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. Homotrimer; disulfide-linked. Interacts with MASP1; probably triggers the lectin pathway of complement. Secreted Q3SXB8-1 1 Q3SXB8-2 2 Highly expressed in embryonic murine craniofacial cartilage, heart, bronchi, kidney and vertebral bodies. Belongs to the COLEC10/COLEC11 family. Alternative splicing Calcium Coiled coil Collagen Complete proteome Developmental protein Disulfide bond Immunity Innate immunity Lectin Mannose-binding Metal-binding Reference proteome Secreted Signal N NALPSPA L V MMMRDLALAGMLISLAFLSLLPSGCPQQTTEDACSVQILVPGLKGDAGEKGDKGAPGRPG RVGPTGEKGDMGDKGQKGTVGRHGKIGPIGAKGEKGDSGDIGPPGPSGEPGIPCECSQLR KAIGEMDNQVTQLTTELKFIKNAVAGLRETESKIYLLVKEEKRYADAQLSCQARGGTLSM PKDEAANGLMASYLAQAGLARVFIGINDLEKEGAFVYSDRSPMQTFNKWRSGEPNNAYDE EDCVEMVASGGWNDVACHITMYFMCEFDKENL Q5U464 ASAP3_MOUSE Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 Development and differentiation-enhancing factor-like 1 Asap3 Ddefl1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Embryonic germ cell Promotes cell proliferation. Cytoplasm ANK repeat Coiled coil Complete proteome Cytoplasm Metal-binding Reference proteome Repeat Zinc Zinc-finger MPEQLSVAEFLAVTAEDLSSPAGAAAFAAKMPRCRGAALAREEALEGDQAILQRIKKAVR AIHSSGLGHVETEEHYREAVEALGNSHLSQNSHELSTGFLNLAVFTREVAALFKNLVQNL NNIVSFPLDSLMKGHLRDGRHDSKKHLEKAWKDYESKVAKLEKERDRARFPGGSHGVMSQ DTQRERRVFQLHMCEYLVKAGESQVKQGPDFLQSLIKFFHAQHNFFQDGWKAAQSLSPFI DKLAASVHGLRQAQEEELHKLTQLRDSLRGMLHLESREDHPNRKNSGGGYSIHQHQGNKQ FGTEKVGFLYKKSDGIRRVWQKRKCGVKYGCLTISHSMINRPPVKLPLLTCQVRPNPEEK RCFDLVTHNRTYHFHAEDEQECEAWVSVLQNSKDEALSNAFHGEPSGGQWSWGTRLDTEP HDLTNMLVAEVKSRPGNDRCCDCGAADPTWLSTNLGVLTCIQCSGVHRELGVRFSRIQSL TLDLLGPSELLLALNIGNSHFNEVMEAHLPSHGSPKPSAESDMSSRRNYIVAKYVEHKFA RHSTPDPQKLRTAICSRDLLSVLEAFANGQDFGQLLPGPDGQAPGELALHLAIRVASHAS LPIVDFLIQNGGHLDAKAADGNTALHCAALHGQLDCLKLLLRGRAPVGAVNDAGETALDI ARNRQHKECEELLEQAQAGTLAFPLHMDYHWGHSMEHGFDSEEEEEEEKHCPSKPPAQAC WGSVRLDISNKTYETVATPGPATTQSQSEDSPPPLPIKNSSRTIVLGRAGHCSGDRSDLP SLRSESPEALENRSSPASSSSSLTSSVEPGGLSQAPSSPEEGLQESASISRPGLASGTTS AEVYLPVKFSSESTRSYRRGGRSLEDSPSARQPLCSRRHIPVGLVEGDGSKIGVLPDSLQ LLHD Q8BJ63 Q3TDF2 Q3TPT5 Q8BII2 Q8BJ31 Q8BJ58 Q8BY11 Q8R5B1 AP5M1_MOUSE AP-5 complex subunit mu-1 Adaptor-related protein complex 5 subunit mu-1 Mu5 Mu-2-related death-inducing protein MuD Ap5m1 Mudeng Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3) C57BL/6J NOD Bone Cerebellum Dendritic cell Embryonic spinal ganglion Embryonic testis Hippocampus Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Czech II Mammary gland TISSUE SPECIFICITY As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. Probably part of the adaptor protein complex 5 (AP-5) a tetramer composed of AP5B1, AP5M1, AP5S1 and AP5Z1. Cytoplasm Cytosol Late endosome membrane Peripheral membrane protein Cytoplasmic side Lysosome membrane Peripheral membrane protein Cytoplasmic side May cycle on and off membranes. Q8BJ63-1 1 Q8BJ63-2 2 May be due to intron retention. Q8BJ63-3 3 May be due to intron retention. Widely expressed, including in small intestine and testis. In small intestine, highly expressed in cytoplasm of villi epithelial cells and internal glands. In testis, selectively expressed in maturing sperm cells (at protein level). Belongs to the adaptor complexes medium subunit family. Alternative splicing Complete proteome Cytoplasm Endosome Lysosome Membrane Protein transport Reference proteome Transport CDLEGVMPAVTISLSLPTNGSPLQDIIVHPCVTSLDSAILTSSSIDTMDDSAFSGPYKFPFTPPLES VRFSPGFALSYHFTLKNSQFCNLYFTFLNGVLVILSNSHEILCYLSVFLTNCLFNDYNVMNHPIALK QKFPKS EYGFVY A V V I L V S K D E K N MALRAVWLIRHEPGTPLGGTVRFSRRYPTVEKRAKAFNGMTYVPVPEDGPFLRALLFQLR LLDDDKDFMERRDGCSRINKTSIYGLSVGGEELWPVIAFLRDSMIYASVPLVEQALSPRP PLISISGVSQGLELLLGIQDFLYSSQKNDTDLHTKLSQLPDLLLQACPLGTLLDANLQNS LNSINSVSVTQPQKQPAWKVGAYKGKAQISISITETVKCMQYGKQDIADTWQVAGTVACK CDLEGVMPAVTISLSLPTNGSPLQDIIVHPCVTSLDSAILTSSSIDTMDDSAFSGPYKFP FTPPLESFNLCHYTSQVPVPPILGSYHMKEEGVQLKVTVNFKLHESVRNNFEVCEAHIPF YNRGPITHLEYKASFGQLEVFREKSLLVWIIGQKFPKSMEISLSGTLTFGVKGHNKQPFD HICIGNTAYIKLNFRIADYTLTGCYADQHSVQVFASGKPKISAYRKLISSDYYIWNSKAP APVTYASLLP Q99L43 Q3TMD1 Q6NSU1 CDS2_MOUSE Phosphatidate cytidylyltransferase 2 2.7.7.41 CDP-DAG synthase 2 CDP-DG synthase 2 CDP-diacylglycerol synthase 2 CDS 2 CDP-diglyceride pyrophosphorylase 2 CDP-diglyceride synthase 2 CTP:phosphatidate cytidylyltransferase 2 Cds2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Cerebellum Embryonic stem cell Lung NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Embryo Mammary tumor PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-36 AND THR-50 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin. a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. Mitochondrion inner membrane Multi-pass membrane protein Matrix side Belongs to the CDS family. Complete proteome Lipid biosynthesis Lipid metabolism Membrane Mitochondrion Mitochondrion inner membrane Nucleotidyltransferase Phospholipid biosynthesis Phospholipid metabolism Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix L P MTELRQRVVREDAPPEDKESESEAKLDGETASDSESRAETAPLPTSVDDTPEVLNRALSN LSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMMIVMCVQIKCFHEIITIGYNVYHSYD LPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFALYLTGFCMF VLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYM FGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFT VDCEPSDLFRLQEYNIPGVIQSAIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFK RAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQQ LHIFNTLKSHLTDKGILTSALEDE Q91ZT7 B2RUP6 ASB10_MOUSE Ankyrin repeat and SOCS box protein 10 ASB-10 Asb10 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Heart Skin NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Protein modification; protein ubiquitination. Nucleus Cytoplasm The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin-protein ligase complexes. Belongs to the ankyrin SOCS box (ASB) family. ANK repeat Complete proteome Cytoplasm Nucleus Reference proteome Repeat Ubl conjugation pathway MLMSWSPEECRDQGEPQGDRYSLCAKLVEKPDRGSEEHLEPGLGPIIIRSASGPTLAFWQ AVLVGDVGSVSRILSDSSTGLAPDSIFDTSDPERWRDYRFNIRALRLWSLTYEEELTTPL HVAASRGHTEVLELLLRRRAKPDSAPGGRTALHEACSAGHAACVRVLLVAGADPNTLDQD GKRPLHLCRGPGILECVELLLKFGAQVDGRTEDEEETPLHIAARLGHVELADLLLRWGAC PDVRNSEGWTPLLAACDIRCQSPKDAEATTNRCFQLCRLLLSVGADADAANQDKQRPLHL ACRHGHSAVVQLLLSCGVNANAMDYGGHTPLHCALLGPTTAVAHSPEHTVRDLLNHGAVR VWPGALPKVLDRWCMSPRTIEVLMNTYRVVQLPEEAKGLVPPEILQKYHGFYSSLFALVR QPRSLQHLCRCALRSHLEGCLPHALPRLPLPPRMLRFLQLDFEDLLY Q99N28 Q8BSQ8 Q8K1H8 CADM3_MOUSE Cell adhesion molecule 3 Immunoglobulin superfamily member 4B IgSF4B Nectin-like protein 1 NECL-1 Synaptic cell adhesion molecule 3 TSLC1-like protein 1 Cadm3 Igsf4b Necl1 Syncam3 Tsll1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] SUBCELLULAR LOCATION TISSUE SPECIFICITY 129/SvJ NUCLEOTIDE SEQUENCE [MRNA] FUNCTION INTERACTION WITH EPB41L1 SUBCELLULAR LOCATION TOPOLOGY DEVELOPMENTAL STAGE TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-396 Eye FUNCTION INTERACTION WITH NECTIN3; DLG3; MPP6 AND CASK SUBCELLULAR LOCATION TISSUE SPECIFICITY PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Involved in the cell-cell adhesion. Has both calcium-independent homophilic cell-cell adhesion activity and calcium-independent heterophilic cell-cell adhesion activity with IGSF4, NECTIN1 and NECTIN3. Interaction with EPB41L1 may regulate structure or function of cell-cell junctions. Homodimer. Can form trans-heterodimers with NECTIN3. Interacts with EPB41L1, DLG3, MPP6 and CASK. Cell membrane Single-pass type I membrane protein Cell junction Mainly expressed in brain, in neuronal cell bodies of cerebellum, cortex, hippocampus, hypothalamus and spinal cord. In spinal cord predominantly expressed in motor neurons. Expressed in axons, presynaptic nerve terminals, glia cell processes. At 14.5 dpc predominantly expressed in the nervous system. The cytoplasmic region mediates interaction with EPB41L1, DLG3, MPP6 and CASK. Belongs to the nectin family. 3D-structure Calcium Cell adhesion Cell junction Cell membrane Complete proteome Disulfide bond Glycoprotein Immunoglobulin domain Membrane Phosphoprotein Reference proteome Repeat Signal Transmembrane Transmembrane helix MGAPSALPLLLLLACSWAPGGANLSQDDSQPWTSDETVVAGGTVVLKCQVKDHEDSSLQW SNPAQQTLYFGEKRALRDNRIQLVSSTPHELSISISNVALADEGEYTCSIFTMPVRTAKS LVTVLGIPQKPIITGYKSSLREKETATLNCQSSGSKPAAQLTWRKGDQELHGDQTRIQED PNGKTFTVSSSVSFQVTREDDGANIVCSVNHESLKGADRSTSQRIEVLYTPTAMIRPEPA HPREGQKLLLHCEGRGNPVPQQYVWVKEGSEPPLKMTQESALIFPFLNKSDSGTYGCTAT SNMGSYTAYFTLNVNDPSPVPSSSSTYHAIIGGIVAFIVFLLLILLIFLGHYLIRHKGTY LTHEAKGSDDAPDADTAIINAEGGQSGGDDKKEYFI Q8K199 Q8CEV6 COXM2_MOUSE COX assembly mitochondrial protein 2 homolog Cmc2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Hippocampus Kidney NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Mammary gland May be involved in cytochrome c oxidase biogenesis. Mitochondrion Belongs to the CMC family. Complete proteome Disulfide bond Mitochondrion Reference proteome MHPDLSPHLHTEECNVLINLLKECHKNHNILKFFGHCNDLDREMRKCLKNEYSERRTRSR EHGAAMRRRLSDPPEEAGR Q9DCZ9 Q3U2R3 APH1C_MOUSE Putative gamma-secretase subunit APH-1C Aph1c Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Kidney NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain Potential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors and APP (amyloid-beta precursor protein). Potential component of the gamma-secretase complex. Membrane Multi-pass membrane protein Belongs to the APH-1 family. Complete proteome Membrane Notch signaling pathway Reference proteome Transmembrane Transmembrane helix MTLPVFFGCAFIAFGPAFALYLFTIATDPLRVIFLIAGAFFWLVSLLLSSMFWFLVRVIT NNRDESVQNYLLIFGALLSVCIQELFRLAYYKLLKKASEGLKSINPEEDIAPSMRLLAYV SGLGFGIMSGVFSFVNTLSNSLGPGTVGIHGDSPQFFLNSAFMTLVVIMLHVFWGVVFFD GCEKNKWYTLLTVLLTHLVVSTQTFLSPYYEVNLVTAYIIMVLMGIWAFYVAGGSCRSLK FCLLCQDKDFLLYNQRSR P01587 CSF2_MOUSE Granulocyte-macrophage colony-stimulating factor GM-CSF Colony-stimulating factor CSF Csf2 Csfgm Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ NUCLEOTIDE SEQUENCE [MRNA] OF 24-141 Lung NUCLEOTIDE SEQUENCE [MRNA] OF 18-141 PROTEIN SEQUENCE OF 24-57 DISULFIDE BONDS MUTAGENESIS Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. Monomer. The signaling GM-CSF receptor complex is a dodecamer of two head-to-head hexamers of two alpha, two beta, and two ligand subunits (By similarity). Secreted Belongs to the GM-CSF family. Complete proteome Cytokine Direct protein sequencing Disulfide bond Glycoprotein Growth factor Reference proteome Secreted Signal E P L P E P L P L P T I V A G S G V MWLQNLLFLGIVVYSLSAPTRSPITVTRPWKHVEAIKEALNLLDDMPVTLNEEVEVVSNE FSFKKLTCVQTRLKIFEQGLRGNFTKLKGALNMTASYYQTYCPPTPETDCETQVTTYADF IDSLKTFLTDIPFECKKPGQK P49300 Q549F6 Q91YT3 CLC10_MOUSE C-type lectin domain family 10 member A MMGL Macrophage asialoglycoprotein-binding protein 1 M-ASGP-BP-1 Macrophage galactose/N-acetylgalactosamine-specific lectin Clec10a Mgl Mgl1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C3H/HeN NUCLEOTIDE SEQUENCE [GENOMIC DNA] 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor PROTEIN SEQUENCE OF 102-120 AND 137-151 C3H/HeN TISSUE SPECIFICITY DEVELOPMENTAL STAGE INTERACTION WITH SIGLEC1 TISSUE SPECIFICITY FUNCTION Recognizes terminal galactose and N-acetylgalactosamine units. May participate in the interaction between tumoricidal macrophages and tumor cells. Plays a role in the recruitment of inflammatory monocytes to adipose tissue in diet-induced obesity. Homooligomer. Interacts with SIGLEC1, which may act as a counter-receptor for CLEC10A in lymph node. Membrane Single-pass type II membrane protein Detected in lymph node in the subcapsular sinus, interfollicular regions, T and B-cell boundary and in the areas surrounding high endothelial venules (at protein level). Expressed on the surface of activated macrophages. Expressed in heart, lung, testis, skeletal muscle, spleen, brain, kidney and thymus. Expressed in P388, RAW 264.7 and M1 cell lines. Detected in 7 dpc, 11 dpc, 15 dpc and 17 dpc embryo. MGL1 Calcium Complete proteome Direct protein sequencing Disulfide bond Glycoprotein Lectin Membrane Reference proteome Signal-anchor Transmembrane Transmembrane helix T I V L MIYENLQNSRIEEKTQEPGKAPSQSFLWRILSWTHLLLFSLGLSLLLLVVVSVIGSQNSQ LRRDLGTLRATLDNTTSKIKAEFQSLDSRADSFEKGISSLKVDVEDHRQELQAGRDLSQK VTSLESTVEKREQALKTDLSDLTDHVQQLRKDLKALTCQLANLKNNGSEVACCPLHWTEH EGSCYWFSESEKSWPEADKYCRLENSHLVVVNSLEEQNFLQNRLANVVSWIGLTDQNGPW RWVDGTDFEKGFKNWAPLQPDNWFGHGLGGGEDCAHITTGGPWNDDVCQRTFRWICEMKL AKES Q9D8U4 C1QT2_MOUSE Complement C1q tumor necrosis factor-related protein 2 mCTRP2 C1qtnf2 Crtp2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C57BL/6J Lung NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Pancreas NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N-3 Mammary tumor INTERACTION WITH ERFE May interact with ERFE. Secreted It is uncertain whether Met-1 or Met-10 is the initiator. Collagen Complete proteome Reference proteome Secreted Signal MTIFKKVTTMISWVLLACALPCAADPMLGAFARRDFQKGGPQLVCSLPGPQGPPGPPGAP GSSGVVGRMGFPGKDGQDGQDGDRGDSGEEGPPGRTGNRGKQGPKGKAGAIGRAGPRGPK GVSGTPGKHGTPGKKGPKGKKGEPGLPGPCSCGSSRAKSAFSVAVTKSYPRERLPIKFDK ILMNEGGHYNASSGKFVCSVPGIYYFTYDITLANKHLAIGLVHNGQYRIRTFDANTGNHD VASGSTILALKEGDEVWLQIFYSEQNGLFYDPYWTDSLFTGFLIYADQGDPNEV P13516 Q922I6 ACOD1_MOUSE Acyl-CoA desaturase 1 1.14.19.1 Delta(9)-desaturase 1 Delta-9 desaturase 1 Fatty acid desaturase 1 Stearoyl-CoA desaturase 1 Scd1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] Adipocyte NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Mammary gland INVOLVEMENT IN AB DISEASE TISSUE SPECIFICITY DEVELOPMENTAL STAGE FUNCTION DISEASE FUNCTION CATALYTIC ACTIVITY DISEASE TISSUE SPECIFICITY SUBCELLULAR LOCATION TISSUE SPECIFICITY DEVELOPMENTAL STAGE FUNCTION CATALYTIC ACTIVITY DISRUPTION PHENOTYPE TISSUE SPECIFICITY SUBCELLULAR LOCATION DISEASE FUNCTION INDUCTION BY HIGH-CARBOHYDRATE DIET TISSUE SPECIFICITY FUNCTION CATALYTIC ACTIVITY DISRUPTION PHENOTYPE TISSUE SPECIFICITY SUBCELLULAR LOCATION DISRUPTION PHENOTYPE FUNCTION INDUCTION BY HIGH CARBOHYDRATE; UNSATURATED FATTY ACIDS AND NR1H3 AGONISTS TISSUE SPECIFICITY DISRUPTION PHENOTYPE FUNCTION DISEASE VARIANT AB PRO-278 INS SUBCELLULAR LOCATION MEMBRANE TOPOLOGY FUNCTION CATALYTIC ACTIVITY SUBCELLULAR LOCATION DISRUPTION PHENOTYPE FUNCTION INDUCTION BY DIETARY STEARATE IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Liver Lung REVIEW REVIEW X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 24-355 IN COMPLEX WITH STEAROYL-COENZYME A AND ZINC IONS FUNCTION TOPOLOGY CATALYTIC ACTIVITY COFACTOR Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the Delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:11500518, PubMed:11533264, PubMed:16275639, PubMed:16443825, PubMed:26098370). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:11500518, PubMed:11533264, PubMed:16443825, PubMed:26098370). Plays an important role in lipid biosynthesis (PubMed:17127673, PubMed:10899171, PubMed:11500518, PubMed:11441127, PubMed:11533264, PubMed:12177411, PubMed:26098370). Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (PubMed:12177411, PubMed:17127673, PubMed:24356954, PubMed:24295027). Plays an important role in body energy homeostasis (PubMed:17127673, PubMed:15210843, PubMed:24295027, PubMed:24356954). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (PubMed:10899171, PubMed:11500518, PubMed:11441127, PubMed:11533264, PubMed:12177411, PubMed:15210843, PubMed:26098370). Required for normal development of sebaceous glands (PubMed:17738154, PubMed:11533264). Required for the biosynthesis of normal levels of Delta-9 unsaturated fatty acids and 1-alkyl-2,3-diacylglycerol in the Harderian gland (PubMed:11500518). Required for normal production of meibum, an oily material that prevents drying of the cornea (PubMed:11533264). 2 [Fe(II)-cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 [Fe(III)-cytochrome b5] + 2 H2O Fe(2+) Expected to bind 2 Fe(2+) ions per subunit, instead of the Zn(2+) ions seen in the 3D-structure. Endoplasmic reticulum membrane Multi-pass membrane protein Microsome membrane Detected in liver (at protein level) (PubMed:10899171, PubMed:11533264). Detected in skin and liver (PubMed:10545940, PubMed:11161812, PubMed:11441127, PubMed:11533264). Detected in sebaceous gland, but not in hair follicle (PubMed:10545940). Detected in white and brown adipose tissue, eyelid, Harderian gland, and at lower levels in Meibomian gland, eyeball and adrenal gland (PubMed:11500518, PubMed:11533264). Highly expressed in liver, and detected at low levels in brain, heart, lung, stomach, skeletal muscle and kidney (PubMed:11161812, PubMed:12815040). Up-regulated during the early anagen phase of the hair cycle. Thereafter, levels decrease and are very low at telogen phase. Up-regulated by agonists that activate NR1H3 (PubMed:12815040). Up-regulated by a high-carbohydrate diet (PubMed:11441127). Up-regulated by a fat-free, high-carbohydrate diet (PubMed:12815040). Down-regulated by a high-carbohydrate diet enriched in unsaturated fatty acids (PubMed:12815040). Up-regulated by a diet containing high levels of stearate (PubMed:17127673). The histidine box domains are involved in binding the catalytic metal ions. Defects is Scd1 are the cause of asebia (ab) (PubMed:17738154, PubMed:10545940, PubMed:10854228, PubMed:10899171, PubMed:15278437). The trait is due to spontaneous autosomal recessive mutations that give rise to deletions or point mutations in Scd1. The ab trait has complete penetrance (PubMed:17738154). Ab mice are characterized by reduced body weight, extreme sebaceous gland hypoplasia leading to nearly complete absence of sebaceous glands, and thickened, scaly skin with hyperkeratosis and alopecia (PubMed:17738154, PubMed:10854228, PubMed:15278437). The hair follicles are abnormally long and extend at a sharp angle into the subcutis, probably due to abnormal persistence of inner root sheath. Frequently the hair shaft ruptures through the base of the hair follicle, giving rise to inflammation that results in scarring alopecia (PubMed:10854228, PubMed:15278437). Besides, ab mice display increased transepithelial water loss (PubMed:10854228). Ab mice present a narrow eye fissure and their eyes are nearly closed (PubMed:10854228, PubMed:15278437). Older mice develop blindness (PubMed:17738154). Scd1 activity is almost absent in liver, and is not compensated by expression of another family member (PubMed:10899171). Liver levels of total cholesterol esters are decreased by 87%, while plasma cholesterol levels are increased by 35% (PubMed:10899171). Likewise, skin sterol esters and diol diesters are strongly reduced (PubMed:10854228). Liver triglyceride levels are decreased by 62%, while plasma triglyceride levels are decreased by 67% (PubMed:10899171). The fatty acid composition of liver triglycerides is altered, with a decrease of about 85% in palmitoleate (C16:1) and oleate (C18:1) levels (PubMed:10899171). These defects cannot be compensated by a diet enriched in unsaturated fatty acids (PubMed:10899171, PubMed:11441127). Mice are viable and fertile (PubMed:11533264). Compared to wild-type, they consume about 25% more food, but are leaner and acumulate less white adipose tissue (PubMed:12177411, PubMed:17127673). Their liver glycogen levels are lower than wild-type, except when their diet is supplemented with high levels of triolein (PubMed:17127673). They gain weight and accumulate white adipose tissue when their diet contains high levels of triolein (PubMed:17127673). They loose weight on a diet rich in tristearin, contrary to wild-type (PubMed:17127673). Mutant mice cannot maintain their body temperature when exposed to cold; they display hypoglycemia, depleted liver glycogen levels, and die of hypothermia (PubMed:15210843). Mutant mice display increased levels of mitochondrial fatty acid oxidation and decreased expression of genes that are important for de novo lipogenesis, especially when their diet is enriched in saturated fatty acids (PubMed:12177411, PubMed:17127673). Their brown adipose tissues shows increased lipolysis and fatty acid oxidation (PubMed:15210843). They display increased metabolic rates during the day and the night (PubMed:12177411). Liver, skin and white adipose tissue from mutant mice show strongly decreased levels of palmitoleate and reduced levels of oleate, with increased levels of saturated fatty acids (PubMed:11533264). Likewise, skin and eyelids are deficient in cholesterol esters, wax esters and triglycerides (PubMed:11533264). These defects cannot be compensated by a diet enriched in unsaturated fatty acids (PubMed:11533264). Mutant mice have decreased levels of liver and plasma triglycerides (PubMed:17127673). Likewise, the levels of triglycerides, 1,2-diacylglycerol and free fatty acids are decreased in the brown adipose tissue (PubMed:15210843). Besides, brown adipose tissue, liver and plasma triglycerides are depleted in unsaturated fatty acids and are enriched in saturated fatty acids (PubMed:15210843, PubMed:17127673). A diet enriched in triolein increases liver and plasma levels of triglycerides (PubMed:17127673). Mutant mice display lower fasting insulin levels, normal fasting glucose levels, increased glucose tolerance and increased insulin sensitivity (PubMed:12177411). Mutant mice display alopecia and atrophy of sebaceous glands and Meibomian glands (PubMed:11533264). Besides, they present a narrow eye fissure and their eyes are nearly closed (PubMed:11533264). This eye phenotype is probably due to a defect in the production of meibum, the oily material that prevents drying of the cornea. Scd1 activity is almost absent in liver, and is not compensated by expression of another family member (PubMed:11533264). Strongly reduced levels of lipids containing Delta-9 unsaturated fatty acids in the Harderian gland, leading to strongly reduced levels of 1-alkyl-2,3-diacylglycerol in the Harderian gland (PubMed:11500518). Belongs to the fatty acid desaturase type 1 family. 3D-structure Complete proteome Disease mutation Endoplasmic reticulum Fatty acid biosynthesis Fatty acid metabolism Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Microsome Oxidoreductase Reference proteome Transmembrane Transmembrane helix S SP C A E D MPAHMLQEISSSYTTTTTITAPPSGNEREKVKTVPLHLEEDIRPEMKEDIHDPTYQDEEG PPPKLEYVWRNIILMVLLHLGGLYGIILVPSCKLYTCLFGIFYYMTSALGITAGAHRLWS HRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGW LLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFILPTLVPWYCWGETFVN SLFVSTFLRYTLVLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTF PFDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKATVLARIKRTGDGSHKSS Q08331 Q60964 Q9JM81 CALB2_MOUSE Calretinin CR Calb2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Eye NUCLEOTIDE SEQUENCE OF 1-31 129/Sv PROTEIN SEQUENCE OF 27-50; 124-133; 179-189 AND 234-244 IDENTIFICATION BY MASS SPECTROMETRY OF1 Hippocampus NUCLEOTIDE SEQUENCE [MRNA] OF 82-271 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Calretinin is a calcium-binding protein which is abundant in auditory neurons. Belongs to the calbindin family. Calcium Complete proteome Direct protein sequencing Metal-binding Phosphoprotein Reference proteome Repeat MAGPQQQPPYLHLAELTASQFLEIWKHFDADGNGYIEGKELENFFQELEKARKGSGMMSK SDNFGEKMKEFMQKYDKNSDGKIEMAELAQILPTEENFLLCFRQHVGSSAEFMEAWRKYD TDRSGYIEANELKGFLSDLLKKANRPYDEPKLQEYTQTILRMFDLNGDGKLGLSEMSRLL PVQENFLLKFQGMKLTSEEFNAIFTFYDKDGSGYIDENELDALLKDLYEKNKKEMNIQQL TTYRKSVMSLAEAGKLYRKDLEIVLCSEPPV Q8CFW1 C4N788 Q8C8N6 ANO2_MOUSE Anoctamin-2 Transmembrane protein 16B Ano2 Tmem16b Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION GLYCOSYLATION SUBCELLULAR LOCATION SUBUNIT INTERACTION WITH DLG4 MUTAGENESIS OF 1000-THR--ASN-1002 TISSUE SPECIFICITY C57BL/6J Retina NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-543 C57BL/6J Retina NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-1002 C57BL/6J Eye DEVELOPMENTAL STAGE FUNCTION ACTIVITY REGULATION FUNCTION IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION TISSUE SPECIFICITY TISSUE SPECIFICITY FUNCTION REVIEW REVIEW FUNCTION Calcium-activated chloride channel (CaCC) which may play a role in olfactory signal transduction. Odorant molecules bind to odor-sensing receptors (OSRs), leading to an increase in calcium entry that activates CaCC current which amplifies the depolarization of the OSR cells, ANO2 seems to be the underlying chloride channel involved in this process. May mediate light perception amplification in retina. Channel activity is repressed by chloride inhibitors; strongly by niflumic acid (NFA), partially by flufenamic acid (FFA), and only slightly by meclofenamic acid (MFA), 5-Nitro-2-(3-phenylpropylamino)benzoic acid (NPPB), 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate (SITS), and 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS). Component of a presynaptic protein complex recruited to specialized plasma membrane domains of photoreceptors. Interacts with DLG4 by its C-terminal region. Cell membrane Multi-pass membrane protein Expressed in retina, especially in the photoreceptor synaptic terminals, and in olfactory epithelium, particularly in sensory neurons (OSNs) and cilia (at protein level). Also observed in retinal pigment epithelium (RPE), olfactory bulb, brain, and cortex. Detected in the mantle layer of the neural tube and in the dorsal root ganglia at 14.5 dpc. In developing skin, expression is restricted to basal layers of the epidermis at 16.5 dpc. Glycosylated. 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. Translation N-terminally extended. Probable cloning artifact. Calcium Cell membrane Chloride Chloride channel Complete proteome Glycoprotein Ion channel Ion transport Membrane Reference proteome Transmembrane Transmembrane helix Transport MAAPGLRDIPLLPGSPRRLSSRTVARGSQGPKHGQQYLKVPGHRAPGQRDNSSLHPSQVS RRESSRDRSVINNYLDANEPPSSEARLSRMHFHDNQRKVDYVLAYHYRKRGAHLGHGSPG HSLAVISNGETGKERHGGGPGDVELGPLDALEEERREQRDEFEHNLMAAGLELEKDLESK SQGSVFVRIHAPWQVLAREAEFLKIKVPTKKMYEIKAGGSIAKKFSAILQTLSSPLQPRV PEHSNNRMKNLSYPFSREKMYLYNIQEKDTFFDNATRSRIVHEILKRTACSRANNTMGIN SLIANNIYEAAYPLHDGEYDSPGDDMNDRKLLYQEWARYGVFYKFQPIDLIRKYFGEKIG LYFAWLGLYTSFLIPSSVIGVIVFLYGCATIEEDIPSKEMCDHQNAFTMCPLCDKSCDYW NLSSACGTARASHLFDNPATVFFSIFMALWATMFLENWKRLQMRLGYFWDLTGIEEEEER SQEHSRPEYETKVREKLLKESGKSAVQKLEANSPEDDEDDEDKLTWKDRFPGYLMNFASI LFMIALTFSIVFGVIVYRITTAAALSLNKATRSNVRVTVTATAVIINLVVILILDEIYGA VAKWLTKIEVPKTEQTFEERLILKAFLLKFVNAYSPIFYVAFFKGRFVGRPGSYVYVFDG YRMEECAPGGCLMELCIQLSIIMLGKQLIQNNIFEIGVPKLKKLFRKLKDETEPGESDPD HSKRPEQWDLDHSLEPYTGLTPEYMEMIIQFGFVTLFVASFPLAPVFALLNNVIEVRLDA KKFVTELRRPDAVRTKDIGIWFDILSGIGKFSVIINAFVIAVTSDFIPRLVYQYSYSHNG TLHGFVNHTLSFFNVSQLKEGTQPENSQFDQEVQFCRFKDYREPPWAPNPYEFSKQYWSV LSARLAFVIIFQNLVMFLSVLVDWMIPDIPTDISDQIKKEKSLLVDFFLKEEHEKVKLAD EPTQRSQGGGDRSRRSRAASSAPSGRSQPGSIASSGSQHTNV Q497N7 Q9D433 Q9D460 CF201_MOUSE Uncharacterized protein C6orf201 homolog Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis Complete proteome Reference proteome G A K N L Q MDVDIDPEQLFTEKMPKNYAQPDVLNHTFDLLSNLHKLLPNHLVEVLHSYRSEEDKNKCE KPEFSGLEKILARHQLPKEISLSPKPSLMPSWRRRIINNISGNWKKCHLWQKSTYEPPMG TIVARWTKKNLQPTEDLKSVIQRLSALGPIISVTPSGRQSAVVVFRDITSACKAVSAFQS MSGGSMFQCSWQHRFMAKNKTWSRKCTSKVHLEKRESTVGEPQELHN P97857 E9QMN9 O54768 ATS1_MOUSE A disintegrin and metalloproteinase with thrombospondin motifs 1 ADAM-TS 1 ADAM-TS1 ADAMTS-1 3.4.24.- Adamts1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] 129/SvJ NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Limb Mammary gland CHARACTERIZATION MUTAGENESIS OF GLU-403 FUNCTION FUNCTION INDUCTION Cleaves aggrecan, a cartilage proteoglycan, at the '1691-Glu-|-Leu-1692' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover. Has angiogenic inhibitor activity (By similarity). Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture (By similarity). Zn(2+) Binds 1 zinc ion per subunit. Secreted Extracellular space Extracellular matrix Induced in vitro in colon adenocarcinoma cells by interleukin-1, or in vivo in kidney and heart by lipopolysaccharide. Also induced by LH stimulation in granulosa cells of preovulatory follicles. 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). Calcium Cleavage on pair of basic residues Complete proteome Disulfide bond Extracellular matrix Glycoprotein Heparin-binding Hydrolase Metal-binding Metalloprotease Protease Reference proteome Repeat Secreted Signal Zinc Zymogen E Q S N S T MQPKVPLGSRKQKPCSDMGDVQRAARSRGSLSAHMLLLLLASITMLLCARGAHGRPTEED EELVLPSLERAPGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSPGSEAQH LDPTGDLAHCFYSGTVNGDPGSAAALSLCEGVRGAFYLQGEEFFIQPAPGVATERLAPAV PEEESSARPQFHILRRRRRGSGGAKCGVMDDETLPTSDSRPESQNTRNQWPVRDPTPQDA GKPSGPGSIRKKRFVSSPRYVETMLVADQSMADFHGSGLKHYLLTLFSVAARFYKHPSIR NSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQKQHNSPSDRDPEHYDTAILFTRQ DLCGSHTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKHCAS LNGVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECLMDKPQNPIKLPSDLPG TLYDANRQCQFTFGEESKHCPDAASTCTTLWCTGTSGGLLVCQTKHFPWADGTSCGEGKW CVSGKCVNKTDMKHFATPVHGSWGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCE GKRVRYRSCNIEDCPDNNGKTFREEQCEAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCK LTCEAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGG NGSTCKKMSGIVTSTRPGYHDIVTIPAGATNIEVKHRNQRGSRNNGSFLAIRAADGTYIL NGNFTLSTLEQDLTYKGTVLRYSGSSAALERIRSFSPLKEPLTIQVLMVGHALRPKIKFT YFMKKKTESFNAIPTFSEWVIEEWGECSKTCGSGWQRRVVQCRDINGHPASECAKEVKPA STRPCADLPCPHWQVGDWSPCSKTCGKGYKKRTLKCVSHDGGVLSNESCDPLKKPKHYID FCTLTQCS Q9Z0F5 Q3TUM6 Q8CHQ2 CH25H_MOUSE Cholesterol 25-hydroxylase 1.14.99.38 Cholesterol 25-monooxygenase m25OH Ch25h Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] FUNCTION CATALYTIC ACTIVITY COFACTOR SUBCELLULAR LOCATION GLYCOSYLATION TISSUE SPECIFICITY MUTAGENESIS OF 242-HIS-HIS-243 129/SvEv C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Adipose tissue Bone marrow NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor DISRUPTION PHENOTYPE FUNCTION Catalyzes the formation of 25-hydroxycholesterol from cholesterol, leading to repress cholesterol biosynthetic enzymes (PubMed:9852097). Plays a key role in cell positioning and movement in lymphoid tissues: 25-hydroxycholesterol is an intermediate in biosynthesis of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC), an oxysterol that acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (PubMed:22999953). May play an important role in regulating lipid metabolism by synthesizing a corepressor that blocks sterol regulatory element binding protein (SREBP) processing (PubMed:9852097). In testis, production of 25-hydroxycholesterol by macrophages may play a role in Leydig cell differentiation (PubMed:9852097). AH2 + cholesterol + O2 = 25-hydroxycholesterol + A + H2O cholesterol + H(+) + NADPH + O2 = 25-hydroxycholesterol + H2O + NADP(+) Fe cation Endoplasmic reticulum membrane Multi-pass membrane protein Widely expressed at low level and at higher level in the lung. Weakly expressed in the heart, lung and kidney. N-glycosylated. Mice do not display any apparent alteration in bile acid synthesis and cholesterol metabolism (PubMed:12543708). Belongs to the sterol desaturase family. Complete proteome Endoplasmic reticulum Glycoprotein Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism Transmembrane Transmembrane helix HH EE V A T S N D MGCYNGSELQDLGCSSQLLLQPLWDTIRTREAFTRSPIFPVTFSIITYVGFCLPFVVLDV LYPWVPILRRYKIHPDFSPSVKQLLPCLGLTLYQHLVFVFPVTLLHWVRSPALLPQEAPE LVQLLSHVLICLLLFDTEIFAWHLLHHKVPWLYRTFHKVHHQNSSSFALATQYMSFWELL SLTFFDVLNVAVLRCHPLTIFTFHVINIWLSVEDHSGYDFPWSTHRLVPFGWYGGVAHHD MHHSQFNCNFAPYFTHWDKMLGTLRSAPLPESLCACGERCVNSRERCAVHLIQKKKQT E9Q816 CP2W1_MOUSE Cytochrome P450 2W1 1.14.14.- Cyp2w1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J TISSUE SPECIFICITY Seems to have broad catalytic activity towards several chemicals, including polycyclic aromatic hydrocarbon dihydrodiols and aromatic amines. Active also in the metabolism of indoline substrates and is able to activate aflatoxin B1 into cytotoxic products. Furthermore, it seems to be involved in the oxydation of lysophospholipids and fatty acids. Membrane Endoplasmic reticulum lumen Cell membrane Detected in colon, ileum, and testes. Belongs to the cytochrome P450 family. Cell membrane Complete proteome Endoplasmic reticulum Glycoprotein Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Reference proteome Signal MALLLLGVWGILLLLGLWGLLQGCTRSPSLAPRWPPGPRPLPFLGNLHLLGVTQQDRALM ELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFS SGARWRAGRQFTVRTLQSLGVQQPSMVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCN ITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFPRLGAFLRLHRPVLSKI EEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAG TETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRY ITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRF MKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTM RPPAQTLCVVPRS Q9JM84 A2ART7 CST10_MOUSE Cystatin 10 Carminerin Cst10 DD72 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) TISSUE SPECIFICITY INDUCTION BY HIGH PHOSPHATE DIET NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) FVB/N Salivary gland FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY DEVELOPMENTAL STAGE INDUCTION BY HIGH PHOSPHATE DIET FUNCTION DISRUPTION PHENOTYPE May play a role in the last steps of the chondrocyte differentiation pathway as an inducer of maturation (PubMed:13679380). Induces chondrocyte calcification during endochondral ossification by playing a role in the transcriptional inhibition of ENPP1, a generator of pyrophosphate which inhibits calcification (PubMed:16680148). Possibly impairs the binding of a transcription factor to the ENPP1 promoter (PubMed:16680148). Unlike other cystatins, does not have thiol protease inhibitor activity (PubMed:16680148). Cytoplasm Cytosol Q9JM84-1 1 Q9JM84-2 2 Gene prediction based on EST data. In cartilage, expressed mainly in mature chondrocytes including prehypertrophic and hypertrophic cells (at protein level) (PubMed:13679380). Expressed exclusively in cartilage (PubMed:11856874). In maturing chondrocytes, expression appears at day 3 and increases thereafter. By high phosphate diet. No visible phenotype. Microscopic decrease in the calcification of hypertrophic chondrocytes at the growth plate. Belongs to the cystatin family. Alternative splicing Biomineralization Complete proteome Cytoplasm Disulfide bond Reference proteome Signal MASLLSPSMPVLAAVALTLTLAVIPEASTNAEAKQVVLGGVEPADPKDKEVQKVVKFAVR TYNDMDNDLYLSKPIRLMSASQQVVAGKNYYLKIELGRTTCTKTESNLVDCPFNEQPDQQ KRVICNFQINVAPWLNKMSMTNFNCYNF P19091 ANDR_MOUSE Androgen receptor Dihydrotestosterone receptor Nuclear receptor subfamily 3 group C member 4 Ar Nr3c4 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] INTERACTION WITH RAD54L2 Swiss Webster Embryo INTERACTION WITH RAD54L2 INTERACTION WITH ZNF318 INTERACTION WITH SLC30A9 INTERACTION WITH ZNF318 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis INTERACTION WITH CRY1 INTERACTION WITH ARID4A AND ARID4B INTERACTION WITH CRY1 AND CRY2 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 649-899 IN COMPLEX WITH NCOA2 AND DIHYDROTESTOSTERONE Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. Binds DNA as a homodimer. Part of a ternary complex containing AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the presence of androgen. The ligand binding domain interacts with KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, SPDEF, SRA1, TGFB1I1, ZNF318 and RREB1. The AR N-terminal poly-Gln region binds Ran resulting in enhancement of AR-mediated transactivation. Ran-binding decreases as the poly-Gln length increases. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its transactivation activity. Interacts with RBAK. Interacts via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. Interacts with HIP1 (via coiled coil domain). Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts with MACROD1. Interacts (via ligand-binding domain) with TRIM68. Interacts with TNK2. Interacts with USP26. Interacts with RNF6. Interacts (regulated by RNF6 probably through polyubiquitination) with RNF14; regulates AR transcriptional activity. Interacts with PRMT2 and TRIM24. Interacts with RACK1. Interacts with RANBP10; this interaction enhances hormone-induced AR transcriptional activity. Interacts with PRPF6 in a hormone-independent way; this interaction enhances hormone-induced AR transcriptional activity. Interacts with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with LPXN. Interacts with MAK. Part of a complex containing AR, MAK and NCOA3. Interacts with CRY1 (PubMed:22170608, PubMed:28751364). Interacts with CCAR1 and GATA2 (By similarity). Interacts with BUD31 (By similarity). Interacts with ARID4A (PubMed:23487765). Interacts with ARID4B (PubMed:23487765). Interacts (via NR LBD domain) with ZBTB7A; the interaction is direct and androgen-dependent (By similarity). Interacts with NCOR1 (By similarity). Interacts with NCOR2 (By similarity). Interacts with CRY2 in a ligand-dependent manner (PubMed:28751364). O89110 Casp8 false 2 Nucleus Cytoplasm Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1. Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. In the presence of bound steroid the ligand-binding domain interacts with the N-terminal modulating domain, and thereby activates AR transcription factor activity. Agonist binding is required for dimerization and binding to target DNA. The transcription factor activity of the complex formed by ligand-activated AR and DNA is modulated by interactions with coactivator and corepressor proteins. Interaction with RANBP9 is mediated by both the N-terminal domain and the DNA-binding domain. Interaction with EFCAB6/DJBP is mediated by the DNA-binding domain (By similarity). Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-514 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity). Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity. Phosphorylation at Ser-61 by CDK9 regulates AR promoter selectivity and cell growth. Phosphorylation by PAK6 leads to AR-mediated transcription inhibition (By similarity). Sumoylated on Lys-381 (major) and Lys-500 (By similarity). Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity (By similarity). Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity). In the absence of ligand, steroid hormone receptors are thought to be weakly associated with nuclear components; hormone binding greatly increases receptor affinity. The hormone-receptor complex appears to recognize discrete DNA sequences upstream of transcriptional start sites. Transcriptional activity is enhanced by binding to RANBP9. Belongs to the nuclear hormone receptor family. NR3 subfamily. 3D-structure Complete proteome Cytoplasm DNA-binding Isopeptide bond Lipid-binding Lipoprotein Metal-binding Nucleus Palmitate Phosphoprotein Receptor Reference proteome Steroid-binding Transcription Transcription regulation Ubl conjugation Zinc Zinc-finger MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREAIQNPGPRHPEAANIAPPGACLQQRQET SPRRRRRQQHTEDGSPQAHIRGPTGYLALEEEQQPSQQQAASEGHPESSCLPEPGAATAP GKGLPQQPPAPPDQDDSAAPSTLSLLGPTFPGLSSCSADIKDILNEAGTMQLLQQQQQQQ QHQQQHQQHQQQQEVISEGSSARAREATGAPSSSKDSYLGGNSTISDSAKELCKAVSVSM GLGVEALEHLSPGEQLRGDCMYASLLGGPPAVRPTPCAPLPECKGLPLDEGPGKSTEETA EYSSFKGGYAKGLEGESLGCSGSSEAGSSGTLEIPSSLSLYKSGALDEAAAYQNRDYYNF PLALSGPPHPPPPTHPHARIKLENPLDYGSAWAAAAAQCRYGDLGSLHGGSVAGPSTGSP PATTSSSWHTLFTAEEGQLYGPGGGGGSSSPSDAGPVAPYGYTRPPQGLTSQESDYSASE VWYPGGVVNRVPYPSPNCVKSEMGPWMENYSGPYGDMRLDSTRDHVLPIDYYFPPQKTCL ICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCY EAGMTLGARKLKKLGNLKLQEEGENSNAGSPTEDPSQKMTVSHIEGYECQPIFLNVLEAI EPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYS WMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQIT PQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLT KLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ Q6PCW6 CNFN_MOUSE Cornifelin Cnfn Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Jaw Limb FUNCTION INTERACTION WITH LORICIN AND INVOLUCRIN Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia. Directly or indirectly cross-linked to CE proteins loricin and involucrin (IVL). Cytoplasm Constituent of the scaffolding of the cornified envelope. Belongs to the cornifelin family. Complete proteome Cytoplasm Keratinization Reference proteome MSYPVTSQPQCANTCYQTQLSDWHTGLTDCCNDMPVCLCGTFAPLCLACRISDDFGECCC APYLPGGLHSLRTGMRERYHIQGSVGHDWAALTFCLPCALCQMARELKIRE Q8CCC3 CL056_MOUSE Uncharacterized protein C12orf56 homolog Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Colon Complete proteome Reference proteome MGSESLETLQVILSGGEFMLHTSVWLVPGSLLSSHPVFTFKVKQENNGPTFWRRKVSRTL NESSLRSQQESSTPFKDPTSHPSDLKELSPAGQGTSRPLPTLSSCQSMAATDMPVCSLSL ASSTNEPQELPDPRDAPREGSFRLDGNQSEFGLGNSLPASPLHSCRNLEKEESELHLYII SATSSIFLHLKSSWNNYIIRATLLQDPLCASEHNDVIGKPKPYRSEEKIKHFCQLKSELF LKDNTLRKILCLITELRVAAQRNFILKRLFWKTSELFYFLVNKLHEYLPESRDKHALQNK SQRADELMACIEIIQTLGLMFRETEIESSRLNTLAAKKGTLFNLLVILISKPKVPKSCSK SDAQPVADPTSAEVFFDSQLQKLTLEYTDTATALLYEILLIFQQGNLGLGSTKFAISWMM SFLQSCPPIMAFVARIVEGVVRGLSASFQLLTPCQAVLLYQQFYILRSCLQHSKALAEYI RNDHREEFRYFIHMPALEQRLPGCYPITEPTTQLCHEVLQLIEQKQCAKC O88512 Q2YDV3 AP1G2_MOUSE AP-1 complex subunit gamma-like 2 Gamma2-adaptin G2ad Ap1g2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NMRI Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Lung Pancreas Spleen May function in protein sorting in late endosomes or multivesucular bodies (MVBs). Involved in MVB-assisted maturation of hepatitis B virus (HBV). Probably interacts with AP1S1/Sigma1A-adaptin AP1S2/Sigma1B-adaptin. Probably does not interact with APB1. Interacts with HBV major surface antigen L. Interacts with HBV core protein C in a ubiquitin-dependent manner. Binds ubiquitin. Golgi apparatus membrane Peripheral membrane protein Cytoplasmic side Cytoplasmic vesicle membrane Peripheral membrane protein Endosome membrane Peripheral membrane protein Mainly localized to perinuclear vesicular structures. Colocalizes with HBV major surface antigen L and HBV core protein C in CD63-containing compartments. Colocalizes with HBV major surface antigen L to cis-Golgi-like structures. Widely expressed. Belongs to the adaptor complexes large subunit family. Complete proteome Cytoplasmic vesicle Endosome Golgi apparatus Membrane Protein transport Reference proteome Transport K E MVVHSLRLQDLIEEIRGAKTQAQEREVIQKECAQIRASFRDGDPLQRHRQLAKLLYVHML GYPAHFGQMECLKLIASPRFTDKRVGYLGAMLLLDERHDSHLLITNSIKNDLSQGNQPVQ GLALCTLSTMGSAEMCRDLAPEVEKLLLQPSPYVRKKAILTAVHMIRKDPELSGIFLPPC TKLLRERHHGIQLGTVTLITELCERNPAALRHFRKVVPQLVQILRTLVTTGYSTEHSISG VSDPFLQVQILRLLRILGRNHEESSETMNDLLAQVATNTDTSRNAGNAVLLETVLTIMAI HSAAGLRVLAVNILGRFLLNNDKNIRYVALTSLLQLVQSDHSAVQRHRSTVVECLQETDA SLSRRALELSLALVNSSNVRAMMQELQAFLESCPPDLRADCASGILLAAERFAPSKRWHI DTILHVLTTAGAHVRDDAVANLTQLIGEAEELHTYSVRRLYSALAEDISQQPLVQVAAWC IGEYGDLLLEGNCEETEPFQVEEEDVLALLEKVLQSHMSLPATRGYAITALMKLSTRLRG DNNRIRQVVSIYGSCVDLELQQRAVEYNTLFQKYDHMRAAILEKMPLVERGDPHVKEGGK EKQTEAQPLEVTAPAPTEPQATKLLDLLDLLGDTSEPLSSGHAQHLPPQTPSPGEALIHL LDLPCTPPPPAPIPSVRVFEREGLQLDLSFMRPLETPALLLVTATTTNSSKEDVTHFVCQ AAVPKSFQLQLQAPSGNTIPAQGGLPITQVFRILNPNQAPLRLKLRLTYNHSGQPVQEIF EVDNLPVETWQ O54942 O88789 CLD5_MOUSE Claudin-5 Brain endothelial cell clone 1 protein Lung-specific membrane protein Cldn5 Bec1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] Brain NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] SUBCELLULAR LOCATION TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Ovary Uterus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain Mammary tumor INTERACTION WITH TJP1; TJP2 AND TJP3 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Lung Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Interacts with MPDZ (By similarity). Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. Cell junction Tight junction Cell membrane Multi-pass membrane protein Widely expressed with highest levels in the lung. Belongs to the claudin family. Cell junction Cell membrane Complete proteome Membrane Reference proteome Tight junction Transmembrane Transmembrane helix S N MGSAALEILGLVLCLVGWVGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTG HMQCKVYESVLALSAEVQAARALTVGAVLLALVALFVTLTGAQCTTCVAPGPVKARVALT GGALYAVCGLLALVPLCWFANIVVREFYDPTVPVSQKYELGAALYIGWAASALLMCGGGL VCCGAWVCTGRPEFSFPVKYSAPRRPTANGDYDKKNYV Q8BW75 Q14CG9 Q8C0B2 AOFB_MOUSE Amine oxidase [flavin-containing] B 1.4.3.4 Monoamine oxidase type B MAO-B Maob Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Medulla oblongata Oviduct NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Liver Lung Pancreas Testis ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-248 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine (By similarity). a secondary aliphatic amine + H2O + O2 = a primary amine + an aldehyde + H2O2 FAD Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer (By similarity). Mitochondrion outer membrane Single-pass type IV membrane protein Cytoplasmic side Belongs to the flavin monoamine oxidase family. Acetylation Complete proteome FAD Flavoprotein Membrane Mitochondrion Mitochondrion outer membrane Oxidoreductase Reference proteome Transmembrane Transmembrane helix T S L M MSNKSDVIVVGGGISGMAAAKLLHDCGLSVVVLEARDRVGGRTYTIRNKNVKYVDLGGSY VGPTQNRILRLAKELGLETYKVNEVERLIHFVKGKSYAFRGPFPPVWNPITYLDNNNLWR TMDEMGQEIPSDAPWKAPLAEEWDYMTMKELLDKICWTKSTKQIATLFVNLCVTAETHEV SALWFLWYVKQCGGTTRIISTTNGGQERKFIGGSGQVSERIKDILGDRVKLERPVIHIDQ TGENVIVKTLNHEIYEAKYVISAIPPALGMKIHYSPPLPMLRNQLISRVPLGSVIKCMVY YKEPFWRKKDFCGTMVIEGEEAPIAYTLDDTKPDGTYAAIMGFILAHKARKLVRLTKEER LRKLCELYAKVLNSQEALQPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVGK IFFAGTETASHWSGYMEGAVEAGERAAREILHAIGKIPEDEIWQPEPESLDVPARPITST FLERHLPSVPGLLKLFGLTTILSATALGFLAHKRGLFVHF P25962 A2RS74 Q9QZ98 ADRB3_MOUSE Beta-3 adrenergic receptor Beta-3 adrenoreceptor Beta-3 adrenoceptor Adrb3 Adrb3r B3bar Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] SWR/J NUCLEOTIDE SEQUENCE [GENOMIC DNA] SEQUENCE REVISION NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B) C57BL/6J Brown adipose tissue NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B) Brain NUCLEOTIDE SEQUENCE OF 378-400 Adipose tissue Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis. Interacts with ARRDC3. Cell membrane Multi-pass membrane protein P25962-1 A P25962-2 B White and brown adipose tissues, and digestive tract. Isoform B highest in brain. Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB3 sub-subfamily. Alternative splicing Cell membrane Complete proteome Disulfide bond G-protein coupled receptor Glycoprotein Lipoprotein Membrane Palmitate Receptor Reference proteome Transducer Transmembrane Transmembrane helix RFDGYEGARPFPT SSLLREPRHLYTCLGYP MAPWPHRNGSLALWSDAPTLDPSAANTSGLPGVPWAAALAGALLALATVGGNLLVIIAIA RTPRLQTITNVFVTSLAAADLVVGLLVMPPGATLALTGHWPLGETGCELWTSVDVLCVTA SIETLCALAVDRYLAVTNPLRYGTLVTKRRARAAVVLVWIVSAAVSFAPIMSQWWRVGAD AEAQECHSNPRCCSFASNMPYALLSSSVSFYLPLLVMLFVYARVFVVAKRQRHLLRRELG RFSPEESPPSPSRSPSPATGGTPAAPDGVPPCGRRPARLLPLREHRALRTLGLIMGIFSL CWLPFFLANVLRALAGPSLVPSGVFIALNWLGYANSAFNPVIYCRSPDFRDAFRRLLCSY GGRGPEEPRAVTFPASPVEARQSPPLNRFDGYEGARPFPT Q60590 A1AG1_MOUSE Alpha-1-acid glycoprotein 1 AGP 1 Orosomucoid-1 OMD 1 Orm1 Agp1 Orm-1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-34; ASN-76 AND ASN-94 C57BL/6J Plasma GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94 AND ASN-104 C57BL/6J Plasma IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction. Secreted Contains a beta-barrel that binds various ligands in its interior. Belongs to the calycin superfamily. Lipocalin family. Acute phase Complete proteome Disulfide bond Glycoprotein Pyrrolidone carboxylic acid Reference proteome Secreted Signal Transport MALHTVLIILSLLPMLEAQNPEHANFTIGEPITNETLSWLSDKWFFMGAAFRKLEYRQAI QTMQSEFFYLTTNLINDTIELRESQTIGDQCVYNSTHLGFQRENGTFSKYEGGVETFAHL IVLRKHGAFMLAFDLKDEKKRGLSLYAKRPDITPELREVFQKAVTHVGMDESEIIFVDWK KDRCGQQEKKQLELGKETKKDPEEGQA Q9WVK8 CP46A_MOUSE Cholesterol 24-hydroxylase CH24H 1.14.14.25 Cholesterol 24-monooxygenase Cholesterol 24S-hydroxylase Cytochrome P450 46A1 Cyp46a1 Cyp46 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY FUNCTION CATALYTIC ACTIVITY Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Liver FUNCTION DISRUPTION PHENOTYPE SUBCELLULAR LOCATION SUBCELLULAR LOCATION TISSUE SPECIFICITY IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain CATALYTIC ACTIVITY FUNCTION PATHWAY P450 monooxygenase that plays a major role in cholesterol homeostasis in the brain. Primarily catalyzes the hydroxylation (with S stereochemistry) at C-24 of cholesterol side chain, triggering cholesterol diffusion out of neurons and its further degradation (PubMed:10377398, PubMed:16505352, PubMed:28190002). By promoting constant cholesterol elimination in neurons, may activate the mevalonate pathway and coordinate the synthesis of new cholesterol and nonsterol isoprenoids involved in synaptic activity and learning (PubMed:16505352). Further hydroxylates cholesterol derivatives and hormone steroids on both the ring and side chain of these molecules, converting them into active oxysterols involved in lipid signaling and biosynthesis (By similarity). Acts as an epoxidase converting cholesta-5,24-dien-3beta-ol/desmosterol into (24S),25-epoxycholesterol, an abundant lipid ligand of nuclear NR1H2 and NR1H3 receptors shown to promote neurogenesis in developing brain (By similarity). May also catalyze the oxidative metabolism of xenobiotics, such as clotrimazole (By similarity). cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (24S)-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] cholestanol + O2 + reduced [NADPH--hemoprotein reductase] = (24S)-hydroxycholestanol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] cholesta-5,7-dien-3beta-ol + O2 + reduced [NADPH--hemoprotein reductase] = cholesta-5,7-dien-3beta,24S-diol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] cholesta-5,7-dien-3beta-ol + O2 + reduced [NADPH--hemoprotein reductase] = cholesta-5,7-dien-3beta,25-diol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] cholesta-5,24-dien-3beta-ol + O2 + reduced [NADPH--hemoprotein reductase] = cholesta-5,24Z-dien-3beta,27-diol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] cholesta-5,24-dien-3beta-ol + O2 + reduced [NADPH--hemoprotein reductase] = (24S)-25-epoxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 4beta-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 4beta,24S-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (24S)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (24S,25R)-24,26-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] (24S)-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 24S,25-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 7alpha-hydroxycholesterol + O2 + reduced [NADPH--hemoprotein reductase] = (24S)-7alpha-dihydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] O2 + progesterone + reduced [NADPH--hemoprotein reductase] = 17alpha-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] O2 + reduced [NADPH--hemoprotein reductase] + testosterone = 16beta,17beta-dihydroxyandrost-4-en-3-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] O2 + reduced [NADPH--hemoprotein reductase] + testosterone = 2-hydroxytestosterone + 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] heme Steroid metabolism; cholesterol degradation. Lipid metabolism; C21-steroid hormone metabolism. Endoplasmic reticulum membrane Single-pass membrane protein Microsome membrane Single-pass membrane protein Cell junction Synapse Cell projection Dendrite Detected in the presynaptic and postsynaptic structures. Expressed in high level in the pyramidal cells of the hippocampus, Purkinje cells of the cerebellum, and neuronal cell bodies in layers II/III, V, and VI of the cortex. Expressed in hippocampal and cerebellar interneurons, in retinal ganglion cells, and in a subset of retinal cells localized to the inner nuclear layer (at protein level). Mutant mice are deficient in spatial, associative and motor learning. Belongs to the cytochrome P450 family. Cell junction Cell projection Cholesterol metabolism Complete proteome Endoplasmic reticulum Heme Iron Lipid metabolism Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome Steroid metabolism Sterol metabolism Synapse Transmembrane Transmembrane helix MSPGLLLLGSAVLLAFGLCCTFVHRARSRYEHIPGPPRPSFLLGHLPYFWKKDEDCGRVL QDVFLDWAKKYGPVVRVNVFYKTSVIVTSPESVKKFLMSTKYNKDSKMYRALQTVFGERL FGQGLVSECDYGRWYKQRKVMDLAFSRSSLVSLMETFNEKAEQLVEILEAKADGQTPVSM QDMLTCATIDILAKAAFGMETSMLLGAQKPLSQAVKVMLEGISASRNTLAKFMPGKRKQL REIRESIRLLRQVGKDWVQRRREALKRGEDMPADILTQILKAEEGAQDDEVLLDNFVTFF IAGHETSANHLAFTVMELSRQPEIVARLQAEVDEVVGSKRHLDYEDLGRLQYLSQVLKES LRLYPPAWGTFRLLEEETLIDGVRVPGNTPLLFSTYVMGRMDTYFEDPLTFNPDRFGPGA PKPRFTYFPFSLGHRSCIGQQFAQMEVKVVMAKLLQRIEFRLVPGQRFGLQEQATLKPLD PVLCTLRPRGWQPAPPPPPC Q9D7J7 CPNS2_MOUSE Calpain small subunit 2 CSS2 Calcium-dependent protease small subunit 2 Capns2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Tongue Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. This small subunit may act as a tissue-specific chaperone of the large subunit, possibly by helping it fold into its correct conformation for activity (By similarity). Heterodimer of a large (catalytic) and a small (regulatory) subunit. Cytoplasm Cell membrane Translocates to the plasma membrane upon calcium binding. Calcium Cell membrane Complete proteome Cytoplasm Membrane Metal-binding Reference proteome Repeat MFLAKAILEGADRGLGGALGGLLGGGGQARAGGGNIGGILGGIVNFISEAAAAQYTPEPP PQQQHFTVVEASESEEVRRFRQQFTQLAGPDMEVGATDLMNILNKVLSKHKELKTEGFSL DTCRSIVSVMDSDTTGKLGFEEFKYLWNNIKKWQCVFKQYDSDHSGSLGSSQLHGAMQAA GFQLNEQLYLMIVRRYADEDGGMDFNNFISCLVRLDAMFRAFKALDRDRDGLIQVSIREW LQLTMYS Q3UEG6 B9EIZ8 AGT2_MOUSE Alanine--glyoxylate aminotransferase 2, mitochondrial AGT 2 2.6.1.44 (R)-3-amino-2-methylpropionate--pyruvate transaminase 2.6.1.40 Beta-ALAAT II Beta-alanine-pyruvate aminotransferase D-AIBAT Agxt2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Liver FUNCTION DISRUPTION PHENOTYPE SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-261; LYS-303; LYS-416 AND LYS-419 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56; LYS-70; LYS-83; LYS-261; LYS-416; LYS-419 AND LYS-453 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. glyoxylate + L-alanine = glycine + pyruvate (R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine pyridoxal 5'-phosphate Homotetramer. Mitochondrion Knockout mice are hypertensive. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Acetylation Aminotransferase Complete proteome Mitochondrion Pyridoxal phosphate Reference proteome Transferase Transit peptide MSLAWRNLQKPFYLETSLRILQMRPSLSLGASRIAVPKLTLHTKHSMPPCDFSPEKYQSL AYSRVLAIHKQHLSPVDTAYFRKPLLLHQGHMEWLFDSEGNRYLDFFSGIVTVSVGHCHP KVSAVAKKQIDRLWHTSSVFFHSPMHEYAEKLSALLPEPLKVIFLVNSGSEANDLAMVMA RAHSNHTDIISFRGAYHGCSPYTLGLTNVGIYKMEVPGGIGCQSTMCPDVFRGPWGGIHC RDSPVQTVRDCSCAPDCCQAKERYIEQFKDTLNTSVATSIAGFFAEPIQGVNGVVQYPKE FLKEAFALVRERGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAAV VTTPEIAKSLAKRLLHFSTFGGNPLACAIGSAVLEVIEEENLQRNSQEVGTYMLLKFAKL RDEFDIVGDVRGKGLMVGIEMVQDKISRQPLPKTEVNQIHEDCKDMGLLVGRGGNFSQTF RIVPPMCVTKMEVDFAYEVFRAALIQHMERRAK Q9CPW0 Q6P2K4 Q6ZQ31 CNTP2_MOUSE Contactin-associated protein-like 2 Cell recognition molecule Caspr2 Cntnap2 Kiaa0868 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) C57BL/6J Embryo Head NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1332 (ISOFORMS 1 AND 2) C57BL/6J FVB/N Brain Mammary gland FUNCTION SUBCELLULAR LOCATION INTERACTION WITH KCNA2 TISSUE SPECIFICITY DEVELOPMENTAL STAGE PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1304 AND SER-1307 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain FUNCTION SUBCELLULAR LOCATION DISRUPTION PHENOTYPE TISSUE SPECIFICITY Required, with CNTNAP1, for radial and longitudinal organization of myelinated axons (PubMed:25378149). Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the juxtaparanodal region of the axo-glial junction (Probable) (PubMed:25378149). Interacts (via C-terminus) with KCNA2. Membrane Single-pass type I membrane protein Cell projection Axon Cell junction Paranodal septate junction Expressed in the juxtaparadonal region. Q9CPW0-1 1 Q9CPW0-2 2 No experimental confirmation available. In sciatic nerve predominantly found at the juxtaparanodal regions (at protein level). Detected at postnatal day 8 in sciatic nerve at the paranodes and the juxtaparanodal region. Is progressively translocated to the adjacent juxtaparanodal region until it becomes completely absent from the paranodes in the adult. Mutants don't show difference of Ranvier nodes length and width compared to wild-type littermates. Double mutants CNTNAP1 and CNTNAP2 have wider Ranvier nodes. Belongs to the neurexin family. Alternative splicing Cell adhesion Cell junction Cell projection Complete proteome Disulfide bond EGF-like domain Glycoprotein Membrane Phosphoprotein Reference proteome Repeat Signal Transmembrane Transmembrane helix G E Q H K N MVMSLRAGYRAALSLWILSSFICRAWTAPSTFQKCDEPLISGLPHVSFSSSSSLSSSYAP GYAKINKRGGAGGWSPSDSDHYQWLQVDFGNRKQISAIATQGRYSSSDWVTQYRMLYSDT GRNWKPYHQDGNIWAFPGNINSDSVVRHDLQHAVVARYVRIVPLDWNGEGHIGLRAEVYG CAYWADVINFDGHGVLPYRFRNKKMKTLKDVIALKFKTSESEGVLLHGEGQQGDYITLEL KKAKLVLSLNLGSNQLGPIYGHTSVTSGSLLDDHHWHSVLIERQGRSINLTLDRSMQHFR TNGEFDYLDLDYEITFGGIPFSGKPSSSNRKNFKGCMESINYNGVNITDLARRKKLGPSN MGNLSFSCVEPYTVPVFFNATSYLEVPGRLNQDLFSVSFQFRTWNPSGLLLFSHFADNLG NVEIDLVESKVGVHINNTQTKTSQIDISSGSGLNDGQWHEVRFLAKENFAVLTIDGDEAS AVRTNSPLQVKTGEKYFFGGFLNHMNNASYSALQPSFQGCMQLIQVDDQLVNLYEVAQRK PGSFANVTIDMCAIIDRCVPNHCEHGGKCSQTWDSFKCTCDETGYSGATCHNSIYEPSCE AYKHLGQTSNYYWIDPDGSGPLGPLKVYCNMTEDKVWTIVSHDLQMQTTVVGYNPEKYSV TQLIYSASMDQISAITSSAEYCEQYVSYFCRMSRLLNTPDGSPYTWWVGKANEKHYYWGG SEPGIQKCACGIERNCTDPKYYCNCDADYKQWRKDAGFLSYKDHLPVSQVVVGDTDRQGS EAKLSVGPLRCQGDRNYWNAASFPNPSSYLHFSTFQGETSADISFYFKTLIPRGVFLENL GNTDFIKLELKSATEVSFSFDVGNGPVEIVVRSPSPLNDDQWHRVTAERNVKQASLQVDR LPQQIRKAPTEGHTRLELYSQLFVGGAGGQQGFLGCIRSLRMNGVTLDLEERAKVTSGFK SGCSGHCTSYGANCENGGKCIEKYHGYSCDCSNTAYDGTFCNKDVGAFFEEGMWLRYNFQ APAVTARDTGSRAENSADQQQHLAPDLAQEQIHFSFSTTKAPCILLYVSSLTTDFLAVLV KPTGNLQIRYNLGGTREPFNIDVDHRNMANGQPHSVNITRHERTIILKLDHYPAVGYHLP SSSDTLFNSPKSLFLGKVIETGKIDQEIHKYNTPGFTGCLSRVQFNHIAPLKAALRQTNA SAHVHIQGELVESNCGASPLTLSPMSSATDPWHLDHLDSASADFPYNPGQGQAIRNGVNR NSAIIGGVIAVVIFTILCTLVFLIRYMFRHKGTYHTNEAKGAESAESADAAIMNNDPNFT ETIDESKKEWLI A2A8L1 Q6ZQB2 CHD5_MOUSE Chromodomain-helicase-DNA-binding protein 5 CHD-5 3.6.4.12 ATP-dependent helicase CHD5 Chd5 Kiaa0444 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1245-1946 Brain FUNCTION IN CELL PROLIFERATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1556 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain IDENTIFICATION IN A NURD-LIKE COMPLEX TISSUE SPECIFICITY DEVELOPMENTAL STAGE FUNCTION IN TRANSCRIPTION UNMETHYLATED HISTONE H3K4-BINDING PHD DOMAINS SUBCELLULAR LOCATION MUTAGENESIS OF ASP-346; GLY-355; ASP-361; ASP-415; CYS-432 AND ASP-434 FUNCTION IN NEURON DIFFERENTIATION HISTONE H3K27ME3-BINDING SUBCELLULAR LOCATION TISSUE SPECIFICITY DEVELOPMENTAL STAGE FUNCTION IN SPERMATOGENESIS DISRUPTION PHENOTYPE TISSUE SPECIFICITY Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. ATP + H2O = ADP + H(+) + phosphate May be part of a nucleosome remodeling and histone deacetylation, NuRD-like, complex composed at least of GATAD2B, HDAC1, HDAC2 and MTA3. Nucleus Associates with heterochromatin. Specifically expressed by neurons in brain, retina and adrenal gland (at protein level). Also detected in testis. Detected at 15.5 dpc, expression increases after birth and to adulthood. Expression increases in late-stage neuronal progenitor during their terminal differentiation. The PHD domains mediate specific binding to histone H3 unmethylated at 'Lys-4' and may preferentially recruit the protein to transcriptionally inactive genes. The chromo domains mediate specific binding to histone H3 trimethylated at 'Lys-27' (H3K27me3) and may be required in neuron differentiation for proper gene regulation. Methylated at Gln-1392 by N6AMT1. Mutant males are infertile. Mating occurs, but the males are sterile, displaying abnormal spermatogenesis. Disruption of the gene has no effect on the fertility of females. Infertility is due to sperm morphological abnormalities and complete immotility that are observed in all mice. A variable sperm counts, with a complete absence is some individuals is also observed. Spermatogenesis is normal from spermatogonia through meiotic division of spermatocytes. However, at stage IX, step 9, abnormal nuclear morphology of differentiating spermatids appears. It is associated with increased histone retention and decreased histone H4 hyperacetylation, an important step in spermatid chromatid condensation. Finally, spermiation is also affected. Belongs to the SNF2/RAD54 helicase family. ATP-binding Chromatin regulator Complete proteome Differentiation DNA-binding Helicase Hydrolase Metal-binding Methylation Neurogenesis Nucleotide-binding Nucleus Phosphoprotein Reference proteome Repeat Spermatogenesis Transcription Transcription regulation Tumor suppressor Zinc Zinc-finger D A G A D A D A C W D A MRGPLGTEEELPRLFAEEMENEEEMSEEEDGGLEGFEDFFPAEPVSLPKKKPKKLKESKS SKGKRKKKEGSNDEMSDNEEDLEEKSESEGSDYSPTKKKKKKLKEKKEKKEKKEKRKKRG EDEDDNDDGGLKEPKSSGQLMAEWGLDDVDYLFSEDDYHTLTNYKAFSQFLRPLIAKKNP KIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTIAPPLAISPQQVPQTL PIRKAKTKEGKGPGVRKKNKGAKDSKKKGRGKRVAGLKFRFGGISKRKKGSSSEEDERED SDLDNASIHSSSVRSECSAALGKKNKRRRKKKRIDDGDGYETDHQDYCEVCQQGGEIILC DTCPRAYHLVCLDPELEKAPEGKWSCPHCEKEGIQWEPKDDDEEEEEGGCEEEEDDHMEF CRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWT EPPAPFVVGLPGPEVEPGMPPPRPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVM YRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMVHRIL NHSFDKKGDIHYLIKWKDLPYDQCTWEIDEIDIPYYDNLKQAYWGHRELMLGEDARLPKR LVKKGKKLKDDKQEKPPDTPIVDPTVKFDKQPWYIDATGGTLHPYQLEGLNWLRFSWAQG TDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVV TYTGDKESRSVIRENEFSFEDNAIRGGKKVFRMKKEVQIKFHVLLTSYELITIDQAILGS IEWACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERF NNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSQMQKK YYKFILTRNFEALNSKGGGNQVSLLNIMMDLKKCCNHPYLFPVAAVEAPVLPNGSYDGSS LVKSSGKLMLLQKMLKKLRDEGHRVLIFSQMTKMLDLLEDFLEYEGYKYERIDGGITGGL RQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIG QNKKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKSGSMTKQELDDILKFGTE ELFKDDVEGMMSQGQRPTTPIPDIQSTKGGSLTAGAKKKHGSTPPGDNKDVEDSSVIHYD DAAISKLLDRNQDATDDTELQNMNEYLSSFKVAQYVVREEDGVEEVEREVIKQEENVDPD YWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDASQEDQEWQDELSDNQSEYSIGSED EDEDFEERPEGQSGRRQSRRQLKSDRDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMR WGMPPQDAFNSHWLVRDLRGKSEKEFRAYVSLFMRHLCEPGADGAETFADGVPREGLSRQ HVLTRIGVMSLVRKKVQEFEHVNGKYSTPDLVPEGAEGKKPGEVISSDPNTPVPASPAQL PPAPLGLTDKMEAQLGYTDEKESGMQKPKKSLEIQTLPTALDRVEGEDKHQSSDSKDRAR EERTEEVEKAQGSPEQPLKEEVLPDKEPIPDKPELSLGHSGDFRPDDPKTEEKEPGETQQ NGDREEDEEGKKEDKNGKFKFMFNIADGGFTELHTLWQNEERAAVSSGKIYEIWHRRHDY WLLAGIVTHGYARWQDIQNDPRYMILNEPFKSEIHKGNYLEMKNKFLARRFKLLEQALVI EEQLRRAAYLNMTQDPNHPAMALNARLAEVECLAESHQHLSKESLAGNKPANAVLHKVLN QLEELLSDMKADVTRLPSMLSRIPPVAARLQMSERSILSRLTNRAGDPTIQQTSSRRRDF PLFQRSFPAEPSHLPNPRGREKLQPF Q8CI96 Q8BW09 Q921Q4 Q9D2S6 CLIP4_MOUSE CAP-Gly domain-containing linker protein 4 Restin-like protein 2 Clip4 Rsnl2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) FVB/N Mammary gland Salivary gland PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Lung STRUCTURE BY NMR OF 266-354 AND 617-696 Q8CI96-1 1 Q8CI96-2 2 No experimental confirmation available. Q8CI96-3 3 No experimental confirmation available. 3D-structure Alternative splicing ANK repeat Complete proteome Phosphoprotein Reference proteome Repeat NDK VRD S Y C S A S Q K MTIEDLPDIPLEGSSLIGRYPFLFTGSDTSVIFSISAAPMPSDCEFSFFDPNDASCQEIL FDPKTSVSELFAILRQWVPQVQQNIDIIGNEILKRGCNVNDRDGLTDMTLLHYTCKSGAH GIGDIETAVKFAAQLIDLGADASLRSRWTNMNALHYASYFDVPELIRVILKTSKPKDVDA TCSDFNFGTALHIAAHNLCAGAVKTLLELGANPAFRNDKGQIPAEVVPDPVDMPLEMADA AAIAKEIKQMLLDAVPLPCTSAKAVLPNSDHTTSRAMLTSLGLKLGDRVVIAGQKVGTLR FCGTTEFASGQWAGIELDEPEGKNNGSVGRVQYFKCAPKYGIFAPLSKISKLKDGRKTTT HTPSTRATPHARSQKVDVAHFTSRVNSGLTTSKKETASESTLTLPPSEEPKTVAENDAAQ PGSMSSSSSSSSLDHKQSYPKKLTTSSGGKKTLSKSPSLPSRASAGLKSSATSAANNSHH EGALHLGERVLVVGQRVGTIKFFGTTNFAPGYWYGIELEKPHGKNDGSVGGVQYFSCSPR YGIFAPPSRVQRLSDSLDTLSEISSNKQNHSYPGFRRSFSTTSASSQKEINRRNAFAKTK TTLRRSWSSSTTAGGLEGTVKLHEGSQVLLTSSNEMATVRYVGPTDFASGIWLGLELRSA KGKNDGAVGDKRYFTCKPNYGVLVRPSRVTYRGISGSKLIDENC Q80YS6 Q3UGX1 Q6ZPE4 AFAP1_MOUSE Actin filament-associated protein 1 110 kDa actin filament-associated protein AFAP-110 Afap1 Kiaa3018 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Melanocyte Placenta Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-284; SER-666; SER-669; THR-676 AND SER-680 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Kidney Lung Pancreas Spleen Testis Can cross-link actin filaments into both network and bundle structures. May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton (By similarity). Monomer and homomultimer. Interacts via its C-terminus with F-actin; probably involving AFAP1 multimers. Interacts with activated SRC SH3-SH2 domains. Interacts via its PH 1 domain with PRKCA, PRKCB and PRKCI (By similarity). Cytoplasm Cytoskeleton Stress fiber Phosphorylated on tyrosine residues by SRC. Acetylation Actin-binding Coiled coil Complete proteome Cytoplasm Cytoskeleton Phosphoprotein Reference proteome Repeat SH3-binding G R K R S G G D MEELIVELRLFLELLDHEYLTSTVREKKAVLTNILLRLQSSKGFEVKDHAQKAEANNLPA PPQMPLPEIPQPWLPPDSGPPPLPTSSLPEGYYEEAVPLSPGKAPEYITSNYDSDAMSSS YESYDEEEEDGKGKKTRHQWPSEEASMDLVKDAKICAFLLRKKRFGQWTKLLCVIKDTKL LCYKSSKDQQPQMELPLQGCSITYIPRDSKKKKHELKITQQGTDPLVLAVQSKEQAEQWL KVIKEAYSGCSGPVDPECSPPPSTSAPVNKAELEKKLSSERPSSDGEGGVENGVTTCNGK EQAKRKKPSKSEAKGTVSKVTGKKITKIIGLGKKKPSTDEQTSSAEEDVPTCGYLNVLSN SRWRERWCRVKDSKLILHKDRADLKTHLVSIPLRGCEVIPGLDSKHPLTFRLLRNGQEVA VLEASSSEDMGRWIGILLAETGSSTDPGALHYDYIDVEMSANVIQTAKQTFCFMNRRAVS TSPYLGSLSNGYAHPSGTALHYDDVPCVNGSLKNKKPPASSNGVPVKGKAPSSQQKKVET AGGVKRTASNAEQYKYGKNRVEADAKRLQSKEEELLKRKEALRNRLAQLRKERKDLRAAI EVNAGRKTQAALEDKLKRLEEECKQREAERVSLELELTEVKESLKKALAGGVTLGLAIEP RSGTSSPQSPVFRHRTLENSPISSCDTSDAEGPLPVNSAAVLKKSQPSSGSSPCRGHVLQ KAKEWELKNGT E9Q4J9 B9EJ67 AGRF2_MOUSE Adhesion G-protein coupled receptor F2 G-protein coupled receptor 111 G-protein coupled receptor PGR20 Adgrf2 Gpr111 Pgr20 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain TISSUE SPECIFICITY DEVELOPMENTAL STAGE DISRUPTION PHENOTYPE Orphan receptor. Membrane Multi-pass membrane protein Mainly expressed in skin and heart, and very weakly in lung and spleen. Detected in all epidermal layers of skin. Expressed during embryonic development in the skin starting at embryonic day 12 with the formation of the basal layer of the skin. No visible phenotype. Most adhesion GPCRs undergo autoproteolysis at the GPS domain. ADGRF2 is not autoproteolyzed at the GPS motif because of the lack of a consensus catalytic triad sequence within GPS domain. Belongs to the G-protein coupled receptor 2 family. Adhesion G-protein coupled receptor (ADGR) subfamily. Complete proteome Glycoprotein Membrane Reference proteome Signal Transmembrane Transmembrane helix W R MIPAHWLYCLMLLLPIESCRILCQASSKSKEKVTSRPHDVCDGVCNNNGTPCFQSCPPDS EGNMKFACKAKKWHKVTETCHTLNTHSIFEEDKELYSVQSSDSTIRTHMFHRELKTIMDT LMEKCPKDLSCVIKGIERSPRMPGNIAVVVQLLHNISTTLTKDVNEEKMQSYSAMANHIL NSKSISNWTFIQDRNSSCVLLQSIHSFASKLFMKEHLINISHVFIHTLGTVVSRGSLGKN FTFSMRINETSDKVTGRLLLSPEELQKVPSAFQVISIAFPTLGAILEASLLENVTVNGLV LSVILPEELKNISLIFEKIRKSGERKSQCVGWHSLESRWDWRACKTIQENSRQAVCRCRP NKLYTSFSILMSPNTLESPVLTYITYIGLGISICSLIICLAIEVLVWSQVTKTEISYLRH LCIANIAATLLMADAWFIVASFLSGPVLHHNGCVAATFFVHFFYLSVFFWMLAKALLILY GILIVFHTLPKSCLVASLFSVGYGCPLVIAIITLAVTEPGKGYLRPEACWLNWDMTKALL AFVVPALAIVVVNLITVTMVIIKTQRAAIGSSMFQEVRAIVRICKNIAILTPLLGLTWGF GIATVINGHSLAFHIIFSLLNALQVSPDAAVDSELRECVHRFCG Q02788 Q05505 Q8C972 Q8K229 CO6A2_MOUSE Collagen alpha-2(VI) chain Col6a2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary gland NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-343 C57BL/6J Cerebellum NUCLEOTIDE SEQUENCE [MRNA] OF 271-1034 NUCLEOTIDE SEQUENCE [MRNA] OF 271-605 C57BL/6J Fibroblast NUCLEOTIDE SEQUENCE [MRNA] OF 664-1034 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Heart Lung Pancreas Collagen VI acts as a cell-binding protein. Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-6(VI). Interacts with CSPG4 (By similarity). Secreted Extracellular space Extracellular matrix Membrane Peripheral membrane protein Recruited on membranes by CSPG4. Highly expressed in adipose tissue, lung, adrenal glands and ovary. Lower levels in testis, tongue, skin, kidney, heart, intestine and spleen. No expression in skeletal muscle or liver. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Belongs to the type VI collagen family. Translation N-terminally extended. Cell adhesion Collagen Complete proteome Extracellular matrix Glycoprotein Hydroxylation Membrane Phosphoprotein Reference proteome Repeat Secreted Signal S P V L H S A S L Q TGNDS GNDSL KQ TR MTTIKMLQGPLSVLLIGGLLGVLHAQQQEAISPQEQEAVSPDISTTERNNNCPEKADCPV NVYFVLDTSESVAMQSPTDSLLYHMQQFVPQFISQLQNEFYLDQVALSWRYGGLHFSDQV EVFSPPGSDRASFTKSLQGIRSFRRGTFTDCALANMTQQIRQHVGKGVVNFAVVITDGHV TGSPCGGIKMQAERAREEGIRLFAVAPNRNLNEQGLRDIANSPHELYRNNYATMRPDSTE IDQDTINRIIKVMKHEAYGECYKVSCLEIPGPHGPKGYRGQKGAKGNMGEPGEPGQKGRQ GDPGIEGPIGFPGPKGVPGFKGEKGEFGSDGRKGAPGLAGKNGTDGQKGKLGRIGPPGCK GDPGSRGPDGYPGEAGSPGERGDQGAKGDSGRPGRRGPPGDPGDKGSKGYQGNNGAPGSP GVKGGKGGPGPRGPKGEPGRRGDPGTKGGPGSDGPKGEKGDPGPEGPRGLAGEVGSKGAK GDRGLPGPRGPQGALGEPGKQGSRGDPGDAGPRGDSGQPGPKGDPGRPGFSYPGPRGTPG EKGEPGPPGPEGGRGDFGLKGTPGRKGDKGEPADPGPPGEPGPRGPRGIPGPEGEPGPPG DPGLTECDVMTYVRETCGCCDCEKRCGALDVVFVIDSSESIGYTNFTLEKNFVINVVNRL GAIAKDPKSETGTRVGVVQYSHEGTFEAIRLDDERVNSLSSFKEAVKNLEWIAGGTWTPS ALKFAYNQLIKESRRQKTRVFAVVITDGRHDPRDDDLNLRALCDRDVTVTAIGIGDMFHE THESENLYSIACDKPQQVRNMTLFSDLVAEKFIDDMEDVLCPDPQIVCPELPCQTELYVA QCTQRPVDIVFLLDGSERLGEQNFHKVRRFVEDVSRRLTLARRDDDPLNARMALLQYGSQ NQQQVAFPLTYNVTTIHEALERATYLNSFSHVGTGIVHAINNVVRGARGGARRHAELSFV FLTDGVTGNDSLEESVHSMRKQNVVPTVVAVGGDVDMDVLTKISLGDRAAIFREKDFDSL AQPSFFDRFIRWIC Q8C6K9 A6H587 A6H588 A6H589 A6H590 CO6A6_MOUSE Collagen alpha-6(VI) chain Col6a6 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) SUBUNIT SUBCELLULAR LOCATION TISSUE SPECIFICITY C57BL/6J Lung NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) C57BL/6J Ovary Collagen VI acts as a cell-binding protein. Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-4(VI) or alpha-5(VI) or alpha-6(VI). Secreted Extracellular space Extracellular matrix Deposed in the extracellular matrix of skeletal muscle. Q8C6K9-1 1 Q8C6K9-2 2 No experimental confirmation available. In newborn, it is expressed in lung, heart, kidney, muscle, brain, intestine, skin, femur and sternum. In adult, it is expressed in lung, heart, muscle, ovary, brain, liver and sternum. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Belongs to the type VI collagen family. Alternative splicing Cell adhesion Collagen Complete proteome Extracellular matrix Glycoprotein Hydroxylation Reference proteome Repeat Secreted Signal N S H N MLLVLCLTMICFHVCVNQDSGPEYADVVFLVDSSDHLGLKSFPLVKTFIHKMISSLPIEA NKYRVALAQYSDALHNEFQLGTFKNRNPMLNHLKKNFGFIGGSLKIGNALQEAHRTYFSA PTNGRDKKQFPPILVVLASAESEDDVEEAAKALREDGVKIISVGVQKASEENLKAMATSQ FHFNLRTARDLSVFAPNMTEIIKDVTQYREGMADDIIVEACQGPSVADVVFLLDMAINGS QEDLDHLKAFLGESISALDIKENCMRVGLVTYSNETRVISSLSTGNNKTEVLQRIQDLSP QVGQAYTGAALRKTRKEIFSAQRGSRKNQGVPQIAVLVTHRASEDNVTKAAVNLRREGVT IFTMGIEGANPDELEKIASHPAEQFTSKLGNFSELATHNQTFLKKLRNQITHTVSVFSER TETLKSACVDTEEADIYLLIDGSGSTQPTDFHEMKTFLSEVVGMFNIAPHKVRVGAVQYA DTWDLEFEISKYSNKPDLGKAIENIRQMGGNTNTGAALNFTLKLLQRAKKERGSKVPCHL VVLTNGMSRDSVLGPAHKLREENIRVHAIGVKEANQTQLREIAGEEKRVYYVHEFDALRN IRNQVVQEICAEEACRDMKADIMFLVDSSGSIGPENFSKMKMFMKNLVSKSQIGADRVQI GVVQFSHENKEEFQLNTFMSQSDIANAIDRMTHIGETTLTGSALTFVSQYFSPDKGARPN VRKFLILITDGEAQDIVRDPAIALRKEGVIIYSVGVFGSNVTQLEEISGKPEMVFYVENF DILQHIEDDLVLGICSPREECKRIEVLDVVFVIDSSGSIDYQEYNIMKDFMIGLVKKADV GKNQVRFGALKYADDPEVLFYLDELGTKLEVVSVLQNDHPMGGNTYTAEALAFSDHMFTE ARGSRLHKGVPQVLIVITDGESHDAEKLNTTAKALRDKGILVLAVGIAGANSWELLAMAG SSDKYYFVETFGGLKGIFSDVSASVCNSSKVDCEIEKVDLVFLMDGSNSIHPDDFQKMKG FLVSVVQDFDVSLNRVRIGVAQFSDSYRSEFLLGTFTGEREISTQIEGIQQIFGYTHIGD ALRKVKYYFQPDMGSRINAGTPQVLLVLTDGRSQDEVAQAAEELRHKGVDIYSVGIGDVD DQELVQITGTAEKKLTVHNFDELKKVKKRIVRNICTSGGESNCFVDVVVGFDISSLQRGQ TLLEGQPWMGSYLQDLLRAISSLNGVSCEVGTETQVSIAFQVTNAMERYPSKFEIYSENI LSSLQGVTVNGPSRLNANLLSSLWDTFQNKSAARGKVVLLFSDGLDDGIEKLEQKSDELR KEGLNALITIAVDGAADSSDLADLLYIEFGKGFEYRTQFTIGMRNLGSQLSRQLINVAER TCCCLLCKCTGGDGAMGDPGSAGKKGPPGFKGSDGYLGEEGIAGERGASGPMGEQGTKGC FGAKGPKGTRGLSGEEGEVGEDGLDGLDGEQGDHGIPGRRGEKGDEGSQGNPGRRGAAGD RGAKGLRGDPGTPGRDSSIQGPKGLKGDLGRQGRRGWPGSPGTPGSRRKMVVHGRRGHIG PQGNPGTPGPDGLAGSPGLRGPQGPRGEVGEKGEKGSLGMKGPQGPPGPGGQAGSQGHLG SQGNKGEPGDLGEKGAAGFPGPRGLQGDDGSPGYGSIGRKGTKGQEGFPGESGLKGDIGD PGDPGEAGPKGARGKTVSAGIPGEPGSPGEPGPPGRKGVKGARGLASFSTCDLIQYVRDH SPGRHGKPECPVHPTELVFVLDQSRDVTEQDFERMKGMMVSLVRDVKVREANCPVGARVA ILAYNSHTRHLIRFSDAYRKDQLLTAIKALPYERSSDSREIGKAMRFISRNVFKRTLPGA HVRRIATFFSSGPSADAQTITTAAMEFSALDIVPVVIAFSNVPSVKRAFSIDDTGTFQVI VVPSGSDEGPALERLQRCTFCYDLCKPDASCDQAKPPPIQSYLDTAFLLDGSRHVGSAEF EDMRDFLEALLDHFEITSEPETSVTGDRVALLSHAPLDFLPNTQRSPVRTEFNLTSYSSK RLMKRHVDQAVQQLHGDAFLGHALGWALDNVFLNTPNLRRNKVIFVISAGETSHLDAETL KKESLRAKCHGYALFVFSLGPDWDDKELEDLASHPVDQHLIQLGRIHKPDHGYSVKFVKS FINSIRHGINKYPPVNLKAKCNRLGSRDLKPPPRQFRSFVPGPQKANLKDHTAEAAKLFQ DKKRLSSMLKGGRATISSLSRSTRYAFKQGKEAIKATSKLGKRSA Q05AA6 Q61095 Q8C4R1 DRP2_MOUSE Dystrophin-related protein 2 DRP-2 Drp2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Head NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain NUCLEOTIDE SEQUENCE [MRNA] OF 391-862 TISSUE SPECIFICITY SUBCELLULAR LOCATION TISSUE SPECIFICITY IDENTIFICATION IN A COMPLEX WITH PRX; UTRN; DMD AND DAG1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain INTERACTION WITH PRX IDENTIFICATION BY MASS SPECTROMETRY PHOSPHORYLATION AT SER-748 AND THR-910 DISRUPTION PHENOTYPE FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY SUBCELLULAR LOCATION Required for normal myelination and for normal organization of the cytoplasm and the formation of Cajal bands in myelinating Schwann cells (PubMed:22764250). Required for normal PRX location at appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane (PubMed:22764250). Possibly involved in membrane-cytoskeleton interactions of the central nervous system. Interacts with PRX; this enhances phosphorylation (PubMed:22764250). Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (PubMed:11430802). Cell junction Synapse Postsynaptic cell membrane Postsynaptic density Cell projection Dendrite Perikaryon Cell membrane Peripheral membrane protein Detected in Schwann cells at periaxonal myelin membranes. Detected in quadriceps nerve Schwann cells (PubMed:22764250). Detected in sciatic nerve (PubMed:11430802, PubMed:22764250). Detected in trigeminal nerve Schwann cells (at protein level) (PubMed:11430802). Detected in brain and spinal cord (PubMed:8640231). Mice with a Schwann cell-specific gene disruption show no obvious impairment of nerve conduction velocity and display no visible defects of their motor skills. After six months, about 6% of their nerve fibers present myelination defects, including myelin outfoldings, focal hypermyelination, and onion bulbs with thin myelin and supernumerary Schwann cells. At the molecular level, Schwann cell-specific gene disruption impairs formation of Cajal bands and location of Prx in patches that colocalize with appositions between the abaxonal surface of the myelin sheath and the Schwann cell plasma membrane. Cytoplasm from mutant Schwann cells forms an annulus under the cell membrane, insted of being strictly compartmentalized. Besides, mutant nerves display increased numbers of Schmidt-Lanterman incisures. Cell junction Cell membrane Cell projection Complete proteome Membrane Metal-binding Phosphoprotein Postsynaptic cell membrane Reference proteome Repeat Synapse Zinc Zinc-finger I F V VLHRV MQPLVMQGCPYTLPRCHEWHAADRFHHSSSLRNTCPQPQVRAAVTIPAPPWDGAGDPCLS PKLLNGTVGATGPLEPSAMNLCWNEIKKKSHNLRARLEAFSDLSGKLQLPLREIIDWLSQ KDEELSAQLPLQGDVALVQQEKETHAAFMEEVKSKGPYISSVLESAQAFLSQHPFEELEE SQSESKDTSPRQRIQNLSRFVWKQATVASELWEKLTARCVDQHRHIEHTLEHLLEIQGAM EELSSTLTQAEGVRATWEPIGDLFIDSLPEHIQAIKLFKEEFSPVKDGVKLVNDLAHQLA ISDVHLSMENSRALEQINIRWKQLQVSVAERLKQLQDAHRDFGPGSQHFLSTSVQVPWER AISPNKVPYYINHQAQTTCWDHPKMTELYQTLADLNNIKFSAYRTAMKLRRVQKALRLDL VTLTTALEIFNEHDLQASEHVMDVVEVIHCLTALYERLEEERGILVNVPLCVDMSLNWLL NVFDSGRSGKMRALSFKTGIACLCGTEVKEKLQYLFSQVANSGSQCDQRHLGALLHEAIQ VPRQLGEVAAFGGSNVEPSVRSCFRFSTGKPVIEASQFLEWVNLEPQSMVWLAVLHRVTI AEQVKHQTKCSICRQCPIKGFRYRSLKQFNVDICQTCFLTGRASKGNKLHYPIMEYYTPT TSSENMRDFATTLKNKFRSKQYFSKHPQRGYLPVQSVLESDCSETPASSPMLPHADTHSR IEHFASRLAEMESQNCSFFNDSLSPDDSIDEDQYLLRHSSPITDREPAFGQQAPCSMATE SKGELEKILAHLEDENRILQGELRRLKWQHEEAAEAPTLVEGSAEATPDHRNEELLAEAR ILRQHKSRLETRMQILEDHNKQLESQLQRLRELLLQPPSESDGNGSAGSSLASSPRQSEG SHPREKGQTTPDTEVADDVGSKSQDVSLCLEDIMEKLRHAFPSVRSSDVTANTLLAS P26883 Q545E9 FKB1A_MOUSE Peptidyl-prolyl cis-trans isomerase FKBP1A PPIase FKBP1A 5.2.1.8 12 kDa FK506-binding protein 12 kDa FKBP FKBP-12 Calstabin-1 FK506-binding protein 1A FKBP-1A Immunophilin FKBP12 Rotamase Fkbp1a Fkbp1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C57BL/6 X CBA NUCLEOTIDE SEQUENCE 129/Sv NUCLEOTIDE SEQUENCE ILS ISS NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Hippocampus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; RYR1 AND PROTEIN PHOSPHATASE 1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Inhibited by both FK506 and rapamycin. Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation (By similarity). Interacts with ACVR1B and SMAD7 (By similarity). Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) (PubMed:18268335). Interacts directly with RYR2 and RYR3 (By similarity). Interacts directly with RYR1 (By similarity). Interacts with GLMN; rapamycin and FK506 abolish the interaction with GLMN in a dose dependent manner (By similarity). E9PZQ0 Ryr1 false 2 Cytoplasm Cytosol Sarcoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side Belongs to the FKBP-type PPIase family. FKBP1 subfamily. Acetylation Complete proteome Cytoplasm Isomerase Membrane Reference proteome Rotamase Sarcoplasmic reticulum MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFTLGKQEVIRGW EEGVAQMSVGQRAKLIISSDYAYGATGHPGIIPPHATLVFDVELLKLE O88537 A4IF56 E9QL30 FPRS3_MOUSE Formyl peptide receptor-related sequence 3 Fpr-rs3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] TISSUE SPECIFICITY FUNCTION TISSUE SPECIFICITY May have an olfactory function associated with the identification of pathogens or of pathogenic states. Cell membrane Multi-pass membrane protein Expressed exclusively in vomeronasal neurons (PubMed:19387439 and PubMed:19497865). Expressed in 0.8 % of a subset of sensory neurons located in the apical layer of the vomeronasal organ. Localized in sensory somata as well as dendritic cells. Each neuron appears to express only one receptor gene. Belongs to the G-protein coupled receptor 1 family. A sickly smell - Issue 114 of February 2010 Cell membrane Chemotaxis Complete proteome Disulfide bond G-protein coupled receptor Glycoprotein Membrane Receptor Reference proteome Transducer Transmembrane Transmembrane helix IG NC MEANSSIPLNGSEVVFYDSTTSRVLWILSVIVLSITFVLGVLGNGLVIWVAGFRMAHTVT TICYLNLALGDFSFMVTLPLHIISMVMKGKWLFGWFLCKFVLSIVHINLFVSVFLITLIA MDRCTCVLHPVWVQNHRTVSLARKVIVGAWILSLLLTLPHFLFLTTVRDARGEVHCTCNF ESVVANPEEQLKVSITVSTATGIISFIIGFSLPMSFIAVCYGLMAAKICRKGFLNSSRPL RVLTAVAISFFMCWFPFQLIILLGNIWNKETPSSIHILLNPASTLASFNSCLNPILYVFL GQEFREKLIYSLSASLERALREDSVLSSGKSSNFSSCPADSEL O70348 Q99KD8 DXO_MOUSE Decapping and exoribonuclease protein DXO 3.1.13.- 3.6.1.- Dom-3 homolog Z Dxo Dom3z Ng6 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] 129 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary gland PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Pancreas Testis X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH GDP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-397 IN COMPLEX WITH MAGNESIUM AND M(7)GPPPG CAP FUNCTION COFACTOR CATALYTIC ACTIVITY MUTAGENESIS OF GLU-234 AND ASP-236 Ribonuclease that specifically degrades pre-mRNAs with a defective 5' end cap and is part of a pre-mRNA capping quality control. Has decapping, pyrophosphohydrolase and 5'-3' exonuclease activities. Has decapping activity toward incomplete 5' end cap mRNAs such as unmethylated 5' end-capped RNA to release GpppN and 5' end monophosphate RNA. The 5' end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5' end triphosphate to release pyrophosphates. Mg(2+) Binds 2 magnesium ions. Nucleus Belongs to the DXO/Dom3Z family. In contrast to canonical decapping enzymes DCP2 and NUDT16, which release m(7)pppG (m(7)GDP), the decapping activity releases the entire cap structure GpppN and a 5' end monophosphate RNA. 3D-structure Complete proteome Exonuclease Hydrolase Magnesium Metal-binding Nuclease Nucleotide-binding Nucleus Phosphoprotein Reference proteome RNA-binding E A D A N H S L MEPRGTKRKAEKTEVEKPLNKLPRAVPSLRTQPSLYSGPFPFYRRPSELGCFSLDAQRQY HGDARALRYYSPPPINGPGPDFDLRDGYPDRYQPRDEEVQERLDHLLRWVLEHRNQLEGG PGWLAGATVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPAARAQRLARPPL LRELMYMGYKFEQYMCADKPGGSPDPSGEVNTNVAYCSVLRSRLGNHPLLFSGEVDCLNP QAPCTQPPSCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPHVVAGFRNPEGFV CSLKTFPTMEMFENVRNDREGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGP VTVSVHRDAPYAFLPSWYVETMTQDLPPLSKTPSPKD Q925U4 Q8CFM1 EDEM1_MOUSE ER degradation-enhancing alpha-mannosidase-like protein 1 Edem1 Edem Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NMRI Mammary gland INTERACTION WITH DNAJC10 INTERACTION WITH DNAJC10 Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It has low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2. Interacts with DERL2 and DERL3. Binds to SEL1L (By similarity). Interacts with DNAJC10. Endoplasmic reticulum membrane Single-pass type II membrane protein Belongs to the glycosyl hydrolase 47 family. Complete proteome Endoplasmic reticulum Glycoprotein Membrane Reference proteome Signal-anchor Transmembrane Transmembrane helix Unfolded protein response MQWRALVLGLVLLRLGLHAVLWLVFGLGPSMGFYQRFPLSFGFQRLRDPDGSGPVGPPGG PAWLHRPRRGTEGRLETPPEPGPTPGPGVCGPAHWGYALGGGGCGPDEYERRYSGAFPPQ LRAQMRDLARGMFVFGYDNYMAHAFPQDELNPIYCRGRGPDRGDPSNLNINDVLGNYSLT LVDALDTLAIMGNSSEFQKAVKLVINTVSFDKDSTVQVFEATIRVLGSLLSAHRIITDSK QPFGDMTIEDYDNELLYMAHDLAVRLLPAFENTKTGIPYPRVNLKTGVPPDSNNETCTAG AGSLLVEFGILSRLLGDSTFEWVARRAVKALWNLRSNDTGLLGNVVNIQTGHWVGKQSGL GAGLDSFYEYLLKSYILFGEKEDLEMFNAAYQSIQSYLRRGREACNEGEGDPPLYVNVNM FSGQLMNTWIDSLQAFFPGLQVLIGDVEDAICLHAFYYAIWKRYGALPERYNWQLQAPDV LFYPLRPELVESTYLLYQATKNPFYLHVGMDILQSLEKYTKVKCGYATLHHVIDKSKEDR MESFFLSETCKYLYLLFDEENPVHKSGTRYMFTTEGHIISVDKRLRELPWKEFFSEDGER DQEEKFVHRPKSQELRVINSSSNCNRVPDERRYSLPLKSIYMRQIDQMVGLI Q9D1Q4 DPM3_MOUSE Dolichol-phosphate mannosyltransferase subunit 3 Dolichol-phosphate mannose synthase subunit 3 DPM synthase subunit 3 Dolichyl-phosphate beta-D-mannosyltransferase subunit 3 Mannose-P-dolichol synthase subunit 3 MPD synthase subunit 3 Dpm3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Mammary gland IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Liver Lung Pancreas Spleen Testis Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the ER. Protein modification; protein glycosylation. Component of the dolichol-phosphate mannose (DPM) synthase complex composed of DPM1, DPM2 and DPM3; in the complex associated with DPM1 via its C-terminal domain and with DPM2 via its N-terminal portion. Endoplasmic reticulum membrane Multi-pass membrane protein Belongs to the DPM3 family. Complete proteome Endoplasmic reticulum Membrane Reference proteome Transmembrane Transmembrane helix MTKLTQWLWGLALLGSAWAALTMGALGLELPFPCREVLWPLPAYLLVSAGCYALGTVGYR VATFHDCEDAARELQSQIVEARADLARRGLRF Q8BL99 Q80XM5 Q8BIX5 Q8BIY4 Q8BLK8 DOP1_MOUSE Protein dopey-1 Dop1a D9Ertd809e Dopey1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1252 (ISOFORM 6) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-726 (ISOFORM 5) C57BL/6J Corpora quadrigemina Embryo Lung Ovary Wolffian duct NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) Eye PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1261 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Lung Spleen Testis May be involved in protein traffic between late Golgi and early endosomes. Golgi apparatus membrane Peripheral membrane protein Q8BL99-1 1 Q8BL99-2 2 No experimental confirmation available. Q8BL99-3 3 Q8BL99-4 4 No experimental confirmation available. Q8BL99-5 5 Q8BL99-6 6 Belongs to the dopey family. Alternative splicing Complete proteome Golgi apparatus Membrane Phosphoprotein Protein transport Reference proteome Transport AMVGILQVNGFGEESTLMQDLKPFRILISLLDKP VTAVFIILCLSYIEKA L LPTRSMRVLCQ QVSSVSMENPAEVF VISVGVHFFGVEFH RKFSFRTGAD MLQFFYAYIQ Q QVPTLHSQVFLFFRVLLLRMSPQHLTSLWPTMITEL MNTEELELLSDSKYRNYVAAIDKALKNFEYSSEWADLISALGKLNKVLQNNAKYQVVPKK LTIGKRLAQCLHPALPGGVHRKALETYEIIFKIIGPKRLAKDLFLYSSGLFPLLANAAMS VKPALLGLYEMYYLPLGKTLKPGLQGLLTGILPGLEEGSEYYERTNTLLEKVAAAVEQSA FYSALWGSLLTSPAVRLPGITYVLAHLNRKLSMEDQLYIIGSDIELMVEAVSTSVQDSSV LVQRSTLDLILFCFPFHMSQATRPDMIRILSAALHVVLRRDMSLNRRLYAWLLGFDNNGA IIGPRSTRHSNPEEHATYYFTTFSKELLVQAMVGILQVNGFGEESTLMQDLKPFRILISL LDKPELGPVILEDVLIEVFRTLYSQCKAELDLQMEPPFSKDHAQLSSKLRENKKTAELIK TANLLFNSFEPYYMWDYIARWFEECCRQSFFLSRRTLHARLQVGPGDSSDSSELQLTNFC LLVDFLLDIVSLETYIEIQTEHLPQLLLRMISALTSHLQTLRLSELTDSLRLCSKILSKV QPPLLSAGNGGVVQFPSGQNSTVKEWEDKKQVSSVSMENPAEVFEDGENPPSSRSSESGF TEFIQYQADRPDDLDRELNGQGAATIPIGSTSSETETASTVGSEETVIQPPSTFTQGAAG RSGKAVQKTAMQCCLEYVQQFLSRLINLYIIHSDSFPQALAADHQGDFSRIQRETSKWDR DSQGDAKERNIHTPKTSKEYLSAFLAACQLFLECSSFPVYIAEGNHTSESHSEKPDTDCE HAHPPQWLRTLMSACSQARDFRVQSAAVSLVMDLVGLTQSVAMVTGENINSMEPAQPLSP NQGRVAVVIRPPLTQGNLKYIAEKTEFFKHVALTLWDQLGDGTPQHHQKSVELFYQLHNL VPSSSICEDVVSQQLTHKDKKIRMEAHAKFAVLWHLTRDLHINKSSFARSFDRSLFIMLD SLTSLDGSTSSVGQAWLNQVLQRHDIARVLEPLLLLLLHPKTQRVSVQRVQAERYWSKTS CYPGEENDKHFMQNFTCNNVSQVHLIASKGNGEKPLTMDEMENFSLTVNPLSDRLSLLST SSETIPMVVSDFDLPDQQMEILQSSDSGCSQSSAGDNFSYEVDPENANAHEDSHMAKASS PDDDVQQVVFDLICKVVSGLEAESESVTSELEIESLQTKSSDLDPGKEATKIEDQAPQHS QHVLLSDDSPRFLSVSTEEGCECLANGISRNSSSPCISGTAQTLNDSSVPSETKSRQRSH SSIQFSFKEKLSEKVSEKETIVKESGKQPGAKPKVKLARKKDEDKKKAASEKLKQANVFF SEGLDLENWYSCGEGEISEIESDMGSPGSRKSPNFNIHPLYQHVLLYLQLYDSSRTLYAF SAIKSILKTNPIAFVNAISTTSVNNAYTPQLSLLQNLLARHRISVMGKDFYSHIPVDSNH NFRSSMYIEILISLCLYYMRSHYPTHVKVTTQDLIGNRNMQMMSIEILTLLFTELAKVIE SSAKGFPSFISDMLSKCKVQKVILHCLLSSIFSVQKWHSEKTAGKSMVAVEEGFSEDSLI NFSEDELDNGSTLQSQLLRVLQRLIVLEHHVMTIPEENEAGFDFVVSDLEHISPHQPMTS LQYLHAQPITCQGMFLCAVIRALHQHCACKMHPQWIGLITSTLPYMGKVLQRVVVSVTLQ LCRNLDNLIQQYKYETGLSDSRPLWVASIIPPDMILTLLEGITAIIHYCLLDPTTQYHQL LVNVDQKHLVEARSGILSILHMIMSSVTLLWSILHQADASEKMAVAASASVTTINLGATK VIPAASEEQLLLVELVRSISVMRAETVIQTVKEVLKQPPAIAKDKVRKLCFCRKFSFRTG ADRIPVPNIVDSWTSLLVLLKDSIQLSLPAPGQFLILGVLNEFIMKNPSLENKKDQRDLQ DVTHKIVDAIGAIAGSSLEQTTWLRRNLEVKPSPKIMVDGTNLESDVEDMLSPAMETSNI TPSVYSVHALTLLSEVLAHLLDMVFYSDEKERVIPLLVNIMHYVVPYLRNHSAHNAPSYR ACVQLLSSLSGYQYTRRAWKKEAFDLFMDPSFFQMDASCVSHWRAIMDNLMTHDKTTFRD LMTRVAVAQSSSLNLFANRDVELEQRAMLLKRLAFAVLSSESDQYQKYLPDIQERLVESL RLPQVQVFLLMEQELTADEDISRTSGPSAAGLETTYTGGNGFSTSYNSQRWLNLYLSACK FLDLALALPSENLPQFQMYRWAFIPEASDDSGLEVRRQGIHQREFKPYVVRLAKLLRKRA KDEEDFKILEGLEMAKHQKNPEEDCSGRTLGWEPGHLLLTLCTMRNMEQLLPFFNVLSQV FNSKVTSRCGGHSGSPVLYPNSFPNKDMKLENHKAFSSKARQKIEEMIEKDFLEGVIKT Q5SWY7 Q5U437 Q8C1B0 FA83G_MOUSE Protein FAM83G Fam83g Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Skin NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Embryo IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Pancreas May regulate the bone morphogenetic proteins (BMP) pathway. Found in a macromolecular complex with SMAD1. Interacts with SMAD1 (via MH2 domain); in a SMAD4-independent manner. Cytoplasm Cytosol Nucleus Detected predominantly in cytosolic. Upon BMP stimulation, a small portion of PAWS1 is detected in the nucleus. BMP signaling induces the phosphorylation of PAWS1 through BMPR1A at Ser-609, Ser-613 and Ser-615. In response to BMP phosphorylation at Ser-609 is necessary for the activation of SMAD4-independent BMP target genes such as NEDD9 and ASNS. Belongs to the FAM83 family. Acetylation Complete proteome Cytoplasm Nucleus Phosphoprotein Reference proteome S F L V S L MAFSQVQCLDDNHVNWRSSESKPEFFYSEEQRLALEALVARGRDAFYEVLKRENIRDFLS ELELSRIVEAIEVYDPGSEDPRVSGRRPEPQDNGGADASEETSAAGGPPATETLPSLEYW PQKSDRSIPQLDLGWPDTIAYRGVTRASVYMQPPIDGQPHIKEVVRKMVSQAQKVIAVVM DMFTDVDIFKDLLDAGFKRKVAVYIIVDESNVKYFLHMCERARMHLGHLKNLRVRSSGGT EFFTRSATKFKGVLAQKFMFVDGDRAVCGSYSFTWSAARTDRNVISVLSGQVVEMFDRQF QELYLMSQSVSLKDIPMEKEPEPEPIVLPSVVPLVPTGTMAKKLVNPKYALVKAKSVDEI AKSSSDKQEVTRPPGLRGPAVAERPGDLSELLPPVHPGLLNLERANMFEYLPTWVEPDPE PGSDILGYINIIDPNIWNPQPNQMNRIKIRDTAHASAQHQLWKQSQGARPCPAPCPPPAP RDSQGVVPAENGFPQGNPEPQAPVPKPRTVPVASVLARDGSDIGWALDTPEKETPQNGID PRLPSTASESEVPQQQHSSMTQDDPDGLERGLPNGLDEDEDDDDDYVTLSDQDSLSGSSG PGPGHRRPSVASSMSDEYFEVRERSVPLQRRHSEQMANGPGHPPRRQLSAPHVTRGTFGG PLSSPLWAQGRSREDVDASRIQGQRPMDRQAQGQHFHRHGSTTSRTPGPPRFRPAADGTQ SSSKKASPAAAGPHHWQPKGSPTPRMLPDPGSPRPTRNTRLRAELRATEEHASPFGIPYS KLSQSKHLKARAGGSQWAPSDSKRRARDHKEP Q8C0Z1 Q3TZ74 F234A_MOUSE Protein FAM234A Protein ITFG3 Fam234a Itfg3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Dendritic cell Head Inner ear NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Kidney GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-116; ASN-120 AND ASN-392 Myoblast GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-116; ASN-120 AND ASN-392 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Heart Kidney Liver Lung Pancreas Testis Membrane Single-pass type II membrane protein Belongs to the FAM234 family. Complete proteome Glycoprotein Membrane Phosphoprotein Reference proteome Signal-anchor Transmembrane Transmembrane helix R G L V V A MMDNKDLEAEIHPLKNEDKKSQENPGNLPRNEDNLKSKPVPSRLSRCRTVAFFLSLFTCL FVVFVLSFIIPCPDRPSSQGTWKLDYNNAVMYDFLALGDINKDKVQDVLFLYKNTNSSNN LTRSCADEGFSTPCAFVVAVSGANGSVLWERPVAQDVALVKCAMPQTLDSDEVSSACIVV GRAGSFVAVSFFTGETLWSHPSSFSGNVSILSPLLQVPDIDGDGDGTPDLLILAQEGQEV SGALYSGSTGYQIGHRGSLGVDGDGVALLHVTRTGAQYILLPCASALCGFSVKSLYERIT GRDGHFKEDPYWENMLNHSVHRRLLHRLGAVRYLMNIPGKAGQDLLLVTSEACVLLDGQD LEPRWTLGEVQVLRKPILGHYKPDTLAVVIENGTSIDRQILLLDLSTGSILWSQPLPSLP GGPPSTSLMTADHRSAFFFWGLHDLVSTNEMDPPDVQHSLYMFHPTLPGILLELANVSAN IVAFDAVLLEPSRHAAYVLLTGPASSDVPGLVSVTKHKVQDLVPGSRVIHLGEGSSDSDQ AIRDRFSRLRYRSEM O08749 Q3TG55 Q3U5W5 Q3UWP7 Q99LD3 DLDH_MOUSE Dihydrolipoyl dehydrogenase, mitochondrial 1.8.1.4 Dihydrolipoamide dehydrogenase Dld Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] DBA/2J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Bone marrow Heart NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Czech II Mammary tumor PROTEIN SEQUENCE OF 73-89; 216-259; 289-334; 316-334; 347-365; 421-428 AND 483-509 IDENTIFICATION BY MASS SPECTROMETRY C57BL/6J Brain Hippocampus SUBCELLULAR LOCATION FUNCTION TISSUE SPECIFICITY PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-410 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122; LYS-132; LYS-143; LYS-159; LYS-166; LYS-273; LYS-277; LYS-334; LYS-410; LYS-430 AND LYS-505 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast Liver ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66; LYS-104; LYS-122; LYS-132; LYS-143; LYS-334; LYS-346; LYS-410; LYS-420 AND LYS-505 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity). (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH FAD Binds 1 FAD per subunit. Homodimer. Part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (subunits PDHA (PDHA1 or PDHA2) and PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (by non covalent bonds). The 2-oxoglutarate dehydrogenase complex is composed of OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase; E3). It contains multiple copies of the three enzymatic components (E1, E2 and E3). In the nucleus, the 2-oxoglutarate dehydrogenase complex associates with KAT2A. Interacts with PDHX. O54910 Nfkbie false 4 Mitochondrion matrix Nucleus Cell projection Cilium Flagellum Cytoplasmic vesicle Secretory vesicle Acrosome Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. Expressed in liver (at protein level). Tyrosine phosphorylated. The active site is a redox-active disulfide bond. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. Acetylation Cell projection Cilium Complete proteome Cytoplasmic vesicle Direct protein sequencing Disulfide bond FAD Flagellum Flavoprotein Mitochondrion NAD Nucleus Oxidoreductase Phosphoprotein Redox-active center Reference proteome Transit peptide Y C Q T H L K E MQSWSRVYRSLAKKGHFNRISHGLQGVSSVPLRTYADQPIEADVTVIGSGPGGYVAAIKS AQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEIPEVRLNL EKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNIL VATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVT AVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGK AEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGP MLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGK FPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDI ARVCHAHPTLSEAFREANLAAAFGKPINF Q8CF27 FA24A_MOUSE Protein FAM24A Fam24a Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis Secreted Belongs to the FAM24 family. Complete proteome Reference proteome Secreted Signal MFDLRTKVMIGIASTLLIAAIMLITLVFCLYQKISKALKLAKEPECCIDPCKDPNEKIIR AKPIIAETCRNLPCCDDCSIYKDVGSLPPCYCVTNEGL Q8BFQ6 DIRC2_MOUSE Solute carrier family 49 member 4 Disrupted in renal carcinoma protein 2 homolog Slc49a4 Dirc2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Diencephalon Spleen NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Salivary gland Electrogenic metabolite transporter. Lysosome membrane Multi-pass membrane protein Cleaved in lysosomes by cathepsin L between Leu-214 and Ala-261, generating a N-glycosylated N-terminal and a non-glycosylated C-terminal fragment. Belongs to the major facilitator superfamily. Complete proteome Glycoprotein Lysosome Membrane Reference proteome Transmembrane Transmembrane helix Transport MGSGWSSEEEERQPLLGPGLGPAPGAARRGREATAVLPAAGPNPGRVYGRRWLVLLLFSL LAFAQGLVWNTWGPIQNSARQAYGFSGWDIALLVLWGPIGFLPCFAFMWLLDKRGLRVTV LLTSFLMVLGTGLRCIPVSDLALKKRLIHGGQILNGLAGPTVMNAAPFLSTTWFSADERA TATAIASMLSYLGGACAFLVGPLVVPAPNGTAPLLAAESSRAHIKDRIETVLYAEFGVVC LIFSATLAYFPPRPPLPPSVAAASQRLSYRRSFCRLLSNLRFLMIALAYAIPLGVFAGWS GVLDLILTPVHVSQVDAGWIGFWSIVGGCVVGIAMARFADFIRGMLKLILLLLFSGATLS STWFTLTCLNSITHLPLTTVTLYASCILLGVFLNSSVPIFFELFVETVYPVPEGITCGVV TFLSNMFMGVLLFFVTFYHTELSWFNWCLPGSCLLSLLLILCFRESYDRLYLDVVVSV B2RQR8 E9Q896 ECE2_MOUSE Endothelin-converting enzyme 2 ECE-2 3.4.24.71 Ece2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ECE2-2) Brain DISRUPTION PHENOTYPE FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides (By similarity). May play a role in amyloid-beta processing (PubMed:12464614). Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1. Zn(2+) Binds 1 zinc ion per subunit. Golgi apparatus membrane Single-pass type II membrane protein Cytoplasmic vesicle Secretory vesicle membrane B2RQR8-1 Ece2-1 B2RQR8-2 Ece2-2 P0DPD9-1 Q80Z60-1 Eef1akmt4-Ece2-1 ECE-2a-1 Based on a naturally occurring readthrough transcript which produces an Eef1akmt4-Ece2 fusion protein. P0DPD9-2 Q80Z60-2 Eef1akmt4-Ece2-2 ECE-2a-2 Based on a naturally occurring readthrough transcript which produces an Eef1akmt4-Ece2 fusion protein. Eef1akmt4-Ece2 and Ece2 double mutant mice are fertile and healthy, and do not display any abnormality in terms of growth or aging. Belongs to the peptidase M13 family. Alternative splicing Complete proteome Cytoplasmic vesicle Disulfide bond Glycoprotein Golgi apparatus Hydrolase Membrane Metal-binding Metalloprotease Phosphoprotein Protease Reference proteome Signal-anchor Transmembrane Transmembrane helix Zinc MNVALHELGGGGSMVEYKRAKLRDEESPEITVEGRATRDSLEVGFQKRTRQLFGSHTQLE LVLAGLILVLAALLLGCLVALWVHRDPAHSTCVTEACIRVAGKILESLDRGVSPCQDFYQ FSCGGWIRRNPLPNGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTRSFYLSCL QSERIEKLGAKPLRDLIDKIGGWNITGPWDEDSFMDVLKAVAGTYRATPFFTVYVSADSK SSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMVELGVLLGGQPTSTREQMQQV LELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPAVDWLEFLSFLLSPLELGDSEPV VVYGTEYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDQRFETAQEKLLETLYGTKKS CTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMINEIRSAFEETLGDLVWMDE KTRLAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMAD QLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYAHNHPKALNFGGIGVVMGH ELTHAFDDQGREYDKEGNLRPWWQNESLTAFQNHTACMEEQYSQYQVNGERLNGLQTLGE NIADNGGLKAAYNAYKAWLRKHGEEQPLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGL VTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW Q8BTM8 B7FAV0 O54934 Q7TQI1 Q8BLK1 Q8BTN7 Q8VHX5 Q8VHX8 Q99KQ2 FLNA_MOUSE Filamin-A FLN-A Actin-binding protein 280 ABP-280 Alpha-filamin Endothelial actin-binding protein Filamin-1 Non-muscle filamin Flna Fln Fln1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-1253 (ISOFORM 1) C57BL/6J NOD Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-2647 (ISOFORM 1) Eye Mammary tumor NUCLEOTIDE SEQUENCE [MRNA] OF 1490-1607 (ISOFORM 1) FUNCTION INTERACTION WITH FURIN NUCLEOTIDE SEQUENCE [MRNA] OF 1691-1805 AND 2076-2226 (ISOFORM 1) DEVELOPMENTAL STAGE C3H/HeJ DISRUPTION PHENOTYPE FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2152 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1459 AND THR-1750 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-20; SER-968; SER-1459; THR-1750; SER-2152; SER-2180; SER-2329; THR-2336; SER-2370; SER-2523; SER-2526 AND THR-2599 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis DISRUPTION PHENOTYPE FUNCTION INTERACTION WITH RFLNA AND RFLNB FUNCTION IN CILIOGENESIS INTERACTION WITH MICALL2 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-376; LYS-700; LYS-865; LYS-906; LYS-1071; LYS-1372; LYS-1538; LYS-2569 AND LYS-2575 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-1071 AND LYS-2569 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast INTERACTION WITH RFLNA AND RFLNB Actin binding protein that promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins (By similarity). Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking. Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs (PubMed:17172441). Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (PubMed:20713593). Homodimer. Interacts with FCGR1A, FLNB, FURIN, HSPB7, KCND2, INPPL1, MYOT, MYOZ1, PDLIM2, ARHGAP24, PSEN1, PSEN2 and ECSCR. Interacts also with various other binding partners in addition to filamentous actin. Interacts (via N-terminus) with TAF1B. Interacts (via N-terminus) with MIS18BP1 (via N-terminus) (By similarity). Interacts with TMEM67 (via C-terminus) and MKS1 (By similarity). Interacts (via actin-binding domain) with MICALL2 (via calponin-homology (CH) domain). Interacts with RFLNA and RFLNB (PubMed:24436304, PubMed:21709252). Interacts (via filamin repeat 5) with SYK; docks SYK to the plasma membrane. Interacts (via filamin repeats 19 and 21) with DRD3; increased PKA-mediated phosphorylation at Ser-2152. Interacts (via filamin repeat 21) with MAS1, AGTR1 and ADRA1D; increases PKA-mediated phosphorylation of FLNA at Ser-2152. Interacts (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) with GP1BA (high affinity), ITGB7, ITGB2 and FBLIM1 (By similarity). Interacts with CEACAM1 (via cytoplasmic domain); inhibits cell migration and cell scattering by interfering with the interaction between FLNA and RALA (By similarity). Interacts with FOXC1 (By similarity). Q8CIH5 Plcg2 false 3 Cytoplasm Cell cortex Cytoplasm Cytoskeleton Q8BTM8-1 1 Q8BTM8-2 2 May be due to an intron retention. Widely expressed. Highly expressed in Purkinje cells. Widely distributed. Expressed at 12.5 dpc in the ventricular and subventricular zones. Highly expressed at 16 dpc in blood vessels, renal cortices, respiratory and alimentary tracts, olfactory epithelium, presumed isles of hematopoiesis within the liver; lower expression in the cerebral cortex and choroid plexus. Comprised of a NH2-terminal actin-binding domain, 24 immunoglobulin-like internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation. Filamin repeat 20 interacts with filamin repeat 21 masking the ligand binding site on filamin repeat 21, resulting in an autoinhibited conformation. The autoinhibition can be relieved by ligands like ITGB7 or FBLIM1. Filamin repeats 19 and 21 can simultaneously engage ligands. Phosphorylation at Ser-2152 is negatively regulated by the autoinhibited conformation of filamin repeats 19-21. Ligand binding induces a conformational switch triggering phosphorylation at Ser-2152 by PKA. Polyubiquitination in the CH1 domain by a SCF-like complex containing ASB2 leads to proteasomal degradation. Prior dissociation from actin may be required to expose the target lysines. Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome. Female heterozygous knockout mice show normal development, but 20% die in the first 3-4 months with many anomalies, including lung edema and emphysema, liver thrombi and necrosis, leukocytosis, and heart dilation. Some females die after birth; only about 50% of expected female heterozygous mice are observed at weaning. Male hemizygous knockout mice die by embryonic day 14.5 dpc with vascular defects; their blood vessels are coarse and dilated and extend aberrant branches and sprouts into somitic tissues. Male hemizygous knockout mice display severe cardiac structural defects involving ventricles, atria, and outflow tracts. Conditional Flna knockout males, in the neural crest, survive until birth but die on the first postnatal day with cyanosis; all males show abnormal cardiac outflow tracts (PubMed:17172441). Female heterozygous knockout mice present a mild thrombocytopenia and conditional Flna knockout males, in platelets display a macrothrombocytopenia (PubMed:20713593). Belongs to the filamin family. Translation N-terminally extended. Translation N-terminally extended. Acetylation Actin-binding Alternative splicing Cilium biogenesis/degradation Complete proteome Cytoplasm Cytoskeleton Isopeptide bond Phosphoprotein Reference proteome Repeat Ubl conjugation DSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVNNAREAMQQADDWLGIPQVITPEEIVD GEGTGYTGALSGCGRGRNKFFLSSPLESLLVVFPSCCTQPRLPLGPLAALFFEVLENKRLAWRACEPLRAPARSALLACSQAELTSSVGRAPNAAPEVGQAQTRLLPLRAAPHPWDTHAFHLQQF A T G D V A MSSSHSRCGQSAAVASPGGSIDSRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCV SKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIK LVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKL PQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVNNAREAMQQADDWLGIPQ VITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKK RAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLF AGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGMGEVEVVI QDPTGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNP AACRAIGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGF EYYPTIPGTYTVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGIVGKSADFVVE AIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFM ADIREAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHAGKAPLRVQVQDNEGCSVE ATVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVA KTGLKAHEPTYFTVDCTEAGQGDVSIGIKCAPGVVGPTEADIDFDIIRNDNDTFTVKYTP CGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLNRTGVELGKPTHFTVNAK TAGKGKLDVQFSGLAKGDAVRDVDIIDHHDNTYTVKYIPVQQGPVGVNVTYGGDHIPKSP FSVGVSPSLDLSKIKVSGLGDKVDVGKDQEFTVKSKGAGGQGKVASKIVSPSGAAVPCKV EPGLGADNSVVRFVPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGG NAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILF ADTHIPGSPFKAHVAPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSE AGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQC YGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTDTYVQDCGDGTYKVE YTPYEEGVHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVET RGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKV PVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVV DNADGTQTVNYVPSREGSYSISVLYGEEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGV PASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVPGRYTILI KYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAG KGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTA LAGDQPTVQTPLRSQQLAPQYNYPQGSQQTWIPERPMVGVNGLDVTSLRPFDLVIPFTIK KGEITGEVRMPSGKVAQPSITDNKDGTVTVRYSPSEAGLHEMDIRYDNMHIPGSPLQFYV DYVNCGHITAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTC SVSYLPVLPGDYSILVKYNDQHIPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDL SLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVIS QSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDG TCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANIGSHC DLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGMHTVSVKYKGQH VPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEVGVPAEFGIWTREAGAGGLAIAVEGPSK AEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSL QESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGIY LIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGSPAEFIVNTSNAGAG ALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPR LVSNHSLHETSSVFVDSLTKVATVPQHATSGPGPADVSKVVAKGLGLSKAYVGQKSNFTV DCSKAGNNMLLVGVHGPRTPCEEILVKHMGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGS PYRIMVP Q9Z218 Q9QWW2 Q9Z219 DPP6_MOUSE Dipeptidyl aminopeptidase-like protein 6 DPPX Dipeptidyl aminopeptidase-related protein Dipeptidyl peptidase 6 Dipeptidyl peptidase IV-like protein Dipeptidyl peptidase VI DPP VI Dpp6 Dpp-6 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] C57BL/6J Embryo PROTEIN SEQUENCE OF 651-664 IDENTIFICATION BY MASS SPECTROMETRY OF1 Hippocampus IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain DISRUPTION PHENOTYPE FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY Promotes cell surface expression of the potassium channel KCND2 (PubMed:22311982). Modulates the activity and gating characteristics of the potassium channel KCND2 (PubMed:22311982). Has no dipeptidyl aminopeptidase activity (By similarity). Homodimer (in vitro). Interacts with KCND2. Identified in a complex with KCND2 and KCNIP2. Forms an octameric complex composed of four DPP6 subunits bound to the KCND2 tetramer. Cell membrane Single-pass type II membrane protein Detected in brain cortex (at protein level). N-glycosylated. Knockdown animals obtained using siRNA technology have smaller brains than their wild-type littermates. Performance on the standard Morris water maze indicated spatial memory defects and learning disabilities. Belongs to the peptidase S9B family. Cell membrane Complete proteome Direct protein sequencing Disulfide bond Glycoprotein Membrane Reference proteome Signal-anchor Transmembrane Transmembrane helix Q P MNQTAGASNNVRCPPGKGHKELVGSNPPQRNWKGIAIALLVILVICSLIVTSVILLTPAE DTSLSQKKKVTVEDLFSEDFKIHDPEAKWISNKEFIYRERKGSVILRNVETNNSTVLIEG KKIESLRAIRYEISPDKEYVLFSYNVEPVYQHSHTGYYVLSKIPHGDPQSLDPPEVSNAK LQYAGWGPKGQQLIFIFENNIYYCAHVGKQAIRVVSTGKEGVIYNGLSDWLYEEEILKSH IAHWWSPDGTRLAYATINDSRVPLMELPTYTGSVYPTVKPYHYPKAGSENPSISLHVIGL NGPTHDLEMMPPDDPRMREYYITMVKWATSTKVAVTWLNRAQNVSILTLCDATTGVCTKK HEDESEAWLHRQNEEPVFSKDGRKFFFVRAIPQGGRGKFYHITVSSSQPNSSNDNIQSIT SGDWDVTKILSYDEKRNKIYFLSTEDLPRRRHLYSANTVDDFNRQCLSCDLVENCTYVSA SFSHNMDFFLLKCEGPGVPTVTVHNTTDKRRMFDLEANEEVQKAINDRQMPKIEYRKIEV EDYSLPMQILKPATFTDTAHYPLLLVVDGTPGSQSVTERFEVTWETVLVSSHGAVVVKCD GRGSGFQGTKLLQEVRRRLGFLEEKDQMEAVRTMLKEQYIDKTRVAVFGKDYGGYLSTYI LPAKGENQGQTFTCGSALSPITDFKLYASAFSERYLGLHGLDNRAYEMTKLAHRVSALED QQFLIIHATADEKIHFQHTAELITQLIKGKANYSLQIYPDESHYFHSVALKQHLSRSIIG FFVECFRVQDKLPTATAKEEEEED Q8K012 Q3U901 FBP1L_MOUSE Formin-binding protein 1-like Transducer of Cdc42-dependent actin assembly protein 1 Toca-1 Fnbp1l Toca1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-108 (ISOFORMS 1/2) C57BL/6J Bone marrow NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-605 (ISOFORM 2) Eye IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-488; SER-501 AND SER-505 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Spleen Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL-WASPIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Essential for autophagy of intracellular bacterial pathogens (By similarity). Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with GTP-bound CDC42. Interacts with DAAM1, DIAPH1, DIAPH2, DNM1, DNM2 and WASL/N-WASP. Interacts with ATG3. Interacts (via SH3 domain) with ABI1, WASF2, CDC42 and WIPF1. Cytoplasm Cytoplasm Cytoskeleton Cytoplasm Cell cortex Cytoplasmic vesicle Cell membrane Peripheral membrane protein Cytoplasmic side Q8K012-1 1 Gene prediction based on EST data. Q8K012-2 2 The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity). Belongs to the FNBP1 family. Alternative splicing Autophagy Cell membrane Coiled coil Complete proteome Cytoplasm Cytoplasmic vesicle Cytoskeleton Endocytosis Lipid-binding Membrane Phosphoprotein Reference proteome SH3 domain S AVTYI MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSK DEEPRFTSCIAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGR KAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTH MADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKV IPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTIS AAKQESGKMDSKSTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTLSIEPV HYCMNEIKTGKPRIPSFRSLKRGVSLIMGPALEDFSHLPPEQRRKKLQQRIDELNRGLQK EADQKEALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTG IRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHSEFDDEFEDDDPLPAI GHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTTYIDVTLEK SSKGS Q61555 E9QJZ4 Q63957 FBN2_MOUSE Fibrillin-2 Fibrillin-2 C-terminal peptide Fbn2 Fbn-2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 210-317 PROTEIN SEQUENCE OF 2429-2441 IDENTIFICATION BY MASS SPECTROMETRY OF1 Hippocampus DISRUPTION PHENOTYPE DISRUPTION PHENOTYPE FUNCTION DISRUPTION PHENOTYPE SUBCELLULAR LOCATION TISSUE SPECIFICITY Fibrillin-2: Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (PubMed:20855508). Interacts with BMP2, BMP4, BMP7, BMP10 and GDF5. Interacts with MFAP2 and MFAP5. Interacts with ADAMTSL5. Interacts with MFAP4. Secreted Extracellular space Extracellular matrix Strongly expressed during the first week of osteoblast differentiation. Limb-patterning defects characterized by bilateral syndactyly due to disorganized matrix (PubMed:11470817). Digit fusion involves both soft and hard tissues and is associated with reduced apoptosis at affected sites (PubMed:11470817). Mice show a well developed and morphologically normal aortic wall (PubMed:16407178). Mice display a low bone mass phenotype that is associated with reduced bone formation (PubMed:20855508). Belongs to the fibrillin family. Calcium Complete proteome Direct protein sequencing Disulfide bond EGF-like domain Extracellular matrix Glycoprotein Reference proteome Repeat Secreted Signal R W A R A R R P T N E R T S S T FR LP A G Y C P A V A Y H W G G A S C A G T M QGY HGD MGRRRRLCLQPYFVWLGCVALWAQGTDGQPQPPPPKTLRPQPPPQQVRPAVAGSEGGFMG PEYRDEGAVAASRVRRRGQQEILRGPNVCGSRFHSYCCPGWKTLPGGNQCIVPICRNSCG DGFCSRPNMCTCSSGQISPTCGAKSIQQCSVRCMNGGTCADDHCQCQKGYIGTYCGQPVC ENGCQNGGRCIGPNRCACVYGFTGPQCERDYRTGPCFTQVNNQMCQGQLTGIVCTKTLCC ATIGRAWGHPCEMCPAQPQPCRRGFIPNIRTGACQDVDECQAIPGLCQGGNCINTVGSFE CRCPAGHKQSETTQKCEDIDECSVIPGVCETGDCSNTVGSYFCLCPRGFVTSTDGSRCID QRAGTCFSGLVNGRCAQELPGRMAKAQCCCEPGRCWSIGTIPEACPVRGSEEYRRLCLDG LPMGGIPGSSVSRPGGTGSTGNGYGPGGTGFLPIPGDNGFSPGVGGAGVGAGGQGPIITG LTILNQTIDICKHHANLCLNGRCIPTVSSYRCECNMGYKQDANGDCIDVDECTSNPCSNG DCVNTPGSYYCKCHAGFQRTPTKQACIDIDECIQNGVLCKNGRCVNTDGSFQCICNAGFE LTTDGKNCVDHDECTTTNMCLNGMCINEDGSFKCVCKPGFILAPNGRYCTDVDECQTPGI CMNGHCINNEGSFRCDCPPGLAVGVDGRVCVDTHMRSTCYGEIKKGVCVRPFPGAVTKSE CCCANPDYGFGEPCQPCPAKNSAEFHGLCSSGIGITVDGRDINECALDPDICANGICENL RGSYRCNCNSGYEPDASGRNCIDIDECLVNRLLCDNGLCRNTPGSYSCTCPPGYVFRTET ETCEDVNECESNPCVNGACRNNLGSFHCECSPGSKLSSTGLICIDSLKGTCWLNIQDNRC EVNINGATLKSECCATLGAAWGSPCERCELDAACPRGFARIKGVTCEDVNECEVFPGVCP NGRCVNSKGSFHCECPEGLTLDGTGRVCLDIRMEHCFLKWDEDECIHPVPGKFRMDACCC AVGAAWGTECEECPKPGTKEYETLCPRGPGFANRGDILTGRPFYKDINECKAFPGMCTYG KCRNTIGSFKCRCNNGFALDMEERNCTDIDECRISPDLCGSGICVNTPGSFECECFEGYE SGFMMMKNCMDIDECERNPLLCRGGTCVNTEGSFQCDCPLGHELSPSREDCVDINECSLS DNLCRNGKCVNMIGTYQCSCNPGYQATPDRQGCTDIDECMIMNGGCDTQCTNSEGSYECS CSEGYALMPDGRSCADIDECENNPDICDGGQCTNIPGEYRCLCYDGFMASMDMKTCIDVN ECDLNPNICMFGECENTKGSFICHCQLGYSVKKGTTGCTDVDECEIGAHNCDMHASCLNV PGSFKCSCREGWVGNGIKCIDLDECANGTHQCSINAQCVNTPGSYRCACSEGFTGDGFTC SDVDECAENTNLCENGQCLNVPGAYRCECEMGFTPASDSRSCQDIDECSFQNICVFGTCN NLPGMFHCICDDGYELDRTGGNCTDIDECADPINCVNGLCVNTPGRYECNCPPDFQLNPT GVGCVDNRVGNCYLKFGPRGDGSLSCNTEVGVGVSRSSCCCSLGKAWGNPCETCPPVNST EYYTLCPGGEGFRPNPITIILEDIDECQELPGLCQGGNCINTFGSFQCECPQGYYLSEET RICEDIDECFAHPGVCGPGTCYNTLGNYTCICPPEYMQVNGGHNCMDMRKSFCYRSYNGT TCENELPFNVTKRMCCCTYNVGKAWNKPCEPCPTPGTADFKTICGNIPGFTFDIHTGKAV DIDECKEIPGICANGVCINQIGSFRCECPTGFSYNDLLLVCEDIDECSNGDNLCQRNADC INSPGSYRCECAAGFKLSPNGACVDRNECLEIPNVCSHGLCVDLQGSYQCICNNGFKASQ DQTMCMDVDECERHPCGNGTCKNTVGSYNCLCYPGFELTHNNDCLDIDECSSFFGQVCRN GRCFNEIGSFKCLCNEGYELTPDGKNCIDTNECVALPGSCSPGTCQNLEGSFRCICPPGY EVRSENCIDINECDEDPNICLFGSCTNTPGGFQCICPPGFVLSDNGRRCFDTRQSFCFTN FENGKCSVPKAFNTTKAKCCCSKMPGEGWGDPCELCPKDDEVAFQDLCPYGHGTVPSLHD TREDVNECLESPGICSNGQCINTDGSFRCECPMGYNLDYTGVRCVDTDECSIGNPCGNGT CTNVIGSFECTCNEGFEPGPMMNCEDINECAQNPLLCAFRCMNTFGSYECTCPVGYALRE DQKMCKDLDECAEGLHDCESRGMMCKNLIGTFMCICPPGMARRPDGEGCVDENECRTKPG ICENGRCVNIIGSYRCECNEGFQSSSSGTECLDNRQGLCFAEVLQTMCQMASSSRNLVTK SECCCDGGRGWGHQCELCPLPGTAQYKKICPHGPGYATDGRDIDECKVMPSLCTNGQCVN TMGSFRCFCKVGYTTDISGTACVDLDECSQSPKPCNFICKNTKGSYQCSCPRGYVLQEDG KTCKDLDECQTKQHNCQFLCVNTLGGFTCKCPPGFTQHHTACIDNNECGSQPSLCGAKGI CQNTPGSFSCECQRGFSLDASGLNCEDVDECDGNHRCQHGCQNILGGYRCGCPQGYVQHY QWNQCVDENECSNPGACGSASCYNTLGSYKCACPSGFSFDQFSSACHDVNECSSSKNPCS YGCSNTEGGYLCGCPPGYFRVGQGHCVSGMGFNKGQYLSVDAEAEDDENALSPEACYECK INGYTKKDGRRKRSAQEPEPASAEEQISLESVAMDSPVNMKFNLSGLGSKEHILELVPAI EPLNNHIRYVISQGNEDGVFRIHQRNGLSYLHTAKKKLAPGTYTLEITSIPLYGKKELRK LEEHNEDDYLLGVLGEALRMRLQIQLY Q9Z2B5 Q9CTK8 Q9CWT5 E2AK3_MOUSE Eukaryotic translation initiation factor 2-alpha kinase 3 2.7.11.1 PRKR-like endoplasmic reticulum kinase Pancreatic eIF2-alpha kinase Eif2ak3 Pek Perk Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] MUTAGENESIS OF LYS-618 NIH Swiss Fibroblast ERRATUM NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-152 AND 769-1114 C57BL/6J FUNCTION SUBUNIT FUNCTION INTERACTION WITH DNAJC3 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Lung Pancreas FUNCTION INTERACTION WITH MFN2 X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 583-701 AND 867-1078 SUBUNIT PHOSPHORYLATION AT THR-980 Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' during the unfolded protein response (UPR) and in response to low amino acid availability (PubMed:11106749). Converts phosphorylated eIF-2-alpha/EIF2S1 either in a global protein synthesis inhibitor, leading to a reduced overall utilization of amino acids, or to a translation initiation activator of specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:23921556). Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1) (PubMed:11035797). Involved in control of mitochondrial morphology and function (PubMed:23921556). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Perturbation in protein folding in the endoplasmic reticulum (ER) promotes reversible dissociation from HSPA5/BIP and oligomerization, resulting in transautophosphorylation and kinase activity induction. Forms dimers with HSPA5/BIP in resting cells (PubMed:21543844). Oligomerizes in ER-stressed cells (PubMed:10854322). Interacts with DNAJC3 (PubMed:12446838). Interacts with MFN2 (PubMed:23921556). Interacts with TMEM33 (By similarity). Interacts with PDIA6 (By similarity). false 2 P27958 true 5 P05198 EIF2S1 true 4 Q80U63 Mfn2 false 2 Endoplasmic reticulum membrane Single-pass type I membrane protein Ubiquitous. By ER stress. The lumenal domain senses perturbations in protein folding in the ER, probably through reversible interaction with HSPA5/BIP. Autophosphorylated. Phosphorylated at Tyr-615 following endoplasmic reticulum stress, leading to activate its tyrosine-protein kinase activity. Dephosphorylated by PTPN1/TP1B, leading to inactivate its enzyme activity (By similarity). Oligomerization of the N-terminal ER luminal domain by ER stress promotes PERK trans-autophosphorylation of the C-terminal cytoplasmic kinase domain at multiple residues including Thr-980 on the kinase activation loop. N-glycosylated. ADP-ribosylated by PARP16 upon ER stress, which increases kinase activity. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily. 3D-structure ADP-ribosylation ATP-binding Complete proteome Endoplasmic reticulum Glycoprotein Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Serine/threonine-protein kinase Signal Stress response Transferase Translation regulation Transmembrane Transmembrane helix Unfolded protein response K A VFGNKMIIPS GTHKTSSKEC MERATRPGPRALLLLLFLLLGCAAGISAVAPARSLLAPASETVFGLGAAAAPTSAARVPA VATAEVTVEDAEALPAAAGEPESRATEPDDDVELRPRGRSLVIISTLDGRIAALDAENDG KKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGDLFQWDRDRESMEAVPFTVESLLES SYKFGDDVVLVGGKSLITYGLSAYSGKLRYICSALGCRRWDSDEMEEEEDILLLQRTQKT VRAVGPRSGSEKWNFSVGHFELRYIPDMETRAGFIESTFKPGGNKEDSKIISDVEEQEAT MLDTVIKVSVADWKVMAFSRKGGRLEWEYQFCTPIASAWLVRDGKVIPISLFDDTSYTAS EEALGDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRVSEKFPTSPKALESVNGENAII PLPTIKWKPLIHSPSRTPVLVGSDEFDKCLSNDKYSHEEYSNGALSILQYPYDNGYYLPY YKRERNKRSTQITVRFLDSPHYSKNIRKKDPILLLHWWKEIFGTILLCIVATTFIVRRLF HPQPHRQRKESETQCQTESKYDSVSADVSDNSWNDMKYSGYVSRYLTDFEPIQCMGRGGF GVVFEAKNKVDDCNYAIKRIRLPNRELAREKVMREVKALAKLEHPGIVRYFNAWLETPPE KWQEEMDEIWLKDESTDWPLSSPSPMDAPSVKIRRMDPFSTKEQIEVIAPSPERSRSFSV GISCGQTSSSESQFSPLEFSGTDCGDNSDSADAAYNLQDSCLTDCEDVEDGTVDGNDEGH SFELCPSEASPYTRSREGTSSSIVFEDSGCGNASSKEEPRGNRLHDGNHYVNKLTDLKCS SSRSSSEATTLSTSPTRPTTLSLDFTKNTVGQLQPSSPKVYLYIQMQLCRKENLKDWMNR RCSLEDREHGVCLHIFLQIAEAVEFLHSKGLMHRDLKPSNIFFTMDDVVKVGDFGLVTAM DQDEEEQTVLTPMPAYATHTGQVGTKLYMSPEQIHGNNYSHKVDIFSLGLILFELLYPFS TQMERVRILTDVRNLKFPLLFTQKYPQEHMMVQDMLSPSPTERPEATDIIENAIFENLEF PGKTVLRQRSRSMSSSGTKHSRQPSCSYSPLPGN Q8BVG4 Q6KAM9 Q8BWT9 DPP9_MOUSE Dipeptidyl peptidase 9 DP9 3.4.14.5 Dipeptidyl peptidase IX DPP IX Dipeptidyl peptidase-like protein 9 DPLP9 Dpp9 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Liver Olfactory bulb NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) FVB/N Salivary gland IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Heart Liver Lung Pancreas Spleen FUNCTION CATALYTIC ACTIVITY MUTAGENESIS OF SER-729 ACTIVE SITE SUBCELLULAR LOCATION TISSUE SPECIFICITY MUTAGENESIS OF SER-729 ACTIVE SITE TISSUE SPECIFICITY DEVELOPMENTAL STAGE Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfluorophosphate. Homodimer. Cytoplasm Cytosol Q8BVG4-1 1 Q8BVG4-2 2 Detected in kidney, skin, brain, thymus and liver (at protein level). Detected in hypoglossal cord and first branchial arch at 10.75 dpc (at protein level). Belongs to the peptidase S9B family. DPPIV subfamily. Alternative splicing Aminopeptidase Complete proteome Cytoplasm Hydrolase Protease Reference proteome Serine protease VAIAGAPVTVWMAYDTGYTERYMDVPENNQQGYEAGSVAL PPHEAESPSSLPATTDPRMASASSSMWEAKPGTPASEGQR S A D Y S F Q K MCSGVSPVEQVAAGDMDDTAARFCVQKHSWDGLRSIIHGSRKSSGLIVSKAPHDFQFVQK PDESGPHSHRLYYLGMPYGSRENSLLYSEIPKKVRKEALLLLSWKQMLDHFQATPHHGVY SREEELLRERKRLGVFGITSYDFHSESGLFLFQASNSLFHCRDGGKNGFMVSPMKPLEIK TQCSGPRMDPKICPADPAFFSFINNSDLWVANIETGEERRLTFCHQGSAGVLDNPKSAGV ATFVIQEEFDRFTGCWWCPTASWEGSEGLKTLRILYEEVDESEVEVIHVPSPALEERKTD SYRYPRTGSKNPKIALKLAELQTDHQGKIVSSCEKELVQPFSSLFPKVEYIARAGWTRDG KYAWAMFLDRPQQRLQLVLLPPALFIPAVESEAQRQAAARAVPKNVQPFVIYEEVTNVWI NVHDIFHPFPQAEGQQDFCFLRANECKTGFCHLYRVTVELKTKDYDWTEPLSPTEDEFKC PIKEEVALTSGEWEVLSRHGSKIWVNEQTKLVYFQGTKDTPLEHHLYVVSYESAGEIVRL TTLGFSHSCSMSQSFDMFVSHYSSVSTPPCVHVYKLSGPDDDPLHKQPRFWASMMEAANC PPDYVPPEIFHFHTRADVQLYGMIYKPHTLQPGRKHPTVLFVYGGPQVQLVNNSFKGIKY LRLNTLASLGYAVVVIDGRGSCQRGLHFEGALKNQMGQVEIEDQVEGLQYVAEKYGFIDL SRVAIHGWSYGGFLSLMGLIHKPQVFKVAIAGAPVTVWMAYDTGYTERYMDVPENNQQGY EAGSVALHVEKLPNEPNRLLILHGFLDENVHFFHTNFLVSQLIRAGKPYQLQIYPNERHS IRCRESGEHYEVTLLHFLQEHL Q9QYE6 O88317 Q3TGE7 Q3U6S5 Q3UUF9 GOGA5_MOUSE Golgin subfamily A member 5 Golgin-84 Protein Ret-II Protein Sumiko Golga5 Retii Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] B-cell lymphoma NUCLEOTIDE SEQUENCE [MRNA] Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Bone marrow Kidney Spinal cord NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J FVB/N Brain Kidney PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Involved in maintaining Golgi structure. Stimulates the formation of Golgi stacks and ribbons. Involved in intra-Golgi retrograde transport (By similarity). Homodimer. Interacts with RAB1A that has been activated by GTP-binding. Interacts with isoform CASP of CUX1 (By similarity). Q99N72 Mcf2 false 3 Golgi apparatus membrane Single-pass type IV membrane protein Found throughout the Golgi. Highly phosphorylated during mitosis. Phosphorylation is barely detectable during interphase (By similarity). Acetylation Coiled coil Complete proteome Golgi apparatus Membrane Methylation Phosphoprotein Reference proteome Transmembrane Transmembrane helix D N G D N D V M A S S R S P G R MSWFADLAGRAEDLLNRVDQGAATALRKENTSNIFYSKNTDYPELQQQNTDSNYQTGQKA NYISSAADNIRHQKATILAGTANVKVGSRTVGDATHPTEHASAPRPSSQFVRRKKSEPDD ELLFDFLNSSQKEPTGRVEVKKEKGRAPVSPSSPSGVSSVNTSVTTTKAMGGNAGSQSPG VNSSDSVPEVHKEPSEESTAPSATSEEHSSTPSDGSSRSQELSNLRLENQLLRNEVQSLN QEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLA VLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLK REQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLE SAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEI QKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEF RYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQ TMLESLSTEKNSLVFQLERLEQQVHSASSGPNSGSAINMSGVDSGEGTRLRNVPVLFNDT ETNLAGMYGKVRKAASSIDQFSIRLGIFLRRYPIARVFVIIYMALLHLWVMIVLLTYSPE MHHDQPYGK Q9QY15 Q53Z03 Q7TMB5 Q8R1B6 DDX25_MOUSE ATP-dependent RNA helicase DDX25 3.6.4.13 DEAD box protein 25 Gonadotropin-regulated testicular RNA helicase Ddx25 Grth Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ Testis SEQUENCE REVISION TO N-TERMINUS ALTERNATIVE INITIATION TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [GENOMIC DNA] SUBCELLULAR LOCATION DISRUPTION PHENOTYPE 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Cerebellum Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Eye Testis FUNCTION SUBCELLULAR LOCATION PHOSPHORYLATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development. ATP + H2O = ADP + H(+) + phosphate Cytoplasm Nucleus Detected in both cytoplasm and nucleus of testicular cells. Also detected in chromatoid bodies of round spermatids. Q9QY15-1 1 Q9QY15-2 2 Isoform 1 is expressed in germ cells. Isoform 2 is expressed in Leydig cells and in round spermatids of adult testis upon gonadotropin stimulation. Phosphorylated on threonine residues. The phosphorylated form is found in the cytoplasm but not in the nucleus. Male mice display normal sexual behavior but are sterile with testes that are 25% smaller than the wild-type. Round spermatids arrest at step 8 and fail to elongate. Chromatoid bodies are unusually condensed, greatly reduced in size and lack the typical amorphous texture throughout all steps of spermiogenesis. Belongs to the DEAD box helicase family. Alternative initiation ATP-binding Complete proteome Cytoplasm Developmental protein Differentiation Helicase Hydrolase mRNA transport Nucleotide-binding Nucleus Phosphoprotein Reference proteome RNA-binding Spermatogenesis Translation regulation Transport H P MASLLWGGDAGAAESERLNSHFSNLVHPRKNLRGIRSTTVPNIDGSLNTEDDDDDEDDVV DLAANSLLNKLIRQSLIESSHRVEVLQKDPSSPLYSVKTFEELRLKEELLKGIYAMGFNR PSKIQEMALPMMLAHPPQNLIAQSQSGTGKTAAFVLAMLSRVNALELFPQCLCLAPTYEL ALQTGRVVERMGKFCVDVEVMYAIRGNRIPRGTEVTKQIIIGTPGTVLDWCFKRKLIDLT KIRVFVLDEADVMIDTQGFSDQSIRIQRALPSECQMLLFSATFEDSVWQFAERIIPDPNV IKLRKEELTLNNIRQYYVLCENRKGKYQALCNIYGGITIGQAIIFCQTRRNAKWLTVEMM QDGHQVSLLSGELTVEQRASIIQRFRDGKEKVLITTNVCARGIDVKQVTIVVNFDLPVNQ SEEPDYETYLHRIGRTGRFGKKGLAFNMIEVDKLPLLMKIQDHFNSNIKQLDPEDMDEIE KIEY O35930 Q5SX47 GP1BA_MOUSE Platelet glycoprotein Ib alpha chain GP-Ib alpha GPIb-alpha GPIbA Glycoprotein Ibalpha CD42b Glycocalicin Gp1ba Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J PROTEOLYTIC CLEAVAGE BY ADAM17 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Heart Liver Lung Spleen 3D-STRUCTURE MODELING OF 52-216 GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium. Two GP-Ib beta are disulfide-linked to one GP-Ib alpha. GP-IX is complexed with the GP-Ib heterodimer via a non covalent linkage. Interacts with FLNB. Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23). Membrane Single-pass type I membrane protein O-glycosylated. Glycocalicin is the product of a proteolytic cleavage/shedding, catalyzed by ADAM17, which releases most of the extracellular domain. Binding sites for vWF and thrombin are in this part of the protein. Platelet activation apparently involves disruption of the macromolecular complex of GP-Ib with the platelet glycoprotein IX (GP-IX) and dissociation of GP-Ib from the actin-binding protein. 3D-structure Blood coagulation Cell adhesion Complete proteome Disulfide bond Glycoprotein Hemostasis Leucine-rich repeat Membrane Phosphoprotein Reference proteome Repeat Signal Sulfation Transmembrane Transmembrane helix L V MALLILLFLLPSPLHSQHTCSISKVTSLLEVNCENKKLTALPADLPADTGILHLGENQLG TFSTASLVHFTHLTYLYLDRCELTSLQTNGKLIKLENLDLSHNNLKSLPSLGWALPALTT LDVSFNKLGSLSPGVLDGLSQLQELYLQNNDLKSLPPGLLLPTTKLKKLNLANNKLRELP SGLLDGLEDLDTLYLQRNWLRTIPKGFFGTLLLPFVFLHANSWYCDCEILYFRHWLQENA NNVYLWKQGVDVKDTTPNVASVRCANLDNAPVYSYPGKGCPTSSGDTDYDDYDDIPDVPA TRTEVKFSTNTKVHTTHWSLLAAAPSTSQDSQMISLPPTHKPTKKQSTFIHTQSPGFTTL PETMESNPTFYSLKLNTVLIPSPTTLEPTSTQATPEPNIQPMLTTSTLTTPEHSTTPVPT TTILTTPEHSTIPVPTTAILTTPKPSTIPVPTTATLTTLEPSTTPVPTTATLTTPEPSTT LVPTTATLTTPEHSTTPVPTTATLTTPEHSTTPVPTTATLTTPEPSTTLTNLVSTISPVL TTTLTTPESTPIETILEQFFTTELTLLPTLESTTTIIPEQNSFLNLPEVALVSSDTSESS PFLNSDFCCFLPLGFYVLGLLWLLFASVVLILLLTWTWHVTPHSLDMEQSAALATSTHTT SLEVQRARQVTMPRAWLLFLQGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGRGQD LLGTVGIRYSGHSL Q91WJ0 FRS3_MOUSE Fibroblast growth factor receptor substrate 3 FGFR substrate 3 FRS2-beta Frs3 Frs2b Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Eye INTERACTION WITH FGFR1 AND NTRK1 PHOSPHORYLATION BY ULK2 Adapter protein that links FGF and NGF receptors to downstream signaling pathways. Involved in the activation of MAP kinases. Down-regulates ERK2 signaling by interfering with the phosphorylation and nuclear translocation of ERK2. Binds NGFR, GRB2, PTPN11 and ERK2 (By similarity). Binds FGFR1 and NTRK1. Membrane Lipid-anchor Phosphorylated on tyrosine residues upon stimulation by BFGF or NGFB. Phosphorylated by ULK2 in vitro. Complete proteome Lipoprotein Membrane Myristate Phosphoprotein Reference proteome MGSCWSCLDRDSVPHNHPTKFKVTNVDDEGVELGSGVMELTQSELVLHLHQREAVRWPYL CLRRYGYDSNLFSFESGRRCQTGQGIFAFKCSRAEDIFNLLQDLMQCNSINVTEEPVIIT RSSHPPELDLPRGPPQPAGYTVSGFSNGFPGCPGEGPRFSSAPRRPSTSSLRHPSPGEES THTLIASEEQSHTYVNTPTGDEDGRSRHCLQPLPEGRVPLPAQTQGSDQRDPQVLLQPGQ VKFVLGPTPARRQVMKCQSLCPGMQDPPHHNNNEGPSECPAQPKCTYENVSGGLQQGAGW RLSPEERGWSGLAHRRAALLHYENLPPLPPVWESQGQQPGGEAGDDGDSRDGLTPSSNGF PDGEEDETPLQKPTSTRASARSHSGFPVPLTRRRGSPRVFNFDFRRQGPEPPRQLNYIQV ELKGWGTARPKGPQNPSVSGAPGPTPHPVRSSDSYAVIDLKKTAAMSDLQRALPRDDGAV RKTRHNSTDLPL P50289 B2RT20 Q9DAM6 ASPX_MOUSE Acrosomal protein SP-10 Acrosomal vesicle protein 1 MSA-63 Acrv1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] CD-1 Testis NUCLEOTIDE SEQUENCE [MRNA] CD-1 Testis NUCLEOTIDE SEQUENCE [MRNA] PROTEIN SEQUENCE OF 56-62; 201-211 AND 247-250 CD-1 Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Testis IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis Testis. The N-terminus is blocked. Complete proteome Direct protein sequencing Reference proteome Repeat Signal I L MKELILLGLYLLGSAQGAPPGQPEELLDSVDQQASVQQLSSEYLSLANPSDAEALYETPL DEKTLSGHSSSEQESSEHAVAEHSAGEHSSGEQSSEHMSGDHMSGEHLSEHTSEEHSSGE HTSTEHTSGEQPATEQSSSDQPSEASSGEVSGDEAGEQVSSETNDKENDAMSTPLPSTSA AITINCHTCAYMNDDAKCLRGEGVCTTQNSQQCMLKKIFEGGKLQFMVQGCENMCPSMNL FSHGTRMQIMCCRNEPLCNKV Q9CRW3 Q8K163 CB076_MOUSE UPF0538 protein C2orf76 homolog Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) C57BL/6J Head NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J Head NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Thymus IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis Q9CRW3-1 1 Q9CRW3-2 2 No experimental confirmation available. Belongs to the UPF0538 family. Alternative splicing Complete proteome Reference proteome TNELVLGLEDDDTLLLKEDRTLKDSGVASETEIAFFCGEDYKRYKANPISSW PVKLKLHSSVEKIISDTKLIPSRPGESGCGPLFHKFCFFINCQINLF MAAEEATLTVRLIRSFEHRNFKPVVYHGVNLHQTVKEFIIFLKQDVPLRTSLPPPLRNYK YDTLKILHQAHKAKTNELVLGLEDDDTLLLKEDRTLKDSGVASETEIAFFCGEDYKRYKA NPISSW Q5NCY3 Q5NCY4 CB5D1_MOUSE Cytochrome b5 domain-containing protein 1 Cyb5d1 Gm740 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis Q5NCY3-1 1 Q5NCY3-2 2 Belongs to the cytochrome b5 family. Alternative splicing Complete proteome Heme Iron Metal-binding Reference proteome VGAQESMWEILHRYLPYNAHAAS LHMEIRWEEFEHGSNPGRKRDPG MPRRGLVAGPDLDNFQRRYFTPSEVAEHNQLEDLWVSYLGFVYNLTPLVEEFKGDLLLKP ILEVAGQDISHWFDPQTRDIRKHIDPLTGCMRYRTPRGRFVHIPPPLPRSDWANDFGVPW WKGANYQVGRLSARTRNIRIINTLATQEHTLQVGAQESMWEILHRYLPYNAHAASYTWKY DGKNLNMDQTLEENGIRDEEEEFDYLNMDGKLHTPAILLYFNDDLTEL Q8K221 Q3U3G6 Q9D7M3 ARFP2_MOUSE Arfaptin-2 ADP-ribosylation factor-interacting protein 2 Arfip2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Tongue NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Lung Pancreas Spleen Testis Putative target protein of ADP-ribosylation factor. Involved in membrane ruffling (By similarity). Interacts with RAC1 by binding directly to it. Specifically binds to GTP-bound ARF1 and ARF6, but binds to RAC1.GTP and RAC1.GDP with similar affinities (By similarity). Directly interacts with ARL1 GTP-bound form; this interaction leads to an increase in the amount of bound GTP at steady state level (By similarity). Complete proteome Phosphoprotein Reference proteome T K MTDGILGKAATMEIPIHGNGEAGQLPEDDGLEQDLQQVMVSGPNLNETSIVSGGYGGSGD GLIPTGSGRHPSHSTSPSGPGDEVARGIAGEKFDIVKKWGINTYKCTKQLLSERFGRGSR TVDLELELQIELLRETKRKYESVLQLGRALTAHLYSLLQTQHALGDAFADLSQKSPELQE EFGYNAETQKLLCKNGETLLGAVNFFVSSINTLVTKTMEDTLMTVKQYEAARLEYDAYRT DLEELSLGPRDAGTRGRLESAQATFQTHRDKYEKLRGDVAIKLKFLEENKIKVMHKQLLL FHNAVSAYFAGNQKQLEQTLQQFNIKLRPPGAEKPSWLEEQ P46737 A3KGA9 A8Y5K0 Q3UDZ4 Q9D025 BRCC3_MOUSE Lys-63-specific deubiquitinase BRCC36 3.4.19.- BRCA1-A complex subunit BRCC36 BRCA1/BRCA2-containing complex subunit 3 BRCA1/BRCA2-containing complex subunit 36 BRISC complex subunit BRCC36 Brcc3 Brcc36 C6.1a Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Bone marrow Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ALTERNATIVE SPLICING (ISOFORMS 1 AND 2) C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Brain Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination. Zn(2+) Binds 1 zinc ion per subunit. Component of the ARISC complex, at least composed of UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Component of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. In the BRCA1-A complex, interacts directly with ABRAXAS1 and BABAM2. Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Identified in a complex with SHMT2 and the other subunits of the BRISC complex. In the BRISC complex, interacts directly with ABRAXAS2. Identified in a complex with ABRAXAS2 and NUMA1. The BRISC complex interacts with the CSN complex. Component of the BRCA1/BRCA2 containing complex (BRCC), which also contains BRCA1, BRCA2, BARD1, BABAM2 and RAD51. BRCC is a ubiquitin E3 ligase complex that enhances cellular survival following DNA damage. Interacts with BRCA1. Binds polyubiquitin. Nucleus Cytoplasm Cytoplasm Cytoskeleton Spindle pole Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm. P46737-1 1 P46737-2 2 Belongs to the peptidase M67A family. BRCC36 subfamily. Acetylation Alternative splicing Cell cycle Cell division Chromatin regulator Complete proteome Cytoplasm Cytoskeleton DNA damage DNA repair Hydrolase Metal-binding Metalloprotease Mitosis Nucleus Phosphoprotein Protease Reference proteome Ubl conjugation pathway Zinc EYERIEIPIHIVPHITIGKVCLESAVELPKILCQEEQDAYRRIHS D A S K E K R MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDIRSDSKFTYTGTEMR TVQEKMDTIRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGW YHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQK SSEYERIEIPIHIVPHITIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNG SVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLQELQQEKEELMEELSSLE P22682 Q3U527 Q8CEA1 CBL_MOUSE E3 ubiquitin-protein ligase CBL 2.3.2.27 Casitas B-lineage lymphoma proto-oncogene Proto-oncogene c-Cbl RING-type E3 ubiquitin transferase CBL Signal transduction protein CBL Cbl Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] MUTANT 70Z/3 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Skin Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain INTERACTION WITH LYN PHOSPHORYLATION PHOSPHORYLATION BY SYK PHOSPHORYLATION BY ZAP70 INTERACTION WITH FLT1 INTERACTION WITH SORBS1 FUNCTION PHOSPHORYLATION BY HCK INTERACTION WITH HCK FUNCTION INTERACTION WITH SLA2 AND ZAP70 MUTAGENESIS OF GLY-304 INTERACTION WITH KDR FUNCTION CATALYTIC ACTIVITY INTERACTION WITH CBLB INTERACTION WITH FLT1 AND CD2AP PHOSPHORYLATION IN RESPONSE TO VEGFA PHOSPHORYLATION INTERACTION WITH SLA2 AND CSF1R INTERACTION WITH PDGFRB PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-667 AND TYR-672 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Mast cell INTERACTION WITH ATX2 INTERACTION WITH EPHB1 PHOSPHORYLATION FUNCTION IN UBIQUITINATION OF KIT PHOSPHORYLATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617; SER-640 AND SER-692 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Heart Kidney Lung Spleen Testis FUNCTION IN UBIQUITINATION OF EPHA8 CATALYTIC ACTIVITY INTERACTION WITH SH3KBP1 INTERACTION WITH SIGLEC10 FUNCTION SUBCELLULAR LOCATION Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, EGFR, CSF1R, EPHA8 and KDR and terminates signaling. Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation. Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis. Essential for osteoclastic bone resorption. The 'Tyr-737' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3 (PubMed:10393178, PubMed:12649282, PubMed:19265199, PubMed:20100865, PubMed:9653117). In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (PubMed:29237719). S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Protein modification; protein ubiquitination. Forms homodimers; IFT20 promotes the formation of stable homodimers (By similarity). Interacts (phosphorylated) with PIK3R1. Interacts with phosphorylated LAT2 (By similarity). Associates with NCK via its SH3 domain. The phosphorylated C-terminus interacts with CD2AP via its second SH3 domain. Binds to UBE2L3. Interacts with adapters SLA, SLA2 and with the phosphorylated C-terminus of SH2B2. Interacts with EGFR, SYK and ZAP70 via the highly conserved Cbl-N region. Interacts with FGR. Also interacts with BLK, SORBS1 and INPPL1/SHIP2. Interacts with CBLB. Interacts with TEK/TIE2 (tyrosine phosphorylated) (By similarity). Interacts with ALK, AXL and FGFR2. Interacts with CSF1R, EPHB1, FLT1, KDR, PDGFRA and PDGFRB; regulates receptor degradation through ubiquitination. Interacts with HCK and LYN. Interacts with ATX2. Interacts with SH3KBP1 and this interaction is inhibited in the presence of SHKBP1 (PubMed:21830225). Interacts with SIGLEC10 (PubMed:23374343). Interacts with IFT20 (By similarity). Q9JLQ0 Cd2ap false 5 P13379 Cd5 false 5 Q6Q899 Ddx58 false 3 P00533 EGFR true 2 Q01279 Egfr false 2 P39688 Fyn false 5 P16056 Met false 2 Cytoplasm Cell membrane Cell projection Cilium Golgi apparatus Colocalizes with FGFR2 in lipid rafts at the cell membrane. The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme. The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. Phosphorylated on tyrosine residues by ALK, EGFR, FGR, INSR, SYK, FYN and ZAP70. Phosphorylated on several tyrosine residues by constitutively activated FGFR3. Phosphorylated on tyrosine residues by activated PDGFRA and PDGFRB (By similarity). Phosphorylated on tyrosine residues in response to CSF1R, FLT1 and KIT signaling. Phosphorylated on tyrosine residues by HCK. Ubiquitinated, leading to its degradation via the proteasome. Ubiquitination is negatively regulated by IFT20. Can be converted to an oncogenic protein by deletions or mutations that disturb its ability to down-regulate RTKs. This protein has one functional calcium-binding site. 3D-structure Calcium Cell membrane Cell projection Complete proteome Cytoplasm Golgi apparatus Membrane Metal-binding Phosphoprotein Polymorphism Proto-oncogene Reference proteome Repeat Transferase Ubl conjugation Ubl conjugation pathway Zinc Zinc-finger G E KL NV E D P T N T MAGNVKKSSGAGGGGSGGSGAGGLIGLMKDAFQPHHHHHHLSPHPPCTVDKKMVEKCWKL MDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTVLSRYEGKMETLGENEYFRVFMENL MKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRIT KADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFD IFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQ WAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIK VTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCE IKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDSLFMMKELAGAKVERPS SPFSMAPQASLPPVPPRLDLLQQRAPVPASTSVLGTASKAASGSLHKDKPLPIPPTLRDL PPPPPPDRPYSVGAETRPQRRPLPCTPGDCPSRDKLPPVPSSRPGDSWLSRPIPKVPVAT PNPGDPWNGRELTNRHSLPFSLPSQMEPRADVPRLGSTFSLDTSMTMNSSPVAGPESEHP KIKPSSSANAIYSLAARPLPMPKLPPGEQGESEEDTEYMTPTSRPVGVQKPEPKRPLEAT QSSRACDCDQQIDSCTYEAMYNIQSQALSVAENSASGEGNLATAHTSTGPEESENEDDGY DVPKPPVPAVLARRTLSDISNASSSFGWLSLDGDPTNFNEGSQVPERPPKPFPRRINSER KASSYQQGGGATANPVATAPSPQLSSEIERLMSQGYSYQDIQKALVIAHNNIEMAKNILR EFVSISSPAHVAT Q8BXL7 ARFRP_MOUSE ADP-ribosylation factor-related protein 1 ARF-related protein 1 Arfrp1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] 129/SvJ Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Cerebellum Retina NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] 129 Mammary tumor SUBCELLULAR LOCATION FUNCTION DISRUPTION PHENOTYPE IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis FUNCTION AND DISRUPTION PHENOTYPE FUNCTION DISRUPTION PHENOTYPE FUNCTION AND DISRUPTION PHENOTYPE FUNCTION DISRUPTION PHENOTYPE Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver. Interacts with SYS1. Golgi apparatus Golgi apparatus trans-Golgi network Located in the trans-Golgi in the GTP-bound active state. Disruption of the gene leads to embryonic lethality during early gastrulation. Intestine-specific knockout mice display severe growth retardation due to reduced fat absorption and decrease in lipid release from the intestinal epithelium to the lymph and blood. Liver-specific knockout mice display impaired VLDL lipidation leading to reduced plasma triglyceride levels in the fasted state. Liver-specific knockout mice also display a disturbed glucose metabolism caused by a reduced plasma membrane localization of the glucose transporter GLUT2. Belongs to the small GTPase superfamily. Arf family. Acetylation Complete proteome Golgi apparatus GTP-binding Nucleotide-binding Reference proteome F L MYTLLSGLYKYMFQKDEYCILILGLDNAGKTTFLEQSKTRFNKNYKGMSLSKITTTVGLN IGTVDVGKARLMFWDLGGQEELQSLWDKYYAECHGVIYVIDSTDEERLSESKEAFEKVVS SEALDGVPILVLANKQDVETCLSIPDIKTAFSDCTCKIGRRDCLTQACSALTGKGVREGI EWMVKCVVRNVHRPPRQRDIT Q8R2S9 Q9CYC4 ARP8_MOUSE Actin-related protein 8 Actr8 Arp8 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FUNCTION Plays an important role in the functional organization of mitotic chromosomes. Exhibits low basal ATPase activity, and unable to polymerize (By similarity). Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex (By similarity). Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80. Exists as monomers and dimers, but the dimer is most probably the biologically relevant form required for stable interactions with histones that exploits the twofold symmetry of the nucleosome core (By similarity). Nucleus Chromosome Specifically localizes to mitotic chromosomes. Belongs to the actin family. ARP8 subfamily. Acetylation ATP-binding Cell cycle Cell division Chromosome Complete proteome DNA damage DNA recombination DNA repair Mitosis Nucleotide-binding Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation R G MTQAEKGDAENGKEKGGEKEKEQRGVKRPIVPALVPESLQEQIQSNFIVVIHPGSTTLRL GRATDTLPVSVPHVIARRHKQQGQPLYKDNWLLREGLNKPESNEQRQNGLKMVDQAIWSK KMSNGTRRIPVSPEQTRSYNKQMRPAILDHCSGNKWTNTSQQPEYLVGEEALYVNPLDCY NIHWPIRRGQLNIHPGPGGSLTAVLADIEVIWSHAIQKYLEIPLKDLKYYRCILLIPDIY NKQHVKELVHMILMKMGFAGIVVHQESVCATFGSGLSSTCVVDVGDQKTSVCCVEDGVSH RNTRLCLAYGGSDVSRCFYWLMQRAGFPYRECQLTNKMDCLLLQHLKETFCHLDQDISGL QDHEFQIRHPDSPALLYQFRLGDEKLQAPMALFYPATFGIVGQKMTTLQHRSQGDPEDPH DEHYLLATQSKQEQSAKATADRKSASKPIGFEGDLRGQSSDLPERLHSQEVDLASSQGDC LMAGNESEEALTALMSRKTAISLFEGKALGLDKAILHSVDCCSSDDTKKKMYSSILVVGG GLMFHKAQEFLQHRILNKMPPSFRRIIENVDVITRPKDMDPRLIAWKGGAVLACLDTTQE LWIYQREWQRFGVRMLRERAAFVW Q8CIL4 Q3UNZ3 Q9CZF4 CA131_MOUSE Uncharacterized protein C1orf131 homolog Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Kidney NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Pancreas Spleen Chromosome Acetylation Chromosome Complete proteome Phosphoprotein Reference proteome H T E G R Q G V MAAEHDSDSVEPPGSEALLDAVLRTLYDLGETEGETEQKRIRKKKAKKRDSETIEDVAVE PLPLPGSPVRGQKKSASSFFQKLREELQSAPAAPSEVPVTTAVSLSPPKNGSKLVEVVEF QSKSKKRKLKSDEDEPAKNKTKVVKKDVDIQEFNLEKARLEVHRFGITGYGKGKERVLER ERAIMLGAKPPKNTYVNYKVLQKQIKEKKIAVEEEKRAARETDIFKKKKKKGRGQEDRRS KKSAPSILSSGQVGQVGKFRNGTLILSPTDIKKINSSRVAK Q5SPX1 Q0P531 Q3V0G5 Q5DTW1 Q8C5Y5 CC157_MOUSE Coiled-coil domain-containing protein 157 Ccdc157 Kiaa1656 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Fetal brain NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Brain IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis Q5SPX1-1 1 Q5SPX1-2 2 Alternative splicing Coiled coil Complete proteome Reference proteome K R MAHLLGSQACMDSLRKDLTDLQGTIVDVFSRAGPVRFPSWKFPDRVACDLDMVALLEHYD HVPGDPEFTQLSHAVLLELVIDRLLLLLQSCASYLENLSVEQMMPPARAAGPCMSVGLTV RRFWSNLLRLGLLYQQAVPQKRANQGEISITKPTAKGEPARSPECMTAKFIKPPSPVPGL PLICQGLQSIPVRVSLRSPGGTSEKTKSVYSQTVETALVPCDACTSVQGSLWEVGKVVIS LCQSQNLPSSLGQFQKLVKDSLGLKPLPAATVGHWAAEQSKDLTRLNKHVGALTQLVGPL RAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDL KTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGAS QQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRS ELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKE RERLLVAFPDLHQPEEAQIQSSSNVTQDMERQVQANAIRIQVLQEENKRLQSMLTKIREV AQQGGLKMVPQGQLWSPPYKGIQGATPPAQAQSAFSGLTGRRQSPGSRTSSTGRTHPGGL RTSPSRQPGGLPSKFSLGDGSHSASCTQNPIRALARLRRKLSPNRQAGSTYQPQERPT O88430 CCL22_MOUSE C-C motif chemokine 22 Activated B and dendritic cell-derived CC chemokine ABCD-1 Small-inducible cytokine A22 Ccl22 Abcd1 Scya22 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Salivary gland Chemotactic for activated T-lymphocytes. May play an important role in the collaboration of dendritic cells and B-lymphocytes with T-cells in immune responses. Secreted Expressed by activated splenic B-lymphocytes and dendritic cells. Low expression in lung, thymocytes, lymph node, and unstimulated splenic cells. Belongs to the intercrine beta (chemokine CC) family. Chemotaxis Complete proteome Cytokine Disulfide bond Inflammatory response Reference proteome Secreted Signal MATLRVPLLVALVLLAVAIQTSDAGPYGANVEDSICCQDYIRHPLPSRLVKEFFWTSKSC RKPGVVLITVKNRDICADPRQVWVKKLLHKLS Q62431 Q3U338 Q80YP8 ARI3A_MOUSE AT-rich interactive domain-containing protein 3A ARID domain-containing protein 3A B-cell regulator of IgH transcription Bright Dead ringer-like protein 1 Arid3a Dri1 Dril1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain TISSUE SPECIFICITY DEVELOPMENTAL STAGE INTERACTION WITH BTK FUNCTION DNA-BINDING SUBUNIT SUBCELLULAR LOCATION MUTAGENESIS OF PRO-268; TRP-299; PHE-317 AND TYR-330 SUBCELLULAR LOCATION MUTAGENESIS OF LYS-457; PRO-463; LYS-466; LYS-467; GLY-532; TYR-535; GLY-537 AND LEU-539 INTERACTION WITH GTF2I AND BTK FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-89; SER-127 AND SER-358 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Lung Pancreas Spleen Testis Transcription factor involved in B-cell differentiation. Binds a VH promoter proximal site necessary for induced mu-heavy-chain transcription. Binds the minor groove of a restricted ATC sequence that is sufficient for nuclear matrix association. This sequence motif is present in matrix-associating regions (MARS) proximal to the promoter and flanking E mu. Activates E mu-driven transcription by binding these sites. May be involved in the control of cell cycle progression by the RB1/E2F1 pathway. Homodimer. Heterodimer with ARID3B. Interacts with E2F1 (By similarity). Interacts with GTF2I and BTK. Nucleus Cytoplasm Shuttles between nucleus and cytoplasm. B-cell specific in the adult. Expressed in B-cell progenitors, down-regulated in the immature B-cell stage, and is up-regulated again at later stages of B-lymphocyte differentiation. Expressed in lymphocytes from fetal liver. Expressed in fetal thymus and brain. Activator Complete proteome Cytoplasm DNA-binding Isopeptide bond Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation Ubl conjugation P A W A F A Y A K A P A K A K A G A Y A Y F G A L A MKLQAVMETLIQRQQRARQELEARQAPPPPPPEPTGVRARTTMTDEDREPENARMHRTQM AALAAMRAAAAGLGHPSSPGGSEDGPPISGDEDTAREGTLSSPALHGSVLEGAGHAEGDR HLMDVGSDDDDTKSKWEEQELEELGEEEEEEEEEDDFEEEEEEEEGLGPPESASLGTAGL FTRKAPPAQAFRGDGGPRMLSGPERLGPGPAHPSHMASQMPPPDHGDWTFEEQFKQLYEL DADPKRKEFLDDLFSFMQKRGTPVNRIPIMAKQVLDLFMLYVLVTEKGGLVEVINKKLWR EITKGLNLPTSITSAAFTLRTQYMKYLYPYECERRGLSSPNELQAAIDSNRREGRRQSFG GSLFAYSPSGAHSMLPSPKLPVTPLGLAASTNGSSITPAPKIKKEEDSAIPITVPGRLPV SLAGHPVVAAQAAAVQAAAAQAAVAAQAAALEQLREKLESTEPPEKKMALVADEQQRLMQ RAVQQSFLAMTAQLPMNIRINSQASESRQDSAVSLTSANGSNSISMSVEMNGIVYTGVLF AQPPPPTAPSAPGKGGVSSIGTNTTTGSRTGASGSTVSGGQVGLPGVSTPTMSSTSNNSL P Q9JIB6 O09121 O09122 P81704 Q8CH68 BIR1F_MOUSE Baculoviral IAP repeat-containing protein 1f Neuronal apoptosis inhibitory protein 6 Naip6 Birc1f Naip-rs4 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-168 129/SvJ FUNCTION SUBUNIT INTERACTION WITH S.TYPHIMURIUM FLAGELLIN Sensor component of the NLRC4 inflammasome that specifically recognizes and binds flagellin from pathogenic bacteria. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria (PubMed:21874021). The NLRC4 inflammasome senses Gram-negative bacteria such as L.pneumophila and P.aeruginosa, enteric pathogens S.typhimurium (Salmonella) and S.flexneri. May contribute to prevent motor-neuron apoptosis induced by a variety of signals (By similarity). Component of the NLRC4 inflammasome, at least composed of NLRC4, caspase-1 (CASP1) and some NAIP protein. (Microbial infection) Interacts with S.typhimurium (Salmonella) flagellin. Q48824 flaA true 2 Apoptosis ATP-binding Complete proteome Immunity Inflammatory response Innate immunity Metal-binding Nucleotide-binding Reference proteome Repeat Zinc AR GE MAEHGESSEDRISEIDYEFLAELSARFGMNLVQLAKSQEEEDHKERMKMKKGFNSQMRSE AKRLKTFESYDTFRSWTPQEMAAAGFYHTGVKLGVQCFCCSLILFGNSLRKLPIERHKKL RPECEFLQGKDVGNIGKYDIRVKSPEKMLRGGKARYHEEEARLESFEDWPFYAHGTSPRA LSAAGFVFTGKRDTVQCFSCGGSLGNWEEGDDPWKEHAKWFPKCEFLQSKKSSEEIAQYI QDYEGFVHVTGEHFVKSWVRRELPMVSAYCNDSVFTNEELRMDMFKDWPQESPVGFEALV RAGFFYTGKKDIVRCFSCGGCLEKWAEGDDPMEDHIKFFPECVFLQTLKSSAEVIPTLQS QYALPEATETTRESNHDDAAAVHSTVVDLGRSEAQWFQEARSLSEQLRDTYTKTSFCHMN LPEVCSSLGTDHLLGCDVSIISKHVSQPVQGALTIPEVFSNLSSVMCVEGEAGSGKTTFL KRIAFLWASGCCPLLYRFQLVFYLSLSSITPDQGLANIICTQLLGAGGCISEVCLSSSIQ QLQHQVLFLLDDYSGLASLPQALHTLITKNYLFRTCLLIAVHTNRVRDIRPYLGTSLEIQ EFPFYNTVFVLRKFFSHDIICVEKLIIYFSENKDLQGVYKTPLFVAAVCNDWNQNASAQD DFQDVTLFHSYMQYLSLKYKATAESLQATVSSCGQLALTGLFSSCFEFNSDDLAEAGVDE DVKLTTFLMSKFTAQRLRPVYRFLGPLFQEFLAAVRLTELLSSDRQEDQDLGLYYLRQID SPLKAINSFNIFLYYVSSHSSSKAAPTVVSHLLQLVDEKESLENMSENEDYMKLHPQTFL WFQFVRGLWLVSPESFSSFVSEHLLRLALIFAYESNTVAECSPFILQFLRGRTLALRVLN LEYFWDHPESLLLLRSLKVSINGNKMSSYVDYSFKTYFENLQPPAINEEYTSAFEHVSEW RRNFAQDEEIIKNYENIWPRALPDISEGYWNLSPKPCKIPKLEVQVNNMGPADQALLQVL MEVFSASQSIEFHLFNSSGFLESIRPALELSKASVTKCSMSRLELSRAEQELLLTLPALQ SLEVSETNQLPDQLFHNLHKFLGLKELCVRLDGKPDVLSVLPEEFLNLHHMEKLSIRTST ESDLSKLVKFIQNFPNLHVFHLKCDFLSNCESLMTALASCKKLREIEFSGQCFEAMTFVN ILPNFVSLKILSLKGQQFADKETSEKFAQALGSLRNLEELLVPTGDGIHQVAKLIVRQCL QLPCLRVLAFHDILDDESVIEIARAATSGSFQKLENLDISMNHKITEEGYRNFFQALDNL PNLQMLNICRNIPGRIQVQATTVKALGHCVSRLPSLTRLGMLSWLLDEEDMKVINDVKER HPQSKRLTIFWKWIVPFSPVVLE O35284 A2RT86 BATF_MOUSE Basic leucine zipper transcriptional factor ATF-like B-cell-activating transcription factor B-ATF Batf Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Cecum NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Lung INDUCTION BY STAT3 SUBCELLULAR LOCATION DNA-BINDING INTERACTION WITH JUNB PHOSPHORYLATION AT SER-43 AND THR-48 MUTAGENESIS OF SER-43 AND THR-48 FUNCTION FUNCTION SUBCELLULAR LOCATION DNA-BINDING TISSUE SPECIFICITY DISRUPTION PHENOTYPE INTERACTION WITH JUNB FUNCTION TISSUE SPECIFICITY DISRUPTION PHENOTYPE FUNCTION DNA-BINDING DISRUPTION PHENOTYPE FUNCTION DISRUPTION PHENOTYPE INDUCTION FUNCTION INDUCTION BY STAT3 FUNCTION INDUCTION BY STAT5 FUNCTION DNA-BINDING INTERACTION WITH IRF4; IRF8 AND JUNB MUTAGENESIS OF HIS-55; LEU-56; LYS-63; 69-ARG-LYS-70 AND GLU-77 FUNCTION DNA-BINDING INTERACTION WITH IRF4 AND JUNB FUNCTION DNA-BINDING INTERACTION WITH IRF4 AND JUNB MUTAGENESIS OF HIS-55 AND GLU-77 AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs. Heterodimer; mainly heterodimerizes with JUNB. The BATF-JUNB heterodimer interacts with IRF4 and IRF8. Interacts (via bZIP domain) with IRF4 and IRF8; the interaction is direct. Also forms heterodimers with JUN and JUND. Interacts with IFI35. Q64287 Irf4 false 7 Nucleus Cytoplasm Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells. Detected in postnatal and adult lymphoid tissues such as thymus, spleen and lymph nodes. In thymus most concentrated expression is found in the immediate cortical layer. Differentially expressed during T-cell development in thymus. Highly expressed in Th17, Th1 and Th2 cells and in activated B-cells. Up-regulated by STAT3 in response to DNA damage. Induces by IL12 at late effector stage. Down-regulated by STAT5 in follicular T-helper cells (TfH). Phosphorylated on serine and threonine residues and at least one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription. Mice are fertile and healthy. They display a normal thymus, spleen and lymph node development, and normal CD4(+) and CD8(+) T-cell development. They also show normal development of natural killer T-cells, B-cells, and conventional and plasmacytoid dendritic cells. They however show defects in T-helper 17 cells (Th17) differentiation and are resistant to experimental autoimmune encephalomyelitis. Loss of follicular T-helper cells (TfH), as well as less production of antibodies with switched isotypes in B-cells is also observed. Belongs to the bZIP family. Activator Complete proteome Cytoplasm Differentiation DNA-binding Nucleus Phosphoprotein Reference proteome Repressor Transcription Transcription regulation S A S D T A H Q L A K D RK QT E K MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESED LEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISS PRFQP Q9D541 D3YY17 CCDC7_MOUSE Coiled-coil domain-containing protein 7 Protein BIOT2 Ccdc7 Biot2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY FUNCTION NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] May play a role in tumorigenesis. Exclusively expressed in the testes. Abundantly expressed in mouse cancer cell line derived from epithelial cells. Coiled coil Complete proteome Reference proteome MKCAKHPSTISMKLTSVPELPYKKGLLNSSPKPKEKHNAKSKYGKNESMVLRSPPTGESI VRFALPIPLSKTKDKISADEMVRRITTNLKMVVSNLEDTYGACYDNGEKAAEKSEAEGLS IGDDVSSFLLCCSQFTSQLEEAVKEECGALESLYKWFQQQVNQMEEISKDQSNLEELQSD GKTASLNIVQIAKLARKFEDFKSRLKTRKEVMQTKNEDKEIMAETLKHYGLMEKQIEEFI TSHSALESQTETESQSGTPSVTTRMARMIKIFENQSTMLEKALNDQQTIESKYKQLETDF QMLIMEKTLLEAEIRRLREIERVKSAAKEEQTKKSGKSEKKKFKEKEKYDMKICYLFIPQ LVKMYLNHGLF Q8K4K1 E9PYP9 E9Q074 J3KMS3 Q3TLH1 Q5SUE1 Q8BIC4 CETN4_MOUSE Centrin-4 Centrin4 Cetn4 Cen4 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) FUNCTION CALCIUM-BINDING SUBCELLULAR LOCATION ALTERNATIVE SPLICING (ISOFORM 3) TISSUE SPECIFICITY MISCELLANEOUS C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3) Mammary gland Urinary bladder NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NOD NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Testis SUBUNIT SUBCELLULAR LOCATION TISSUE SPECIFICITY SUBCELLULAR LOCATION PHOSPHORYLATION AT THR-134 BY CK2 IDENTIFICATION BY MASS SPECTROMETRY IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis Ca(2+)-binding protein that may be involved in basal body assembly or in a subsequent step of ciliogenesis. Interacts with G-protein beta-gamma dimers in a calcium-dependent manner. Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Centriole Cytoplasm Accumulates at procentrioles during their elongation. Isoform 3 is not observed in the centriole. Q8K4K1-1 1 Q8K4K1-2 2 Q8K4K1-3 3 Splice4A In brain, specifically expressed in ciliated cells. In retina, expression is localized to the connecting cilium and basal body of photoreceptors (at protein level). Highly expressed in brain, kidney, lung, retina and ovary, and weakly expressed in spleen. Not detected in testis, colon, stomach, thymus, skeletal muscle, heart, intestine or liver. The fourth EF-hand domain has been proven to bind calcium. Phosphorylated on Thr-134 by casein kinase II (CK2) in a light-dependent manner. Belongs to the centrin family. Alternative splicing Calcium Complete proteome Cytoplasm Cytoskeleton Phosphoprotein Reference proteome Repeat N S S G R P MASSQRITLDQWKKKAAKVELNDTQKQEIKEAFDLFDIDGSGTIDLKELKIAMRALGFEP KKEEVKQLIAEIDKEGTGTICFEDFFAIMSVKMSEKDEKEEILKAFKLFDDDATGSISLN NIKRVAKELGENLTEDELQEMLDEADRDGDGEINEEEFLKMMKKTSLY Q9DCT1 O09125 AKCL2_MOUSE 1,5-anhydro-D-fructose reductase AF reductase 1.1.1.263 Aldo-keto reductase family 1 member C-like protein 2 Aldo-keto reductase family 1 member E1 Aldo-keto reductase family 1 member E2 Akr1e2 Akr1cl2 Akr1e1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] CHARACTERIZATION 129/Sv Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Kidney NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Mammary tumor FUNCTION CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY BIOPHYSICOCHEMICAL PROPERTIES C57BL/6J IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Testis Catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. 1,5-anhydro-D-glucitol + NADP(+) = 1,5-anhydro-D-fructose + H(+) + NADPH Inhibited by p-chloromercuribenzoic acid and alkyliodines. 1.02 mM for 1,5-anhydro-D-fructose 0.57 umol/min/mg enzyme Monomer. Cytoplasm Belongs to the aldo/keto reductase family. Complete proteome Cytoplasm NADP Oxidoreductase Reference proteome M I L F MENIPTVGLGTWKASPGEVTDAVKLAINLGYRHFDCAYLYHNESEVGMGISEKIKEGVVK REDLFVVSKLWCTCHKKSLVKTACTNTLEALNLDYLDLYLIHWPMGFKPGEKDIPLDRNG KVIPSHTSFLDTWEAMEDLVFEGLVKNLGVSNFNHEQLERLLDKPGLRVRPITNQIECHP YLNQKKLIDFCHKRNVSVTAYRPLGGSGGGFHLMDDTVIRKIAKKHGKSPAQILIRFQIQ RNLIVIPKSVTPSRIRENIQVFDFELTEKDMEELLSLDKNLRLATFPTTENHQDYPFHIE Y P56485 Q91WI0 ACKR3_MOUSE Atypical chemokine receptor 3 C-X-C chemokine receptor type 7 CXC-R7 CXCR-7 Chemokine orphan receptor 1 G-protein coupled receptor RDC1 homolog RDC-1 Ackr3 Cmkor1 Cxcr7 Rdc1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY 129/SvJ Peritoneal exudate NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Forelimb NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Kidney TISSUE SPECIFICITY DEVELOPMENTAL STAGE FUNCTION TISSUE SPECIFICITY DEVELOPMENTAL STAGE DISRUPTION PHENOTYPE FUNCTION DISRUPTION PHENOTYPE PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; SER-350 AND SER-355 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Lung Spleen DEVELOPMENTAL STAGE FUNCTION FUNCTION DEVELOPMENTAL STAGE DISRUPTION PHENOTYPE FUNCTION SUBCELLULAR LOCATION DEVELOPMENTAL STAGE DISRUPTION PHENOTYPE Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Homodimer. Can form heterodimers with CXCR4; heterodimerization may regulate CXCR4 signaling activity (By similarity).Interacts with ARRB1 and ARRB2 (By similarity). Cell membrane Multi-pass membrane protein Cytoplasm Perinuclear region Early endosome Recycling endosome Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits in a beta-arrestin -dependent manner. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane (By similarity). Not detected in blood, liver, lung and heart, but high expression detected in several tumor cell lines (at protein level). Expressed in heart, spleen, kidney, lung, ovary, brain, testis, astrocytes, neutrophils and B-lymphocytes. Expression detected after 9.5 dpc in the endothelial layer of the forming heart, neural tube, brain and septum transversum. At 10.5 dpc, expressed at high levels in the prosencephalon and in a part of the rhombencephalon and at lower levels in the neural tube, somites and heart. Detected in liver at 11 dpc and 13 dpc, but not at 15 dpc and 17 dpc. During heart development, expression detected mainly in endocardial cells and endocardial cushion mesenchymal cells in both outflow tract and atrioventricular canal regions and to a lesser degree in myocardial cells at 10.5 dpc, in the mesenchyme of the forming valves and in numerous microvessels in the myocardium at 12.5 dpc, and from 14.5 dpc onward mainly in the microvasculature associated with myocardium, valves and great vessels. In developing telencephalon, observed at 11.5 dpc in the ventral telencephalon in proliferative zones of the medial ganglionic eminence (MGE), in ventral part of the lateral ganglionic eminence (LGE) and in Cajal-Retzius (CR) neurons of dorsal telencephalon. At 12.5 dpc, detected in migrating olfactory tubercle neuron precursors and cortical interneurons, and in CR cells and subplate neurons of the cortex. At 13.5 dpc, observed in the germinal zone of MGE in the subpallium, in the marginal zone and cortical subventricular zone (SVZ) of the lateral cortex as well as in pyramidal cells and tangentially migrating interneurons. At postnatal stages, expressed in postnatal cortical plate and in migrating olfactory bulb interneurons in the striatal SVZ and rostral migratory stream. The C-terminal cytoplasmic tail, plays a key role in: correct trafficking to the cell membrane, recruitment of beta-arrestin, ubiquitination, and in chemokine scavenging and signaling functions. The Ser/Thr residues and the Lys residues in the C-terminal cytoplasmic tail are essential for beta-arrestin recruitment and ubiquitination respectively (By similarity). The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated. Ubiquitinated at the Lys residues in its C-terminal cytoplasmic tail and is essential for correct trafficking from and to the cell membrane. Deubiquitinated by CXCL12-stimulation in a reversible manner (By similarity). Lethal at perinatal stages, with most of the neonates dying within 24 hours. Mutants display slightly enlarged heart, but no clear effect on heart functionality is observed. Mutant mice display abnormalities in semilunar valves and ventricles, myocardial degeneration and fibrosis, as well as abnormal intracortical migration of interneurons and premature invasion of the cortical plate. According to PubMed:17804806, mutants display ventricular septal and atrial septal defects. According to PubMed:21246655, mutants display ventricular septal defects but no atrial septal defects. According to PubMed:18442043, no abnormalities in semilunar valve formation or ventricular septal defects are observed. No effect on hematopoiesis, neural development and gastrointestinal vascularization is observed. No apparent bone phenotype is observed. Belongs to the G-protein coupled receptor 1 family. Atypical chemokine receptor subfamily. Cell adhesion Cell membrane Complete proteome Cytoplasm Developmental protein Disulfide bond Endosome G-protein coupled receptor Glycoprotein Membrane Phosphoprotein Receptor Reference proteome Transducer Transmembrane Transmembrane helix Ubl conjugation I T T A MDVHLFDYAEPGNYSDINWPCNSSDCIVVDTVQCPTMPNKNVLLYTLSFIYIFIFVIGMI ANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVITIPVWVVSLVQHNQWPMGELTCKIT HLIFSINLFGSIFFLACMSVDRYLSITYFTGTSSYKKKMVRRVVCILVWLLAFFVSLPDT YYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVILGFAVPFTIIAIFYFLLARAMS ASGDQEKHSSRKIIFSYVVVFLVCWLPYHFVVLLDIFSILHYIPFTCQLENVLFTALHVT QCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQN TK P23198 Q921C4 CBX3_MOUSE Chromobox protein homolog 3 Heterochromatin protein 1 homolog gamma HP1 gamma M32 Modifier 2 protein Cbx3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [MRNA] OF 11-183 C57BL/6J Embryo PROTEIN SEQUENCE OF 160-171 Brain SUBCELLULAR LOCATION INTERACTION WITH TIF1A INTERACTION WITH KMT5B AND KMT5C PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95 AND SER-176 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-5 AND LYS-44 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast FUNCTION IN CIRCADIAN RHYTHMS IDENTIFICATION IN A LARGE PER COMPLEX Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Probably involved in the repression of many genes located in euchromatin, such as E2F1, MYC and CDC25A. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the methyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1 (PubMed:24413057). Mediates the recruitement of NIPBL to sites of DNA damage at double-strand breaks (DSBs) (By similarity). Binds directly to CHAF1A. Interacts with histone H3 methylated at 'Lys-9' (By similarity). Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2 (By similarity). Interacts with INCENP, TRIM28/TIF1B and SP100 (By similarity). Interacts with TIF1/TIF1A (PubMed:8978696). Interacts with MIS12 and DSN1 (By similarity). Can interact directly with CBX5 via the chromoshadow domain (By similarity). Interacts with KMT5B and KMT5C (PubMed:15145825). Interacts with POGZ (By similarity). Interacts with CHAMP1 (By similarity). The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex (PubMed:24413057). Interacts with INCENP (By similarity). Interacts with NIPBL (via PxVxL motif) (By similarity). Interacts with LRIF1 (via PxVxL motif) (By similarity). Q13263 TRIM28 true 2 Nucleus May be associated with microtubules and mitotic poles during mitosis (Potential). Associates with euchromatin and is largely excluded from constitutive heterochromatin. Phosphorylated by PIM1. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis (By similarity). Acetylation Biological rhythms Chromatin regulator Complete proteome Direct protein sequencing Isopeptide bond Nucleus Phosphoprotein Reference proteome Repeat Repressor Transcription Transcription regulation Ubl conjugation MASNKTTLQKMGKKQNGKSKKVEEAEPEEFVVEKVLDRRVVNGKVEYFLKWKGFTDADNT WEPEENLDCPELIEDFLNSQKAGKEKDGTKRKSLSDSESDDSKSKKKRDAADKPRGFARG LDPERIIGATDSSGELMFLMKWKDSDEADLVLAKEANMKCPQIVIAFYEERLTWHSCPED EAQ Q8CDE2 CALI_MOUSE Calicin Ccin Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis Possible morphogenetic cytoskeletal element in spermiogenic differentiation. Cytoplasm Cytoskeleton Perinuclear theca Calyx Sperm head cytoskeletal structure tightly associated to the nucleus. Complete proteome Cytoplasm Cytoskeleton Developmental protein Differentiation Kelch repeat Phosphoprotein Reference proteome Repeat Spermatogenesis MKLEFTEKNYNSFVLQNLNKQRKRKEYWDMALTVDHHVFFAHRNVLAAVSPLVKSLISSN DMKTTDELYITIDPNYLSPATVDQLLDYFYSGKVVISEQNVEELLRGAQYFNTPRLRIHC NDFLIKSIRRVNCLRYLFLAELFELKEVSDLAYSGIRDNFHFWASPEGSMHFMRCPPVIF GRLLRDENLHVLNEDQALSALISWVYFRKEEREKYFKKFFNYINLNAVSNKTLMFASNKL VGLENNSAHATLIESVLMDRKQERPCSLLSYQRKGALLDSVVILGGQKAHGKFNDGVFAY IIQENLWLKLSEMPYRAAALSATAAGRYIYISGGTTEQISGLKTAWRYDMDDNSWTKLPD LPIGLVFHTMVTCGGTVYSVGGSIAPRRYVSNIYRYDERKEAWCLAGKMSIPMDGTAVIT KGDRNLYIVTGRCLVKGYISRVGVVDCFDTCTGEVVQCITFPIEFNHRPLLSFHQDNILR VHSHRQSVEINLQKIKANKSTTSVPLLPNSCPLDVSHAICSIGDSKVFVCGGVTTASDVQ TKDYTINPNAYLLDQKIGEWQTLACPPEALDCPACCLAKLPCKILQRI A2A6Q5 A2A6Q6 B2RXS0 CDC27_MOUSE Cell division cycle protein 27 homolog Cdc27 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ALTERNATIVE SPLICING (ISOFORMS 2 AND 3) C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3) Brain INTERACTION WITH FAM168B Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Protein modification; protein ubiquitination. Homodimer. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5 (By similarity). Interacts with RB. Interacts with FAM168B/MANI (PubMed:20716133). Interacts with MCPH1 (By similarity). Nucleus A2A6Q5-1 1 A2A6Q5-2 2 No experimental confirmation available. A2A6Q5-3 3 No experimental confirmation available. Phosphorylated. Phosphorylation on Ser-427 and Thr-447 occurs specifically during mitosis (By similarity). Belongs to the APC3/CDC27 family. Alternative splicing Complete proteome Nucleus Phosphoprotein Reference proteome Repeat TPR repeat Ubl conjugation pathway K KTFCVLQ MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRL LKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDLVTEFGDSACFTLSL LGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKLTSLQNFSSCL PNTCTTLVSNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSVSYIDSTVI SPDNVPLGPGTAILSKQVQNKPKTGRSLLGGPTALSPLTPSFGILPLETPSPGDGSYLQN YTNTPSVIDVAPTGAPTKKSVARMGQTGTKSVFSQSGNSREVTPVLVAQTQSSGPQTSTT PQVLSPTITSPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKIPNRKTKSKTNKGGLT QPSINDSLEITKLDSSIISEGKITTVTPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSY NCKEAINILSHLPSHHYSTGWVLCQIGRAYFELSEYMQAERIFSEVRRIESFRVEGMEIY STTLWHLQKDVALSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPN YAYAYTLLGHEFVLTEELDKALACFRNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQ KALDINPQSSVLLCHIGVVQHALKKSEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKY KSALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAI DKRYLPDDEEPITQEEQIMGTDESQESSMTDADDTQLHAAESDEF P06797 Q91UZ0 CATL1_MOUSE Cathepsin L1 3.4.22.15 Cathepsin L Major excreted protein MEP p39 cysteine proteinase Cathepsin L1 heavy chain Cathepsin L1 light chain Ctsl Ctsl1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] PARTIAL PROTEIN SEQUENCE NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE GLYCOSYLATION AT ASN-221 Liver NUCLEOTIDE SEQUENCE [MRNA] C3H/An NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain PROTEIN SEQUENCE OF 18-34; 273-292 AND 295-313 CATALYTIC ACTIVITY NUCLEOTIDE SEQUENCE OF 89-300 BNL GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221 Epidermis IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Important for the overall degradation of proteins in lysosomes. Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity. Dimer of a heavy and a light chain linked by disulfide bonds. Lysosome Belongs to the peptidase C1 family. 3D-structure Complete proteome Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Lysosome Protease Reference proteome Signal Thiol protease Zymogen M I G R MNLLLLLAVLCLGTALATPKFDQTFSAEWHQWKSTHRRLYGTNEEEWRRAIWEKNMRMIQ LHNGEYSNGQHGFSMEMNAFGDMTNEEFRQVVNGYRHQKHKKGRLFQEPLMLKIPKSVDW REKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHAQGNQGCNG GLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEFAVANDTGFVDIPQQEKALMKAVA TVGPISVAMDASHPSLQFYSSGIYYEPNCSSKNLDHGVLLVGYGYEGTDSNKNKYWLVKN SWGSEWGMEGYIKIAKDRDNHCGLATAASYPVVN Q6PD28 Q3V3S8 Q8R342 2A5B_MOUSE Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform PP2A B subunit isoform B'-beta PP2A B subunit isoform B56-beta PP2A B subunit isoform PR61-beta PP2A B subunit isoform R5-beta Ppp2r5b Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Dendritic cell Diencephalon NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Embryonic brain IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Spleen As the regulatory component of the serine/threonine-protein phosphatase 2A (PP2A) holoenzyme, modulates substrate specificity, subcellular localization, and responsiveness to phosphorylation. The phosphorylated form mediates the interaction between PP2A and AKT1, leading to AKT1 dephosphorylation. Component of the serine/threonine-protein phosphatase 2A complex (PP2A). This complex consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant scaffold subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with SGO1. Interacts with AKT1. Cytoplasm Ubiquitinated by CUL3-KLHL15 complex; this modification leads to proteasomal degradation. Belongs to the phosphatase 2A regulatory subunit B56 family. Complete proteome Cytoplasm Phosphoprotein Reference proteome Ubl conjugation Q R METKLPPASTPTSPSSPGLSPVPPPDKVDGFSRRSLRRARPRRSHSSSQFRYQSNQQELT PLPLLKDVPASELHELLSRKLAQCGVMFDFLDCVADLKGKEVKRAALNELVECVGCTRGV LIEPVYPDIIRMISVNIFRTLPPSENPEFDPEEDEPNLEPSWPHLQLVYEFFLRFLESPD FQPSVAKRYVDQKFVLMLLELFDSEDPREREYLKTILHRVYGKFLGLRAYIRKQCNHIFL RFIYELEHFNGVAELLEILGSIINGFALPLKTEHKQFLVRVLIPLHSVKSLSVFHAQLAY CVVQFLEKDATLTEHVIRGLLKYWPKTCTQKEVMFLGEMEEILDVIEPSQFVKIQEPLFK QVARCVSSPHFQVAERALYFWNNEYILSLIEDNCHTVLPAVFGTLYQVSKEHWNQTIVSL IYNVLKTFMEMNGKLFDELTASYKLEKQQEQQKAQERQELWRGLEELRLRRLQGTQGAKE APVPRPTPQVAASGGQS Q91VK1 Q9D0N4 BZW2_MOUSE Basic leucine zipper and W2 domain-containing protein 2 Bzw2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Heart Kidney Lung Pancreas Spleen May be involved in neuronal differentiation. Belongs to the BZW family. Acetylation Complete proteome Developmental protein Differentiation Neurogenesis Phosphoprotein Reference proteome F L A R MNKHQKPVLTGQRFKTRKRDEKEKFEPTVFRDTLVQGLNEAGDDLEAVAKFLDSTGSRLD YRRYADTLFDILVAGSMLAPGGTRIDDGDKTKMTNHCVFSANEDHETIRNYAQVFNKLIR RYKYLEKAFEDEMKKLLLFLKAFSEAEQTKLAMLSGILLGNGTLPATILTSLFTDSLVKE GIAASFAVKLFKAWMAEKDANSVTSSLRKANLDKRLLELFPVNRQSVDHFAKYFTDAGLK ELSDFLRVQQSLGTRKELQKELQERLSQECPIKEVVLYVKEEMKRNDLPETAVIGLLWTC IMNAVEWNKKEELVAEQALKHLKQYAPLLAVFSSQGQSELVLLQKVQEYCYDNIHFMKAF QKIVVLFYKADVLSEEAILKWYKEAHAAKGKSVFLDQMKKFVEWLQNAEEESESEGEES P55096 ABCD3_MOUSE ATP-binding cassette sub-family D member 3 68 kDa peroxisomal membrane protein PMP68 70 kDa peroxisomal membrane protein PMP70 Abcd3 Pmp70 Pxmp1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] Swiss Webster Liver NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [MRNA] OF 271-647 Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-260; LYS-399 AND LYS-533 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver DISRUPTION PHENOTYPE Probable transporter involved in the transport of branched-chain fatty acids and C27 bile acids into the peroxisome; the latter function is a crucial step in bile acid biosynthesis. The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity. Homodimer or heterodimer (Potential). Interacts with PEX19 (By similarity). Peroxisome membrane Multi-pass membrane protein Animals show normal activity and have no obvious malformations. However, necroscopy show increased liver size compared to controls, and fibroblasts show reduced numbers of enlarged peroxisomes. They show however a defect in bile acid biosynthesis and they have impaired beta-oxidation of the branched-chain pristanic and phytanic fatty acids on a phytol-loaded diet. Belongs to the ABC transporter superfamily. ABCD family. Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily. Acetylation ATP-binding Complete proteome Glycoprotein Membrane Nucleotide-binding Peroxisome Phosphoprotein Reference proteome Transmembrane Transmembrane helix Transport E G AN NH C R R T S C MAAFSKYLTARNTSLAGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVD KVFLSRLSQILKIMVPRTFCKETGYLLLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSSK DFKRYLFNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTRYLYEEYLQAFTYYKMGNLDN RIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLLVS GLFLTRLRRPIGKMTIMEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTIHSVFRKLV EHLHNFIFFRFSMGFIDSIIAKYVATVVGYLVVSRPFLDLAHPRHLHSTHSELLEDYYQS GRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGRYERTMVSQQEKGIEG AQASPLVPGAGEIINTDNIIKFDHVPLATPNGDILIQDLSFEVRSGANVLICGPNGCGKS SLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGKEDQKKRGISDQ VLKEYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSA VSVDVEDYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKKITEDTVEFGS Q99PU5 Q6ZQ79 ACBG1_MOUSE Long-chain-fatty-acid--CoA ligase ACSBG1 6.2.1.3 Acyl-CoA synthetase bubblegum family member 1 mBG1 Gonadotropin-regulated long chain acyl CoA synthetase GR-LACS Lipidosin Acsbg1 Kiaa0631 Lpd Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION ENZYME ACTIVITY TISSUE SPECIFICITY MUTAGENESIS OF GLY-281 AND LYS-287 Brain NUCLEOTIDE SEQUENCE [GENOMIC DNA] 129/SvJ NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Oviduct NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY ENZYME ACTIVITY FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY DEVELOPMENTAL STAGE TISSUE SPECIFICITY IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-655 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-70 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Testis Catalyzes the conversion of fatty acids such as long-chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (By similarity) (PubMed:11112418, PubMed:12975357, PubMed:14516277). Can activate diverse saturated, monosaturated and polyunsaturated fatty acids (PubMed:11112418, PubMed:14516277). a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate (E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphate ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA Cytoplasm Cytoplasmic vesicle Microsome Endoplasmic reticulum Cell membrane Mainly expressed in brain. Also expressed in adrenal gland and testis. In brain, it is present in cerebral cortical and cerebellar neurons and in steroidogenic cells of the adrenal gland, testis and ovary (at protein level). First detected on embryonic day 18 and increases steadily towards adulthood. Belongs to the ATP-dependent AMP-binding enzyme family. Bubblegum subfamily. Translation N-terminally shortened. ATP-binding Cell membrane Complete proteome Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Fatty acid metabolism Ligase Lipid metabolism Membrane Microsome Nucleotide-binding Phosphoprotein Reference proteome G A K M T I MPRGSEAGYCCLSRDSNMPDSRDDQQQGASLGTSQDNSQTSSLIDGQTLSKESPSHGLEL SAPEKARAASLDGAEEALWTTRADGRVRLRLEPFCTQRPYTVHQMFYEALDKYGNLSALG FKRKDKWERISYYQYYLIARKVAKGFLKLGLERAHSVAILGFNSPEWFFSAVGTVFAGGI VTGIYTTSSPEACQYISHDCRANVIVVDTQKQLEKILKIWKDLPHLKAVVIYQEPPPKKM ANVYTMEELIELGQEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTA RYGSQAGDIQPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFADPDALKGTLVNT LREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPSNDLKPF TSRLADYLVLARVRQALGFAKCQKNFYGAAPMTAETQRFFLGLNIRLYAGYGLSESTGPH FMSSPYNYRLYSSGRVVPGCRVKLVNQDADGIGEICLWGRTIFMGYLNMEDKTCEAIDSE GWLHTGDMGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISSAMLIGDQ RKFLSMLLTLKCTLDPETSEPTDSLTEQAVEFCQRVGSKASTVSEIVGQRDEAVYQAIHE GIQRVNANAAARPYHIQKWAILQRDFSISGGELGPTMKLKRLTVLEKYKDIIDSFYQEQK Q Q9D180 A2ACY9 CFA57_MOUSE Cilia- and flagella-associated protein 57 WD repeat-containing protein 65 Cfap57 Wdr65 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1100-1249 Uterus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1102-1249 C57BL/6J Embryo IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Testis TISSUE SPECIFICITY DEVELOPMENTAL STAGE Predominanly expressed in testis, lung and skin. Weak expression in brain and kidney. Expression in the palate increases from 12.5 up to 15.5 dpc. At 14.5, detected in the nasal epithelium and detected in the medial edge epithelium. At 15.5 dpc, very strong expression in the nasal respiratory epithelium and epidermis, but not in the oral epithelium. In the nasal epithelium, limited to the respiratory, but not the olfactory, epithelium. Translation N-terminally extended. Translation N-terminally extended. Coiled coil Complete proteome Reference proteome Repeat WD repeat MSTVVAQALHVFGLRPHVTNNVFFFDEQIIIFPSGNHCVKYNIDQKWQKFIAGSDKSQGM LALAISPNRRYLAISETVQEKPAVTIYELSSIPCRKRKVLNNFDFQVQKFTSMAFSPDSK YLLTQTSPPDSNLVYWLWEKQKVMAIIKADSQNNPIYQVSISSQDNSQVCITGSGVFKLL RFAEGTLKQINFQRGESSNYLAHAWVSEDRVIVGTDTGKLFLFESGDQRWETSIMVKEST SSRSLEVIQESESLIEFPPLSSPVSSVERMDITTNTQQQAMPQVFAIAAYSKGFACSAGP GRVLLFEKVEEKDFYRESREIRIPTDQQSNDPSQSDKQDVLCLCFSPSEETLIASTNKNQ LYSITMSLTEISKGEAAHFEYLLYPLHSASITGLDTCIRKPLIATCSLDRSVRIWNYESN TLELYKEYQEEAYTVSLHPSGHYIVVGFADKLRLMNLLIDDIRPFKEYSVRGCKECSFSN GGHLFAAVNGNVIHIFTTTSLENINILKGHTGKIRSLVWNLDDSKLVSAGTDGAVYEWNL STGKRETECVLKSCSYNSVTTSPDAKVIFAVGSDQTLKEISDSLILREIPAFDVIYTSIT ISHSGRMIFVGTSVGTIRAMKYPLSLQKEYNEYQAHAGPVMKMLLTFDDQFLLTVGEDGC LFTWKVFDKDGRGIKREREVGFAEEVLVTKTDMEEKAQIMLELKTRVEELKMENEYQLRL KDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTRELQDLE CCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTGL LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRK KFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYD LKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELN ITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKY VQRADMVEIAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYVRIMQENVSLI KEINELRRELKLTRSQIYDLESALKVSKKTRSQEVPESVISKDVVGSTSTMRLNEQEETG RIIEMQRLEIRRLRDQIQEQEQVPGFHTIAGVRLPSIVDSDVDFEVHTK Q8BH83 Q3TA09 Q8BHR3 ANKR9_MOUSE Ankyrin repeat domain-containing protein 9 Ankrd9 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Cerebellum Spleen NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor ANK repeat Complete proteome Hydrolase Reference proteome Repeat MPWDTRPGRSANGGPEGPGAARLRVQKQCRKSSFAFYLAVRDQLPVWLLEDIRASEAFHC DERGRAAAYSPSEALLYALVHDHQAYAHYLLATFPRCALAPPSAGFRCCTAPGPHVALAV RYNRVGILRRILRTVQDFPVEERVRLLDRRGCSRVEGGGTSLHVACELARPECLFLLLGH GASPGLRDGSGFTPLELLLRQLNQDASSAPTKAEAASATVNAATANTTSSEEVCQRRLLL LDLLVLYTPGGVVGPARCELLGDQLRWQRLLGEDKFQWLAGLAPPSLFVRAMQVLVTTIS PGRFPEALDELPLPSFLQPLDLTGKG P70408 Q3UUB3 Q80WS7 CAD10_MOUSE Cadherin-10 T2-cadherin Cdh10 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Spinal cord NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain NUCLEOTIDE SEQUENCE [MRNA] OF 516-788 DEVELOPMENTAL STAGE C57BL/6J Testis NUCLEOTIDE SEQUENCE [MRNA] OF 732-771 CBA/J Thymocyte PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-784 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Cell membrane Single-pass type I membrane protein Expressed at all stages of testicular development with highest levels found in fetal gonad. Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. 3D-structure Calcium Cell adhesion Cell membrane Cleavage on pair of basic residues Complete proteome Glycoprotein Membrane Metal-binding Phosphoprotein Reference proteome Repeat Signal Transmembrane Transmembrane helix P S PLGGQKFF VDRRSFS T A AGLS WPH D G N K A S MTIYQFLRLFVLWACLPHFCCPELTFRRTPGIQQMTAESRAPRSDGKILHRQKRGWMWNQ FFLLEEYTGSDYQYVGKLHSDQDKGDGSLKYILSGDGAGTLFIIDEKTGDIHATRRIDRE EKAFYTLRAQAINRRTLRPVEPESEFVIKIHDINDNEPTFPEEIYTASVPEMSVVGTSVV QVTATDADDPSYGNSARVIYSILQGQPYFSVEPETGIIRTALPNMNRENKEQYQVVIQAK DMGGQMGGLSGTTTVNITLTDVNDNPPRFPQNTIHLRVLESSPVGTAVGSVKATDADTGK NAEVDYRIIDGDGTDMFDIITEKDTQEGIITVKKPLDYENRRLYTLKVEAENTHVDPRFY YLGPFKDTTIVKISIEDVDEPPVFSRSSYLFEVHEDIEVGTIIGTVMARDPDSTSSPIRF TLDRHTDLDRIFNIHSGNGSLYTSKPLDRELSQWHNLTVIAAEINNPKETTRVSVFVRIL DVNDNAPQFAVFYDTFVCENARPGQLIQTISAVDKDDPLGGQKFFFSLAAVNPNFTVQDN EDNTARILTRKNGFNRHEISTYLLPVVISDNDYPIQSSTGTLTIRVCACDSQGNMQSCSA EALLLPAGLSTGALIAILLCIIILLVIVVLFAALKRQRKKEPLILSKEDIRDNIVSYNDE GGGEEDTQAFDIGTLRNPAAIEEKKLRRDIIPETLFIPRRTPTAPDNTDVRDFINERLKE HDLDPTAPPYDSLATYAYEGNDSVAESLSSLESGTTEGDQNYDYLREWGPRFNKLAEMYG GGESDKDA Q9CVD2 ATX3_MOUSE Ataxin-3 3.4.19.12 Machado-Joseph disease protein 1 homolog Atxn3 Mjd Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NOD Stomach Thymus PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268 AND SER-273 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-268; SER-272; SER-273 AND SER-321 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Heart Kidney Lung Spleen Testis FUNCTION INTERACTION WITH STUB1 UBIQUITINATION MUTAGENESIS OF CYS-14 INTERACTION WITH BECN1 FUNCTION DOMAIN 3D-STRUCTURE MODELING Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (By similarity). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (By similarity). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (PubMed:21855799). Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription (By similarity). Regulates autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of BECN1 (PubMed:28445460). Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Interacts with DNA repair proteins RAD23A and RAD23B (By similarity). Interacts with STUB1/CHIP (when monoubiquitinated) (PubMed:21855799). Interacts with BECN1 (via its poly-Gln domain) (PubMed:28445460). Nucleus The UIM domains bind ubiquitin and interact with various E3 ubiquitin-protein ligase, such as STUB1/CHIP. They are essential to limit the length of ubiquitin chains (PubMed:21855799). Monoubiquitinated by UBE2W, possibly leading to activate the deubiquitinating enzyme activity (By similarity). Complete proteome Hydrolase Isopeptide bond Nucleus Phosphoprotein Protease Reference proteome Repeat Thiol protease Transcription Transcription regulation Ubl conjugation Ubl conjugation pathway C A MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERLRMAEGGVTSEDYRT FLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHW FTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQM IKVQQMHRPKLIGEELAHLKEQSALKADLERVLEAADGSGIFDEDEDDLQRALAISRQEI DMEDEEADLRRAIQLSMQGSSRSMCENSPQTSSPDLSSEELRRRREAYFEKQQQQQQEVD RPGPLSYPRERPTTSSGGRRSDQGGDAVSEEDMLRAAVTMSLETAKDNLKAERKK Q3UPP8 Q80ZM0 CEP63_MOUSE Centrosomal protein of 63 kDa Cep63 Cep63 D9Mgc48e Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) C57BL/6J Ovary NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-700 (ISOFORM 3) Embryo PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488 AND SER-492 (ISOFORM 3) IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Spleen SUBCELLULAR LOCATION FUNCTION 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. Also recruits CDK1 to centrosomes. 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 in delay mitotic progression. Interacts with CEP152 and CDK1; these interactions recruit both ligands to centrosomes. 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. A2AUM9 Cep152 false 2 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 WDR62in 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. Q3UPP8-1 1 Q3UPP8-2 2 No experimental confirmation available. Q3UPP8-3 3 Contains a phosphoserine at position 488. Contains a phosphoserine at position 492. 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. Acetylation Alternative splicing Cell cycle Cell division Coiled coil Complete proteome Cytoplasm Cytoskeleton DNA damage Mitosis Phosphoprotein Reference proteome AKEISLADLQENYIEALN VHTSTLSFCVFEAFERNC MEALLEGIQNRGHSGGFLTSCEAELQELMKQIDIMVAHKKSEWEGQTHALETCLDIRDRE LKALRSQLDMKHKEVGILHQQIEEHEKTKQEMAMEYKEELLKLQEELSRLKRSYEKLQKK QLREFRGNTKSFREDRSEIERLTGKIEEFRQKSLDWEKQRLIYQQQVSSLEAQRKALAEQ SEIIQAQLANRKQKLESVELSSQSEIQHLNSKLERAKDTICANELEIERLNIRVNDLMGT NMTILQDHRQKEEKLRESEKLLEALQEEQKELKASLQSQETFILEAKMQEKLQTTLKAVG TQQSVERPLEDCQKERKYSSPGQGVLDNVLSQLDFSHSSEELLQAEVTRLEGSLESVSAT CKQLSQELMEKYEELKRMEGHNNEYRTEIKKLKEQILQADQTYSSALEGMKMEISQLTRE LHQRDITIASAKCSSSDMEKQLKAEMQKAEEKAVEHKEILSQLESLKLENHRLSETVMKL ELGLHEAKEISLADLQENYIEALNKLVSENQQLQKDLMSTKSELEHATNMCKKKDGEIFN PAHSRAAGFKNAELKPIHGQHRHDGIKTEQYKTGHHSPRGQTLDSIDPVARGPSPLSSHI SPGSSTVSLPSNFLFEAHSLPSVLDINDVNFSDSLSDCMNDQEEFVSSGSLPTSPLGSIA TRFLEEEELRSHHILERLDAHIEELKRESEKTVRQFTALV Q91ZK0 A7MCU6 AP2D_MOUSE Transcription factor AP-2-delta AP2-delta Activating enhancer-binding protein 2-delta Tfap2d Tcfap2d Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] FUNCTION SUBUNIT TISSUE SPECIFICITY C57BL/6J Fetal head NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] DEVELOPMENTAL STAGE 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. Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Q91X20 Ash2l false 4 Nucleus Expressed in both embryonic and newborn brain. Expression is first detected at 9.5 dpc in the central nervous system and the developing heart. The signal detected in heart persists through to 10.5 dpc. Diffusely expressed in developing brain at 10.5 dpc to 11.5 dpc, but by 13.5 dpc expression is mostly confined to the midbrain and forebrain. Also expressed in the spinal cord at 10.5 dpc, and in retinal epithelium from 13.5 dpc to 16.5 dpc. No signals detected in tissues such as the neural crest, facial mesenchyme, and limbs where other Tfap2 genes are expressed. Belongs to the AP-2 family. Activator Complete proteome DNA-binding Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation T A MSTTFPGLVHDAEIRHDGSNSYRLMQLGCLESVANSTVAYSSSSPLTYSTTGTEFASPYF STNHQYTPLHHQSFHYEFQHSHPAVTPDAYSLNSLHHSQQYYQQIHHGEPTDFINLHNAR ALKSSCLDEQRRELGCLDAYRRHDLSLMSHGSQYGMHPDQRLLPGPSLGLAAAGADDLQG SVEAQCGIVLNGQGGVIRRGGTCVVNPTDLFCSVPGRLSLLSSTSKYKVTIAEVKRRLSP PECLNASLLGGILRRAKSKNGGRCLREKLDRLGLNLPAGRRKAANVTLLTSLVEGEALHL ARDFGYTCETEFPAKAVGEHLARQHMEQKEQTARKKMILATKQICKEFQDLLSQDRSPLG SSRPTPILDLDIQRHLTHFSLITHGFGTPAICAALSTFQTVLSEMLNYLEKHTTHKNGGA ADSGQGHANSEKAPLRKASEAAVKEGKTEKTD Q8VE42 Q9Z2S1 ANR49_MOUSE Ankyrin repeat domain-containing protein 49 Fetal globin-increasing factor Fetal globin-inducing factor Ankrd49 Fgif Gbif Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] DEVELOPMENTAL STAGE TISSUE SPECIFICITY Fetal liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Spleen FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY DEVELOPMENTAL STAGE May have a role in spermatogenesis where it promotes autophagy in response to serum starvation, via the NF-kappaB pathway. Nucleus Expressed in spermatogonia, spermatocytes and round spermatids. Expressed in liver at embryonic stage 13 dpc, and in liver, brain and lung at 16 dpc (PubMed:11162141). In testis, expression levels steadily increase from 1 week after birth and plateau by 8 weeks after birth (PubMed:26043108). ANK repeat Complete proteome Differentiation Nucleus Phosphoprotein Reference proteome Repeat Spermatogenesis L Q MEKEKKDDEKPDLENSVDFSEQFNQLELLKTHGHLIPTGTQSLWVGNSDEDEEQEEKNEE WYQLQEKKMEKDPSKLLLWAAEKNRLATVQRLLSEKAAEVNTRDEDEYTPLHRAAYSGHI DVVRELVAKGADVHAVTVDGWTPLHSACKWNNTKVASFLLQHDADINAQTKGLLTPLHLA AGNRDSRDTLELLLMNRYIKPELKNNSQETASDIARRTSIYHYLFEIAEGCTNSSPPS Q3TCJ1 Q3TB08 Q8K0R4 ABRX2_MOUSE BRISC complex subunit Abraxas 2 Abraxas brother protein 1 Protein FAM175B Abraxas2 Abro1 Fam175b Kiaa0157 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-415 FVB/N Kidney IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Liver Lung Pancreas Spleen Testis FUNCTION TISSUE SPECIFICITY INDUCTION BY HEART ISCHEMIA INTERACTION WITH ATF4 FUNCTION DISRUPTION PHENOTYPE FUNCTION Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm (By similarity). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (PubMed:21195082). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression (PubMed:24075985, PubMed:26344097). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985). Required for normal induction of p53/TP53 in response to DNA damage. Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage (By similarity). Component of the BRISC complex, at least composed of ABRAXAS2, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1. Interacts with BRCC3/BRCC36; the interaction is direct. Interacts with BABAM1. Does not interact with BRCA1. Interacts with SHMT1 and SHMT2; the interaction is direct. Identified in a complex with SHMT2 and the other subunits of the BRISC complex. The BRISC complex binds monoubiquitin and both 'Lys-48'- and 'Lys-63'-linked polyubiquitin. Identified in complexes with IFNAR1, IFNAR2 and SHMT2. Interacts with THAP5 (By similarity). Interacts with ATF4 (PubMed:22974638). Identified in a complex with p53/TP53 and USP7; interacts directly with both proteins. Interacts with NUMA1. Interacts with microtubule minus ends. Binds polyubiquitin (By similarity). Cytoplasm Nucleus Cytoplasm Cytoskeleton Spindle pole Cytoplasm Cytoskeleton A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K-fibers. Co-localizes with NUMA1 at mitotic spindle poles. Detected in heart (at protein level). Up-regulated in heart in response to ischemia and reperfusion (at protein level). Mice are viable and fertile, and are protected against toxic shock caused by bacterial lipopolysaccharide (LPS). IFNAR1 'Lys-63'-linked ubiquitination and IFNAR1 internalization are increased. Interaction with THAP5 has been shown in human, but rodents lack a THAP5 homolog. Belongs to the FAM175 family. Abro1 subfamily. Although strongly related to the ABRAXAS1 protein, lacks the C-terminal pSXXF that constitutes a specific recognition motif for the BRCT domain of BRCA1. Cell cycle Cell division Coiled coil Complete proteome Cytoplasm Cytoskeleton Microtubule Mitosis Nucleus Phosphoprotein Reference proteome Ubl conjugation pathway MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSISDSQISNTEFLQVIEIHNHQ PCSQLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNTQQQMSYREQVIHKQLTRIL GVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLAIPNLGNTSQQEYKVSSVPN TSQSYAKVIKEHGTDFFDKDGVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAE VNKLRRQITQKKNEKEQERRLQQALLSRQMPSESLEPAFSPRMSYSGFSAEGRSTLAETE PSDPPPPYSDFHPNNQESTLSHSRMERSVFMPRPQAVGSSSYASTSGGLKFTGSGADLLP SQSAAGDSGEESDDSDYENLIDPAESPHSEYSHSKNSRPSTHPDEDPRNTQTSQI Q9JHH9 A2A6D6 COPZ2_MOUSE Coatomer subunit zeta-2 Zeta-2-coat protein Zeta-2 COP Copz2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Salivary gland SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Heart Liver Lung Pancreas Testis The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity). Oligomeric complex. Cytoplasm Cytosol Endoplasmic reticulum-Golgi intermediate compartment membrane Peripheral membrane protein Cytoplasmic side Golgi apparatus membrane Peripheral membrane protein Cytoplasmic side Cytoplasmic vesicle COPI-coated vesicle membrane Peripheral membrane protein Cytoplasmic side The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows a significant preference for ERGIC and cis-Golgi apparatus compared with trans-Golgi network. Belongs to the adaptor complexes small subunit family. Complete proteome Cytoplasm Cytoplasmic vesicle ER-Golgi transport Golgi apparatus Membrane Protein transport Reference proteome Transport MQRPEAWPRPHPGEGASAAQAGGAAPPTRATEQREPSLYTIKAVFILDNDGRRLLAKYYD DTFPSVKEQMVFEKNVFNKTSRTESEIAFLGGMTIVYKSSIDIFLYVVGSSSENELMLMS VLACLFDSLSHILRKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQKVNFRTDD SGLTEQSVAQVLQSAKEQIKWSLLK Q3U3W5 D3YU52 Q8BLF8 Q8BLG1 ANM9_MOUSE Protein arginine N-methyltransferase 9 Protein arginine N-methyltransferase 10 2.1.1.320 Prmt9 Prmt10 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J NOD Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of SF3B2. Involved in the regulation of alternative splicing of pre-mRNA. L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Found in a complex with PRMT9, SF3B2 and SF3B4. Interacts with SF3B2. Cytoplasm Q3U3W5-1 1 Q3U3W5-2 2 Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. This protein should not be confused with Fbxo11 (AC Q7TPD1) that was initially erroneously named Prmt9. Alternative splicing Complete proteome Cytoplasm Methyltransferase Reference proteome Repeat S-adenosyl-L-methionine TPR repeat Transferase LSLVVTETV CVYKSLKTL L V E G Q H MPNSRPRPRRGAGGGAGAAGRDRLVARSLQSAEHCLGDQDFGTAYAHYLLVLSLAPELKD DVKETFQYTLFKWAEELHALSRIQDLLGCYEQALELFPDDEVICNSMGEHLFRMGFRDEA AGYFHKAVKLNPDFNDAKENFYRVANWLVERWHFIMLNDTRRNMVYNAAIQKAVCLGSRT VLDIGTGTGILSMFAKKAGAQSVYACELSKTMYELACDVVAANKMENGIKLLHMKSLDIE IPKHIPERLSLVVTETVDAGVFGEGIVESLIHAWEHLLLQPKTKEENGNCGKYGKVIPAG AVIFGMAVECAEIRRHHRVGAKDIAGIHLPTNVKFQSPAYTSVDTEETVEPYTTEKMSGI PGGYLPLTECFQIMKVDFNNLQELKSLATKKPHSLNVPAIKEGVLDAIMVWFVLQLDDEY SLSTSPSEETCWEQAVYPVQALEDYCIQPGDRVTMEASCHDCYLRIQGISILHLEHEMEV MKGFTKSKDLLSLGNEAELCSALANLQTSRPEALEQTCMLEPTEIALLNNIPYHEGFKTA MRKVLSSLAPELLWQPMDTHCQYMEMNSGSGQSDAAPSTADPFYVLDVSEGFSLLPILAG TLGHVKPYSSVEKDQHCIALDLIAEANHFPKETLEFWLRHIEDEAAVLQRPKSDKLWSII ILDVIEPSGLIQQELMEKAAISRCLLQSGGKIFPQYVLMFGMLVESQTLVEESAVQGTEH TLGLNIAPFINQFQVPIRVCLDLSSLPCVPLSQPVELLRLDLMTPYLNTSNKEVKVRVCR SGRVTAVPFWFHLCLDDEVRLDTSGEASHWKQAAVVLDNPIQVQAGEELVLSVEHHKSNV SIAVKP Q9D8L0 Q9CPS4 CK052_MOUSE Uncharacterized protein C11orf52 homolog Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J Pancreas Tongue NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) C57BL/6J FVB/N Mammary tumor Q9D8L0-1 1 Q9D8L0-2 2 Alternative splicing Complete proteome Phosphoprotein Reference proteome M MSENQLGSLGDTTAM MGNRLCCGGTWSCPSTFQKKSKTGSHPRPTLSILKQQQLWQNGTKDYETTAPTYEQVLYP PASQKKTSNSTSEESDLHYADIHVLRQIRPHSLHTVKCLHSESATEYATLRFPQATPQYD SNNGTLV O54754 Q9WU85 Q9Z2Z5 AOXA_MOUSE Aldehyde oxidase 1 1.2.3.1 Azaheterocycle hydroxylase 1 1.17.3.- Retinal oxidase Aox1 Ao Ro Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] SUBCELLULAR LOCATION INDUCTION TISSUE SPECIFICITY CD-1 Liver NUCLEOTIDE SEQUENCE [MRNA] FUNCTION AS RETINAL OXIDASE CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES HOMODIMER C57BL/6 X CBA Liver NUCLEOTIDE SEQUENCE [GENOMIC DNA] DEVELOPMENTAL STAGE 129/Sv Thymus NUCLEOTIDE SEQUENCE [MRNA] OF 561-746 TISSUE SPECIFICITY C57BL/6J Liver FUNCTION IN ADIPOGENESIS DEVELOPMENTAL STAGE INDUCTION FUNCTION AS OXIDASE CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY HOMODIMER KINETIC PARAMETERS REACTION MECHANISM ACTIVE SITE MUTAGENESIS OF VAL-806; MET-884 AND GLU-1265 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Liver Lung TISSUE SPECIFICITY IDENTIFICATION OF PARALOGS FUNCTION IN XENOBIOTIC METABOLISM TISSUE SPECIFICITY Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Also plays a role in the reductive metabolism of the xenobiotic imidacloprid (IMI) via its nitroreduction to nitrosoguanidine (IMI-NNO) and aminoguanidine (IMI-NNH(2)). Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis. Cannot use xanthine and hypoxanthine as substrate. an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2 H2O + O2 + retinal = H(+) + H2O2 + retinoate [2Fe-2S] cluster Binds 2 [2Fe-2S] clusters per subunit. FAD Binds 1 FAD per subunit. Mo-molybdopterin Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. 3.8 uM for retinal (at 37 degrees Celsius and pH 7.8) 97.7 uM for benzaldehyde (at 30 degrees Celsius and pH 7.5) 11.4 uM for phthalazine (at 30 degrees Celsius and pH 7.5) 55.8 uM for retinal (at 30 degrees Celsius and pH 7.5) 17.5 mM for acetaldehyde (at 30 degrees Celsius and pH 7.5) 807 nmol/min/mg enzyme with retinal as substrate (at 37 degrees Celsius and pH 7.8) kcat is 317.6 min(-1) for benzaldehyde oxidation, 128.1 min(-1) for phthalazine oxidation, 49.5 min(-1) for retinal oxidation, and 519.9 min(-1) for acetaldehyde oxidation (at 30 degrees Celsius and pH 7.5) (PubMed:19401776). However in this article, the measures are done with the recombinant protein, which is only 20% active, due to an incomplete saturation of the molybdenum cofactor with the sulfido ligand (PubMed:19401776). Homodimer. Cytoplasm Highest expression in esophagus. Moderately low expression in lung, liver, heart, Harderian gland, olfactory mucosa, skin and testis. In brain, expression is very high in choroid plexus, high in hind brain and low in hippocampus and cerebellum. In spinal cord expression is strongest in anterior horns. Low expression detected in spleen and eye. AOX1 expression in the livers of mice is approximately seven times greater in males than females. Expressed in adult liver but not in neonatal or embryonic liver. Not detected in preadipocytes but strongly induced in mature adipocytes. Repressed by pioglitazone, fenofibrate and PPARA agonists. Induced by testosterone. AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (PubMed:23263164). Belongs to the xanthine dehydrogenase family. 2Fe-2S Complete proteome Cytoplasm FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum Oxidoreductase Phosphoprotein Polymorphism Reference proteome H Q A G R T R A KQ NE E D E D N D C W V E M R E Q MDPIQLLFYVNGQKVVEKNVDPEMMLLPYLRKNLRLTGTKYGCGGGGCGACTVMISRYNP STKAIRHHPVNACLTPICSLHGTAVTTVEGLGNTRTRLHPIQERIAKCHGTQCGFCTPGM VMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKASACCQSKENGVCCL DQEINGLAESQEEDKTSPELFSEEEFLPLDPTQELIFPPELMRIAEKQPPKTRVFYGERV TWISPVTLKELVEAKFKYPQAPIVMGYTSVGPEVKFKGVFHPIIISPDRIEELGVISQAR DGLTLGAGLSLDQVKDILADIVQKLPEEKTQTYRALLKHLRTLAGSQIRNMASLGGHIVS RHLDSDLNPLLAVGNCTLNLLSKDGERRIPLSEEFLRKCPEADLKPQEVLVSVNIPWSRK WEFVSAFRQAQRQQNALAIVNSGMRVLFREGGGVIEELSILYGGVGSTIISAKNSCQRLI GRPWNEGMLDTRCRLVLDEVTLAASAPGGKVEFKRTLIISFLFKFYLEVSQGLKREDPGH SPSLAGNHESALDDLHSKHPWRTLTHQNVDPAQLPQDPIGRPIMHLSGIKHATGEAIYCD DMPAVDRELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITADHLQEANTFGTETFLAT DEVHCVGHLVCAVIADSETRAKQAAKQVKVVYQDLAPLILTIEEAIQHKSFFKSERKLEC GNVDEAFKIVDQILEGEIHIGGQEHFYMETQSMLVVPKGEDGEIDIYVSTQFPKYIQDIV AATLKLSANKVMCHVRRVGGAFGGKVGKTSILAAITAFAASKHGRAVRCILERGEDMLIT GGRHPYLGKYKAGFMNEGRILALDVEHYCNGGCSLDESLWVIEMGLLKLDNAYKFPNLRC RGWACRTNLPSNTALRGFGFPQAGLVTEACITEVAIKCGLSPEQVRTINMYKHVDTTHYK QEFSAKALSECWRECMAKCSYFERKAAIGKFNAENSWKKRGMAVIPLKFPVGIGSVAMGQ AAALVHIYLDGSALVSHGGIEMGQGVHTKMIQVVSRELRMPMSSVHLRGTSTETVPNTNA SGGSVVADLNGLAVKDACQTLLKRLEPIISKNPQGTWKDWAQTAFDQSISLSAVGYFRGY ESNIDWEKGEGHPFEYFVFGAACSEVEINCLTGDHKNIRTNIVMDVGHSINPALDIGQVE GAFIQGMGLYTIEELSYSPQGTLYSRGPNQYKIPAICDIPTEMHISFLPPSEHSNTLYSS KGLGESGVFLGCSVFFAIHDAVKAARQERGISGPWKLNSPLTPEKIRMACEDKFTKMIPR DEPGSYVPCNIPV Q9CQF3 Q3UJK1 CPSF5_MOUSE Cleavage and polyadenylation specificity factor subunit 5 Nucleoside diphosphate-linked moiety X motif 21 Nudix motif 21 Nudix hydrolase 21 Nudt21 Cpsf5 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J DBA/2J Embryo Embryonic head Embryonic liver Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J FVB/N Embryonic brain Mammary tumor INTERACTION WITH PAPOLA DOMAIN FUNCTION SUBCELLULAR LOCATION TISSUE SPECIFICITY INDUCTION CHROMATIN BINDING IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Spleen Testis ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast METHYLATION [LARGE SCALE ANALYSIS] AT ARG-15 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain FUNCTION 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. 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). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. 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. NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7. Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (By similarity). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function(PubMed:29249356). Binds to chromatin (PubMed:18032416). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (By similarity). Homodimer (via N- and C-terminus); binds RNA as homodimer. 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. The cleavage factor Im (CFIm) complex associates with the CPSF and CSTF complexes to promote the assembly of the core mRNA 3'-processing machinery. Interacts with CPSF6 (via the RRM domain); this interaction is direct and enhances binding to RNA. Interacts with CPSF7. Interacts with FIP1L1; this interaction occurs in a RNA sequence-specific manner. Interacts with PABPN1 (By similarity). Interacts (via N-terminus) with PAPOLA (via C-terminus); this interaction is direct and diminished by acetylation (PubMed:11716503). Interacts with SNRNP70 (By similarity). Interacts with VIRMA (By similarity). 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). In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles. Expressed in testis (PubMed:18032416). Expressed in male germ cells (at protein level) (PubMed:18032416). Up-regulated during spermatogenesis (PubMed:18032416). 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 is not expected to have hydrolase activity. Acetylation Complete proteome Cytoplasm Differentiation Methylation mRNA processing Nucleus Phosphoprotein Reference proteome RNA-binding L F MSVVPPNRSQTGWPRGVNQFGNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSV AARFQRMREEFDKIGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEG LKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQ EKALFAVPKNYKLVAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYN Q91V76 CK054_MOUSE Ester hydrolase C11orf54 homolog 3.1.-.- Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Kidney Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate. Monomer. Nucleus Complete proteome Hydrolase Metal-binding Nucleus Reference proteome Zinc MACSEFSFHMPSLEELAEVLQKGLTDNFADVQVSVVDCPDLTKEPFTFPVRGICGQTRIA EVGGVPYLLPLVNKKKVYDLNEIAKVIKLPGAFILGAGAGPFQTLGFNSEFMPIVQTASE HNQPVNGSYFAHKNPADGACLLEKYSQKYHDFGCALLANLFASEGQPGKVIEVQAKRRTG ELNFVSCMRQTLEEHYGDKPVGMGGTFIVQKGKVKAHIMPAEFSSCPLNSDEAVNKWLHF YEMKAPLVCLPVFVSKDPGLDLRLEHTHFFSHHGEGGHYHYDTTPDTVEYLGYFSPAQFL YRIDQPKETHAFGRD P09920 CSF3_MOUSE Granulocyte colony-stimulating factor G-CSF Csf3 Csfg Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] PARTIAL PROTEIN SEQUENCE Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes. Monomer. Secreted O-glycosylated. Belongs to the IL-6 superfamily. Complete proteome Cytokine Direct protein sequencing Disulfide bond Glycoprotein Growth factor Reference proteome Secreted Signal MAQLSAQRRMKLMALQLLLWQSALWSGREAVPLVTVSALPPSLPLPRSFLLKSLEQVRKI QASGSVLLEQLCATYKLCHPEELVLLGHSLGIPKASLSGCSSQALQQTQCLSQLHSGLCL YQGLLQALSGISPALAPTLDLLQLDVANFATTIWQQMENLGVAPTVQPTQSAMPAFTSAF QRRAGGVLAISYLQGFLETARLALHHLA Q6PE87 A2AT45 A2AT46 A2AT47 Q9DAP6 CF206_MOUSE Cilia- and flagella-associated protein 206 Cfap206 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Olfactory epithelium NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 351-622 (ISOFORM 1) C57BL/6J Testis May regulate cilium motility through its role in the assembly of the axonemal radial spokes. Cytoplasm Cytoskeleton Cilium axoneme Q6PE87-1 1 Q6PE87-2 2 Belongs to the CFAP206 family. Alternative splicing Cell projection Cilium Cilium biogenesis/degradation Complete proteome Cytoplasm Cytoskeleton Reference proteome MRDVDK VNMAFS MPPTQAESVIKNIIREIGQECAAHGEIASETVVAFMVKAVVLDPSNGFNMDRTLIKTDVQ KLVKLCVARLLDNKNPSLDTIKMQVYFDMNYTSREDFLEEHHRVLESRLGIVSREITDNR ASAREELENLYRKIVSYVLLRSGLGSPTDIKIVREATAALQSVFPQAELATFLTLSKKDK ERQLKELTMIVTGIRLFNRDCGKGGEGIDDLPAILHEAIPTTTQHIDSQLQIAQDQAFRY TAILEKVTNNPLMAKELQPYMLKEALYNVRQYEIFLQTVLSDIITCAEEVEMMIKQLAAQ LEQLKMAVKSKTAVPTSQVFPIFVALASLWMSFQDETVLISVLSNLTTNLELFLGTHELL FPEKVMLGLLDGVVVKSDLTRIEEHMEERVELADFRTQEWLFPETTANFNKLLIQYRGFC GYTFAVTDGLLLPGNPAIGILKYKEKYYTFSTRDAAYTFAENPDHYIHLIKEKAKKNAEL IQLLELHQQFETLIPYSQMRDVDKHYIKPITKCDNGTQTDTHILPPTTMRTYEWNEWELR RKAIKLANLRQKITHSVQTDLSHMRRDNTSQVYPLKEASTQSKREGSSRVPRPQIFIAGL RGGQSKTTYGVKVNLTRAVDET O08585 CLCA_MOUSE Clathrin light chain A Lca Clta Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] MDF1 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-223 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (By similarity). Clathrin coats are formed from molecules containing 3 heavy chains and 3 light chains. Interacts with CALY; the interaction stimulates clathrin self-assembly and clathrin-mediated endocytosis (By similarity). Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; the complex implicates clathrin triskelions (By similarity). Cytoplasmic vesicle membrane Peripheral membrane protein Cytoplasmic side Membrane Coated pit Peripheral membrane protein Cytoplasmic side Cytoplasm Cytoskeleton Spindle Cytoplasmic face of coated pits and vesicles.In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles. Belongs to the clathrin light chain family. Acetylation Calcium Cell cycle Cell division Coated pit Complete proteome Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane Mitosis Phosphoprotein Reference proteome A D QQ HE A G VAD AAE L V R P MAELDPFGAPAGAPGGPALGNGVAGAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAP GRATRRAAGGPDAVDGVMNGEYYQESNGPTDSYAAISEVDRLQSEPESIRKWREEQTERL EALDANSRKQEAEWKEKAIKELEEWYARQDEQLQKTKANNRVADEAFYKQPFADLIGYVA AEEAFVNDIDESSPGTEWERVARLCDFNPKSSKQAKDVSRMRSVLISLKQAPLVH Q99K67 Q9Z1I9 AASS_MOUSE Alpha-aminoadipic semialdehyde synthase, mitochondrial LKR/SDH Lysine ketoglutarate reductase LKR LOR 1.5.1.8 Saccharopine dehydrogenase SDH 1.5.1.9 Aass Lorsdh Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C57BL/6J X CBA/J Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Liver Pancreas Testis SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-93; LYS-138; LYS-274; LYS-286; LYS-333; LYS-458; LYS-523; LYS-535; LYS-584; LYS-732 AND LYS-761 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48; LYS-52; LYS-56; LYS-93; LYS-128; LYS-138; LYS-286; LYS-458; LYS-523; LYS-535; LYS-584; LYS-707; LYS-739; LYS-761; LYS-778 AND LYS-780 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-oxoglutarate reductase and saccharopine dehydrogenase activity, respectively. H2O + L-saccharopine + NADP(+) = 2-oxoglutarate + H(+) + L-lysine + NADPH H2O + L-saccharopine + NAD(+) = (S)-2-amino-6-oxohexanoate + H(+) + L-glutamate + NADH Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 1/6. Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 2/6. Homodimer. Mitochondrion Both enzymes are highly expressed in kidney and liver, very low expression is seen in heart, brain, spleen, lung, skeletal muscle and testis. SDH was detected only in cortical regions of the kidney. Induced by starvation. In the N-terminal section; belongs to the AlaDH/PNT family. In the C-terminal section; belongs to the saccharopine dehydrogenase family. Acetylation Complete proteome Mitochondrion Multifunctional enzyme NAD NADP Oxidoreductase Reference proteome Transit peptide V I L A MLRAQRPRLARLRACLSRGLHHKPVMALRREDVNAWERRAPLAPKHIKGITKLGYKVLIQ PSNRRAIHDKEYVRAGGILQEDITEACLILGVKRPPEEKLMSKKTYAFFSHTIKAQEANM NLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVAGMINILHGMGLRLLALGHHTPFM HLGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEVFNELPC EYVEPHELREVSKTGDLRKVYGTVLSRHHHLVRKTDGVYDPVEYEKYPERYTSRFNTDIA PYTTCLINGIYWEQNTPRLLTRQDAQSLLVPVKSSVVPVEGCPELPHKLVAICDISADTG GSIDFMTECTTIERPFCMYDADQQIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGDMLY PYVEEMLLSDASQPLESQNFSPVVRDAVITSNGLLTDKYKYIQKLRESRERIQFLSMSTK KKVLVLGSGYVSGPVLEYLSRDNNIEITLGSDMTNQMQQLSKKYNINPVSLTVGKQEAKL QSLVESQDLVISLLPYVLHPVVAKACIESRVNMVTASYITPAMKELEKSVDDAGITVIGE LGLDPGLDHMLAMETIDTAKELGATVESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMN IMQPASYLLNGKVVNVTGGVSFLNSVTPMDYFPGLNLEGYPNRDSIKYAEIYGISSAHTL LRGTLRYKGYSKALNGFVKLGLINREAYPALRPEANPLTWKQLLCDLVGISRSSPCEKLK EVVFTKLGGDNTQLEAAEWLGLLGDEQVPQAESIVDAFSKHLVSKLSYGPEEKDMIVMRD SFGIRHPSGHLENKTIDLVVYGDFNGFSAMAKTVGLPTAMAAKMLLDGEIEAKGLMGPFT KEIYGPILERIKAEGIVFNTQSTIKL Q64436 Q9CV46 ATP4A_MOUSE Potassium-transporting ATPase alpha chain 1 7.2.2.19 Gastric H(+)/K(+) ATPase subunit alpha Proton pump Atp4a Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ Gastric mucosa PROTEIN SEQUENCE OF 222-249; 369-386; 486-496; 622-634; 659-667 AND 776-783 IDENTIFICATION BY MASS SPECTROMETRY C57BL/6J Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 822-1033 C57BL/6J Tongue Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for acid production in the stomach. ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) + K(+)(in) + phosphate Composed of two subunits: alpha (catalytic) and beta. Cell membrane Multi-pass membrane protein Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. ATP-binding Cell membrane Complete proteome Direct protein sequencing Hydrogen ion transport Ion transport Magnesium Membrane Metal-binding Nucleotide-binding Phosphoprotein Potassium Potassium transport Reference proteome Translocase Transmembrane Transmembrane helix Transport S F DF EL MGKEKYELYSVELGSGPGGDMTAKMSKKKAGGGGGKKKEKLENMKKEMEINDHQLSVSEL EQKYQTSATKGLKASLAAELLLRDGPNALRPPRGTPEYVKFARQLAGGLQCLMWVAAAIC LIAFAIQASEGDLTTDDNLYLAVALIAVVVVTGCFGYYQEFKSTNIIASFKNLVPQQATV IRDGDKFQINADQLVVGDLVEMKGGDRVPADIRILSAQGCKVDNSSLTGESEPQTRSPEC THESPLETRNIAFFSTMCLEGTAQGLVVSTGDRTIIGRIASLASGVENEKTPIAIEIEHF VDIIAGLAILFGATFFVVAMCIGYTFLRAMVFFMAIVVAYVPEGLLATVTVCLSLTAKRL ASKNCVVKNLEAVETLGSTSVICSDKTGTLTQNRMTVSHLWFDNHIHTADTTEDQSGQTF DQSSETWRALCRVLTLCNRAAFKSGQDAVPVPKRIVIGDASETALLKFSELTLGNAMGYR DRFPKVCEIPFNSTNKFQLSIHTLEDPRDSRHLLVMKGAPERVLERCSSILIKGQELPLD EQWREAFQTAYLSLGGLGERVLGFCQLYLNEKDYPPGYAFDVEAMNFPSSGLCFAGLVSM IDPPRATVPDAVLKCRTAGIRVIMVTGDHPITAKAIAASVGIISEGSETVEDIAARLRMP VDQVNRKDARACVINGMQLKDMDPSELVEALRTHPEMVFARTSPQQKLVIVESCQRLGAI VAVTGDGVNDSPALKKADIGVAMGIAGSDAAKNAADMILLDDNFASIVTGVEQGRLIFDN LKKSIAYTLTKNIPELTPYLIYITVSVPLPLGCITILFIELCTDIFPSVSLAYEKAESDI MHLRPRNPKRDRLVNEPLAAYSYFQIGAIQSFAGFADYFTAMAQEGWFPLLCVGLRPQWE DHHLQDLQDSYGQEWTFGQRLYQQYTCYTVFFISIEMCQIADVLIRKTRRLSVFQQGFFR NKILVIAIVFQVCIGCFLCYCPGMPNIFNFMPIRFQWWLVPMPFGLLIFVYDEIRKLGVR CCPGSWWDQDFYY P35585 AP1M1_MOUSE AP-1 complex subunit mu-1 AP-mu chain family member mu1A Adaptor protein complex AP-1 subunit mu-1 Adaptor-related protein complex 1 subunit mu-1 Clathrin assembly protein complex 1 mu-1 medium chain 1 Clathrin coat assembly protein AP47 Clathrin coat-associated protein AP47 Golgi adaptor HA1/AP1 adaptin mu-1 subunit Mu-adaptin 1 Mu1A-adaptin Ap1m1 Cltnm Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Mammary gland PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152 AND THR-154 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152 AND THR-154 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. 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). Interacts with MARCH11 (By similarity). Q10567 AP1B1 true 5 P22892 Ap1g1 false 6 Q10589 BST2 true 2 Golgi apparatus Cytoplasmic vesicle Clathrin-coated vesicle membrane Peripheral membrane protein Cytoplasmic side Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. Phosphorylation of membrane-bound AP1M1/AP1M2 increases its affinity for sorting signals. Belongs to the adaptor complexes medium subunit family. 3D-structure Acetylation Complete proteome Cytoplasmic vesicle Golgi apparatus Membrane Phosphoprotein Protein transport Reference proteome Transport MSASAVYVLDLKGKVLICRNYRGDVDMSEVEHFMPILMEKEEEGMLSPILAHGGVRFMWI KHNNLYLVATSKKNACVSLVFSFLYKVVQVFSEYFKELEEESIRDNFVIIYELLDELMDF GYPQTTDSKILQEYITQEGHKLETGAPRPPATVTNAVSWRSEGIKYRKNEVFLDVIEAVN LLVSANGNVLRSEIVGSIKMRVFLSGMPELRLGLNDKVLFDNTGRGKSKSVELEDVKFHQ CVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIEKHSHSRIEYMVKAKSQ FKRRSTANNVEIHIPVPNDADSPKFKTTVGSVKWVPENSEIVWSVKSFPGGKEYLMRAHF GLPSVEAEDKEGKPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQL RTQ O70333 Q99LR6 Q9DBP4 CRIPT_MOUSE Cysteine-rich PDZ-binding protein Cysteine-rich interactor of PDZ three Cysteine-rich interactor of PDZ3 Cript Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] BALB/cJ Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Head Lung Small intestine NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Czech II FVB/N-3 Mammary tumor INTERACTION WITH DLG4 Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses. Interacts with TUBB1. Interacts strongly with the PDZ3 domain of members of the DLG4 family. Associates with microtubules (By similarity). Interacts with DLG4. Cytoplasm Cell junction Synapse Cell projection Dendritic spine Colocalizes with DLG4 in asymmetric synapses. Belongs to the CRIPT family. Cell junction Cell projection Complete proteome Cytoplasm Reference proteome Synapse C Y MVCEKCEKKLGRVITPDTWKDGARNTTESGGRKLNENKALTSKKARFDPYGKNKFSTCRI CKSSVHQPGSHYCQGCAYKKGICAMCGKKVLDTKNYKQTSV Q99LJ0 Q6ZPR0 Q8BSV1 Q922L8 CT2NL_MOUSE CTTNBP2 N-terminal-like protein Cttnbp2nl Kiaa1433 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Embryonic tail NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Pituitary Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Heart Kidney Lung Spleen INTERACTION WITH CTTN SUBCELLULAR LOCATION May form homomers (By similarity). May interact with MOB4, PPP2R1A, PPP2CB, STK24, STK25, STK26, STRN4, STRIP1 and STRIP2 (By similarity). Interacts with CTTN/cortactin; this interaction may redistribute CTTN to stress fibers. Cytoplasm Cytoskeleton Stress fiber Predominantly expressed in skin, also detectable in spleen and lung (at protein level). Very low levels, if any, in brain (at protein level). Coiled coil Complete proteome Cytoplasm Cytoskeleton Phosphoprotein Reference proteome N D MNLEKLSKPELLTLFSILEGELEARDLVIEALKAQHRDTFIEERYGKYNISDPLMALQRD FETLKEKNDSEKQPVCTNPLSVLKAVMKQCKNMQERMLSQLAAAESRHRKVILDLEEERQ RHAQDTAEGDDVTYMLEKERERLTQQLEFEKSQVKKFEKEQKKLSSQLEEERTRHKQLSS MLVLECRKATSKAAEEGQKAGELSLKLDKEKSRASKLEEELAAERKRGLQTEAQVEKQLS EFDIEREQLRAKLNREENRTRALKEEVESLKKLVKDLEAAQQHRSTSEQGREPVTMSRGT ATEPPMRVSAFCQTESVQTERSHGSVITKLTDTGLPGPTTAAYSYAKANGHCDPEIQTTR ELTSDSSTENQGPPREKSAVAAQEKPVENGGCPVGTETPVTMPSHLPSSGSSLSPSSTAS SSLTSSPCSSPVLTKRLLGSAASSPGYQSSYQVGINQRFHAARHKFQSQADQDQQASGLQ SPPSRDLSPTLLDNSAAKQLARNTVTQVLSRFTNQGPIKPVSPNSSPFGTDYRNLASTAS PRGDTSHSPTPGKVSSPLSPLSPGIKSPTIPRAERGNPPPIPPKKPGLTPSQSATTPVTK THSQASSLAATEDLASSCSPSAVVANGKDVEILLPTSS Q812C9 A2A4J0 Q80WP3 AOC2_MOUSE Retina-specific copper amine oxidase RAO 1.4.3.21 Amine oxidase [copper-containing] Aoc2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina (By similarity). an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+) Cu cation Binds 1 copper ion per subunit. Ca(2+) Binds 2 calcium ions per subunit. L-topaquinone Contains 1 topaquinone per subunit. Homodimer; disulfide-linked (By similarity). Forms a heterodimer with AOC3 (By similarity). Significantly much highly expressed in retina. Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. Belongs to the copper/topaquinone oxidase family. Calcium Catecholamine metabolism Complete proteome Copper Disulfide bond Glycoprotein Metal-binding Oxidoreductase Reference proteome Signal TPQ S N V A MNLKVLLLLLGLSFLTVFALVYVLLTRQGSFSQSPRCPSIPPRIHPWTHPSQSQLFADLT PEELTAVMSFLTKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREA LAIIFFGGQPKPNVSELVVGPLPHPSYMRDVTVERHGGPLPYYRRPMQKTEFVQIWRHLK EVELPKAPTFLASVLNYNGSTLAPLHSTASGFHAGDRATWIALYHNISGLGVFLHPVGLE LLLDHGALDPADWVVQQVFYLGHYYADLAQLEWEFKVGRLEVIRVPLPTPGGASSLRPRV TPDPPLPPLQFSLQGPQYNIQGNSVTSPLWTFTFGHGVFSGLRIFDIRFKGERVAYEVSV QECLTVYGADSPKTMTIRYLDSSYGLGLNSRALVRGVDCPYQATMVDIHVLVGTGSVQLL PGAVCVFEEAQGLPLRRHHNGIGGHFYGGLASSSLVVRSVSSVGNYDYIWDFMLHPTGAL EARVHATGYINTAFMSGGAESLLFGNRVGERVLGAVHTHAFHFKLDLDVAGLKNWVIAED AVFKPVAAPWNPELQLQRPQLTRQVLSREDLAAFPWGSPLPRYLYLATNQTNAWGHQRGY RIQIHSPPGVHVPLESSEERALSWGRYQLVVTQRKEAEPHSSSIYYQNDMRSPATVFADF INNETLLGEDLVAWVTASFLHIPHAEDIPNTVTVGNRVGFLLRPYNFFNEDPSIFSPGSV YFERDQDAGLCSINPVACTQQLADCVPNLPSFSYEGL Q8BZI0 Q8BKB8 AF1L1_MOUSE Actin filament-associated protein 1-like 1 AFAP1-like protein 1 Afap1l1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J Urinary bladder PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-329; TYR-557 AND SER-747 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brown adipose tissue Heart Kidney Lung May be involved in podosome and invadosome formation. Interacts with CTTN. Cytoplasm Cell projection Podosome Cell projection Invadopodium Cytoplasm Cytoskeleton Stress fiber Q8BZI0-1 1 Q8BZI0-2 2 No experimental confirmation available. Alternative splicing Cell junction Cell projection Coiled coil Complete proteome Cytoplasm Cytoskeleton Phosphoprotein Reference proteome Repeat KGKKNSLAELKGSMSRAAGRKITRIISFSKKKALSEDLQTFSSEDEVPCCGYLNVLVNQGWKERWCRLRCNTLYFHKDRTDLHTHV RSYHELPLVHAGECQRWEGLCYRSTVTEQITGTRVRPLGLSYLVITGRLQGLLGRPEVGRSGTVASFPIPVSPLLWCQAKGRRTAWLSLRAP MDRSRVLEQLIPELTGLLSLLDHEYLSDSTLEKKMAVASLLQSLQPLPAKEVSFLYVNTA DLHSGPSFVESLFEEFDCDLGDLRDMSDDGEPSKGASPEPTKSPSLRSAAADVPPPLPNK PPPEDYYEEALPLGPGKSPEYISSHNGCSPAQSIVDGYYEDADNSYPTTRMNGELKNSYN DSDAMSSSYESYDEEEEEEKGRQPKHQWPSEEASMHLVRDCRICAFLLRKKRFGQWAKQL TVIKEEQLLCYKSSKDRQPHLRLALDVCTVIYVPKDSRHKRHELRFSQGATEVLVLALQS REQAEEWLKVIREVSRPIVGAEGLEVPRSPVILCKADQDKRLSQEKQNSDSDSLGMNDSG STLGRREACEHGKGKKNSLAELKGSMSRAAGRKITRIISFSKKKALSEDLQTFSSEDEVP CCGYLNVLVNQGWKERWCRLRCNTLYFHKDRTDLHTHVNSIALRGCEVAPGFGPRHPFAF RILRNRQEVAILEASCSEDMGRWLGLLLVEMGSKVTPEALHYDYVDVETLTSIVSAGRNS FLYAQSCQDQWPEPRIYDEVPYEKVQDEEPQRPTGAQVKRHASSCSEKSHRADPQVKVKR HASSANQYKYGKNRAEEDARRYLVEKERLEKEKETIRTELTALRQEKKELKEAIRNNPGA KSKALEEAVATLEAQCRAKEEQRIDLELKLVAVKERLQQSLAGGPALGLSVSNKNKSQDT TNKPQSNAPEQSLPVNCVSELRKRSPSIVTSNQGRVLQKAKEWEMKKT O88552 CLD2_MOUSE Claudin-2 Cldn2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J FVB/N Brain Kidney FUNCTION INTERACTION WITH CLDN1 AND CLDN3 INTERACTION WITH TJP1; TJP2 AND TJP3 SUBCELLULAR LOCATION TISSUE SPECIFICITY INDUCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219 AND SER-223 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Kidney Liver Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Can form homo- and heteropolymers with other CLDN. Homopolymers interact with CLDN3, but not CLDN1, homopolymers. Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. Cell junction Tight junction Cell membrane Multi-pass membrane protein Expressed in the kidney, liver and intestine, with higher levels in the ileum than in the jejunum. Low levels in the brain. By CDX1 and CDX2. Induction by CDX2, but not CDX1, is potentiated by TCF1. The disulfide bond is necessary for pore formation, but is not required for correct protein trafficking. Belongs to the claudin family. 3D-structure Cell junction Cell membrane Complete proteome Disulfide bond Isopeptide bond Membrane Phosphoprotein Reference proteome Tight junction Transmembrane Transmembrane helix Ubl conjugation MASLGVQLVGYILGLLGLLGTSIAMLLPNWRTSSYVGASIVTAVGFSKGLWMECATHSTG ITQCDIYSTLLGLPADIQAAQAMMVTSSAMSSLACIISVVGMRCTVFCQDSRAKDRVAVV GGVFFILGGILGFIPVAWNLHGILRDFYSPLVPDSMKFEIGEALYLGIISALFSLVAGVI LCFSCSPQGNRTNYYDGYQAQPLATRSSPRSAQQPKAKSEFNSYSLTGYV Q8BTC1 CL073_MOUSE Uncharacterized protein C12orf73 homolog Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Secreted Complete proteome Reference proteome Secreted Signal MPGGVPWSAYLKMLSSSLLAMCAGAQVVHWYYRPDLTIPEIPPKPGELKTELLGLKERRH EPHVSQQ Q8BTU1 P70212 Q3T9D6 CFA20_MOUSE Cilia- and flagella-associated protein 20 Gene trap locus 3 protein Cfap20 Gtl3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) TISSUE SPECIFICITY DEVELOPMENTAL STAGE BALB/cJ Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) NOD Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) Brain DEVELOPMENTAL STAGE IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Lung Spleen Testis Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Involved in the regulation of the size and morphology of cilia. Required for axonemal microtubules polyglutamylation (By similarity). Nucleus Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Centriole Cytoplasm Cytoskeleton Cilium basal body Cell projection Cilium Q8BTU1-1 1 Q8BTU1-2 2 Widely expressed, with highest levels in testis and lowest in muscle. Expressed at high levels in germinal vesicle stage oocytes at the mRNA level. Expression progressively decreases until blastocyst stage (PubMed:15803458). Detected in later embryonic stages from 9.5 to 19.5 dpc. At 11.5 dpc, the expression is widespread, with no preference for any particular organ or structure (PubMed:8688464). Belongs to the CFAP20 family. Alternative splicing Cell projection Cilium Complete proteome Cytoplasm Cytoskeleton Microtubule Nucleus Reference proteome IHANCRIRRVYFSDRLYSEDELPAEFKLYLPVQNKAKQ VLHLPHRESHTGGFRTLWLANWLAYGPWSRTM K I MFKNTFQSGFLSILYSIGSKPLQIWDKKVRNGHIKRITDNDIQSLVLEIEGTNVSTTYIT CPADPKKTLGIKLPFLVMIIKNLKKYFTFEVQVLDDKNVRRRFRASNYQSTTRVKPFICT MPMRLDDGWNQIQFNLSDFTRRAYGTNYIETLRVQIHANCRIRRVYFSDRLYSEDELPAE FKLYLPVQNKAKQ Q8CBW7 O08904 Q8K3S5 CHIC1_MOUSE Cysteine-rich hydrophobic domain-containing protein 1 Brain X-linked protein Chic1 Brx Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] TISSUE SPECIFICITY DEVELOPMENTAL STAGE BALB/cJ Brain NUCLEOTIDE SEQUENCE [GENOMIC DNA] 129/Sv NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Diencephalon Cell membrane Cytoplasmic vesicle Also present at a Golgi-like vesicular compartment and at scattered vesicles. Expressed moderately in the brain. Detected in the 7, 11, 15, or 19 dpc. Palmitoylated. Belongs to the CHIC family. It is uncertain whether Met-1 or Met-8 is the initiator. Cell membrane Coiled coil Complete proteome Cytoplasmic vesicle Lipoprotein Membrane Palmitate Reference proteome A V MSILLPNMAEFDTISELEEEEEAATSSSSPSSSPSSSSSSSVSGPDEDEEDEEEEEEEDE EEEDEEEEEEEVPPPPRVVSEEHLRRYAPDPVLVRGAGHITVFGLSNKFDTEFPSVLTGK VAPEEFKTSIGRVNSCLKKALPVNVKWLLCGCLCCCCTLGCSLWPVICLNKRTRRSIQKL LEWENNRLYHKLALHWKLTKRKCETSNMMEYVILIEFLPKYPIFRPD Q99LI7 CSTF3_MOUSE Cleavage stimulation factor subunit 3 CF-1 77 kDa subunit Cleavage stimulation factor 77 kDa subunit CSTF 77 kDa subunit CstF-77 Cstf3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Liver Lung Pancreas Spleen Testis One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. Homodimer. The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF3 directly interacts with CSTF1 and CSTF2. Interacts with FIP1L1 (By similarity). Nucleus 3D-structure Acetylation Complete proteome mRNA processing Nucleus Phosphoprotein Reference proteome Repeat MSGDAAAEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKARKTYERLVAQ FPSSGRFWKLYIEAEIKAKNYDKVEKLFQRCLMKVLHIDLWKCYLSYVRETKGKLPSYKE KMAQAYDFALDKIGMEIMSYQIWVDYINFLKGVEAVGSYAENQRITAVRRVYQRGCVNPM INIEQLWRDYNKYEEGINIHLAKKMIEDRSRDYMNARRVAKEYETVMKGLDRNAPSVPPQ NTPQEAQQVDMWKKYIQWEKSNPLRTEDQTLITKRVMFAYEQCLLVLGHHPDIWYEAAQY LEQSSKLLAEKGDMNNAKLFSDEAANIYERAISTLLKKNMLLYFAYADYEESRMKYEKVH SIYNRLLAIEDIDPTLVYIQYMKFARRAEGIKSGRMIFKKAREDARTRHHVYVTAALMEY YCSKDKSVAFKIFELGLKKYGDIPEYVLAYIDYLSHLNEDNNTRVLFERVLTSGSLPPEK SGEIWARFLAFESNIGDLASILKVEKRRFTAFREEYEGKETALLVDRYKFMDLYPCSASE LKALGYKDVSRAKLAAIIPDPVVAPSIVPVLKDEVDRKPEYPKPDTQQMIPFQPRHLAPP GLHPVPGGVFPVPPAAVVLMKLLPPPICFQGPFVQVDELMEIFRRCKIPNTVEEAVRIIT GGAPELAVEGNGPVESSAVLTKAVKRPNEDSDEDEEKGAVVPPVHDIYRARQQKRIR P0CG09 C2C4D_MOUSE C2 calcium-dependent domain-containing protein 4D C2cd4d Gm659 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J Complete proteome Reference proteome MWLLEKAGYRVRTAEARALQAHPSLVPKRQARGSPSRCNPNVLTPDRIPQFFIPPRLRDP RGAEGRVDRNPGGRNLPVACSLPHLAGREGWAFLPESPHTRRRESLFHGPRGLAAGLAPA QSRLHVSAPDLRLCRAPDSDTASSPDSSPCGSPHTPRPQSLSPDEASSADTSPYAPRRAP PLFHLDFLCCQLRPTKDSVLRLGPRGGQLRLSTEYQAGPGRLRLRLVSAEGLPRPRTRPG SGGGGCCVILRLQPRVRPGAQRSRVVQSSCNPIFNEDFFFEGLRPPDLAVRSLRAKVLDR GAGLRRDVLLGECETPLIALLPPLAGGLGPGSSLAPTHLSL Q921H9 COA7_MOUSE Cytochrome c oxidase assembly factor 7 Beta-lactamase hcp-like protein Respiratory chain assembly factor 1 Sel1 repeat-containing protein 1 Coa7 Selrc1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] BALB/cJ C57BL/6J Embryo Head NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Testis Required for assembly of mitochondrial respiratory chain complex I and complex IV. Mitochondrion intermembrane space Belongs to the hcp beta-lactamase family. Acetylation Complete proteome Mitochondrion Reference proteome Repeat MAGLVDFQDEEQVKSFLENMEVECHYQCYREKDPEGCYRLVDYLEGIQKNFDEAAKVLKF NCEKYGHGDSCYKLGAYYVTGKGGLTQDLKAASSCFLMACEKPGKKSVESCHNVGLLAHD GQVNEDGQPDLGKARDYYSRACDGGYAASCFNLSAMFLQGAPGFPKDMGLACKYSMKACD LGHVWACANASRMYKLGDGVDKDEAKAEVLKNRARQLHKEQQKNVQPLTFG P07361 A1AG2_MOUSE Alpha-1-acid glycoprotein 2 AGP 2 Orosomucoid-2 OMD 2 Orm2 Agp-2 Orm-2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] BALB/cJ NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Liver NUCLEOTIDE SEQUENCE [MRNA] OF 70-207 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-76 C57BL/6J Plasma Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction. Secreted Expressed by the liver and secreted in plasma. Synthesis is controlled by glucocorticoids, interleukin-1 and interleukin-6, It increases 5- to 50-fold upon inflammation. Contains a beta-barrel that binds various ligands in its interior. Belongs to the calycin superfamily. Lipocalin family. Acute phase Complete proteome Disulfide bond Glycoprotein Pyrrolidone carboxylic acid Reference proteome Secreted Signal Transport MALHMILVMVSLLPLLEAQNPEHVNITIGDPITNETLSWLSDKWFFIGAAVLNPDYRQEI QKTQMVFFNLTPNLINDTMELREYHTIDDHCVYNSTHLGIQRENGTLSKYVGGVKIFADL IVLKMHGAFMLAFDLKDEKKRGLSLNAKRPDITPELREVFQKAVTHVGMDESEIIFVDWK KDRCSQQEKQQLELEKETKKDPEEGQA O88962 Q9R217 CP8B1_MOUSE 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase 1.14.18.8 7-alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase CYPVIIIB1 Cytochrome P450 8B1 Sterol 12-alpha-hydroxylase Cyp8b1 Cyp12 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] VARIANT LYS-242 129/SvJ BALB/cJ Liver NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Liver IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver Involved in bile acid synthesis and is responsible for the conversion of 7 alpha-hydroxy-4-cholesten-3-one into 7 alpha, 12 alpha-dihydroxy-4-cholesten-3-one. Responsible for the balance between formation of cholic acid and chenodeoxycholic acid. Has a rather broad substrate specificity including a number of 7-alpha-hydroxylated C27 steroids. 7alpha-hydroxycholest-4-en-3-one + 2 [Fe(II)-cytochrome b5] + 2 H(+) + O2 = 7alpha,12alpha-dihydroxycholest-4-en-3-one + 2 [Fe(III)-cytochrome b5] + H2O heme Endoplasmic reticulum membrane Single-pass membrane protein Microsome membrane Single-pass membrane protein Expressed in liver. Belongs to the cytochrome P450 family. Complete proteome Endoplasmic reticulum Heme Iron Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Phosphoprotein Polymorphism Reference proteome Transmembrane Transmembrane helix E K MTLWCTVLGALLTVVGCLCLSLLLRHRRPWEPPLDKGFVPWLGHSMAFRKNMFEFLKGMR AKHGDVFTVQLGGQYFTFVMDPLSFGPIIKNTEKALDFQSYAKELVLKVFGYQSVDGDHR MIHLASTKHLMGQGLEELNQAMLDSLSLVMLGPKGSSLGASSWCEDGLFHFCYRILFKAG FLSLFGYTKDKQQDLDEADELFRKFRRFDFLFPRFVYSLLGPREWVEVSQLQRLFHQRLS VEQNLEKDGISCWLGYMLQFLREQGIASSMQDKFNFMMLWASQGNTGPTCFWVLLFLLKH QDAMKAVREEATRVMGKARLEAKKSFTFTPSALKHTPVLDSVMEESLRLCATPTLLRVVQ EDYVLKMASGQEYQIRRGDKVALFPYLSVHMDPDIHPEPTAFKYDRFLNPDGTRKVDFYK SGKKIHHYSMPWGSGVSKCPGRFFALSEMKTFVLLMIMYFDFKLVDPDIPVPPIDPRRWG FGTSQPSHEVRFLYRLKPVQ Q922J3 Q571L7 CLIP1_MOUSE CAP-Gly domain-containing linker protein 1 Cytoplasmic linker protein 170 CLIP-170 Restin Clip1 Kiaa4046 Rsn Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Embryonic tail NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) FVB/N Mammary tumor PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic brain SUBCELLULAR LOCATION ASSOCIATION WITH MICROTUBULES PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-203 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic fibroblast PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-199; SER-203; SER-314 AND SER-1317 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis PHOSPHORYLATION STRUCTURE BY NMR OF 58-128 Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking. Interacts with MTOR; phosphorylates and regulates CLIP1. Interacts (via CAP-Gly domains) with tubulin. Interacts with SLAIN2. Interacts with TUBA1B, MAPRE1 and MAPRE3. Interacts (via zinc finger) with DCTN1 (By similarity). Binds preferentially to tyrosinated microtubules, and only marginally to detyrosinated microtubules (PubMed:16954346). Cytoplasm Cytoplasm Cytoskeleton Cytoplasmic vesicle membrane Peripheral membrane protein Cytoplasmic side Cell projection Ruffle Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed:16954346). Accumulates in plasma membrane regions with ruffling and protrusions. Associates with the membranes of intermediate macropinocytic vesicles (By similarity). Q922J3-1 1 Q922J3-2 2 Intramolecular interaction between the zinc finger domain and the CAP-Gly domains may inhibit interaction with tubulin. Phosphorylated (PubMed:26972003). Phosphorylation induces conformational changes by increasing the affinity of the N-terminus for C-terminus, resulting in inhibition of its function thus decreasing its binding to microtubules and DCTN1. Exhibits a folded, autoinhibited conformation when phosphorylated and an open conformation when dephosphorylated with increased binding affinity to microtubules and DCTN1. Phosphorylation regulates its recruitment to tyrosinated microtubules and the recruitment of vesicular cargo to microtubules in neurons. Phosphorylation by MTOR may positively regulate CLIP1 association with microtubules (By similarity). 3D-structure Alternative splicing Cell projection Coiled coil Complete proteome Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane Metal-binding Microtubule Phosphoprotein Reference proteome Repeat Transport Zinc Zinc-finger S F MSMLKPSGLKAPTKILKPGSTALKTPAAAAAPVEKTIPSEKASGPPSSETQEEFVDDFRV GERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTR PSKLTRKVQAEDEANGLQAAPGRTASPLSTAAATMVSSSPATPSNIPHKPSQSTAKEPSA TPQISNLTKTASESISNLSEAGSVKKGERELKVGDRVLVGGTKAGVVRFLGETDFAKGEW CGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAPVHKVTKIGFPSTTPAKAKAAAVRRVMA ATPASLKRSPSASSLSSMSSVASSVSSKPSRTGLLTETSSRYARKISGTTALQEALKEKQ QHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAAD REKVELLNQLEEEKRKVEDLQFRVEEESITKGDLEVATVSEKSRIMELEKDLALRAQEVA ELRRRLESSKPPGDVDMSLSLLQEISALQEKLEAIHTDHQGEMTSLKEHFGAREEAFQKE IKALHTATEKLSKENESLRSKLDHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSK GIGTDSAEFAELKTQIERLRLDYQHEIESLQSKQDSERSAHAKEMETMQAKLMKIIKEKE DSLEAVKARLDSAEDQHLVEMEDTLNKLQEAEIKVKELEVLQAKYTEQSEVIGNFTSQLS AVKEKLLDLDALRKANSEGKLELETLRQQLEGAEKQIKNLETERNAESSKANSITKELQE KELVLTGLQDSLNQVNQVKETLEKELQTLKEKFASTSEEAVSAQTRMQDTVNKLHQKEEQ FNVLSSELEKLRENLTDMEAKFKEKDDREDQLVKAKEKLENDIAEIMKMSGDNSSQLTKM NDELRLKERSVEELQLKLTKANENASFLQKSIGEVTLKAEQSQQQAARKHEEEKKELEEK LLELEKKMETSYNQCQDLKAKYEKASSETKTKHEEILQNLQKMLADTEDKLKAAQEANRD LMQDMEELKTQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNARLQNELDTLK ENNLKTVEELNKSKELLSVENQKMEEFKKEIETLKQAAAQKSQQLSALQEENVKLAEELG RTRDEVTSHQKLEEERSVLNNQLLEMKKRESEFRKDADEEKASLQKSISLTSALLTEKDA ELEKLRNEVTVLRGENATAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGN TDAQAEEDERAQESQIDFLNSVIVDLQRKNQDLKMKVEMMSEAALNGNGEDLNSYDSDDQ EKQSKKKPRLFCDICDCFDLHDTEDCPTQAQMSEDPPHSTHHGSRSEERPYCEICEMFGH WATNCNDDETF O35089 CNIH2_MOUSE Protein cornichon homolog 2 CNIH-2 Cornichon family AMPA receptor auxiliary protein 2 Cornichon-like protein Cnih2 Cnil Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] C57BL/6J Fetal brain PROTEIN SEQUENCE OF 40-49 IDENTIFICATION BY MASS SPECTROMETRY C57BL/6J Brain TISSUE SPECIFICITY DEVELOPMENTAL STAGE FUNCTION SUBUNIT SUBCELLULAR LOCATION TISSUE SPECIFICITY INTERACTION WITH CACGN8 FUNCTION Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. Blocks CACNG8-mediated resensitization of AMPA receptors. Acts as an auxiliary subunit for AMPA-selective glutamate receptors (AMPARs). Found in a complex with GRIA1, GRIA2, GRIA3, GRIA4, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with GRIA1 (By similarity). Interacts with CACGN8. Endoplasmic reticulum membrane Multi-pass membrane protein Cell junction Synapse Postsynaptic cell membrane Postsynaptic density Cell projection Dendrite Cell projection Dendritic spine Cell junction Synapse Postsynaptic cell membrane Multi-pass membrane protein Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells). Brain. Highest levels seen in the hippocampus, intermediate levels in the cerebral cortex, striatum olfactory bulb, and thalamus and lower levels in the cerebellum (at protein level). Also expressed in the lung. First detected at the eight-cell stage. Expressed in eight-cell embryo, blastocyst, 6.5-day whole embryo, 7.5-day primitive streak, 11.5-day limb bud and in 13.5-day whole embryo. Belongs to the cornichon family. Cell junction Cell membrane Cell projection Complete proteome Direct protein sequencing Endoplasmic reticulum Membrane Postsynaptic cell membrane Reference proteome Synapse Transmembrane Transmembrane helix MAFTFAAFCYMLTLVLCASLIFFVIWHIIAFDELRTDFKNPIDQGNPARARERLKNIERI CCLLRKLVVPEYSIHGLFCLMFLCAAEWVTLGLNIPLLFYHLWRYFHRPADGSEVMYDAV SIMNADILNYCQKESWCKLAFYLLSFFYYLYSMVYTLVSF Q9D7X8 Q3URJ2 Q66JQ5 GGCT_MOUSE Gamma-glutamylcyclotransferase 4.3.2.9 Ggct Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Liver Skin Spinal cord Stomach NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Heart Kidney Liver Lung Pancreas Spleen Testis Catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and may play a significant role in glutathione homeostasis. Induces release of cytochrome c from mitochondria with resultant induction of apoptosis. an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline + an L-alpha-amino acid Homodimer. Belongs to the gamma-glutamylcyclotransferase family. Complete proteome Lyase Phosphoprotein Reference proteome R C MASSDCEGHAGQEGETFLYFAYGSNLLTERIHLRNPSAVFCCVARLQDFKLDFGNFQGKM SERWHGGIATIFQSPGDEVWGVVWRMNKSNISSLDEQEGVKSGVYVVIEIKVSTREGKEI TCRSYLMTNYESAPPSPQYKKVICMGAKENGLPQEYQEKLKAIEPNEYKGKISDEMEDII KKGESKLS Q5PR73 DIRA2_MOUSE GTP-binding protein Di-Ras2 Distinct subgroup of the Ras family member 2 Diras2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Brain PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-126 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Displays low GTPase activity and exists predominantly in the GTP-bound form. Cell membrane Lipid-anchor Cytoplasmic side Belongs to the small GTPase superfamily. Di-Ras family. Cell membrane Complete proteome GTP-binding Lipoprotein Membrane Methylation Nucleotide-binding Phosphoprotein Prenylation Reference proteome MPEQSNDYRVAVFGAGGVGKSSLVLRFVKGTFRESYIPTVEDTYRQVISCDKSICTLQIT DTTGSHQFPAMQRLSISKGHAFILVYSITSRQSLEELKPIYEQICEIKGDVESIPIMLVG NKCDESPNREVQSSEAEALARTWKCAFMETSAKLNHNVKELFQELLNLEKRRTVSLQIDG KKSKQQKRKEKLKGKCVVM Q5MPP0 Q2M2M0 Q5RL53 Q8BTH1 Q8R0M0 Q8R0V1 FA2H_MOUSE Fatty acid 2-hydroxylase 1.14.18.- Fatty acid alpha-hydroxylase Fa2h Faah Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) VARIANTS ILE-103; LEU-348 AND PRO-354 FUNCTION SUBCELLULAR LOCATION DEVELOPMENTAL STAGE TISSUE SPECIFICITY PATHWAY FVB/N NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) VARIANTS ILE-103; LEU-348 AND PRO-354 C57BL/6J Diencephalon Testis NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3) FVB/N Colon FUNCTION DEVELOPMENTAL STAGE TISSUE SPECIFICITY DISRUPTION PHENOTYPE FUNCTION TISSUE SPECIFICITY PATHWAY FUNCTION TISSUE SPECIFICITY DISRUPTION PHENOTYPE FUNCTION Catalyzes stereospecific hydroxylation of free fatty acids at the C-2 position to produce (R)-2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neural tissue and epidermis (PubMed:15658937, PubMed:16998236). Plays an essential role in the synthesis of galactosphingolipids of the myelin sheath (PubMed:15658937, PubMed:18815260). Responsible for the synthesis of sphingolipids and glycosphingolipids involved in the formation of epidermal lamellar bodies, critical for skin permeability barrier (By similarity). Participates in the synthesis of glycosphingolipids and a fraction of type II wax diesters in sebaceous gland, specifically regulating hair follicle homeostasis (PubMed:21628453). Involved in the synthesis of sphingolipids of plasma membrane rafts, controlling lipid raft mobility and trafficking of raft-associated proteins (PubMed:22517924). 2 [Fe(II)-cytochrome b5] + a 1,2-saturated fatty acid + 2 H(+) + O2 = 2 [Fe(III)-cytochrome b5] + a (R)-2-hydroxy fatty acid + H2O Zn(2+) Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center. Sphingolipid metabolism; galactosylceramide biosynthesis. Lipid metabolism; fatty acid metabolism. Endoplasmic reticulum membrane Multi-pass membrane protein Microsome membrane Multi-pass membrane protein Q5MPP0-1 1 Q5MPP0-2 2 Q5MPP0-3 3 Expressed in brain (at protein level) (PubMed:16998236). Detected in cerebellum and forebrain (PubMed:18815260, PubMed:15658937). Expression in the white matter is mainly restricted in oligodendrocytes (PubMed:15658937). Expressed in stomach, kidney, skin and testis (PubMed:15658937). Expressed in sebaceous gland (PubMed:21628453). Levels increase rapidly in brains from newborns, in parallel with myelination in the central nervous system. Present at very low levels in newborns. Levels are highest at 2 to 3 weeks, and then decrease slightly to reach an constant, intermediate level after 4 months. Constitutively expressed at an intermediate level throughout adult life. The histidine box domains may contain the active site and/or be involved in metal ion binding. The N-terminal cytochrome b5 heme-binding domain is essential for catalytic activity. Knockout mice have normal oligodentrocyte differentiation and develope structural and functional normal myelin up to early adulthood. However, aged knockout mice show a massive axon and myelin sheath degeneration in the spinal cord (PubMed:18815260). Knockout mice show delayed fur development and a cyclic alopecia (PubMed:21628453). Belongs to the sterol desaturase family. SCS7 subfamily. Alternative splicing Complete proteome Electron transport Endoplasmic reticulum Fatty acid biosynthesis Fatty acid metabolism Heme Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Microsome Oxidoreductase Polymorphism Reference proteome Transmembrane Transmembrane helix Transport Zinc T I F L L P MAPAPPPAASFTPAEVQRRLAAGACWVRRGASLYDLTSFVRHHPGGEQLLLARAGQDISA DLDGPPHRHSDNARRWLEQYYVGELRADPQDPTENGAVASAETQKTDPALEPQFKVVDWD KDLVDWQKPLLWQVGHLGEKYDEWVHQPVARPIRLFHSDLIEAFSKTVWYSVPIIWVPLV LYLSWSYYRTLTQDNIRLFASLTREYSMMMPESVFIGLFVLGMLFWTFVEYVIHRFLFHM KPPSNSHYLIMLHFVMHGQHHKAPFDGSRLVFPPVPASLVIAFFYVFLRLILPETVGGII FAGGLLGYVLYDMTHYYLHFGSPHKGSYLYNMKAHHVKHHFEYQKSGFGISTKLWDYFFH TLIPEEAHPKMQ Q68EF4 Q80UC2 GRM4_MOUSE Metabotropic glutamate receptor 4 mGluR4 Grm4 Gprc1d Mglur4 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-642 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity (By similarity). Interacts with PICK1. Cell membrane Multi-pass membrane protein Q68EF4-1 1 Q68EF4-2 2 Belongs to the G-protein coupled receptor 3 family. Alternative splicing Cell membrane Complete proteome Disulfide bond G-protein coupled receptor Glycoprotein Membrane Receptor Reference proteome Signal Transducer Transmembrane Transmembrane helix LYIQTTTLTVSVSLSASV VTSEALPVEFSPPLLAHN C G MSGKGGWAWWWARLPLCLLLSLYGSWVPSSLGKPKGHPHMNSIRIDGDITLGGLFPVHGR GSEGKACGELKKEKGIHRLEAMLFALDRINNDPDLLPNITLGARILDTCSRDTHALEQSL TFVQALIEKDGTEVRCGSGGPPIITKPERVVGVIGASGSSVSIMVANILRLFKIPQISYA STAPDLSDNSRYDFFSRVVPSDTYQAQAMVDIVRALKWNYVSTLASEGSYGESGVEAFIQ KSRENGGVCIAQSVKIPREPKTGEFDKIIKRLLETSNARAIIIFANEDDIRRVLEAARRA NQTGHFFWMGSDSWGSKSAPVLRLEEVAEGAVTILPKRTSVRGFDRYFSSRTLDNNRRNI WFAEFWEDNFHCKLSRHALKKGSHIKKCTNRERIGQDSAYEQEGKVQFVIDAVYAMGHAL HAMHRDLCPGRVGLCPRMDPVDGTQLLKYIRNVNFSGIAGNPVTFNENGDAPGRYDIYQY QRRNGSAEYKVIGSWTDHLHLRIERMQWPGSGQQLPRSICSLPCQPGERKKTVKGMACCW HCEPCTGYQYQVDRYTCKTCPYDMRPTENRTSCQPIPIVKLEWDSPWAVLPLFLAVVGIA ATLFVVVTFVRYNDTPIVKASGRELSYVLLAGIFLCYATTFLMIAEPDLGTCSLRRIFLG LGMSISYAALLTKTNRIYRIFEQGKRSVSAPRFISPASQLAITFVLISLQLLCICVWFVV DPSHSVVDFQDQRTLDPRFARGVLKCDISDLSLICLLGYSMLLMVTCTVYAIKTRGVPET FNEAKPIGFTMYTTCIVWLAFIPIFFGTSQSADKLYIQTTTLTVSVSLSASVSLGMLYMP KVYIILFHPEQNVPKRKRSLKAVVTAATMSNKFTQKGNFRPNGEAKSELCENLEAPALAT KQTYVTYTNHAI O88958 Q91WJ4 Q9R188 GNPI1_MOUSE Glucosamine-6-phosphate isomerase 1 3.5.99.6 Glucosamine-6-phosphate deaminase 1 GNPDA 1 GlcN6P deaminase 1 Oscillin Gnpda1 Gnpi Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] SUBCELLULAR LOCATION TISSUE SPECIFICITY Testis NUCLEOTIDE SEQUENCE [MRNA] Testis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Kidney PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo (By similarity). alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+) Homohexamer. Cytoplasm Widely expressed. Detected in brain, liver, kidney, muscle, ovary, testis, spermatids and spermatozoa. In spermatids, located close to the developing acrosome vesicle. In spermatozoa, found close to the acrosomal region. Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. Carbohydrate metabolism Complete proteome Cytoplasm Hydrolase Phosphoprotein Reference proteome S F N D A G MKLIILEHYSQASEWAAKYIRNRIIQFNPGPDKYFTLGLPTGSTPLGCYQKLIEYYKNGD LSFQYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAADLQAECDA FEEKIQAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGDLAK VPTMALTVGVGTVMDAKEVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKEIQKSQSAKKPYSD E9Q5L8 GLYL3_MOUSE Glycine-N-acyltransferase-like protein 3 2.3.1.13 Acyl-CoA:glycine-N-acyltransferase-like protein 3 Glyatl3 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J FUNCTION CATALYTIC ACTIVITY Catalyzes the conjugation of long-chain fatty acyl-CoA thioester and glycine to produce long-chain N-(fatty acyl)glycine, an intermediate in the primary fatty acid amide biosynthetic pathway. an acyl-CoA + glycine = an N-acylglycine + CoA + H(+) (9Z)-octadecenoyl-CoA + glycine = CoA + H(+) + N-(9Z-octadecenoyl)glycine glycine + hexadecanoyl-CoA = CoA + H(+) + N-hexadecanoylglycine Lipid metabolism. Acyltransferase Complete proteome Reference proteome Transferase MLVLKCSTKLFILENMLKSHFPESLKVYGAVMNINRGNPFQKEVVLDSWPNFKVIITRRE REAETDNLDHYTNAYAVFYKDIRAYQQLLEEHDVINWDQVFQIQGLQSELYAASKAVAKA RLLDLDINLASFKAVHFSPVSSVPDHSFLTGPTPRLTYLSVSDADLLNRTWSRGGNQQCL RYLANLIACFPSVCVRDEKGNPVSWGITDQFATMCHGYTLPDHRRKGYSRLVALTLARKL QSRGFPSQGNVLDDNLASINLLKSVQAEFLPCRFHRLILTPAAFSRQAHL O35382 EXOC4_MOUSE Exocyst complex component 4 Exocyst complex component Sec8 Exoc4 Sec8 Sec8l1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] 129/Sv NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N INTERACTION WITH MYRIP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts with BIRC6/bruce (By similarity). Interacts with MYRIP. Interacts with SH3BP1; required for the localization of both SH3BP1 and the exocyst to the leading edge of migrating cells (By similarity). O35250 Exoc7 false 2 Midbody Midbody ring Cell projection Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). Localizes at the leading edge of migrating cells (By similarity). Belongs to the SEC8 family. Acetylation Cell projection Coiled coil Complete proteome Exocytosis Phosphoprotein Protein transport Reference proteome Transport G A S R S T RLQRLKEIICEQAAIKQATKDKKITTV SCRDSRRSSVSRLPSSKPPRTRK MAAEAAGGKYRSTVSKSKDPSGLLISVIRTLSTSDDVEDRENEKGRLEEAYEKCDRDLDE LIVQHYTELTTAIRTYQSITERITNSRNKIKQVKENLLSCKMLLHCKRDELRKLWIEGIE HKHVLNLLDEIENIKQVPQKLEQCMASKHYLSATDMLVSAVESLEGPLLQVEGLSDLRLE LHSKKMNLHLVLIEELHRHLYIKSTSRVVQRNKEKGKMSSHGKDPSPGPLIDVSNIPTPR KFLDASQYSAAGGSSVREMNLQDVKEDLECDPEENSTLFMGILIQGLARLKKIPETVKAI KERLEQELKQIVKRSTTQVADSAYQRGESLTVDNQPRLLLELLELLFDKFNAVATAHSVV LGYLQDSVGTQLTQQEEIKLYDMADVWVKIQDVLQMLLTEYLDMKNTRTASEPSAQLSYA STGREFAAFFAKKKPQRPKNSLFKFESSSHAISMSAYLREQRRELYSRSGELQGGPDDNL IEGGGTKFVCKPGARNITVIFHPLLRFIQEIEHALGLGPAKQCPLREFLTVYIKSIFLNQ VLAEINKEIEGVTKTSDPLKILANADTMKVLGVQRPLLQSTIIVEKTVQDLMNLMHDLSA YSDQFLNMVCVKLQEYKDTCSTAYRGIVQSEEKLVISASWAKDDDISRLLKSLPNWTNMA QPKQLRPKREEEEDFIRAAFGKESEVLIGNLGDKLIPPQDILRDVSDLKALANMHESLEW LAGRTKSAFSNLSTSQMLSPAQESHVNMDLPPVSEQIMQTLSELAKTFQDMADRCLLVLH LEVRVHCFHYLIPLAKEGNYAIVANVESMDYDPLVVKLNKDISAMEEAMSASLQQHKFQY IFEGLGHLISCILINGAQYFRRISESGIKKMCRNIFVLQQNLTNITMSREADLDFARQYY EMLYNTADELLNLVVDQGVKYTELEYIHALTLLHRSQTGVGDQTTQNTRLQRLKEIICEQ AAIKQATKDKKITTV Q7TNV0 Q80VC5 Q8BZV6 DEK_MOUSE Protein DEK Dek Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Colon NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] FVB/N Mammary gland Salivary gland FUNCTION SUBCELLULAR LOCATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis Involved in chromatin organization. Found in a mRNA splicing-dependent exon junction complex (EJC) with DEK, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with histones H2A, H2B, H3, H4, acetylated histone H4, non-phosphorylated DAXX and HDAC2. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Binds DNA (By similarity). Nucleus Enriched in regions where chromatin is decondensed or sparse in the interphase nuclei. Phosphorylated by CK2. Phosphorylation fluctuates during the cell cycle with a moderate peak during G(1) phase, and weakens the binding of DEK to DNA (By similarity). ADP-ribosylation Chromatin regulator Complete proteome DNA-binding Nucleus Phosphoprotein Reference proteome R S Y C MSAAAAPAAEGEDAPVPPSSEKEPEMPGPREESEEEEEDDEDDDEEDEEEEKEKSLIVEG KREKKKVERLTMQVSSLQREPFTVTQGKGQKLCEIERIHFFLSKKKPDELRNLHKLLYNR PGTVSSLKKNVGQFSGFPFEKGSTQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELV KRILNFLMHPKPSGKPLPKSKKSSSKGSKKERNSSGTTRKSKQTKCPEILSDESSSDEDE KKNKEESSEDEEKESEEEQPPKKTSKKEKAKQKATAKSKKSVKSANVKKADSSTTKKNQK SSKKESESEDSSDDEPLIKKLKKPPTDEELKETVKKLLADANLEEVTMKQICKEVYENYP AYDLTERKDFIKTTVKELIS Q9ES28 O08757 Q3UTS5 Q6XPA5 Q6ZQI5 Q8C750 Q91ZZ6 Q9ES27 ARHG7_MOUSE Rho guanine nucleotide exchange factor 7 Beta-Pix PAK-interacting exchange factor beta p85SPR Arhgef7 Kiaa0142 Pak3bp Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E) Brain NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS G AND H) ICR Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND F) C57BL/6J Cerebellum Lung NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D) FVB/N Mammary tumor NUCLEOTIDE SEQUENCE [MRNA] OF 59-862 (ISOFORM B) NUCLEOTIDE SEQUENCE [MRNA] OF 150-862 (ISOFORM C) TISSUE SPECIFICITY C57BL/6J Brain NUCLEOTIDE SEQUENCE [MRNA] OF 63-862 (ISOFORM E) TISSUE SPECIFICITY C57BL/6J Brain NUCLEOTIDE SEQUENCE [MRNA] OF 126-862 (ISOFORM A) Thymus INTERACTION WITH GIT1 INTERACTION WITH GIT1 AND TGFB1I1 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Embryonic brain INTERACTION WITH YWHAZ FUNCTION PHOSPHORYLATION SUBCELLULAR LOCATION INTERACTION WITH PTK2/FAK1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain cortex PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-497 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Liver SUBCELLULAR LOCATION INTERACTION WITH PARVB PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497 AND SER-673 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-155; SER-164; SER-497; SER-673 AND SER-776 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 164-220 Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. May function as a positive regulator of apoptosis. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons (By similarity). Interacts with PAK kinases through the SH3 domain. Interacts with unphosphorylated PAK1. Interacts with ITCH. Interacts with SCRIB; interaction is direct and may play a role in regulation of apoptosis (By similarity). Interacts with GIT1 and TGFB1I1. Interacts with FRMPD4 (via N-terminus). Interacts with CaMK1. Interacts with BIN2 (By similarity). Interacts with PTK2/FAK1 and RAC1. Interacts with PARVB. Interacts with YWHAZ (PubMed:16959763). Q68FF6 Git1 false 2 Q9Z272 Git1 true 2 Q14161 GIT2 true 2 Q9JLQ2 Git2 false 6 Q9HBI1 PARVB true 10 Q9ES46 Parvb false 2 Q9WV48 Shank1 true 6 Q9QX74 Shank2 true 4 Q9JLU4 Shank3 true 2 Cell junction Focal adhesion Cell projection Ruffle Cytoplasm Cell cortex Cell projection Lamellipodium Detected at cell adhesions. A small proportion is detected at focal adhesions. Q9ES28-1 B Q9ES28-2 A Q9ES28-3 C Q9ES28-4 D Q9ES28-5 E d Q9ES28-6 F Q9ES28-7 G b(L) Q9ES28-8 H b Produced by alternative initiation at Met-158 of isoform G. Seems to be expressed in the central nervous system. Isoform B, isoform C and isoform E are expressed with highest levels in brain and testis. Phosphorylated on Ser-673 by CaMK1; enhancement of GEF activity and downstream activation of RAC1 (By similarity). Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally shortened. 3D-structure Alternative initiation Alternative splicing Cell junction Cell projection Coiled coil Complete proteome Cytoplasm Guanine-nucleotide releasing factor Neurogenesis Phosphoprotein Reference proteome SH3 domain IEK MLQ TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASRSRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQEL SECRSSPRVGTDYKQLLHGLAALEREVSGA TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASR S SRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQDN KSCCSYISHQN NLLL KPSV A P S R KT PH P A S G C W RP WT MNSAEQTVTWLITLGVLESPKKTISDPEVFLQASLKDGVVLCRLLERLLPGTIEKVYPEP RNESECLSNIREFLRACGASLRLETFDANDLYQGQNFNKVLSSLVTLNKVTADIGLGSDS VCARPSSHRIKSFDSLGSQSSHSRTSKLLQSQYRSLDMTDNTNSQLVVRAKFNFQQTNED ELSFSKGDVIHVTRVEEGGWWEGTHNGRTGWFPSNYVREIKPSEKPVSPKSGTLKSPPKG FDTTAINKSYYNVVLQNILETEHEYSKELQSVLSTYLRPLQTSDKLSSANTSYLMGNLEE ISSFQQVLVQSLEECTKSPEAQQRVGGCFLSLMPQMRTLYLAYCANHPSAVSVLTEHSED LGEFMETKGASSPGILVLTTGLSKPFMRLDKYPTLLKELERHMEDYHPDRQDIQKSMTAF KNLSAQCQEVRKRKELELQILTEPIRSWEGDDIKTLGSVTYMSQVTIQCAGSEEKNERYL LLFPNLLLMLSASPRMSGFIYQGKLPTTGMTITKLEDSENHRNAFEISGSMIERILVSCT SQQDLHEWVEHLQKQTKVTSVSNPTIKPHSVPSHTLPSHPLTPSSKHADSKPVALTPAYH TLPHPSHHGTPHTTISWGPLEPPKTPKPWSLSCLRPAPPLRPSAALCYKEDLSKSPKTMK KLLPKRKPERKPSDEEFAVRKSTAALEEDAQILKVIEAYCTSAKTRQTLNSTWQGTDLMH NHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHSYRMGSASRSRKESAPQV LLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQDNKKMKKSLEEEQRARKD LEKLVRKVLKNMNDPAWDETNL Q9CZX2 Q8C127 CEP89_MOUSE Centrosomal protein of 89 kDa Cep89 Coiled-coil domain-containing protein 123 Cep89 Ccdc123 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Embryo Skin IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Required for ciliogenesis. Also plays a role in mitochondrial metabolism where it may modulate complex IV activity (By similarity). Cytoplasm Cytosol Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Cytoplasm Cytoskeleton Spindle pole Cytoplasm Cytoskeleton Microtubule organizing center Centrosome Centriole Mitochondrion intermembrane space Localizes to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. Cilium biogenesis/degradation Coiled coil Complete proteome Cytoplasm Cytoskeleton Mitochondrion Phosphoprotein Reference proteome MLLSFRRNRRSQFNHIIHGFLPAASIAPKPAVPRTPPPRSPNPSPERPRSALAAAILATT LTGQTVAIPQPRQRSRSESDASDIEKDSFIKPYATTSELRLRQSWQNEPRRTSLPSFEML GYGEDEDAETQVSTSCRESESTWKDVGDGRDATYTVPHRDQVLPSQKLVRKDDAPQPDWL SDSSSSSSSSTPQHTQQKDVKHSVLNLEGEKVRLHEKPPPSPDVAGRIHQRYTEITKEKF AELKEETVHLYSANQALSCELSALRQAMKDLQLKLKLVEKDNRKLKETEKASCQEGVTPE LLCLRKQSQDLVDENEGLKMIVHRLNVELSRYQTKFRPLSEEESSHIQGLPSKGPTPPWL VDIKYLSPLLLAYEDRMKEKDKLSTALEEEMKTFRLRVQEVVKENEALHQELTKRSPVTV EEWRQLQTQAELVLDENKLLIEQLEIQQAKARDTHQAHLQDVSKLTKQLVLLEAKTQGQE KQLVESTEQLESLQAKCTELKAQLDSKIAVDVHTSIVNELKSQLQKEEEKDSAEMEELMA KLTALQVQKKSLLLEKSSWATRNRALEAELERTRKANRRYQKRIDVLRKQVEKAMGKEMS AHQYLANLVGLAETVTKERDSLKYLAQCLESEKHGVLNKILKGNIRLGKLEERVKGYKKQ AALKLGDIHHRLKEQQEDFAGKAAQYQKEVKHLHRMLQEKQEVLDEALQQKRNMEGELEM VLESTAKENRRMRSLLQATLERRSTQHVTAPPDTCLRRSSQGDLLIGHDFSYGDVQLLAT TNRQSLGESMA Q8K4M5 Q3V012 Q80WG2 Q80Z41 Q8BNL9 Q8K2S9 COMD1_MOUSE COMM domain-containing protein 1 Protein Murr1 Commd1 Murr1 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J Ovary Uterus NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59 NUCLEOTIDE SEQUENCE [MRNA] OF 1-23 C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-188 C57BL/6J Mammary gland IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Lung Pancreas Spleen Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2. Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Involved in the regulation of membrane expression and ubiquitination of SLC12A2. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes. Promotes CFTR cell surface expression through regulation of its ubiquitination. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Involved in the regulation of HIF1A-mediated transcription; competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1. Negatively regulates neuroblastoma G1/S phase cell cycle progression and cell proliferation by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a FAM107A- and actin-dependent manner. Monomer, homodimer. Can form heterodimers with other COMM domain-containing proteins but only certain combinations may exist in vivo. Interacts (via COMM domain) with COMMD2, COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8 and COMMD10 (via COMM domain). Identified in a complex with an E3 ubiquitin ligase complex composed of TCEB1/elongin C, CUL2, SOCS1 and RBX1; in the complex interacts directly with SOCS1 and CUL2. Interacts directly with ATP7B (via the N-terminal region). Interacts with CCS, CDKN2A, RELA, REL, RELB, NFKB1/p105, NFKB2/p100, NFKBIB, SCNN1D, SCNN1B, CFTR, CLU, SGK1, AKT1, CUL1, CUL2, CUL3, CUL4A, CUL4B, CUL5, CUL7, HIF1A. Identified in a complex with NF-kappa-B. Interacts directly with SLC12A2. Interacts with CCDC22 and CCDC93; proposed to be a component of the CCC (COMMD/CCDC22/CCDC93) complex which contains at least COMMD1 (and possibly other COMM domain-containing proteins), CCDC22, CCDC93. Interacts with VPS35L; the interaction associates CCC complex with retriever complex. Interacts with ATP7A. Interacts with FAM107A; this interaction stabilizes COMMD1 in the nucleus. Nucleus Cytoplasm Endosome membrane Cytoplasmic vesicle Early endosome Recycling endosome Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (By similarity). Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked polyubiquitination. Ubiquitinated by XIAP, leading to its proteasomal degradation (By similarity). Complete proteome Copper Cytoplasm Cytoplasmic vesicle Endosome Membrane Metal-binding Nucleus Protein transport Reference proteome Transcription Transcription regulation Transport Ubl conjugation Ubl conjugation pathway L H MAGDLEGGKSLSGLLSGLAQNAFHGHSGVTEELLHSQLYPEVPPEEFRPFLAKMRGLLKS IASADMDFNQLEAFLTAQTKKQGGITSEQAAVISKFWKSHKIKIRESLMKQSRWDNGLRG LSWRVDGKSQSRHSTQIHSPVAIIELEFGKNGQESEFLCLEFDEVKVKQILKKLSEVEES INRLMQAA Q9WVG6 Q3TYB9 Q8K1Y5 Q91W24 Q99KX8 CARM1_MOUSE Histone-arginine methyltransferase CARM1 2.1.1.319 Coactivator-associated arginine methyltransferase 1 Protein arginine N-methyltransferase 4 Carm1 Prmt4 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) MUTAGENESIS OF 189-VAL--ASP-191 FUNCTION TISSUE SPECIFICITY METHYLATION OF HISTONE H3 INTERACTION WITH NCOA1; NCOA2 AND NCOA3 Embryo NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-608 (ISOFORM 1) FVB/N Mammary gland Mammary tumor NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-608 (ISOFORM 1) C57BL/6J Visual cortex FUNCTION IN METHYLATION OF HISTONE H3 CATALYTIC ACTIVITY METHYLATION OF HISTONE H3 FUNCTION METHYLATION OF EP300 AND CREBBP MUTAGENESIS OF 189-VAL--ASP-191 INTERACTION WITH EP300 AND CREBBP METHYLATION OF HISTONE H3 METHYLATION OF HISTONE H3 METHYLATION OF PABPC1 FUNCTION SUBCELLULAR LOCATION DEVELOPMENTAL STAGE INTERACTION WITH MEF2C FUNCTION MUTAGENESIS OF GLU-267 INTERACTION WITH CTNNB1 METHYLATION OF ELAVL1 CHARACTERIZATION HOMOOLIGOMERIZATION FUNCTION IDENTIFICATION IN A COMPLEX WITH EP300 AND NCOA2 MUTAGENESIS OF GLU-267 FUNCTION DISRUPTION PHENOTYPE METHYLATION OF PABPC1 FUNCTION INTERACTION WITH TP53 METHYLATION OF HISTONE H3 FUNCTION INTERACTION WITH FLII METHYLATION OF HISTONE H3 FUNCTION INTERACTION WITH RELA TISSUE SPECIFICITY FUNCTION INTERACTION WITH TRIM24 IDENTIFICATION IN A COMPLEX WITH TRIM24 AND NCOA2 FUNCTION DISRUPTION PHENOTYPE FUNCTION FUNCTION CATALYTIC ACTIVITY SUBUNIT INTERACTION WITH EP300 AND NCOA3 SUBCELLULAR LOCATION MUTAGENESIS OF TYR-154; SER-217 AND SER-229 PHOSPHORYLATION AT SER-217 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Heart Spleen Testis FUNCTION CATALYTIC ACTIVITY DISRUPTION PHENOTYPE SUBUNIT MUTAGENESIS OF ARG-169 AND TYR-173 METHYLATION AT ARG-551 FUNCTION CATALYTIC ACTIVITY MUTAGENESIS OF ARG-551 IDENTIFICATION BY MASS SPECTROMETRY X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 147-490 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE CATALYTIC ACTIVITY FUNCTION INTERACTION WITH NCOA2/GRIP1 ACTIVITY REGULATION SUBUNIT Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs. L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine Methylation of H3R17 (H3R17me) by CARM1 is stimulated by preacetylation of H3 'Lys-18' (H3K18ac) H3 'Lys-23' (H3K23ac) by EP300 and blocked by citrullination of H3 'Arg-17' (H3R17ci) by PADI4. Homodimer. Interacts with NR1H4. Interacts with SNRPC (By similarity). Interacts with the C-terminus of NCOA2/GRIP1, NCO3/ACTR and NCOA1/SRC1. Part of a complex consisting of CARM1, EP300/P300 and NCOA2/GRIP1. Interacts with FLII, TP53, myogenic factor MEF2, EP300/P300, TRIM24, CREBBP and CTNNB1. Interacts with RELA. Identified in a complex containing CARM1, TRIM24 and NCOA2/GRIP1. Interacts with NCOA3/SRC3. Nucleus Cytoplasm Mainly nuclear during the G1, S and G2 phases of the cell cycle. Cytoplasmic during mitosis, after breakup of the nuclear membrane (By similarity). Q9WVG6-1 1 Q9WVG6-2 2 No experimental confirmation available. Ubiquitously expressed. Within the brain, present in proliferating cells from lateral ventricular zone and dentate gyrus (at protein level). At 9 dpc, expression is prominent in the neural tube and somites. Phosphorylation at Ser-217 is strongly increased during mitosis, and decreases rapidly to a very low, basal level after entry into the G1 phase of the cell cycle (By similarity). Phosphorylation at Ser-217 interferes with S-adenosyl-L-methionine binding and strongly reduces methyltransferase activity. Phosphorylation at Ser-217 may promote cytosolic location. Auto-methylated on Arg-551. Methylation enhances transcription coactivator activity. Methylation is required for its role in the regulation of pre-mRNA alternative splicing. Neonatal lethality. The lungs of neonates do not inflate and they do not breathe. The same neonate lethality is observed with mutants that produce CARM1 protein without enzyme activity. Embryos are distinctly smaller at 18.5 dpc. They show reduced lipid accumulation in brown adipose tissue and reduced amounts of brown adipose tissue. Thymocyte differentiation is blocked at an early stage. Mutants display complete loss of protein methylation of the CARM1 substrates PABPC1 and EP300/P300. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. 3D-structure Alternative splicing Chromatin regulator Complete proteome Cytoplasm Methylation Methyltransferase Nucleus Phosphoprotein Reference proteome S-adenosyl-L-methionine Transcription Transcription regulation Transferase Y A F R R A Y A VLD AAA S A S C T S E S E E Q R K I L MAAAAATAVGPGAGSAGVAGPGGAGPCATVSVFPGARLLTIGDANGEIQRHAEQQALRLE VRAGPDAAGIALYSHEDVCVFKCSVSRETECSRVGRQSFIITLGCNSVLIQFATPHDFCS FYNILKTCRGHTLERSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQN HTDFKDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIP GKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLAPFTD EQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDIRILMAKSVKYTVNF LEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVR CLFQSPLFAKAGDTLSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYTGT TPSPPPGSHYTSPSENMWNTGSTYNLSSGVAVAGMPTAYDLSSVIAGGSSVGHNNLIPLA NTGIVNHTHSRMGSIMSTGIVQGSSGAQGGGGSSSAHYAVNNQFTMGGPAISMASPMSIP TNTMHYGS Q8C3W1 Q3TCS2 Q3U2K7 Q3U3E1 Q6PDM3 CA198_MOUSE Uncharacterized protein C1orf198 homolog Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J NOD Heart NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] C57BL/6J PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Liver Lung Spleen Testis Cytoplasm Acetylation Complete proteome Cytoplasm Phosphoprotein Reference proteome E D R H D E MASMAAAIAASRSAVMSGNRPLDDRERKRFTYFSSLSPMARKIMQDKEKIREKYGPEWAR LPPAQQDEIIDRCLVGPRAPAAAADAGDVRDPARFPGLRGPTGQKLVRFGDEDITWQDEH SAPFSWETRSQMEFSISSLSIQEPSAATVTSDARSLAKAPQGTQGSKPAQSSRSSSLDAL GPARKEEEAPFWKINAERSREGPEAEFQSLTPSQIKSMEKGEKVLPACYRQEPTTKDREA KPVPQEQQTLPSVSAEQEVPQPVQAPASLLPKATPTESPEKPPPPAVQRDEDDDALFSEP ALAQISSSNVLLKTGFDFLDNW Q8BTZ4 Q3TGA7 Q80UJ6 Q80W43 Q8BWW7 Q8C0F7 Q9CRX0 Q9CSL1 Q9JJB8 APC5_MOUSE Anaphase-promoting complex subunit 5 APC5 Cyclosome subunit 5 Anapc5 MNCb-2778 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Brain NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J NOD Embryo Heart Kidney Spinal cord Testis Thymus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) Czech II Brain Mammary tumor IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Kidney Lung Spleen Testis Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Protein modification; protein ubiquitination. The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5. Q8BTZ4-1 1 Q8BTZ4-2 2 Belongs to the APC5 family. Alternative splicing Cell cycle Cell division Complete proteome Mitosis Phosphoprotein Reference proteome Repeat TPR repeat Ubl conjugation pathway E V A E R H F S H Y I V V I S T I V A T MMTNGVVHANLFGIKDWVTPYKIAVLVLLNEMGRTGEGAVSLVERRKLNQLLLPLLQGPD ITLSKLYKLIEESCPQLANSVQIRIKLMAEGELKDMEQFFDDLSDSFSGTEPEVHKTSVV GLFLRHMILAYSKLSFSQVFKLYTALQQYFQNGEKKTVEDADMDREDGEKQMEKEELDVS VREEEVSCSGPLSQKQAEFFLSQQAALLKNDETKALTPASLQKELNNLLKFNPDFAEAHY LSYLNNLRVQDVFSSTHSLLHYFDRLILTGAEGKSNGEEGYGRSLRYAALNLAALHCRFG HYQQAELALQEAIRIAQESNDHVCLQHCLSWLYVLGQKRADSYVLLEHSVKKAVHFGLPY LASLGIQSLVQQRAFAGKTANKLMDALKDSDLLHWKHSLSELIDISIAQKTAIWRLYGRS TMALQQAQMLLSMNSLESLNAGVQQNNTESFAVALCHLAELHAEQGCFAAAGEVLKHLKD RFPPNSQHAQLWMLCDQKIQFDRAMNDGKFHLADSLVTGITALNGIEGVYRKAVVLQAQN QMTEAHKLLQKLLTYCQKLKNTEMVISVLLSVAELYWRSSSPTIAMPVLLEALALSKEYR LQYLASETVLNLAYAQLILGIPEQALTLLHMAIEPILADGAVLDKGRAMFLVSKCQVASA ASYDPVKKAEALEAAIQNLSEAKNYFAQVDCRERIRDVAYFQARLYHALGKTQERNHCAM IFRQLHQELPAHGVPLINHL P68254 P35216 Q3TW69 Q3UJN5 Q5SP76 Q5U423 Q66JR6 1433T_MOUSE 14-3-3 protein theta 14-3-3 protein tau Ywhaq Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) INTERACTION WITH CDK16 Brain NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1) 129/Sv NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1) C57BL/6J Amnion Blastocyst Bone marrow Egg NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] C57BL/6J NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2) C57BL/6J FVB/N Brain Mammary tumor Olfactory epithelium PROTEIN SEQUENCE OF 12-49; 61-68; 75-80; 84-115; 128-167 AND 194-245 IDENTIFICATION BY MASS SPECTROMETRY C57BL/6J OF1 Brain Hippocampus PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Brain Brown adipose tissue Heart Kidney Liver Lung Pancreas Spleen Testis INTERACTION WITH DAPK2 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. Negatively regulates the kinase activity of PDPK1 (By similarity). Homodimer (By similarity). Interacts with CDKN1B ('Thr-198' phosphorylated form); the interaction translocates CDKN1B to the cytoplasm. Interacts with SSH1 (By similarity). Interacts with GAB2. Interacts with RGS7 (phosphorylated form) (By similarity). Interacts with CDK16 (PubMed:9197417). Interacts with the 'Ser-241' phosphorylated form of PDPK1 (By similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with SLITRK1 (By similarity). Interacts with RIPOR2 (By similarity). Interacts with INAVA; the interaction increases upon PRR (pattern recognition receptor) stimulation and is required for cellular signaling pathway activation and cytokine secretion (By similarity). Interacts with MARK2, MARK3 and MARK4 (By similarity). P23242 Gja1 false 3 P11688 Itga5 false 2 Q5S006 Lrrk2 false 4 Cytoplasm P68254-1 1 P68254-2 2 No experimental confirmation available. Belongs to the 14-3-3 family. Translation N-terminally shortened. Translation N-terminally shortened. Acetylation Alternative splicing Complete proteome Cytoplasm Direct protein sequencing Isopeptide bond Nitration Phosphoprotein Reference proteome Ubl conjugation LWTSDSAGEECDAAEGAEN FTCVELETVSVCFSLLS M I L S MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWR VISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLK MKGDYFRYLAEVACGDDRKQTIENSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYE ILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAA EGAEN Q3URY6 ARMC2_MOUSE Armadillo repeat-containing protein 2 Armc2 Mus musculus Mouse Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Myomorpha Muroidea Muridae Murinae Mus Mus NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2) C57BL/6J Cerebellum