Q07442 D6VRS8 BDF2_YEAST Bromodomain-containing factor 2 BDF2 YDL070W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c DOMAIN BROMODOMAIN INTERACTION WITH TAF7 FUNCTION INTERACTION WITH HISTONE H4 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION BY THE CK2 PROTEIN KINASE COMPLEX PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Transcription factor involved in the expression of a broad class of genes including snRNAs. Required for sporulation and DNA-damage repair. Prevents the spreading of SIR silencing at telomeres and protects histone H4, but not H3, from deacetylation (By similarity). Interacts with the TFIID subunit TAF7 and with histone H4. P35817 BDF1 false 5 Cytoplasm Nucleus Phosphorylated by the casein kinase CK2 complex. Present with 2930 molecules/cell in log phase SD medium. Bromodomain Coiled coil Complete proteome Cytoplasm DNA damage DNA repair Nucleus Phosphoprotein Reference proteome Repeat Sporulation Transcription Transcription regulation MSRTNMDTRHAHSALLAAPQSATANSRSSNSSSESSSNKNNINVGVGDDSGNVSAVSIDD GPHFRDIFHYGHEENYKLASSGITNLNSSSHAHQTLSPISISNASTPESFPEHPLGLERE TEPALEAEMEAEELPPHQSKYLLSSIKATKRLKDARPFLKPVDPIALNIPHYFNYVQTPM DLSLIETKLQGNVYHSVEQVTSDFKTMVDNCLNFNGPESSISSMAKRIQKYFEKKLSAMP PRVLPASALKKTSRNRKKNEDMDSPLVIRRSVSTTNDNIGESGNREGVSGGRPKRTIHPP KSKDLFDIYENSKPKSKTLQKKFRTCLKILKVLMSKKNSDINFPFLQPVDPIALNLPNYF DVVKNPMDLGTISNNLMNWKYKTIDQFVDDLNLVFYNCFQFNPEGNEVHSMGKKLKELFN FHWLENQDILNEIETDSDLEEDNYSSSYSSDDEYDDEDINENDITNPAIQYLEQKLKKME VELQQLKRQELSKLSKERKRKHLGKTLLRRKAMKHSVDDLKKSITDKINELSDLEMNGMI RIIKNSLPADEILTSNEDEIEIDLDILDEATIARIYERYFEKKNNNNSKRKLSGNYSTAP TNKKKKTLKFLEKDEIINNNNYSDSEEDSSDSSDSDSD Q12365 D6W3B6 BBP1_YEAST Spindle pole component BBP1 BFR1-binding protein 1 BBP1 YPL255W P0745 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION INTERACTION WITH KAR1; MPS2 AND SPC29 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] DOMAIN SUBCELLULAR LOCATION SUBUNIT FUNCTION INTERACTION WITH CDC5 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-73 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Component of the spindle pole body (SPB) required for insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. Connects the central plaque of the SPB with the half-bridge. Required for proper localization of CDC5 at the SPB and for proper M-phase progression. Homodimer. Interacts with KAR1, MPS2 and SPC29. P53159 MPS2 false 6 P33419 SPC29 false 3 Cytoplasm Cytoskeleton Microtubule organizing center Spindle pole body Associates with the periphary of the central plaque. The C-ter coiled-coil domain is sufficient for localization and homodimerization. Present with 922 molecules/cell in log phase SD medium. Belongs to the BBP1 family. Coiled coil Complete proteome Cytoplasm Cytoskeleton Phosphoprotein Reference proteome MNQEDNTGGGGIFGLFKWTKDALFGTDISPSMKYKDQEERRDRSRYAQDDTNFSMKFGND SNRRSTNLSRSNSWSGLDSTLHRKYELLPEYNENGFNSIVNGDHHSKERIRSLRSPAPIV PREPLRNEPTDTFGHRLHTKRRTINELSNSQIPFIPPQEDDPLLSKLFNKDGVNEVRRSP YKLSVKDIPGKFPSPLTKRDEIDNYYVRDEDACHKNREYKKAYFDLFAQMDLNSRDLEDL CEDVREQREQFHRNEQTYKQAYEEMRAELVNELKKSKTLFENYYSLGQKYKSLKKVLDQT ISHEAELATSRERLYQEEDLKNFEIQTLKQRLSDLELKYTNLQIEKDMQRDNYESEIHDL LLQLSLRNNERKDTSAGSNIFSTGQ P50277 D6W1N3 E9P967 Q4R1J0 BIOA_YEAST Adenosylmethionine-8-amino-7-oxononanoate aminotransferase 2.6.1.62 7,8-diamino-pelargonic acid aminotransferase DAPA AT DAPA aminotransferase Diaminopelargonic acid synthase BIO3 YNR058W N3510 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION ATCC 28383 / FL100 / VTT C-80102 NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS GLU-229; ARG-295 AND ASP-384 ATCC 204626 / S288c / A364A NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor. 8-amino-7-oxononanoate + S-adenosyl-L-methionine = 7,8-diaminononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate pyridoxal 5'-phosphate Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. Aminotransferase Biotin biosynthesis Complete proteome Pyridoxal phosphate Reference proteome S-adenosyl-L-methionine Transferase K E H R N D S P MSQEISYTPDVAELLDFDKKHIWHPYTSLSSPLNVYPVKSAHGCKLVLDTDSPVDVEVID AMSSWWCVIHGYNNPELNEALTKQMLKFSHVLLGGFTHKGAVNLVQKLLKVIDEPSLQYC FLADSGSVAVEVALKMALQSNMSGEATKNRTKFLTIKNGYHGDTFGAMSVCDPENSMHHI YNDRLSENIFAQAPSIVDGLPTSQNGFEDHWNAEEVTDLKKQFELHSDKICAVILEPILQ GAGGLRPYHPQFLIEVQKLCNQYDVLFIMDEIATGFGRTGEIFAFKHCQKYQDQHGISPS DQIKVVPDILCVGKGLTSGYMTMSAVVVNDKVASRISSPNSPTGGCFMHGPTFMGNALAC SVAEKSMDILLRGEWRKQVSAIENQIYRELYQYIKNPDNGLIGTVVKRVSVIGAVGIVEL YKKTDPEWFQKKFISKGVHIRPFNCLCYIMPPYVITTEELTKVNQVLIEVLHEWKSHINQ P36062 D6VX50 AVT3_YEAST Vacuolar amino acid transporter 3 AVT3 YKL146W YKL600 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-165 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-121 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in amino acid efflux from the vacuole to the cytoplasm. Capable of transporting large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine. P32568 SNQ2 false 2 Vacuole membrane Multi-pass membrane protein Belongs to the amino acid/polyamine transporter 2 family. Amino-acid transport Complete proteome Membrane Phosphoprotein Reference proteome Transmembrane Transmembrane helix Transport Vacuole MNGKEVSSGSGRTQSNNNKKNNNGGSTGISHASGSPLTDGNGGNSNGNSRSRSRSRKSSG TTGGLLKKPPLLVNNEAVHASVPDASHTSCNNGTLEVSINNPEPHVVDAVARHLIRNPSN SLQLQGGDITRDLYKWTNDHPSSPSQYQYPSQPALSTSIPSQAPSFSNRKRSMSFSAASI ASSSHLNNNSEANGNPLAAIGLAPAPMTHEEIRAPGGFRRSFIIQKRRKHNVDAPIPNFF TRNFIEFLTLYGHFAGEDLSEEEEEEEETEEEPEEEALETESTQLVSREHGRHPHKSSTV KAVLLLLKSFVGTGVLFLPKAFHNGGWGFSALCLLSCALISYGCFVSLITTKDKVGVDGY GDMGRILYGPKMKFAILSSIALSQIGFSAAYTVFTATNLQVFSENFFHLKPGSISLATYI FAQVLIFVPLSLTRNIAKLSGTALIADLFILLGLVYVYVYSIYYIAVNGVASDTMLMFNK ADWSLFIGTAIFTFEGIGLLIPIQESMKHPKHFRPSLSAVMCIVAVIFISCGLLCYAAFG SDVKTVVLLNFPQDTSYTLTVQLLYALAILLSTPLQLFPAIRILENWTFPSNASGKYNPK VKWLKNYFRCAIVVLTSILAWVGANDLDKFVSLVGSFACIPLIYIYPPLLHYKASILSGT SRARLLLDLIVIVFGVAVMAYTSWQTIKMWSQ P53841 B2Y304 B2Y305 B2Y306 B2Y308 D6W0S5 BSC4_YEAST Bypass of stop codon protein 4 BSC4 YNL269W N0670 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] VARIANTS VAL-3; GLN-6; THR-9; LEU-16; GLN-19; SER-22; GLY-32; ASN-42 AND HIS-92 AS2.101 AS2.1406 AS2.148 AS2.179 AS2.2 AS2.2079 AS2.2080 AS2.3 AS2.7 AS2.724 AS2.771 AS2.820 AS2.93 XH1549 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c GENE NAME Open reading frame that exhibits genomic organization compatible with a translational readthrough-dependent mode of expression. The sequence can give a readthrough frequency of 9% when cloned in a plasmid with reporter genes. When the initial stop codon is bypassed, translation will go on to the second stop codon 321 bp downstream. This protein has no orthologs in any species other than the S.cerevisiae lineage. It may be the result of de novo origination of a protein-coding gene. Complete proteome Reference proteome I V R Q NK T I L K Q T S V G S N R H MSIVLRKSNKKNKNCITSKFYTIHIIKISTPVFRAPIAIGESPYVEWSCLQVVFRKDMVT KKTTFAQLITRLNHFLCQALKRRDSKTYILCRTAVFGAMTPFSPRKSHINNKLPMQPRKK KIVIIYVVRFH P32562 D6VZH5 CDC5_YEAST Cell cycle serine/threonine-protein kinase CDC5/MSD2 2.7.11.21 CDC5 MSD2 PKX2 YMR001C YM8270.03C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE ATCC 204626 / S288c / A364A NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION IN PHOSPHORYLATION OF SCC1 CATALYTIC ACTIVITY FUNCTION IN PHOSPHORYLATION OF NET1 CATALYTIC ACTIVITY FUNCTION AS A COMPONENT OF THE FEAR NETWORK INTERACTION WITH CDC48 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-23 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Protein kinase required for the cell cycle where it is involved in mitotic exit. A component of the fear (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. Phosphorylates SCC1/MCD1 and NET1. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Interacts with CDC48; the interaction is likely to result in CDC5 degradation. Q00684 CDC14 false 2 P06243 CDC7 false 11 P41813 FKH2 false 2 Q04087 LRS4 false 6 P22216 RAD53 false 3 P14737 RAD9 false 2 P23624 SPO13 false 8 P32944 SWE1 false 4 Present with 1480 molecules/cell in log phase SD medium. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily. ATP-binding Cell cycle Cell division Complete proteome Kinase Mitosis Nucleotide-binding Phosphoprotein Reference proteome Repeat Serine/threonine-protein kinase Transferase MSLGPLKAINDKQLNTRSKLVHTPIKGNTADLVGKENHFKQTKRLDPNNDHHHQPAQKKK REKLSALCKTPPSLIKTRGKDYHRGHFLGEGGFARCFQIKDDSGEIFAAKTVAKASIKSE KTRKKLLSEIQIHKSMSHPNIVQFIDCFEDDSNVYILLEICPNGSLMELLKRRKVLTEPE VRFFTTQICGAIKYMHSRRVIHRDLKLGNIFFDSNYNLKIGDFGLAAVLANESERKYTIC GTPNYIAPEVLMGKHSGHSFEVDIWSLGVMLYALLIGKPPFQARDVNTIYERIKCRDFSF PRDKPISDEGKILIRDILSLDPIERPSLTEIMDYVWFRGTFPPSIPSTVMSEAPNFEDIP EEQSLVNFKDCMEKSLLLESMSSDKIQRQKRDYISSIKSSIDKLEEYHQNRPFLPHSLSP GGTKQKYKEVVDIEAQRRLNDLAREARIRRAQQAVLRKELIATSTNVIKSEISLRILASE CHLTLNGIVEAEAQYKMGGLPKSRLPKIKHPMIVTKWVDYSNKHGFSYQLSTEDIGVLFN NGTTVLRLADAEEFWYISYDDREGWVASHYLLSEKPRELSRHLEVVDFFAKYMKANLSRV STFGREEYHKDDVFLRRYTRYKPFVMFELSDGTFQFNFKDHHKMAISDGGKLVTYISPSH ESTTYPLVEVLKYGEIPGYPESNFREKLTLIKEGLKQKSTIVTVD P09119 D6VVZ7 CDC6_YEAST Cell division control protein 6 CDC6 YJL194W J0347 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-513 INDUCTION FUNCTION SUBCELLULAR LOCATION MUTAGENESIS OF LYS-29 NUCLEAR LOCALIZATION SIGNAL FUNCTION INDUCTION FUNCTION FUNCTION INTERACTION WITH CDC4 FUNCTION INTERACTION WITH ORC1 MUTAGENESIS OF LYS-114 FUNCTION SUBCELLULAR LOCATION INTERACTION WITH CDC28 PHOSPHORYLATION BY CDC28 UBIQUITINATION MUTAGENESIS OF LYS-114 FUNCTION INTERACTION WITH CDC28 PHOSPHORYLATION BY CDC28 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-368 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] INTERACTION WITH DIA2 AND TOM1 UBIQUITINATION SUBCELLULAR LOCATION INTERACTION WITH THE ORC AND MCM2-7 COMPLEXES FUNCTION Plays a crucial role in forming the pre-replicative complexes. Interacts with the origin recognition complex (ORC) and MCM2-7 helicase complex leading to the linking of those complexes and loading of the replicative helicase MCM2-7 onto the pre-replicative complexes. Required for the initiation of DNA replication and then actively participates in the suppression of nuclear division. Associates with the ORC complex and the MCM2-7 helicase complex. Interacts with CDC4, CDC28, DIA2, ORC1, and TOM1. P00546 CDC28 false 2 P43603 LSB3 false 2 P29469 MCM2 false 4 Nucleus Chromosome Transcribed at the end of mitosis, but in cells with a prolonged G1 phase there is a second burst of transcription in late G1. Ubiquitinated by the E3 ubiquitin ligase complex SCF(CDC4), DIA2, and TOM1; and targeted to the 26S proteasome for degradation. Phosphorylated by CDC28. Phosphorylation is a prerequisite to ubiquitination and degradation. Belongs to the CDC6/cdc18 family. 3D-structure ATP-binding Cell cycle Cell division Chromosome Complete proteome DNA replication Nucleotide-binding Nucleus Phosphoprotein Reference proteome Ubl conjugation K R T K E A G M I M I L P L F R S SK LQN S L L S S L MSAIPITPTKRIRRNLFDDAPATPPRPLKRKKLQFTDVTPESSPEKLQFGSQSIFLRTKA LLQKSSELVNLNSSDGALPARTAEYEQVMNFLAKAISEHRSDSLYITGPPGTGKTAQLDM IIRQKFQSLPLSLSTPRSKDVLRHTNPNLQNLSWFELPDGRLESVAVTSINCISLGEPSS IFQKIFDSFQDLNGPTLQIKNMQHLQKFLEPYHKKTTFVVVLDEMDRLLHANTSETQSVR TILELFLLAKLPTVSFVLIGMANSLDMKDRFLSRLNLDRGLLPQTIVFQPYTAEQMYEIV IQKMSSLPTIIFQPMAIKFAAKKCAGNTGDLRKLFDVLRGSIEIYELEKRFLLSPTRGSL NSAQVPLTPTTSPVKKSYPEPQGKIGLNYIAKVFSKFVNNNSTRTRIAKLNIQQKLILCT IIQSLKLNSDATIDESFDHYIKAITKTDTLAPLQRNEFLEICTILETCGLVSIKKTKCKG KTKRFVDKIDVDLDMREFYDEMTKISILKPFLH P32781 D6VUA6 AGA2_YEAST A-agglutinin-binding subunit AGA2 YGL032C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [MRNA] FUNCTION ATCC 26786 / X2180-1A NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBUNIT MUTAGENESIS OF CYS-25 AND CYS-68 INTERACTION WITH SAG1 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Receptor binding subunit of the a-agglutinin heterodimer. S.cerevisiae a and alpha cells express the complementary cell surface glycoproteins a-agglutinin and alpha-agglutinin, respectively, which interact with one another to promote cellular aggregation during mating. Heterodimer; disulfide-linked (Probable). Interacts with SAG1. Present with 1160 molecules/cell in log phase SD medium. Cell adhesion Complete proteome Disulfide bond Glycoprotein Reference proteome Signal C S C S MQLLRCFSIFSVIASVLAQELTTICEQIPSPTLESTPYSLSTTTILANGKAMQGVFEYYK SVTFVSNCGSHPSTTSKGSPINTQYVF Q08965 D6W3F3 BMS1_YEAST Ribosome biogenesis protein BMS1 BMS1 YPL217C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION INTERACTION WITH RCL1 FUNCTION SUBCELLULAR LOCATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-478; SER-492; THR-504; THR-516; SER-518; SER-523; SER-574 AND SER-578 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. The depletion of BMS1 interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Associates with RCL1. Q08096 RCL1 false 4 Cytoplasm Nucleus Nucleolus Belongs to the TRAFAC class translation factor GTPase superfamily. Bms1-like GTPase family. BMS1 subfamily. 3D-structure ATP-binding Complete proteome Cytoplasm Nucleotide-binding Nucleus Phosphoprotein Reference proteome Ribosome biogenesis MEQSNKQHRKAKEKNTAKKKLHTQGHNAKAFAVAAPGKMARTMQRSSDVNERKLHVPMVD RTPEDDPPPFIVAVVGPPGTGKTTLIRSLVRRMTKSTLNDIQGPITVVSGKHRRLTFLEC PADDLNAMIDIAKIADLVLLLIDGNFGFEMETMEFLNIAQHHGMPRVLGVATHLDLFKSQ STLRASKKRLKHRFWTEVYQGAKLFYLSGVINGRYPDREILNLSRFISVMKFRPLKWRNE HPYMLADRFTDLTHPELIETQGLQIDRKVAIYGYLHGTPLPSAPGTRVHIAGVGDFSVAQ IEKLPDPCPTPFYQQKLDDFEREKMKEEAKANGEITTASTTRRRKRLDDKDKLIYAPMSD VGGVLMDKDAVYIDIGKKNEEPSFVPGQERGEGEKLMTGLQSVEQSIAEKFDGVGLQLFS NGTELHEVADHEGMDVESGEESIEDDEGKSKGRTSLRKPRIYGKPVQEEDADIDNLPSDE EPYTNDDDVQDSEPRMVEIDFNNTGEQGAEKLALETDSEFEESEDEFSWERTAANKLKKT ESKKRTWNIGKLIYMDNISPEECIRRWRGEDDDSKDESDIEEDVDDDFFRKKDGTVTKEG NKDHAVDLEKFVPYFDTFEKLAKKWKSVDAIKERFLGAGILGNDNKTKSDSNEGGEELYG DFEDLEDGNPSEQAEDNSDKESEDEDENEDTNGDDDNSFTNFDAEEKKDLTMEQEREMNA AKKEKLRAQFEIEEGENFKEDDENNEYDTWYELQKAKISKQLEINNIEYQEMTPEQRQRI EGFKAGSYVRIVFEKVPMEFVKNFNPKFPIVMGGLLPTEIKFGIVKARLRRHRWHKKILK TNDPLVLSLGWRRFQTLPIYTTTDSRTRTRMLKYTPEHTYCNAAFYGPLCSPNTPFCGVQ IVANSDTGNGFRIAATGIVEEIDVNIEIVKKLKLVGFPYKIFKNTAFIKDMFSSAMEVAR FEGAQIKTVSGIRGEIKRALSKPEGHYRAAFEDKILMSDIVILRSWYPVRVKKFYNPVTS LLLKEKTEWKGLRLTGQIRAAMNLETPSNPDSAYHKIERVERHFNGLKVPKAVQKELPFK SQIHQMKPQKKKTYMAKRAVVLGGDEKKARSFIQKVLTISKAKDSKRKEQKASQRKERLK KLAKMEEEKSQRDKEKKKEYFAQNGKRTTMGGDDESRPRKMRR Q12048 D6W3C0 ATG41_YEAST Autophagy-related protein 41 Interacting with cytoskeleton protein 2 ATG41 ICY2 YPL250C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] DISRUPTION PHENOTYPE FUNCTION INDUCTION SUBCELLULAR LOCATION INTERACTION WITH ATG9 DOMAIN Involved in both selective and non-selective autophagy (PubMed:26565778). Does not appear to play a role in determining the size of autophagosomes, but rather influences their formation rate (PubMed:26565778). With ATG9, plays a role in the delivery of donor membrane to expanding phagophore (PubMed:26565778). Interacts with ATG9 (PubMed:26565778). Preautophagosomal structure membrane Peripheral membrane protein Shows a peri-mitochondrial distribution similar to ATG9 (PubMed:26565778). Expression is dramatically increased under nitrogen starvation conditions and is regulated by the transcription factor GCN4 (PubMed:26565778). The C-terminal 10 residues are required for the association with ATG9 (PubMed:26565778). Reduces the autophagy flux induced by nitrogen starvation as well as the flux of the cytoplasm-to-vacuole targeting (cvt) pathway (PubMed:26565778). Present with 450 molecules/cell in log phase SD medium. Autophagy Complete proteome Membrane Reference proteome MSSVESSPISRYEDEVFPLSFSNVAFEPPMLSHSPDRSTYADDFSQSYQQELLTFPLSYP IVDESECTHTKDKTDSNIITSTEDDCMFDMEFNGNAASAVAAASKESNSASGFAFASNDA FANVAQQNYRLWLSSV P32316 D6VPY5 ACH1_YEAST Acetyl-CoA hydrolase 3.1.2.1 Acetyl-CoA deacylase Acetyl-CoA acylase ACH1 YBL015W YBL03.18 YBL0304 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [MRNA] PARTIAL PROTEIN SEQUENCE ACETYLATION AT THR-2 NUCLEOTIDE SEQUENCE ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 174-181 SUBCELLULAR LOCATION ATCC 201238 / W303-1B LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Presumably involved in regulating the intracellular acetyl-CoA pool for fatty acid and cholesterol synthesis and fatty acid oxidation. It may be involved in overall regulation of acetylation during melatonin synthesis. acetyl-CoA + H2O = acetate + CoA + H(+) Monomer. Cytoplasm Glycosylated; contains mannose. Present with 4890 molecules/cell in log phase SD medium. Belongs to the acetyl-CoA hydrolase/transferase family. Acetylation Complete proteome Cytoplasm Direct protein sequencing Glycoprotein Hydrolase Phosphoprotein Reference proteome F L A S LG FP MTISNLLKQRVRYAPYLKKVKEAHELIPLFKNGQYLGWSGFTGVGTPKAVPEALIDHVEK NNLQGKLRFNLFVGASAGPEENRWAEHDMIIKRAPHQVGKPIAKAINQGRIEFFDKHLSM FPQDLTYGFYTRERKDNKILDYTIIEATAIKEDGSIVPGPSVGGSPEFITVSDKVIIEVN TATPSFEGIHDIDMPVNPPFRKPYPYLKVDDKCGVDSIPVDPEKVVAIVESTMRDQVPPN TPSDDMSRAIAGHLVEFFRNEVKHGRLPENLLPLQSGIGNIANAVIEGLAGAQFKHLTVW TEVLQDSFLDLFENGSLDYATATSVRLTEKGFDRAFANWENFKHRLCLRSQVVSNNPEMI RRLGVIAMNTPVEVDIYAHANSTNVNGSRMLNGLGGSADFLRNAKLSIMHAPSARPTKVD PTGISTIVPMASHVDQTEHDLDILVTDQGLADLRGLSPKERAREIINKCAHPDYQALLTD YLDRAEHYAKKHNCLHEPHMLKNAFKFHTNLAEKGTMKVDSWEPVD P53264 D6VUP3 CLD1_YEAST Cardiolipin-specific deacylase 1, mitochondrial 3.5.1.- CLD1 YGR110W G6140 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c INDUCTION INDUCTION SUBCELLULAR LOCATION FUNCTION DOMAIN Mitochondrial cardiolipin-specific phospholipase which deacylates de novo synthesized cardiolipin. Part of the remodeling process of cardiolipin, which involves deacylation-reacylation of premature cardiolipin. Has a strong substrate preference for palmitic acid residues and generates monolysocardiolipin for TAZ1-dependent reacylation with unsaturated fatty acids. Mitochondrion Expressed in aerobic conditions and under genotoxic stress. The HXXXXD motif is essential for acyltransferase activity. Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily. Complete proteome Hydrolase Mitochondrion Reference proteome Transferase Transit peptide MFKSTLNSIIRRPLKGFQLLRGADSSNTRPQSPRASARDVTEKQILRTPSAPTAIPLREI IYRVPSLFPRPLEDSVKDFRDFIKNEDAFQTELLKTLPFYPTPSESKTARLIRTVVDDEG NYINEFCIRPRKTSVPEADLKHLVFIHGYGAGLGFFIKNFEDIPLLDNEWCIHAIDLPGY GFSSRPKFPFEYPRDNIHSVQDWFHERIHTWFSKRNLLNRPEKNIVMAHSLGSYLMALYL QKYKESPSFKKLILCSPAGVSYRDFNNTASEVEKWKPPPWWYVKLWDRNISPFTLVRNFR QLGSKITSGWSYRRFKHILNGDPEQSKRFEALHRYAYAIFNKRGSGEYLLSFALKCGGEP RLSLEQQLFDGKKSDILKNSNCDWLWLYGDDDWMDVNGGLRVSRFLKEKLKQKSNVIIVP HSGHHLYLDNYKFFNNILTKEMQKI Q03153 D6VZS1 ATP25_YEAST ATPase synthesis protein 25, mitochondrial OLI1 mRNA stabilization factor ATP25 YMR098C YM6543.05C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY FUNCTION SUBCELLULAR LOCATION mRNA stabilization factor specific for the 0.95 kb OLI1 mRNA. Also involved in OLI1 ring formation. Mitochondrion inner membrane Peripheral membrane protein Matrix side Present with 2430 molecules/cell in log phase SD medium. Belongs to the ATP25 family. Complete proteome Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Transit peptide MNKFCLLPFHGKRIGVANIPFTILFKKGPYFLHSHITAVYYSTKGKNDSHEQSRVSKKST FTPLETPWYLRIVDNEKELMEGKKNNHHTMNKELEIPKTSPNSLRKIADLLTGKLGLDDF LVFDLRKKSPNSVSAVNKLGDFMVICTARSTKHCHKSFLELNKFLKHEFCSSAYVEGNFN ERQESRRKRRLARKSNLSKLLGRSSECSAKDLNSEAWYMIDCRVDGIFVNILTQRRRNEL NLEELYAPENEKSKFQNIDSGNVPTISGVNEISSNNNILLGLRRLAQQRRRYSTINPNGL SNLRYFLQKEDFKGANKIIQSSSGTETHNIRTLEHVKNTLKDLVGQERKVDVVQWKSLFD EHSTFLTINQSAAYWPLRLEYAILLNKADPQFYSDRVFLKDYLLLKKSLGQELIREDLIA LLEMVLKTQHSSHSYFNLVKQNRVIIRALNLFKGLQTEDDGSVVYDEVVISLLLNSMVAD ERVKLRSLYETIDHIFQTFGDKLTSGMIVSILQNLAKIKDWNKLLQVWEAITPTEGEGQD KRPWNEFINVINQSGDSHVISKIVNNGHLLWIRRLNVNVTPELCNSIKALLKTAGMENST LEEFLVRGTNNQ P38728 D3DKS7 ECM34_YEAST Protein ECM34 Extracellular mutant protein 34 ECM34 YHL043W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION May be involved in cell wall organization and biogenesis. Membrane Multi-pass membrane protein Belongs to the DUP/COS family. Cell wall biogenesis/degradation Complete proteome Glycoprotein Membrane Reference proteome Transmembrane Transmembrane helix MEGRKSEDEKNEAALACDVFESSNAKLPKNVFRSSFTWYCYEVINRSAFHIWLLLCLTLI VGWKVFSGIGGRRPSDSNMDGPQTKHKRNPGFLRRHSTIVILVISLAVSFSWEAFKMYRE RTFGKQITQFAKEIIKSAPSTDMESWDRVAADFNSYMYENKLWNTEYFFC P16151 D6VT45 ERD1_YEAST Protein ERD1 ERD1 YDR414C D9461.4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION SEQUENCE REVISION TO 168 ATCC 204508 / S288c TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A Required for the retention of luminal endoplasmic reticulum proteins, affects glycoprotein processing in the Golgi apparatus. Endoplasmic reticulum membrane Multi-pass membrane protein Belongs to the ERD1 family. Complete proteome Endoplasmic reticulum Membrane Protein transport Reference proteome Transmembrane Transmembrane helix Transport A G MEKSESNSEGLYLQNILNVPPPQRFIVLIILALWIWTWILKFFLHSNLDVSQVILTRVPH DIRPGYTLQQLHRTARNFALKITRIIIPFHFATVFLFEFMNIIEGPLKNIILIVYFLPLI QCVTIFWFLLKECQIIKYCTRRCLLIESSPRSLRNTYILISDTLTSFAKPLIDFTLFTSL IFREPFTHFDLSVALLPVLVRLLQCLREYRLLHEATLLFNALKYSCNLPILFCTWRSRVY EGSINEERLHHVQRWFMLINSSYTLFWDVRMDWSLDSLTSLRSRSKSAVTLKKKMYHSAI LVDFLLRFWWLWVYLSQNLKLVAADSDYIFFQGEMQYFEVIRRGIWVVFKLDAEYYIKFA SK P00358 D6VWI4 G3P2_YEAST Glyceraldehyde-3-phosphate dehydrogenase 2 GAPDH 2 1.2.1.12 TDH2 GPD2 YJR009C J1433 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 24-37; 72-77; 81-86; 199-213; 226-232 AND 322-331 ATCC 38531 / Y41 PROTEIN SEQUENCE OF 2-13 ATCC 26786 / X2180-1A LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-63 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = 3-phospho-D-glyceroyl phosphate + H(+) + NADH Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. Homotetramer. P0CG63 UBI4 false 2 Cytoplasm There are three genes for G3PDH in yeast. Present with 121000 molecules/cell in log phase SD medium. Belongs to the glyceraldehyde-3-phosphate dehydrogenase family. Complete proteome Cytoplasm Direct protein sequencing Glycolysis Isopeptide bond NAD Oxidoreductase Phosphoprotein Reference proteome Ubl conjugation E A MVRVAINGFGRIGRLVMRIALQRKNVEVVALNDPFISNDYSAYMFKYDSTHGRYAGEVSH DDKHIIVDGHKIATFQERDPANLPWASLNIDIAIDSTGVFKELDTAQKHIDAGAKKVVIT APSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSMT ATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSV VDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSNSSIFDAAAGIQ LSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA Q08387 D6W271 Q02913 Q02914 DNLI4_YEAST DNA ligase 4 6.5.1.1 DNA ligase II DNA ligase IV Polydeoxyribonucleotide synthase [ATP] 4 DNL4 LIG4 YOR005C UND407 UNE452 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CHARACTERIZATION INTERACTION WITH LIF1 INTERACTION WITH POL4 X-RAY CRYSTALLOGRAPHY (3.92 ANGSTROMS) OF 681-944 IN COMPLEX WITH LIF1 Has minor DNA joining activity. Can act on oligo(PDT)/poly(rA) substrate. ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate. Mg(2+) Interacts with LIF1 via its BRCT domain. Interacts with POL4 in the DNL4-LIF1 complex. P53150 LIF1 false 3 Nucleus Belongs to the ATP-dependent DNA ligase family. Produces 2 separate ORFs. Produces 2 separate ORFs. 3D-structure ATP-binding Cell cycle Cell division Complete proteome DNA damage DNA recombination DNA repair DNA replication Ligase Magnesium Metal-binding Nucleotide-binding Nucleus Reference proteome Repeat MISALDSIPEPQNFAPSPDFKWLCEELFVKIHEVQINGTAGTGKSRSFKYYEIISNFVEM WRKTVGNNIYPALVLALPYRDRRIYNIKDYVLIRTICSYLKLPKNSATEQRLKDWKQRVG KGGNLSSLLVEEIAKRRAEPSSKAITIDNVNHYLDSLSGDRFASGRGFKSLVKSKPFLHC VENMSFVELKYFFDIVLKNRVIGGQEHKLLNCWHPDAQDYLSVISDLKVVTSKLYDPKVR LKDDDLSIKVGFAFAPQLAKKVNLSYEKICRTLHDDFLVEEKMDGERIQVHYMNYGESIK FFSRRGIDYTYLYGASLSSGTISQHLRFTDSVKECVLDGEMVTFDAKRRVILPFGLVKGS AKEALSFNSINNVDFHPLYMVFDLLYLNGTSLTPLPLHQRKQYLNSILSPLKNIVEIVRS SRCYGVESIKKSLEVAISLGSEGVVLKYYNSSYNVASRNNNWIKVKPEYLEEFGENLDLI VIGRDSGKKDSFMLGLLVLDEEEYKKHQGDSSEIVDHSSQEKHIQNSRRRVKKILSFCSI ANGISQEEFKEIDRKTRGHWKRTSEVAPPASILEFGSKIPAEWIDPSESIVLEIKSRSLD NTETNMQKYATNCTLYGGYCKRIRYDKEWTDCYTLNDLYESRTVKSNPSYQAERSQLGLI RKKRKRVLISDSFHQNRKQLPISNIFAGLLFYVLSDYVTEDTGIRITRAELEKTIVEHGG KLIYNVILKRHSIGDVRLISCKTTTECKALIDRGYDILHPNWVLDCIAYKRLILIEPNYC FNVSQKMRAVAEKRVDCLGDSFENDISETKLSSLYKSQLSLPPMGELEIDSEVRRFPLFL FSNRIAYVPRRKISTEDDIIEMKIKLFGGKITDQQSLCNLIIIPYTDPILRKDCMNEVHE KIKEQIKASDTIPKIARVVAPEWVDHSINENCQVPEEDFPVVNY P32768 A7U4Y7 D6VPN7 Q58HH7 Q58HH8 Q58HH9 Q58HI0 FLO1_YEAST Flocculation protein FLO1 Flocculin-1 FLO1 FLO2 FLO4 FLO8 YAR050W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] SUBCELLULAR LOCATION REPEATS STX347-1D NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] REPEATS S288c / KV1 S288c / KV291 S288c / KV295 S288c / KV333 NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION Sigma 1278B NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c GENE MAPPING REVIEW SUBCELLULAR LOCATION SUBCELLULAR LOCATION FUNCTION FUNCTION SUBCELLULAR LOCATION FUNCTION BIOTECHNOLOGY BIOTECHNOLOGY SUBCELLULAR LOCATION REPEATS Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose. Also involved in cell-substrate adhesion. Cell membrane Lipid-anchor GPI-anchor Secreted Cell wall Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. The number of the intragenic tandem repeats varies between different S.cerevisiae strains. There is a linear correlation between protein size and the extend of adhesion: the more repeats, the stronger the adhesion properties and the greater the fraction of flocculating cells. The Ser/Thr-rich repeats are also important for proper cell wall targeting of the protein. Extensively N- and O-glycosylated. The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. For many industrial applications in which the yeast S.cerevisiae is used, e.g. beer, wine and alcohol production, appropriate flocculation behavior is one of the most important characteristics of a good production strain. The ability of yeast cells to flocculate is of considerable importance, as it provides an effective, environment-friendly, simple and cost-free way to separate yeast cells from the fermentation product at the end of fermentation. Belongs to the flocculin family. 3D-structure Cell membrane Cell wall Complete proteome Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Repeat Secreted Signal S G R P S G L M QPWNDTF HHGTTLL L M N K N D S P L M I M P T M L I M I M T N H T MTMPHRYMFLAVFTLLALTSVASGATEACLPAGQRKSGMNINFYQYSLKDSSTYSNAAYM AYGYASKTKLGSVGGQTDISIDYNIPCVSSSGTFPCPQEDSYGNWGCKGMGACSNSQGIA YWSTDLFGFYTTPTNVTLEMTGYFLPPQTGSYTFKFATVDDSAILSVGGATAFNCCAQQQ PPITSTNFTIDGIKPWGGSLPPNIEGTVYMYAGYYYPMKVVYSNAVSWGTLPISVTLPDG TTVSDDFEGYVYSFDDDLSQSNCTVPDPSNYAVSTTTTTTEPWTGTFTSTSTEMTTVTGT NGVPTDETVIVIRTPTTASTIITTTEPWNSTFTSTSTELTTVTGTNGVRTDETIIVIRTP TTATTAITTTEPWNSTFTSTSTELTTVTGTNGLPTDETIIVIRTPTTATTAMTTTQPWND TFTSTSTELTTVTGTNGLPTDETIIVIRTPTTATTAMTTTQPWNDTFTSTSTELTTVTGT NGLPTDETIIVIRTPTTATTAMTTTQPWNDTFTSTSTEITTVTGTNGLPTDETIIVIRTP TTATTAMTTPQPWNDTFTSTSTEMTTVTGTNGLPTDETIIVIRTPTTATTAITTTEPWNS TFTSTSTEMTTVTGTNGLPTDETIIVIRTPTTATTAITTTQPWNDTFTSTSTEMTTVTGT NGLPTDETIIVIRTPTTATTAMTTTQPWNDTFTSTSTEITTVTGTTGLPTDETIIVIRTP TTATTAMTTTQPWNDTFTSTSTEMTTVTGTNGVPTDETVIVIRTPTSEGLISTTTEPWTG TFTSTSTEMTTVTGTNGQPTDETVIVIRTPTSEGLVTTTTEPWTGTFTSTSTEMTTITGT NGVPTDETVIVIRTPTSEGLISTTTEPWTGTFTSTSTEMTTITGTNGQPTDETVIVIRTP TSEGLISTTTEPWTGTFTSTSTEMTHVTGTNGVPTDETVIVIRTPTSEGLISTTTEPWTG TFTSTSTEVTTITGTNGQPTDETVIVIRTPTSEGLISTTTEPWTGTFTSTSTEMTTVTGT NGQPTDETVIVIRTPTSEGLVTTTTEPWTGTFTSTSTEMSTVTGTNGLPTDETVIVVKTP TTAISSSLSSSSSGQITSSITSSRPIITPFYPSNGTSVISSSVISSSVTSSLFTSSPVIS SSVISSSTTTSTSIFSESSKSSVIPTSSSTSGSSESETSSAGSVSSSSFISSESSKSPTY SSSSLPLVTSATTSQETASSLPPATTTKTSEQTTLVTVTSCESHVCTESISPAIVSTATV TVSGVTTEYTTWCPISTTETTKQTKGTTEQTTETTKQTTVVTISSCESDVCSKTASPAIV STSTATINGVTTEYTTWCPISTTESRQQTTLVTVTSCESGVCSETASPAIVSTATATVND VVTVYPTWRPQTANEESVSSKMNSATGETTTNTLAAETTTNTVAAETITNTGAAETKTVV TSSLSRSNHAETQTASATDVIGHSSSVVSVSETGNTKSLTSSGLSTMSQQPRSTPASSMV GYSTASLEISTYAGSANSLLAGSGLSVFIASLLLAII Q07716 D6VRB9 Q6B312 AIM6_YEAST Altered inheritance of mitochondria protein 6 AIM6 YDL237W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION SEQUENCE REVISION TO 44 ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c DISRUPTION PHENOTYPE Impairs respiratory growth. Belongs to the AIM6 family. Complete proteome Reference proteome Signal N D MLGLKGCLTILIGYVIAVCALFSSRGRNPSLTDWEKLKDQKISNIDNFGLTGQHLLEFFQ ENLPFLSFSEEKYRHKHVSLYYDVFKEYILRRASSKKCLPVDSAIAKLNKDVNPMPVHSH NDYWRKLPLFEGLAYGASSTEADVWNIDEKILAVGHNEAYLDPVELTLDKLYTGPLLEIL DEVNCQDSDADRKNGVFFNSPETSLFFYIDFKSDDNELTYKLLMEQYFKSLIDSGYLTYY DMKKDEIIWRPVTVILTGNYPTSLDILDNGNDNGYFESSQRFAFLDAPLLSLEPKYSKLS VAATVSFSQLMKHCGSDHWKVSLRGRMDSNEISCAKSIIDGAHALKLKTRIWGAPTWPAN LVETISRQIIHDLGSDLLNLDNLFMASSLI Q03233 D6W008 ADD37_YEAST Alpha1-proteinase inhibitor-degradation deficient protein 37 ADD37 YMR184W YM8010.14 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 INDUCTION IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in ER-associated protein degradation (ERAD). Cytoplasm In response to the DNA-damaging agent MMS. Present with 1270 molecules/cell in log phase SD medium. Complete proteome Cytoplasm Phosphoprotein Reference proteome MAIKPTKSFQNCLEAEVPGYNDCPTVLFSIDPNSGPRSKSKQRTKSKRCVSGRLATEVLD LYGNTKTATTPPPVLRRPSVTAAQQESACEGVLVKDQGDRQLQPILCSKEELVAKINDLC VCGSKLSSKELEFYKKKLDSNITKILQNEHTKTVLSQIFNEKDKNMAVKTIKHWMVTDTT ISNWCPAFLKIFENAMPN P32799 D6VTW3 COX13_YEAST Cytochrome c oxidase subunit 6A, mitochondrial 1.9.3.1 Cytochrome c oxidase polypeptide VIa COX13 YGL191W G1341 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] S288c / GRF88 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c PARTIAL PROTEIN SEQUENCE COMPOSITION OF THE CYTOCHROME C OXIDASE COMPLEX Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Not necessary for assembly of the enzyme complex but interacts with ATP and thereby modulates the enzyme activity. 4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] + 2 H2O Energy metabolism; oxidative phosphorylation. Cytochrome c oxidase is composed of 11 subunits: one copy each of COX1, COX2, COX3, COX4, COX5A or COX5B, COX6, COX7, COX9, COX12, COX13 and two copies of COX8. Mitochondrion inner membrane Belongs to the cytochrome c oxidase subunit 6A family. 3D-structure Complete proteome Direct protein sequencing Membrane Mitochondrion Mitochondrion inner membrane Oxidoreductase Reference proteome Transit peptide MFRQCAKRYASSLPPNALKPAFGPPDKVAAQKFKESLMATEKHAKDTSNMWVKISVWVAL PAIALTAVNTYFVEKEHAEHREHLKHVPDSEWPRDYEFMNIRSKPFFWGDGDKTLFWNPV VNRHIEHDD P32453 D6W0N0 ATP11_YEAST Protein ATP11, mitochondrial ATP11 YNL315C N0357 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] S288c / FY1676 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Essential for the assembly of the mitochondrial F1-F0 complex. May interact with the alpha and/or beta subunits of F1-ATPase. Mitochondrion Present with 2840 molecules/cell in log phase SD medium. Belongs to the ATP11 family. Complete proteome Mitochondrion Phosphoprotein Reference proteome Transit peptide MWRLTRKIGTRIHISNQLSPIFNKAIGTVPVFRFYSSSPEQKYRKKLLEEAQKQGFNSIE ELKNHLKETIESKKREFNKIDPLKELEDYQQKTQMENNNSKHLMTKSRSPLDPSAPKVPF KTLDSFLDVGKLKDLSKQEVEFLWRARWAQKDNTLCAVIPVSVYDKMMANARNNPIFVLP LPRQVQSEDAKPNEEQGMELHYIQWQFVGPQTTHCMMTSLAEYKLHQEFARPHTTLQFHS DLVKDKGIVFMNGHVEPDTNVNVQDAQLLLLNVQRFYGAMGEETPVAKQRVQLLRDFSKA SPGFTVEKLISLSQSMEN P53197 D6VUD5 CDH1_YEAST APC/C activator protein CDH1 CDC20 homolog 1 Homolog of CDC twenty 1 CDH1 HCT1 YGL003C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c ASSOCIATION WITH THE APC/C COMPLEX PHOSPHORYLATION BY CDC28 MUTAGENESIS OF THR-12; SER-16; SER-42; THR-157; SER-169; THR-173; THR-176; SER-227 AND SER-239 DEPHOSPHORYLATION BY CDC14 FUNCTION AS SPINDLE CHECKPOINT TARGET FUNCTION INTERACTION WITH CLB2; CLB3 AND CDC5 DOMAIN C-BOX MOTIF INTERACTION WITH HSL1 FUNCTION IN ASE1 AND CDC20 DEGRADATION SUBCELLULAR LOCATION INTERACTION WITH MSN5 AND PSE1 PHOSPHORYLATION BY CDC28 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). During telophase and in the subsequent G1 phase of the cell cycle, recognizes and binds proteins containing a destruction box (D-box) and an additional degradation signal termed the KEN box including ASE1, CDC20, the B-type cyclins CLB2 and CLB3, the polo-like kinase CDC5 and HSL1, and recruits them in a C-box-dependent manner to the APC/C for ubiquitination and subsequent proteolysis. Required for exit from mitosis, cytokinesis and formation of prereplicative complexes in G1. Probably is the target of a BUB2-dependent spindle checkpoint pathway. Associates with the APC/C complex. Interacts with CLB2, CLB3, CDC5, HSL1, MSN5 and PSE1. Q08981 ACM1 false 8 Cytoplasm Nucleus Nuclear import and export are mediated by the importin PSE1 and the exportin MSN5. The C-box is required for the association with the APC/C complex. Phosphorylated at multiple sites by CDC28, probably in its CLB5 bound form, in S, G2 and M phase of the cell cycle, thereby blocking the association of CDH1 to the APC/C and promoting nuclear export of CDH1 by MSN5. Dephosphorylated and activated by CDC14 in late anaphase, which may be necessary for PSE1-dependent nuclear localization. Belongs to the WD repeat CDC20/Fizzy family. 3D-structure Cell cycle Cell division Complete proteome Cytoplasm Mitosis Nucleus Phosphoprotein Reference proteome Repeat WD repeat T A S A S A T A S A T A T A S A S A MSTNLNPFMNNTPSSSPLKGSESKRVSKRPISSSSSASLLSSPSRRSRPSTVYGDRYIPS RTDIDFNSIVSISSMASVPALNPSSTEDQVEYQKERQAHETYNTLLKNELFGEMLSKDTV GSESSIDRIKNTRPSTRGNVHAENTTRHGYELERVSTPPPEAAGLEEFSPHSTPVTPRRL FTSQQDEITRPSSNSVRGASLLTYQQRKGRRLSAASLLQSQFFDSMSPVRPDSKQLLLSP GKQFRQIAKVPYRVLDAPSLADDFYYSLIDWSSTDVLAVALGKSIFLTDNNTGDVVHLCD TENEYTSLSWIGAGSHLAVGQANGLVEIYDVMKRKCIRTLSGHIDRVACLSWNNHVLTSG SRDHRILHRDVRMPDPFFETIESHTQEVCGLKWNVADNKLASGGNDNVVHVYEGTSKSPI LTFDEHKAAVKAMAWSPHKRGVLATGGGTADRRLKIWNVNTSIKMSDIDSGSQICNMVWS KNTNELVTSHGYSKYNLTLWDCNSMDPIAILKGHSFRVLHLTLSNDGTTVVSGAGDETLR YWKLFDKPKAKVQPNSLIFDAFNQIR P38845 D3DL95 CRP1_YEAST Cruciform DNA-recognizing protein 1 CRP1 short N-terminal subpeptide CRP1 short C-terminal subpeptide CRP1 YHR146W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CRUCIFORM DNA-BINDING FUNCTION DOMAIN PROTEOLYTIC AUTOCLEAVAGE LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-156 AND SER-440 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-295; SER-319; SER-394 AND SER-440 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182; SER-271; THR-295; SER-343; THR-366 AND SER-440 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cruciform DNA-binding protein which exerts an enhancing effect on the cleavage of cruciform DNA (X-DNA) by endonuclease VII from bacteriophage T4. Cleaved in the vicinity of position 160 to give an X-DNA-binding N-terminal subpeptide and a non-DNA-binding C-terminal subpeptide. Present with 2990 molecules/cell in log phase SD medium. Belongs to the CRP1/MDG1 family. Complete proteome DNA-binding Phosphoprotein Reference proteome MSSELMFNYTFSWPAGPKDVILTGTFDDWRGTLPLVKTAKGNFEITMPVKLANKDDTFQF KFIVDGVWCVSDSYKKEHVSEGIENNFLQITDLVETQEVAGASRIPEAGGLLCGKPPRSA GPPSTSNRKKNKRNNKKRRSKLKKKSTKNNKKSNESLDDNEEEDGVTGTTTEDVTGTSRE ETPLAEPTNVSKEAPGNFHILPIDQSADTTQSNGIIGGPGPVLVPNPGEIKEFTEIRDVD ARELNERLNKKEEVPEPVAGPIVESSVTEKSPALPQADDPIVETKEVAHNVQELTPQVEA VTPLINEPEPLPTPEAQISIPESSKVEPVEGSLQSKLVEKRESTEGVLDGSKKVENKAKK DEEVFTLDPIVNKAPKLPLTDEQTAEGRKSPAVSEEKEKKKKQEKGSKEVKRSETSKEKK PSAKEVKKQTVKAPKKQTASPLSSSTEEPKKKKTGFFGKLKKLFK P43636 D6VU76 ALG2_YEAST Alpha-1,3/1,6-mannosyltransferase ALG2 2.4.1.132 2.4.1.257 Asparagine-linked glycosylation protein 2 GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase ALG2 YGL065C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY MUTAGENESIS OF GLU-335 AND GLU-343 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] INTERACTION WITH ALG1 SUBCELLULAR LOCATION CHARACTERIZATION Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+) alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+) Protein modification; protein glycosylation. Interacts with ALG1. P16661 ALG1 false 2 Endoplasmic reticulum membrane Multi-pass membrane protein Present with 1840 molecules/cell in log phase SD medium. Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily. Complete proteome Endoplasmic reticulum Glycoprotein Glycosyltransferase Membrane Reference proteome Transferase Transmembrane Transmembrane helix E A E A T S KA NG T A M I FLFMATFMVLYFKNYLWGIYWAFVFALSYPYEEI SYLWPLLWYYILRTTYGEFTGHLYSLSPTLMKKYNVYLNKQCIPPEEKIIYIGEEISKCK MIEKDKRTIAFIHPDLGIGGAERLVVDAALGLQQQGHSVIIYTSHCDKSHCFEEVKNGQL KVEVYGDFLPTNFLGRFFIVFATIRQLYLVIQLILQKKVNAYQLIIIDQLSTCIPLLHIF SSATLMFYCHFPDQLLAQRAGLLKKIYRLPFDLIEQFSVSAADTVVVNSNFTKNTFHQTF KYLSNDPDVIYPCVDLSTIEIEDIDKKFFKTVFNEGDRFYLSINRFEKKKDVALAIKAFA LSEDQINDNVKLVICGGYDERVAENVEYLKELQSLADEYELSHTTIYYQEIKRVSDLESF KTNNSKIIFLTSISSSLKELLLERTEMLLYTPAYEHFGIVPLEAMKLGKPVLAVNNGGPL ETIKSYVAGENESSATGWLKPAVPIQWATAIDESRKILQNGSVNFERNGPLRVKKYFSRE AMTQSFEENVEKVIWKEKKYYPWEIFGISFSNFILHMAFIKILPNNPWPFLFMATFMVLY FKNYLWGIYWAFVFALSYPYEEI P27351 D6VWH9 AP2B_YEAST AP-2 complex subunit beta Beta-2-adaptin Beta-adaptin Clathrin assembly protein complex 2 beta large chain Clathrin assembly protein large beta chain APL1 YAP80 YJR005W J1422 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBUNIT INTERACTION WITH APS2 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; THR-652 AND SER-683 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Beta adaptin is a subunit of the plasma membrane adaptor. Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit APL3 and beta-type subunit APL1), a medium chain (mu-type subunit APM4) and a small adaptin (sigma-type subunit APS2). Interacts with APS2. Cell membrane Membrane Coated pit Peripheral membrane protein Cytoplasmic side Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. Present with 1670 molecules/cell in log phase SD medium. Belongs to the adaptor complexes large subunit family. Cell membrane Coated pit Complete proteome Endocytosis Membrane Phosphoprotein Protein transport Reference proteome Transport V L S N S N I T F I MSDQKVFARYKANEIVTDLQHFGVKKFKSNITRRKNALRKIIANLVLGNYGEMSVLFSEL LKFWQIEDDLEVKRICHEYIRVIGALKPQQAREALPFIMDDFKSRDEKLQIMALRTLVLV PVKELSDQAFDCIISLVNHKSPPEQVTRTAIYALLDLDEIDHERVLGLSSILHDIVKAQS SSPEVIVAALHTLYSIHEKNANMEPFRIPLELAFDMLELLPELNEWNKATVLEVLTTSVV PQHYLDTHEMIELALPYLQQVNTYVVLNSLKFIMYLLNYVDVIKETLAEKLSNSVIALLD KPPELQFLVLRNVILLLLSRESSLLRLDISYFFIEYNDPIYIKDTKLECLYLLANKETLP RILEELEQYATDIDIQMSRKSVRAIGNLAVKLDEDSVHDCVAVLLDLLEFGVDYVVQEII SVFRNILRKYPNNFKANVTELVKHTEVVQEPESKNAMIWIITQYSDVIPNYLELFRVFSS NMFSETLEVQFSILNSAIKFFIRSPTKETEELCMDLLKGCIDHENNPDLRDKTLMYWRLL SLTKTSRISNAITFESLKSVLDGELPLIEMNTKLDPTVLEELELNIGTIVSIYLKPVSHI FRLNKTKLLPQSPILNPNKDLLPVVGNSFPPTGANRDRQNSESQSSTKSRKTAMMDDYDK PAEKINQLKGKRKSSSNNPSKLSRKPSTLLRKLSMKRPFS P46962 D6VWG9 CTK2_YEAST CTD kinase subunit beta CTDK-I subunit beta CTD kinase 38 kDa subunit CTD kinase subunit 2 CTK2 YJL006C J1390 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 217-225 CTD KINASE ACTIVITY SUBUNIT DISRUPTION PHENOTYPE NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION IN RNA POLYMERASE II TRANSCRIPTION PHOSPHORYLATION UBIQUITINATION CTK1 ACTIVATION INTERACTION WITH CTK1 AND CTK3 FUNCTION DISRUPTION PHENOTYPE FUNCTION IN H3 METHYLATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION OF THE CTDK-I COMPLEX SUBCELLULAR LOCATION FUNCTION IN ADAPTATION TO ALTERNATIVE CARBON SOURCES FUNCTION IN THE INTEGRITY OF RDNA Cyclin subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA 3'-end processing and SET2 mediated H3K36 methylation. Together with CTK3, required for CTK1 CTD kinase activation. Required for DNA damage induced transcription. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus. CTDK-I consists of three subunits, CTK1, CTK2 and CTK3 (also called alpha, beta and gamma). Interacts with CTK1. Heterodimerization with CTK3 is required to protect this subunit from degradation. Q03957 CTK1 false 9 P46963 CTK3 false 10 Nucleus Nucleolus Phosphorylated. Ubiquitinated. Phosphorylation and ubiquitination lead to degradation in growth-related way by the ubiquitin-proteasome pathway. Neither phosphorylation nor degradation requires association with CTK1. Null mutants are viable, but grow more slowly than wild-type cells at 30 degrees Celsius. They are cold-sensitive, failing to grow at 12 degrees Celsius. They display flocculent growth in liquid media and they show abnormal cell morphologies, for example, a significant fraction of the cells are greatly enlarged. Deletion mutant is sensitive to the DNA synthesis inhibitor hydroxyurea (HU) and UV irradiation. Present with 1590 molecules/cell in log phase SD medium. Belongs to the cyclin family. Complete proteome Cyclin Direct protein sequencing DNA damage mRNA processing Nucleus Phosphoprotein Reference proteome Transcription Ubl conjugation MPSTFESQLFFSRPFLSKRQIQRAQKNTISDYRNYNQKKLAVFKFLSDLCVQLKFPRKTL ETAVYFYQRYHLFNRFETEVCYTVATSCLTLGCKEVETIKKTNDICTLSLRLRNVVKINT DILENFKKRVFQIELRILESCSFDYRVNNYVHIDEYVIKIGRELSFDYKLCNLAWVIAYD ALKLETILVIPQHSIALAILKIAYELLDNKNWSSKRYSLFETDEKSVNEAYFDIVNFYIN SFDMCDLQRHLPADLLPIGVERFMELKKNAGPESGLPQIPDHLLNADPYITITRDNNVQE RRYVLSLELINGESSINSSTRHA Q03957 D6VX57 CTK1_YEAST CTD kinase subunit alpha CTDK-I subunit alpha 2.7.11.23 CTD kinase 58 kDa subunit CTD kinase subunit 1 CTK1 YKL139W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CTD KINASE ACTIVITY SUBUNIT DISRUPTION PHENOTYPE FUNCTION IN RNA POLYMERASE II TRANSCRIPTION FUNCTION IN PHOSPHORYLATION REGULATION DISRUPTION PHENOTYPE DISRUPTION PHENOTYPE ACTIVATION INTERACTION WITH CTK2 AND CTK3 FUNCTION IN PRE-MRNA END PROCESSING FUNCTION MUTAGENESIS OF ASP-324 DISRUPTION PHENOTYPE FUNCTION IN H3K36 METHYLATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION OF THE CTDK-I COMPLEX IN PHOSPHORYLATION FUNCTION IN RNA POLYMERASE I TRANSCRIPTION INTERACTION WITH RNA POLYMERASE I SUBCELLULAR LOCATION FUNCTION IN TELOMERE MAINTENANCE FUNCTION IN RESPONSE TO GLUCOSE LIMITATION INTERACTION WITH SNF1 PHOSPHORYLATION AT THR-338 BY CAK1 MUTAGENESIS OF ASP-324 AND THR-338 FUNCTION FUNCTION IN TRANSLATION INTERACTION WITH RIBOSOMES FUNCTION IN H3K4 METHYLATION Catalytic subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase II transcriptional elongation, and through PTI1, pre-mRNA 3'-end processing. Participates in both positive and negative regulation of CTD phosphorylation. Required for DNA damage induced transcription, including the expression of the RNR genes, and reprogramming of gene expression upon amino acid starvation. Required for SET2 mediated H3K36 methylation. Also regulates H3K4 methylation. Controls the maintenance of suppressive chromatin in the coding regions of genes by both promoting H3K36 methylation, which leads to histone deacetylation, and catalyzing phosphorylation of the CTD required to localize H3K4 chromatin modification specifically to the 5' ends of genes, thereby creating a boundary for H3K4 methylation that prevents a mark associated with transcriptional initiation from spreading into the bodies of genes. Involved in RNA polymerase I transcription. Involved in telomere maintenance. Acts together with SNF1 to induce GSY2 transcription in response to glucose limitation. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus. Functions in translation elongation by enhancing decoding fidelity. Needed for translational accuracy by phosphorylating RPS2. [DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase] CTDK-I consists of three subunits, CTK1, CTK2 and CTK3 (also called alpha, beta and gamma). Interacts directly with the CTK2 and CTK3 subunits, this interaction is required for kinase activity. Interacts with RNA polymerase I. Interacts with SNF1, but only at low glucose concentrations. Interacts with translating ribosomes. P46962 CTK2 false 9 P46963 CTK3 false 7 Nucleus Nucleolus Cytoplasm Phosphorylated on Thr-338 by CAK1. Phosphorylation is essential for the elevated CTD Ser-2 phosphorylation and required to activate transcription of stationary-phase genes during the diauxic shift. Null mutants are viable, but grow more slowly than wild-type cells at 30 degrees Celsius. They are cold-sensitive, failing to grow at 12 degrees Celsius. They display flocculent growth in liquid media and they show abnormal cell morphologies, for example, a significant fraction of the cells are greatly enlarged. Deletion mutant has increased phosphorylation of 'Ser-5' of the CTD repeat during logarithmic growth. Deletion eliminates transient increase in CTD 'Ser-2' phosphorylation observed during diauxic shift. Deletion mutant is synthetically lethal when combined with deletion of DST1 or ELP genes. Deletion mutants are modestly sensitive to the uracil analog 6-azauracil (6AU), which inhibits elongation by depleting nucleotide pools. Deletion mutant is sensitive to the DNA synthesis inhibitor hydroxyurea (HU) and UV irradiation. 'Ser-2' phosphorylation within the CTD repeats is not increased in deletion mutants upon treatment with DNA-damaging agents. Present with 125 molecules/cell in log phase SD medium. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. ATP-binding Complete proteome Cytoplasm DNA damage Kinase mRNA processing Nucleotide-binding Nucleus Phosphoprotein Protein biosynthesis Reference proteome Serine/threonine-protein kinase Stress response Transcription Transferase D N T A MSYNNGNTYSKSYSRNNKRPLFGKRSPNPQSLARPPPPKRIRTDSGYQSNMDNISSHRVN SNDQPGHTKSRGNNNLSRYNDTSFQTSSRYQGSRYNNNNTSYENRPKSIKRDETKAEFLS HLPKGPKSVEKSRYNNSSNTSNDIKNGYHASKYYNHKGQEGRSVIAKKVPVSVLTQQRST SVYLRIMQVGEGTYGKVYKAKNTNTEKLVALKKLRLQGEREGFPITSIREIKLLQSFDHP NVSTIKEIMVESQKTVYMIFEYADNDLSGLLLNKEVQISHSQCKHLFKQLLLGMEYLHDN KILHRDVKGSNILIDNQGNLKITDFGLARKMNSRADYTNRVITLWYRPPELLLGTTNYGT EVDMWGCGCLLVELFNKTAIFQGSNELEQIESIFKIMGTPTINSWPTLYDMPWFFMIMPQ QTTKYVNNFSEKFKSVLPSSKCLQLAINLLCYDQTKRFSATEALQSDYFKEEPKPEPLVL DGLVSCHEYEVKLARKQKRPNILSTNTNNKGNGNSNNNNNNNNDDDDK Q12734 D6W440 CSR2_YEAST Transcription factor CSR2 CHS5 SPA2 rescue protein 2 CSR2 MRG19 YPR030W YP9367.10 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION FUNCTION FUNCTION INDUCTION SUBCELLULAR LOCATION PHOSPHORYLATION BY CDC28 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-841 IDENTIFICATION BY MASS SPECTROMETRY SUB592 FUNCTION FUNCTION INDUCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-46; SER-127; SER-327 AND SER-987 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Transcription factor involved in the regulation of fermentation and aerobic oxidation. Acts as a repressor of CYC1, which is involved in electron flow through the mitochondria under aerobic condition. Required for pseudohyphal formation upon nitrogen starvation. May be involved in viability at stationary phase and aging. P39940 RSP5 false 2 Cytoplasm Nucleus Repressed by glucose and increased expression upon nitrogen depletion. Phosphorylated by CDC28. Belongs to the CSR2 family. Complete proteome Cytoplasm Isopeptide bond Nucleus Phosphoprotein Reference proteome Repressor Transcription Transcription regulation Ubl conjugation MQSTVPIAIASNGNKRDVVQNVSAGDEGDILQRLARNREMISTSLSPQKSSGFSGRRRSS SVRDALSSFFGTGNSPTSSMDDYSNLMNRNYSTASTAMCRGNSFPSDVGTKAYNITGSYQ PDRHRNSVPYTTIDQLHTRQDTGLRRESDPVAAKQISSNNDIVRSFITHHASNSTMFINR VLSDYLADRGFIKQTPLYNKKSVLEISIATSAESVFLPTTKSDETEYLSLIHGSLNQART QPVGSTNTAESDFLPSCPTMDTLNENNDLSLFPLHTQRTSPSNTARTGNAMDTSNSDRAS PASNNNTTDADSFVASGNNNPMNNNNSPARNRHPNSHSRSLPNAWNSQMPSFSFALIFSL NKSTTLSDIKVELTSNVRVVWFNGLPPTKNVNEECYNIGSLDWTLNADNFNLFIPQGAKS PLDIVENHSNNRKLKVLQKLSMRKRRSFSNKAVLRENILNNLNASNSTNKLNAGVYVFTI PIVLASRIPESLYYPSARVSYSLRLATKLKDEHTQLVASRPRSSSISSPQKLRSYSCSDS YEYSQIDDTIEGETYNNDKNSTGKIAFPSSWLKSAKGRLKRNNSNGRSDNNGASSSGLAM QHDSEDTINLQYPLNLVRTPPEISVTTANKPLYINKVWENCLSYEISFAQKYVPLNGEIP ITIKVAPLVKSLSVKRIRVSCREKISYRSKDYQYDFDQLDPLASDPCNPYHMRYLVRKKK DRSLPLFEVASKCTSGPSIREEVVTNTVDDNLLAYTSSKENNKDIPFSESFTVKTKLKFP KYCEVDATKAASLPPYGIDLFDPIKDPTQSENTSNNGNVLGFLVGRPNRASKTVHKIPQD KNHNEVNDTNGNSNTSLQTSSNVPIQHYTRLNKPRRGLYLDSMHFKNIQCSHKLEIVLRV SKTDSGSSKIIRHYEVIVDTPIYLISDLCNTSNIDLPTYDMATTESSKVLPPTFEEATSV SASPRSSVSYYPDDISMQQLNLSRSTSLANGYLSTLHPKTTAVSDSSNGAPIRDQQEQQA RPLRTEDYALQMGNENNAYSNMDGLLSQDIFEQETAATLFKRDIVTMNFNNNIFTPRYSP RTFTNTDYNYNDNDNNDNDTEGPGPIIHPGPEPPRYDEISS P07246 D6VZQ6 ADH3_YEAST Alcohol dehydrogenase 3, mitochondrial 1.1.1.1 Alcohol dehydrogenase III YADH-3 ADH3 YMR083W YM9582.08 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c REVIEW LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH a secondary alcohol + NAD(+) = a ketone + H(+) + NADH Zn(2+) Binds 2 Zn(2+) ions per subunit. Homotetramer. Mitochondrion matrix Present with 11600 molecules/cell in log phase SD medium. Belongs to the zinc-containing alcohol dehydrogenase family. Complete proteome Metal-binding Mitochondrion NAD Oxidoreductase Reference proteome Transit peptide Zinc R K K N MLRTSTLFTRRVQPSLFSRNILRLQSTAAIPKTQKGVIFYENKGKLHYKDIPVPEPKPNE ILINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVKLGSNVKGWKVGDLAGIKW LNGSCMTCEFCESGHESNCPDADLSGYTHDGSFQQFATADAIQAAKIQQGTDLAEVAPIL CAGVTVYKALKEADLKAGDWVAISGAAGGLGSLAVQYATAMGYRVLGIDAGEEKEKLFKK LGGEVFIDFTKTKNMVSDIQEATKGGPHGVINVSVSEAAISLSTEYVRPCGTVVLVGLPA NAYVKSEVFSHVVKSINIKGSYVGNRADTREALDFFSRGLIKSPIKIVGLSELPKVYDLM EKGKILGRYVVDTSK P07248 D6VSJ9 Q04919 ADR1_YEAST Regulatory protein ADR1 ADR1 YDR216W YD8142.16 YD8142B.08 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND THR-327 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; THR-188; THR-193; SER-230; SER-258; THR-259; SER-299 AND SER-325 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] STRUCTURE BY NMR OF ZINC-FINGERS STRUCTURE BY NMR OF 131-159 STRUCTURE BY NMR OF 102-161 MUTAGENESIS MUTAGENESIS MUTAGENESIS MUTAGENESIS PHOSPHORYLATION AT SER-230 MUTAGENESIS MUTAGENESIS Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2). Nucleus Phosphorylation at Ser-230 by cAMP-dependent protein kinase A does not affect DNA binding but appears to prevent transcription of ADH2 during glucose repression. 3D-structure Activator Complete proteome DNA-binding Metal-binding Nucleus Phosphoprotein Reference proteome Repeat Transcription Transcription regulation Zinc Zinc-finger C Y C Y A V H Y H Y C Y T I D H MANVEKPNDCSGFPVVDLNSCFSNGFNNEKQEIEMETDDSPILLMSSSASRENSNTFSVI QRTPDGKIITTNNNMNSKINKQLDKLPENLRLNGRTPSGKLRSFVCEVCTRAFARQEHLK RHYRSHTNEKPYPCGLCNRCFTRRDLLIRHAQKIHSGNLGETISHTKKVSRTITKARKNS ASSVKFQTPTYGTPDNGNFLNRTTANTRRKASPEANVKRKYLKKLTRRASFSAQSASSYA LPDQSSLEQHPKDRVKFSTPELVPLDLKNPELDSSFDLNMNLDLNLNLDSNFNIALNRSD SSGSTMNLDYKLPESANNYTYSSGSPTRAYVGANTNSKNASFNDADLLSSSYWIKAYNDH LFSVSESDETSPMNSELNDTKLIVPDFKSTIHHLKDSRSSSWTVAIDNNSNNNKVSDNQP DFVDFQELLDNDTLGNDLLETTAVLKEFELLHDDSVSATATSNEIDLSHLNLSNSPISPH KLIYKNKEGTNDDMLISFGLDHPSNREDDLDKLCNMTRDVQAIFSQYLKGEESKRSLEDF LSTSNRKEKPDSGNYTFYGLDCLTLSKISRALPASTVNNNQPSHSIESKLFNEPMRNMCI KVLRYYEKFSHDSSESVMDSNPNLLSKELLMPAVSELNEYLDLFKNNFLPHFPIIHPSLL DLDLDSLQRYTNEDGYDDAENAQLFDRLSQGTDKEYDYEHYQILSISKIVCLPLFMATFG SLHKFGYKSQTIELYEMSRRILHSFLETKRRCRSTTVNDSYQNIWLMQSLILSFMFALVA DYLEKIDSSLMKRQLSALCSTIRSNCLPTISANSEKSINNNNEPLTFGSPLQYIIFESKI RCTLMAYDFCQFLKCFFHIKFDLSIKEKDVETIYIPDNESKWASESIICNGHVVQKQNFY DFRNFYYSFTYGHLHSIPEFLGSSMIYYEYDLRKGTKSHVFLDRIDTKRLERSLDTSSYG NDNMAATNKNIAILIDDTIILKNNLMSMRFIKQIDRSFTEKVRKGQIAKIYDSFLNSVRL NFLKNYSVEVLCEFLVALNFSIRNISSLYVEEESDCSQRMNSPELPRIHLNNQALSVFNL QGYYYCFILIIKFLLDFEATPNFKLLRIFIELRSLANSILLPTLSRLYPQEFSGFPDVVF TQQFINKDNGMLVPGLSANEHHNGASAAVKTKLAKKINVEGLAMFINEILVNSFNDTSFL NMEDPIRNEFSFDNGDRAVTDLPRSAHFLSDTGLEGINFSGLNDSHQTVSTLNLLRYGEN HSSKHKNGGKGQGFAEKYQLSLKYVTIAKLFFTNVKENYIHCHMLDKMASDFHTLENHLK GNS P38995 D6VSQ3 ATU2_YEAST Copper-transporting ATPase 7.2.2.8 Cu(2+)-ATPase CCC2 YDR270W D9954.6 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c METAL-BINDING SITES STRUCTURE BY NMR OF 1-72 IN APO AND COPPER-BOUND FORMS Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone ATX1 and incorporates it into trans-Golgi vesicles. ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate Golgi apparatus trans-Golgi network membrane Multi-pass membrane protein Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. 3D-structure ATP-binding Complete proteome Copper Copper transport Golgi apparatus Ion transport Magnesium Membrane Metal-binding Nucleotide-binding Reference proteome Repeat Translocase Transmembrane Transmembrane helix Transport MREVILAVHGMTCSACTNTINTQLRALKGVTKCDISLVTNECQVTYDNEVTADSIKEIIE DCGFDCEILRDSEITAISTKEGLLSVQGMTCGSCVSTVTKQVEGIEGVESVVVSLVTEEC HVIYEPSKTTLETAREMIEDCGFDSNIIMDGNGNADMTEKTVILKVTKAFEDESPLILSS VSERFQFLLDLGVKSIEISDDMHTLTIKYCCNELGIRDLLRHLERTGYKFTVFSNLDNTT QLRLLSKEDEIRFWKKNSIKSTLLAIICMLLYMIVPMMWPTIVQDRIFPYKETSFVRGLF YRDILGVILASYIQFSVGFYFYKAAWASLKHGSGTMDTLVCVSTTCAYTFSVFSLVHNMF HPSSTGKLPRIVFDTSIMIISYISIGKYLETLAKSQTSTALSKLIQLTPSVCSIISDVER NETKEIPIELLQVNDIVEIKPGMKIPADGIITRGESEIDESLMTGESILVPKKTGFPVIA GSVNGPGHFYFRTTTVGEETKLANIIKVMKEAQLSKAPIQGYADYLASIFVPGILILAVL TFFIWCFILNISANPPVAFTANTKADNFFICLQTATSVVIVACPCALGLATPTAIMVGTG VGAQNGVLIKGGEVLEKFNSITTFVFDKTGTLTTGFMVVKKFLKDSNWVGNVDEDEVLAC IKATESISDHPVSKAIIRYCDGLNCNKALNAVVLESEYVLGKGIVSKCQVNGNTYDICIG NEALILEDALKKSGFINSNVDQGNTVSYVSVNGHVFGLFEINDEVKHDSYATVQYLQRNG YETYMITGDNNSAAKRVAREVGISFENVYSDVSPTGKCDLVKKIQDKEGNNKVAVVGDGI NDAPALALSDLGIAISTGTEIAIEAADIVILCGNDLNTNSLRGLANAIDISLKTFKRIKL NLFWALCYNIFMIPIAMGVLIPWGITLPPMLAGLAMAFSSVSVVLSSLMLKKWTPPDIES HGISDFKSKFSIGNFWSRLFSTRAIAGEQDIESQAGLMSNEEVL P08679 D6VR15 CISY2_YEAST Citrate synthase, peroxisomal 2.3.3.16 CIT2 YCR005C YCR043 YCR5C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-354 AND LYS-385 IDENTIFICATION BY MASS SPECTROMETRY SUB592 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-218 AND LYS-239 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+) Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. Peroxisome Citrate synthase is found in nearly all cells capable of oxidative metabolism. Present with 2310 molecules/cell in log phase SD medium. Belongs to the citrate synthase family. Complete proteome Isopeptide bond Peroxisome Phosphoprotein Reference proteome Transferase Tricarboxylic acid cycle Ubl conjugation MTVPYLNSNRNVASYLQSNSSQEKTLKERFSEIYPIHAQDVRQFVKEHGKTKISDVLLEQ VYGGMRGIPGSVWEGSVLDPEDGIRFRGRTIADIQKDLPKAKGSSQPLPEALFWLLLTGE VPTQAQVENLSADLMSRSELPSHVVQLLDNLPKDLHPMAQFSIAVTALESESKFAKAYAQ GISKQDYWSYTFEDSLDLLGKLPVIAAKIYRNVFKDGKMGEVDPNADYAKNLVNLIGSKD EDFVDLMRLYLTIHSDHEGGNVSAHTSHLVGSALSSPYLSLASGLNGLAGPLHGRANQEV LEWLFALKEEVNDDYSKDTIEKYLWDTLNSGRVIPGYGHAVLRKTDPRYMAQRKFAMDHF PDYELFKLVSSIYEVAPGVLTEHGKTKNPWPNVDAHSGVLLQYYGLKESSFYTVLFGVSR AFGILAQLITDRAIGASIERPKSYSTEKYKELVKNIESKL P03876 A0A0A7NYJ2 Q9ZZX4 AI2M_YEAST Putative COX1/OXI3 intron 2 protein AI2 Q0055 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 24657 / D273-10B NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 96604 / S288c / FY1679 GENOME REANNOTATION ATCC 96604 / S288c / FY1679 Mitochondrion This protein is coded in group-II intron 2 of OXI3 (COX1). Complete proteome Mitochondrion Reference proteome V A R S MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVV GHAVLMIFCAPFRLIYHCIEVLIDKHISVYSINENFTVSFWFWLLVVTYMVFRYVNHMAY PVGANSTGTMACHKSAGVKQPAQGKNCPMARLTNSCKECLGFSLTPSHLGIVIHAYVLEE EVHELTKNESLALSKSWHLEGCTSSNGKLRNTGLSERGNPGDNGVFMVPKFNLNKVRYFS TLSKLNARKEDSLAYLTKINTTDFSELNKLMENNHNKTETINTRILKLMSDIRMLLIAYN KIKSKKGNMSKGSNNITLDGINISYLNKLSKDINTNMFKFSPVRRVEIPKTSGGFRPLSV GNPREKIVQESMRMMLEIIYNNSFSYYSHGFRPNLSCLTAIIQCKNYMQYCNWFIKVDLN KCFDTIPHNMLINVLNERIKDKGFMDLLYKLLRAGYVDKNNNYHNTTLGIPQGSVVSPIL CNIFLDKLDKYLENKFENEFNTGNMSNRGRNPIYNSLSSKIYRCKLLSEKLKLIRLRDHY QRNMGSDKSFKRAYFVRYADDIIIGVMGSHNDCKNILNDINNFLKENLGMSINMDKSVIK HSKEGVSFLGYDVKVTPWEKRPYRMIKKGDNFIRVRHHTSLVVNAPIRSIVMKLNKHGYC SHGILGKPRGVGRLIHEEMKTILMHYLAVGRGIMNYYRLATNFTTLRGRITYILFYSCCL TLARKFKLNTVKKVILKFGKVLVDPHSKVSFSIDDFKIRHKMNMTDSNYTPDEILDRYKY MLPRSLSLFSGICQICGSKHDLEVHHVRTLNNAANKIKDDYLLGRMIKMNRKQITICKTC HFKVHQGKYNGPGL Q01976 D6VQB0 ADPP_YEAST ADP-ribose pyrophosphatase 3.6.1.13 ADP-ribose diphosphatase ADP-ribose phosphohydrolase Adenosine diphosphoribose pyrophosphatase ADPR-PPase YSA1 YBR111C YBR0907 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47 ATCC 204508 / S288c CHARACTERIZATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2) CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2) IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+) Mg(2+) Mn(2+) Binds 3 Mg(2+) ions per subunit. Can also accept Mn(2+) ions. Q01976-1 1 Q01976-2 2 Initiator Met-1 is removed. Contains a N-acetylserine at position 2. Present with 7330 molecules/cell in log phase SD medium. Belongs to the Nudix hydrolase family. NudF subfamily. Acetylation Alternative initiation Complete proteome Hydrolase Magnesium Manganese Metal-binding Reference proteome MFLRNVRVISLNSRRLFRTMSTVKGKPEDAKIIEARHVKETSDCKWIGLQKIIYKDPNGK EREWDSAVRTTRSSGGVDGIGILTILKYKDGKPDEILLQKQFRPPVEGVCIEMPAGLIDA GEDIDTAALRELKEETGYSGKIISKSPTVFNDPGFTNTNLCLVTVEVDMSLPENQKPVTQ LEDNEFIECFSVELHKFPDEMVKLDQQGYKLDARVQNVAQGILMAKQYHIK Q06350 D6VT02 CHI2_YEAST Sporulation-specific chitinase 2 3.2.1.14 CTS2 YDR371W D9481.7 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Secreted Present with 3050 molecules/cell in log phase SD medium. Belongs to the glycosyl hydrolase 18 family. Chitinase class III subfamily. Carbohydrate metabolism Chitin degradation Complete proteome Glycoprotein Glycosidase Hydrolase Polysaccharide degradation Reference proteome Secreted Signal Sporulation MVGHSAQHRSKSSLVSHLLILLIFITIIIEMCLYNKIFKNQRSDDIRDNFNNGGHRVPSN VQNHGTHIRDEAFISGVYYSNWSPYKPRFHFPHDINLKQVSHIYYAFFKINSRTGGIENT DSWSDLEMNLYKSLAIKNSELIKESSNNSVQNILPLGCIGELFYLKNTCSDKKFKVIMSI GGWSDSENFKIIIKDDKLLQNFVDSSVETMFRLGFDGIDLDWEFPGNNESEPRGYLKLVR MLRLKLNSLESQIFGKRTEDHFQLSIAAPAFKDKLFYLPITEIDQYVDYWNMMTYDYYGS WSETTGYHSNLFSETELNGNFAMHYMIDRFGVNSRKLVLGMAAYGRSFHIKDNKFEPFNQ NTVLINKIFKGVGKPTKEIDKADGKEGIWPYKNLPKIGTIEQYDPKYVSAYCFDEKNSIF ISYDNTKSVKTKAEYVTHNNLGGGFWWESCGEAYANESRSLINAFNEGLHFNVSSKPSIF QDVRVKKYYLNKYGDGGFLSPYLKHLDSRKQ P40019 D3DLS9 CHZ1_YEAST Histone H2A.Z-specific chaperone CHZ1 CHZ1 YER030W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION OF PROBABLE INITIATION SITE SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION OF PROBABLE INITIATION SITE FUNCTION SUBCELLULAR LOCATION SUBUNIT PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-70 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-70 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Forms a chaperone-bound H2A.Z-H2B complex that acts as a source for SWR1 complex-dependent H2A to H2A.Z histone replacement in chromatin. Forms a heterotrimer with H2A.Z-H2B, stabilizing the association of the histone dimer. Also, with a lower affinity, forms a heterotrimer with H2A-H2B. Nucleus Present with 623 molecules/cell in log phase SD medium. Belongs to the CHZ1 family. 3D-structure Acetylation Chaperone Complete proteome Nucleus Phosphoprotein Reference proteome MSDEAKEKRELESQKESSHNKSEKSVEPKPKRRRRRNYDDYDAEVAKEETKAKNGLTKSE NNGTVEDSESDMDDAKLDALMGNEGEEEEDDLAEIDTSNIITSGRRTRGKVIDYKKTAEE LDKKEPSTGSKDDVGYGEKEEDDEDEEDDDFKE P00163 A0A0A7NYK0 Q35802 Q35807 Q36301 Q9ZZW9 CYB_YEAST Cytochrome b Complex III subunit 3 Complex III subunit CYTB Complex III subunit III Cytochrome b-c1 complex subunit 3 Cytochrome b-c1 complex subunit CYTB Ubiquinol-cytochrome-c reductase complex cytochrome b subunit COB CYTB Q0105 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] D273-10B/A21 NUCLEOTIDE SEQUENCE [GENOMIC DNA] D273-10B/A21 NUCLEOTIDE SEQUENCE [MRNA] WR200 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 96604 / S288c / FY1679 GENOME REANNOTATION ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-143 ATCC 44821 / 777-3A NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 144-169 ATCC 44821 / 777-3A MUTANT W7 FUNCTION FUNCTION SUBCELLULAR LOCATION TOPOLOGY PROTEIN SEQUENCE OF 66-76 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HEME AND OTHER SUBUNITS OF THE BC1 COMPLEX COFACTOR TOPOLOGY SUBUNIT X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) IN COMPLEX WITH HEME AND OTHER SUBUNITS OF THE BC1 COMPLEX COFACTOR TOPOLOGY SUBUNIT Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis. heme Binds 2 heme groups non-covalently. Fungal cytochrome b-c1 complex contains 10 subunits; 3 respiratory subunits, 2 core proteins and 5 low-molecular weight proteins. Cytochrome b-c1 complex is a homodimer. Mitochondrion inner membrane Multi-pass membrane protein Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm. Belongs to the cytochrome b family. The protein contains only eight transmembrane helices, not nine as predicted by bioinformatics tools. 3D-structure Complete proteome Direct protein sequencing Electron transport Heme Iron Membrane Metal-binding Mitochondrion Mitochondrion inner membrane Reference proteome Respiratory chain Transmembrane Transmembrane helix Transport Ubiquinone G S I T I ID MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIEL AFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFF ALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAIL VLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK P24814 D6VWQ8 GRR1_YEAST SCF E3 ubiquitin ligase complex F-box protein GRR1 F-box and leucine-rich repeat protein GRR1 F-box/LRR-repeat protein GRR1 GRR1 CAT80 COT2 YJR090C J1885 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION SUBCELLULAR LOCATION LEUCINE-RICH REPEATS NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION IN UBIQUITINATION OF CLN1 AND CLN2 FUNCTION IN UBIQUITINATION OF GIC2 IDENTIFICATION IN SCF COMPLEX FUNCTION IN UBIQUITINATION OF CLN1 INTERACTION WITH SKP1 RECONSTITUTION OF THE SCF(GRR1) COMPLEX PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-300 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and directs ubiquitination of phosphorylated CLN1, CLN2 and GIC2. Probably constitutes the primary response element required for the generation or interpretation of the signal that induces glucose repression. Protein modification; protein ubiquitination. Interacts with SKP1. Component of the probable SCF(GRR1) complex containing CDC53, SKP1, RBX1 and GRR1. Q12018 CDC53 false 9 P52286 SKP1 false 7 Membrane Associated with the particulate fraction. Probably forms a complex by protein-protein interactions via its leucine-rich segment. Expressed constitutively at low levels. Carbohydrate metabolism Complete proteome Glucose metabolism Leucine-rich repeat Membrane Phosphoprotein Reference proteome Repeat Ubl conjugation pathway MDQDNNNHNDSNRLHPPDIHPNLGPQLWLNSSGDFDDNNNNNNNNNNNNSTRPQMPSRTR ETATSERNASEVRDATLNNIFRFDSIQRETLLPTNNGQPLNQNFSLTFQPQQQTNALNGI DINTVNTNLMNGVNVQIDQLNRLLPNLPEEERKQIHEFKLIVGKKIQEFLVVIEKRRKKI LNEIELDNLKLKELRIDNSPQAISYLHKLQRMRLRALETENMEIRNLRLKILTIIEEYKK SLYAYCHSKLRGQQVENPTDNFIIWINSIDTTESSDLKEGLQDLSRYSRQFINNVLSNPS NQNICTSVTRRSPVFALNMLPSEILHLILDKLNQKYDIVKFLTVSKLWAEIIVKILYYRP HINKKSQLDLFLRTMKLTSEETVFNYRLMIKRLNFSFVGDYMHDTELNYFVGCKNLERLT LVFCKHITSVPISAVLRGCKFLQSVDITGIRDVSDDVFDTLATYCPRVQGFYVPQARNVT FDSLRNFIVHSPMLKRIKITANNNMNDELVELLANKCPLLVEVDITLSPNVTDSSLLKLL TRLVQLREFRITHNTNITDNLFQELSKVVDDMPSLRLIDLSGCENITDKTIESIVNLAPK LRNVFLGKCSRITDASLFQLSKLGKNLQTVHFGHCFNITDNGVRALFHSCTRIQYVDFAC CTNLTNRTLYELADLPKLKRIGLVKCTQMTDEGLLNMVSLRGRNDTLERVHLSYCSNLTI YPIYELLMSCPRLSHLSLTAVPSFLRPDITMYCRPAPSDFSENQRQIFCVFSGKGVHKLR HYLVNLTSPAFGPHVDVNDVLTKYIRSKNLIFNGETLEDALRRIITDLNQDSAAIIAATG LNQINGLNNDFLFQNINFERIDEVFSWYLNTFDGIRMSSEEVNSLLLQVNKTFCEDPFSD VDDDQDYVVAPGVNREINSEMCHIVRKFHELNDHIDDFEVNVASLVRVQFQFTGFLLHEM TQTYMQMIELNRQICLVQKTVQESGNIDYQKGLLIWRLLFIDKFIMVVQKYKLSTVVLRL YLKDNITLLTRQRELLIAHQRSAWNNNNDNDANRNANNIVNIVSDAGANDTSNNETNNGN DDNETENPNFWRQFGNRMQISPDQMRNLQMGLRNQNMVRNNNNNTIDESMPDTAIDSQMD EASGTPDEDML P07267 D6W3L4 CARP_YEAST Saccharopepsin 3.4.23.25 Aspartate protease PrA Proteinase A Carboxypeptidase Y-deficient protein 4 Proteinase YSCA PEP4 PHO9 PRA1 YPL154C P2585 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 77-405 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 373-405 ATCC 204508 / S288c PROTEIN SEQUENCE OF 23-31 AND 68-86 MUTAGENESIS OF ASP-294 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself. Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg. Vacuole Lysosome-like vacuoles. Belongs to the peptidase A1 family. 3D-structure Aspartyl protease Complete proteome Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Protease Reference proteome Signal Vacuole Zymogen D A MFSLKALLPLALLLVSANQVAAKVHKAKIYKHELSDEMKEVTFEQHLAHLGQKYLTQFEK ANPEVVFSREHPFFTEGGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSN ECGSLACFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQDFAE ATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEKRFAFYLGDTSKDTE NGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEGIGLGDEYAELESHGAAIDTGTSLI TLPSGLAEMINAEIGAKKGWTGQYTLDCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGS CISAITPMDFPEPVGPLAIVGDAFLRKYYSIYDLGNNAVGLAKAI P39010 D6VSP8 AKR1_YEAST Palmitoyltransferase AKR1 2.3.1.225 Ankyrin repeat-containing protein AKR1 AKR1 YDR264C D9954.9 YD9230B.03C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION FUNCTION FUNCTION SUBCELLULAR LOCATION ACTIVE SITE MUTAGENESIS OF 497-ASP--HIS-498 AND CYS-500 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION TOPOLOGY TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Palmitoyltransferase specific for casein kinase 1. Palmitoylates isoforms YCK1 and YCK2 at both C-terminal cysteine residues, which is required for their proper plasma membrane localization. Required for constitutive endocytosis of a-factor receptor STE3 and both constitutive and pheromone-induced endocytosis of alpha-factor receptor STE2. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] P18851 STE4 false 3 Early endosome membrane Multi-pass membrane protein Golgi apparatus membrane Multi-pass membrane protein The DHHC domain is required for palmitoyltransferase activity. Present with 4072 molecules/cell in log phase SD medium. Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily. Acyltransferase ANK repeat Complete proteome Endosome Golgi apparatus Lipoprotein Membrane Palmitate Phosphoprotein Reference proteome Repeat Transferase Transmembrane Transmembrane helix DH AA C A MVNELENVPRASTLTNEEQTVDPSNNDSQEDISLGDSNEITSLASLKAIRSGNEEESGNE QVNHNDEAEEDPLLTRYHTACQRGDLATVKEMIHGKLLEVNNDGDSTEHITGLHWASINN RLSVVDFLVSQGADVNARAGALHATPLHWAARYGYVYIVDFLLKHGADPTMTDDQGFNLL HLSVNSSNIMLVLYVLFNVVSKGLLDIDCRDPKGRTSLLWAAYQGDSLTVAELLKFGASI KIADTEGFTPLHWGTVKGQPHVLKYLIQDGADFFQKTDTGKDCFAIAQEMNTVYSLREAL THSGFDYHGYPIKKWFKKSQHAKLVTFITPFLFLGIAFALFSHINPLFVIIVLFLLAIAT NKGLNKFVLPSYGRMGVHNVTLLRSPLLSGVFFGTLLWVTIVWFFKVMPRTFSDEQYTNI LMLVILVSVFYLFGQLVIMDPGCLPEETDHENVRQTISNLLEIGKFDTKNFCIETWIRKP LRSKFSPLNNAVVARFDHYCPWIFNDVGLKNHKAFIFFITLMESGIFTFLALCLEYFDEL EDAHEDTSQKNGKCFILGASDLCSGLIYDRFVFLILLWALLQSIWVASLIFVQAFQICKG MTNTEFNVLMKESKSIGPDGLSFNENFNTTPEGFAPSIDPGEESNDTVLAPVPGSTIRKP RTCFGVCYAVTGMDQWLAVIKETIGIKDSTGHNVYSITSRIPTNYGWKRNVKDFWLTSDI NAPLWRRILYPPSGSKALLNGIEVDYFKLYKLPNKDVEQGNDMV P38328 D6VQN0 ARPC1_YEAST Actin-related protein 2/3 complex subunit 1 Arp2/3 complex 41 kDa subunit p41-ARC ARC40 YBR234C YBR1532 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c IDENTIFICATION IN THE ARP2/3 COMPLEX IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Component of the Arp2/3 complex composed of ARP2, ARP3, ARC40/p41-ARC, ARC35/p34-ARC, ARC18/p21-ARC, ARC19/p20-ARC and ARC16/p16-ARC. Q05933 ARC18 false 4 P33204 ARC19 false 4 P53731 ARC35 false 6 P32381 ARP2 false 6 P47117 ARP3 false 4 Q12446 LAS17 false 2 Q04439 MYO5 false 3 Cytoplasm Cytoskeleton Actin patch Belongs to the WD repeat ARPC1 family. Actin-binding Complete proteome Cytoplasm Cytoskeleton Reference proteome Repeat WD repeat MSFSNSKDKSVVAVYKLVKAPIYSHCFSQDKSILAVTCETDCLVYRVSNNTPPVLFATLK DHDKTITAVDISIHGRIVTCSQDRNAYVWEPLSDGTYKPTLVLLRINRAATSVTWAPNGY KFAVGSSARIIAVCYYEHENNWWVSKHIKKPIKSTINCLSWHANGVLLAAGGTDGFMRVF SGFIKGLDSKESVAGSPWGQKFPFGCLIREWYQGSYIHDVEWRSQMERIAYVAHDGTLNV VDYQSPVQSVNAPEGLPYRSLVWINDHEIVCGGYSCHPVLFSEASEGWKFAKNLDKSDNN KSSALTASGNTDELSGNNDESSTFGISALRKFKELDLKGKVSTDVQESAHENAIVELRPF AESNGQITQVSSCGLDGKIVIYTI P06787 D6VQA8 CALM_YEAST Calmodulin CaM CMD1 YBR109C YBR0904 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c PROTEIN SEQUENCE OF 15-30 AND 128-145 CALCIUM-BINDING DATA MUTAGENESIS SUBCELLULAR LOCATION INTERACTION WITH SPC110 FUNCTION IDENTIFICATION IN THE SPC110 COMPLEX PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] STRUCTURE BY NMR OF 1-78 Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Component of the SPC110 complex containing at least CMD1, SPC29, SPC42 and SCP110. Interacts with SPC110. P23287 CNA1 false 4 Q04439 MYO5 false 8 P32380 SPC110 false 5 P36094 SPC42 false 2 Cytoplasm Cytoskeleton Microtubule organizing center Spindle pole body The N-terminus is blocked. This protein has three functional calcium-binding sites. Belongs to the calmodulin family. 3D-structure Calcium Complete proteome Cytoplasm Cytoskeleton Direct protein sequencing Metal-binding Phosphoprotein Reference proteome Repeat D A E V D A E V D A E V MSSNLTEEQIAEFKEAFALFDKDNNGSISSSELATVMRSLGLSPSEAEVNDLMNEIDVDG NHQIEFSEFLALMSRQLKSNDSEQELLEAFKVFDKNGDGLISAAELKHVLTSIGEKLTDA EVDDMLREVSDGSGEINIQQFAALLSK P36154 D6VXD4 Q6Q573 AIM29_YEAST Altered inheritance rate of mitochondria protein 29 AIM29 YKR074W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PREDICTION OF FUNCTION IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] May be involved in mitochondrial organization and biogenesis. Cytoplasm Present with 1230 molecules/cell in log phase SD medium. Belongs to the UPF0538 family. Complete proteome Cytoplasm Phosphoprotein Reference proteome E G MNSTKRLKMSTTFHDYDLEEPLTSNARPLKNSVITIRVIKSFPYRNVKNIVLHDYDLADK TAKDLFNDVLNKIQNEGSFRPFRNVKFDTLKIYTHAHGSKTVNLVINFDHDDDWTLDIEN DKKKLFEYGIENETEISLFNKEDYLRFKENPEEKW Q03862 D6VS88 ARX1_YEAST Probable metalloprotease ARX1 3.-.-.- Associated with ribosomal export complex protein 1 ARX1 YDR101C YD8557.10c Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION IDENTIFICATION BY MASS SPECTROMETRY IDENTIFICATION IN THE PRE-60S RIBOSOMAL PARTICLES SUBCELLULAR LOCATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION INTERACTION WITH REI1 ASSOCIATION WITH PRE-60S PARTICLES Probable metalloprotease involved in proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Accompanies the pre-60S particles to the cytoplasm. Component of the nucleoplasmic and cytoplasmic pre-60S ribosomal particles. Interacts directly with REI1. P47019 ALB1 false 3 Q12080 NOP53 false 3 P38344 REI1 false 5 Cytoplasm Nucleus Present with 45100 molecules/cell in log phase SD medium. Belongs to the peptidase M24 family. 3D-structure Complete proteome Cytoplasm Hydrolase Metal-binding Metalloprotease Nucleus Protease Reference proteome MALAISHEDTQILLKDKNILQESVLNKYRTAGQIAQTALKYVTSLINDSYHSKTTQRQLT VPELCLLTDSFILTRLEQYYKNKVNERGIAIPTTIDIDQISGGWCPEIDDTQNLLNWNKG KDSTFASSVTGTLRPGDLVKITLGVHIDGYTSEVSHTMVIYPVDETKPILQPTGPLLGGK ADAVAAAHIAMETVVALLACALTPEKLPASLGGTSSGITGQLIRTIVDTIARSYNCGVVP GSRVRRIRRFLAGQNEGIVAEREYKGVVWTESHQEADLLSNTDAKDLTVVDRGQSTPFTN VSAIPSDDFVVQSGEVYLIDLKMASLEHCTKKGLVTLETVDSYTGKSHKAGELIARPGAY VRDFAQTHILKLKTSRQLLTKIDKQGVYPFKLSHLSSNFPFVHENEEELQSLKKDLKSFR LGMSEISNNYLCVESPIQIARWVPWDHILKATNPNGNLSYDATSTLTLPGHELPLPKLGV SAIKLKSLMNSTKESISLPVARECNTIVLCDSSVSTTDRPELLRLTGGSKTCQPSWIHSQ HELNPQDSIVQGIFQLATLAKDKRFGLLLKETQPMKQKSVETSNGGVEETMKM P27637 D6VPM3 BUD14_YEAST Bud site selection protein 14 BUD14 YAR014C FUN2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c SEQUENCE REVISION TO C-TERMINUS GENOME REANNOTATION SEQUENCE REVISION TO 439; 573-595 AND 609 ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-142 FUNCTION INTERACTION WITH GLC7 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION INTERACTION WITH GLC7 FUNCTION OF THE BUD14-GLC7 COMPLEX PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-222 AND SER-658 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-376 AND SER-378 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159; SER-160; SER-162; THR-177; SER-212; SER-222; SER-376; SER-378; SER-401; SER-507; SER-655; SER-658 AND SER-670 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Important for bud site selection. Seems to be a regulatory subunit of the BUD14-GLC7 type-I phosphatase complex. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may function as a specific activator of the dynein complex. Interacts with GLC7. P39960 BEM2 false 3 P32598 GLC7 false 7 P13186 KIN2 false 4 Present with 538 molecules/cell in log phase SD medium. Acetylation Cell cycle Cell division Complete proteome Phosphoprotein Reference proteome SH3 domain G A KDISQYIHAKSKIEETTNVENTE RTFTYIMQNRKLRDNKRGKHR A P MSNKEEHVDETSASGVKEVSSIAARHDNGYAPSLITSTSGMDSFQSHALLNDPTLIEDYS DIINNRPTSGSKLTLGNEDSESMGGSVVVTPTSNKSSPFNSKLNILSNAAEKGHDVLRNR DDDKELEEENVEKHMHSNSKRDQRHYKENSSELPDSYDYSDSEFEDNLERRLQEIETDSV DSADKDEVHFSVNNTMNPDVDDFSDGLKYAISEDEDEEENYSDDDDFDRKFQDSGFQGEK DDLEEENDDYQPLSPPRELDPDKLYALYAFNGHDSSHCQLGQDEPCILLNDQDAYWWLVK RITDGKIGFAPAEILETFPERLARLNCWKNENMSSQSVASSDSKDDSISSGNKNQSDAES IIPTPALNGYGKGNKSVSFNDVVGYADRFIDDAIEDTSLDSNDDGGEGNGQSYDDDVDND KETKVTHRDEYTEAKLNFGKFQDDDTSDVVSDVSFSTSLNTPLNVKKVRRQDNKNESEPK TSSSKDREDDYNANRYVGQEKSEPVDSDYDTDLKKVFEAPRMPFANGMAKSDSQNSLSTI GEFSPSSSEWTNESPSTPIVEESSSIPSSRAIKDISQYIHAKSKIEETTNVENTEGQIQA SLGSSGGMANQTDAEQPKEELEKHHSTPEEEKQSTLSLHSSSEEDFYMDEQRAVSSASIN SSLSGSRALSNTNMSDPASKPNSLVQHLYAPVFDRMDVLMKQLDEIIRK Q04347 D6VZI8 Q6B299 BUD22_YEAST Bud site selection protein 22 BUD22 YMR014W YM9711.01 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-367; THR-371 AND SER-375 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-367; THR-371 AND SER-375 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in positioning the proximal bud pole signal. Nucleus Present with 3250 molecules/cell in log phase SD medium. Belongs to the BUD22 family. Coiled coil Complete proteome Nucleus Phosphoprotein Reference proteome I V MPSESSVSIYKLDQLEYQYHYLTKSLQKFEPRYPKTAKLYNCIGKKNKKKIEKLLNSLEL KTLDKELDESYSKLLNNKIHYYETHLSKCIKEQIQKISKKNSSKVKDAQKNKSPSIDIEK MLATQLSLDDLALFMTRFRLIKILHQRIKQKSKKIEGDTNNKTWLNNNDYSGYINDKTSK WNPSNIWNEVITKLPSCEKLNALIGQSKIVQNLTESFDLSICLIFGFDVSAMKAKKYGAR EKTANANQTHSNIDYDTDDGNEKNAIDSKSNAIGAQTQSNKETTSDNEDLLIKEYEGMLG SSGDEGEGGGYLNPNINYNEVTDEEPSEASSDEDDSDERFSDSEENEPRRKKPKLHNLPE LMAGYYSGNDTEEESDEDNKNVKGKKKKRDTAEDRTAREQMSNEPKRKNRRGQRARRKIW EKKYGSQAKHVQRELEKEMEDRKQRQIEYEARVAKREAKAASLEASRSREREDRRTETNN KKEKESASTGEEHPSWIAKRLAEEKLQKAKFEGKKIKFD P38910 D6W286 E9P935 CH10_YEAST 10 kDa heat shock protein, mitochondrial HSP10 10 kDa chaperonin HSP10 CPN10 YOR020C OR26.10 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c PROTEIN SEQUENCE OF 10-24; 29-35 AND 63-78 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. Homohexamer. Mitochondrion matrix The N-terminus is blocked. Present with 149 molecules/cell in log phase SD medium. Belongs to the GroES chaperonin family. Acetylation Chaperone Complete proteome Direct protein sequencing Mitochondrion Phosphoprotein Reference proteome T S MSTLLKSAKSIVPLMDRVLVQRIKAQAKTASGLYLPEKNVEKLNQAEVVAVGPGFTDANG NKVVPQVKVGDQVLIPQFGGSTIKLGNDDEVILFRDAEILAKIAKD P08019 D6VVI8 Q07070 AMYG_YEAST Glucoamylase, intracellular sporulation-specific 3.2.1.3 1,4-alpha-D-glucan glucohydrolase Glucan 1,4-alpha-glucosidase SGA1 SGA YIL099W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-190 SPX101-1C Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Belongs to the glycosyl hydrolase 15 family. Carbohydrate metabolism Complete proteome Glycosidase Hydrolase Polysaccharide degradation Reference proteome Sporulation D H HVGTDGELSEQFNKYTGFMQGAQHLTWSYTSFWDAYQIRQEVLQSL TWEQTGN MARQKMFYNKLLGMLSVGFGFAWALENITIYEFDFGKGILDQSYGGVFSNNGPSQVQLRD AVLMNGTVVYDSNGAWDSSALEEWLQGQKKVSIEKIFENIGPSAVYPSISPGVVIASPSQ THPDYFYQWIRDSALTINSIVSHSAGPAIETLLQYLNVSFHLQRSNNTLGAGIGYTNDTV ALGDPKWNVDNTAFTEDWGRPQNDGPALRSIAILKIIDYIKQSGTDLGAKYPFQSTADIF DDIVRWDLRFIIDHWNSSGFDLWEEVNGMHFFTLLVQLSAVDKSLSYFNASERSSPFVEE LRQTRRDISKFLVDPANGFINGKYNYIVGTPMIADTLRSGLDISTLLAANTVHDAPSASH LPFDINDPAVLNTLHHLMLHMRSIYPINDSSKNATGIALGRYPEDVYDGYGFGEGNPWVL ATCTASTTLYQLIYRHISEQHDLVVPMNNDCSNAFWSELVFSNLTTLGNDEGYLILEFNT PAFNQTIQKIFQLADSFLVKLKAHVGTDGELSEQFNKYTGFMQGAQHLTWSYTSFWDAYQ IRQEVLQSL P22580 D6VSM2 AMDY_YEAST Probable amidase 3.5.1.4 AMD2 AMDY AMDY1 YDR242W YD8419.09 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+) Belongs to the amidase family. Complete proteome Hydrolase Reference proteome G S MTVHSTWKEKVQLKKDQLNSKIKDEWKLNSTTITRLKNDKKNLIKNIDDLCSSSENQITH STIMALRQALEAKELSCHEITAAFCHRAALIHQVVNCLSEIMFSEALRLADYYDSNRPAI LPPLYGIPISLKDQCNVEGVDTSLGYLCRTFKPKTKNEESLIVSFLRDLGAIIFVKTTVP SSMMATDTQSNTFGYTYNSINLSFSSGGSSGGEGSLIGAHGSLLGLGTDIGGSIRIPSSY QGLFGLKPTFGRVPYLRVDNSFEGRETIPSVIGPLARDLSDLRYFMSCVINICQPWVQDV KCIPYHFDSSTSKLHDNYVVGIWYGDGVIDPPPSDIRALKTCEDLVNKTKGMKAVKWEPS SELSRELFDLANEADVADSGNEIKNEFEISGEPLLDILKPMVLENGRPPYTVNEWWDLTK RVYNAQQLMRDYYLSFPESERPDVIISPTTLMPFRPGDMLKTTLRYILLFNVLNFPSLSI PVGSVDCQIDGLMDTTSALNPEDKMIKTYWNDLIQSGEIDGFPIGLQVVSPTFNDNEVCK FASWLFSKI P38041 D6VPR9 BOB1_YEAST Protein BOB1 BEM1-binding protein Growth inhibitory protein 7 BOI1 BOB1 GIN7 YBL085W YBL0717 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] YAL6B PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-209; SER-528; SER-644 AND THR-919 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-106; SER-128; THR-151; THR-158; SER-209; SER-393; SER-412; SER-525; SER-528; SER-589; SER-590; SER-593 AND SER-644 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Binds to the BEM1 protein. P29366 BEM1 false 5 Q00684 CDC14 false 2 P40020 FIR1 false 2 Q08229 NBA1 false 3 Q03780 YDR239C false 2 P40095 YER158C false 4 P47115 YJR056C false 3 P54786 ZDS2 false 3 Present with 1040 molecules/cell in log phase SD medium. Complete proteome Phosphoprotein Reference proteome SH3 domain MSLEGNTLGKGAKSFPLYIAVNQYSKRMEDELNMKPGDKIKVITDDGEYNDGWYYGRNLR TKEEGLYPAVFTKRIAIEKPENLHKSPTQESGNSGVKYGNLNDSASNIGKVSSHQQENRY TSLKSTMSDIDKALEELRSGSVEQEVSKSPTRVPEVSTPQLQDEQTLIQEKTRNEENTTH DSLFSSTADLNLSSESLKNISKSNISTKSLEPSSESVRQLDLKMAKSWSPEEVTDYFSLV GFDQSTCNKFKEHQVSGKILLELELEHLKELEINSFGIRFQIFKEIRNIKSAIDSSSNKL DADYSTFAFENQAAQLMPAATVNRDEIQQQISSKCNKLSSESSDRKSSSVTTELQRPSSV VVNPNFKLHDPAEQILDMTEVPNLFADKDIFESPGRAPKPPSYPSPVQPPQSPSFNNRYT NNNARFPPQTTYPPKNKNPTVYSNGLIPNSSTSSDNSTGKFKFPAMNGHDSNSRKTTLTS ATIPSINTVNTDESLPAISNISSNATSHHPNRNSVVYNNHKRTESGSSFVDLFNRISMLS PVKSSFDEEETKQPSKASRAVFDSARRKSSYGHSRDASLSEMKKHRRNSSILSFFSSKSQ SNPTSPTKQTFTIDPAKMTSHSRSQSNSYSHARSQSYSHSRKHSLVTSPLKTSLSPINSK SNIALAHSETPTSSNNKEAVSQPSEGKHKHKHKHKSKHKHKNSSSKDGSSEEKSKKKLFS STKESFVGSKEFKRSPSELTQKSTKSILPRSNAKKQQTSAFTEGIRSITAKESMQTADCS GWMSKKGTGAMGTWKQRFFTLHGTRLSYFTNTNDEKERGLIDITAHRVLPASDDDRLISL YAASLGKGKYCFKLVPPQPGSKKGLTFTEPRVHYFAVENKSEMKAWLSAIIKATIDIDTS VPVISSYATPTIPLSKAQTLLEEARLQTQLRDAEEEEGRDQFGWDDTQNKRNSNYPIEQD QFETSDYLESSAFEYPGGRL P38013 D6VYA9 AHP1_YEAST Peroxiredoxin AHP1 Prx 1.11.1.15 Alkyl hydroperoxide reductase AHPC1 Cytoplasmic thiol peroxidase 3 cTPx 3 Thiol-specific antioxidant II TSA II Thioredoxin peroxidase type II TPx type II AHP1 YLR109W L2916 L9354.5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 90840 / EAY235 / FY23 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 2-8; 16-48; 80-102 AND 114-176 CLEAVAGE OF INITIATOR METHIONINE ACETYLATION AT SER-2 IDENTIFICATION BY MASS SPECTROMETRY PROTEIN SEQUENCE OF 8-15; 33-41; 80-102 AND 125-176 URMYLATION PROTEIN SEQUENCE OF 16-41; 49-68; 82-96; 114-123 AND 142-150 POST-TRANSLATIONAL MODIFICATION DISULFIDE BONDS CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES PARTIAL PROTEIN SEQUENCE OF 33-37; 82-96; 126-139 AND 157-170 FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES SUBUNIT PROTEIN SEQUENCE OF 82-99 ATCC 204508 / S288c FUNCTION FUNCTION SUBUNIT FUNCTION INDUCTION SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-116 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] FUNCTION URMYLATION AT LYS-32 MUTAGENESIS OF LYS-32 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-113 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] 3D-STRUCTURE MODELING STRUCTURE BY NMR X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH TRX2 ACTIVE SITE DISULFIDE BOND SUBUNIT X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) DISULFIDE BONDS Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide (PubMed:10391912, PubMed:9988687, PubMed:10681558). Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation (PubMed:20145245). Involved in cellular Mn(2+) homeostasis (PubMed:10635552). [protein]-dithiol + a hydroperoxide = [protein]-disulfide + an alcohol + H2O 150 uM for H(2)O(2) 14 uM for H(2)O(2) 8 uM for cumene hydroperoxide 45 uM for tert-butyl hydroperoxide 76.9 uM for tert-butyl hydroperoxide 3 uM for TRX1 2 uM for TRX2 1.3 uM for TRX2 20 umol/min/mg enzyme for H(2)O(2) 14 umol/min/mg enzyme for cumene hydroperoxide 17 umol/min/mg enzyme for tert-butyl hydroperoxide 17 umol/min/mg enzyme for TRX1 16 umol/min/mg enzyme for TRX2 Optimum pH is 6.5. Homodimer; disulfide-linked, upon oxidation. P34230 PXA2 false 2 Cytoplasm By H(2)O(2). Conjugated to URM1, a ubiquitin-like protein. The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys Prx, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin. Present with 16228 molecules/cell in log phase SD medium. Belongs to the peroxiredoxin family. Prx5 subfamily. Biochemical and mutational analysis assigned Cys-120 as the resolving cysteine (C(R)) (PubMed:9888818). However, crystal structures showed that Cys-120 is deeply buried within the protein and revealed formation of a disulfide bond between the peroxidatic cysteine Cys-62 and the therefore more likely C(R) Cys-31 (PubMed:22474296, Ref.21). 3D-structure Acetylation Antioxidant Complete proteome Cytoplasm Direct protein sequencing Disulfide bond Isopeptide bond Oxidoreductase Peroxidase Phosphoprotein Redox-active center Reference proteome Ubl conjugation C S K R C S C S I T S V I E MSDLVNKKFPAGDYKFQYIAISQSDADSESCKMPQTVEWSKLISENKKVIITGAPAAFSP TCTVSHIPGYINYLDELVKEKEVDQVIVVTVDNPFANQAWAKSLGVKDTTHIKFASDPGC AFTKSIGFELAVGDGVYWSGRWAMVVENGIVTYAAKETNPGTDVTVSSVESVLAHL P16892 D6VPY4 FUS3_YEAST Mitogen-activated protein kinase FUS3 MAP kinase FUS3 2.7.11.24 FUS3 DAC2 YBL016W YBL03.21 YBL0303 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c PHOSPHORYLATION AT THR-180 AND TYR-182 FUNCTION REGULATION OF STE12 ACTIVITY FUNCTION COMPLEX WITH DIG1; DIG2 AND STE12 FUNCTION REGULATION OF KSS1 ACTIVITY SUBCELLULAR LOCATION FUNCTION REGULATION OF STE12 PROMOTER SELECTIVITY LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-345 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Together with closely related KSS1, FUS3 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated FUS3 activates the mating but suppresses the filamentation pathway, whereas activated KSS1 activates both pathways. Pheromone-activated FUS3 functions by inhibiting the binding of the transcriptional activator STE12 to filamentation specific genes while inducing its binding to and activity at mating specific genes. Non-activated FUS3 has a repressive effect on STE12 transcriptional activity. KSS1 can partially compensate for the lack of FUS3 but mating efficiency is reduced and the filamentation program is partially activated upon pheromone signaling. FUS3 phosphorylates STE7, STE5, FAR1, DIG1, DIG2 and STE12. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Mg(2+) Activated by tyrosine and threonine phosphorylation after pheromone treatment. In the nucleus, FUS3 forms a complex with DIG1, DIG2 and STE12. The interaction of FUS3 with STE12 depends on the presence of both DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after pheromone treatment. During its activation and phosphorylation, FUS3 forms a membrane-associated complex with the scaffold protein STE5, the MAPKK STE7, the MAPKKK STE11, and the G-protein beta subunit GBB/STE4; interacting directly with STE7 and STE5. false 2 P33306 BCK2 false 2 A7TJH8 Kpol_1061p54 true 2 P23561 STE11 false 6 P32917 STE5 false 11 P06784 STE7 false 15 P32830 TIM12 false 2 Nucleus Cytoplasm Periplasm FUS3 shuttles rapidly between the cytoplasm and the nucleus independent of pheromone treatment or FUS3 phosphorylation level. Activated FUS3 translocates rapidly to the nucleus. The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases. Dually phosphorylated on Thr-180 and Tyr-182 by STE7 in response to pheromone induction, which activates the enzyme. Activated FUS3 initiates a feedback signal, down-regulating phosphorylation of both, FUS3 and KSS1. Present with 8480 molecules/cell in log phase SD medium. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. 3D-structure ATP-binding Cell cycle Cell division Complete proteome Conjugation Cytoplasm Isopeptide bond Kinase Mitosis Nucleotide-binding Nucleus Periplasm Phosphoprotein Reference proteome Serine/threonine-protein kinase Transferase Ubl conjugation Y H MPKRIVYNISSDFQLKSLLGEGAYGVVCSATHKPTGEIVAIKKIEPFDKPLFALRTLREI KILKHFKHENIITIFNIQRPDSFENFNEVYIIQELMQTDLHRVISTQMLSDDHIQYFIYQ TLRAVKVLHGSNVIHRDLKPSNLLINSNCDLKVCDFGLARIIDESAADNSEPTGQQSGMT EYVATRWYRAPEVMLTSAKYSRAMDVWSCGCILAELFLRRPIFPGRDYRHQLLLIFGIIG TPHSDNDLRCIESPRAREYIKSLPMYPAAPLEKMFPRVNPKGIDLLQRMLVFDPAKRITA KEALEHPYLQTYHDPNDEPEGEPIPPSFFEFDHYKEALTTKDLKKLIWNEIFS Q12186 D6VYB4 BBP_YEAST Branchpoint-bridging protein Mud synthetic-lethal 5 protein Splicing factor 1 Zinc finger protein BBP MSL5 BBP SF1 YLR116W L2949 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 90840 / EAY235 / FY23 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION INTERACTION WITH MUD2 AND PRP40 MUTAGENESIS OF GLY-230 FUNCTION INTERACTION WITH MUD2 FUNCTION MUTAGENESIS OF ARG-60; ILE-72; PRO-155; VAL-195 AND GLU-258 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] INTERACTION WITH SMY2 AND SYH1 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95; TYR-100 AND SER-382 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. 2 commitment complexes, CC1 and CC2, have been defined. CC1 is a basal complex dependent only on the 5'-splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5'-splice site region. This protein is involved in CC2 formation where it binds to the snRNP U1-associated protein PRP40, bridging the U1 snRNP-associated 5'-splice site and the MSL5-associated branch point 3' intron splice site. Involved in nuclear retention of pre-mRNA. Interacts with MUD2 and PRP40. The proline-rich sequence of this protein interacts with the GYF domains of SMY2 and SYH1. P36084 MUD2 false 5 Nucleus Present with 4380 molecules/cell in log phase SD medium. Belongs to the BBP/SF1 family. 3D-structure Complete proteome Metal-binding mRNA processing mRNA splicing Nucleus Phosphoprotein Reference proteome Repeat RNA-binding Zinc Zinc-finger R G I N P S V D G S E V MSFRRINSRYFENRKGSSMEEKKAKVPPNVNLSLWRKNTVESDVHRFNSLPSKISGALTR EQIYSYQVMFRIQEITIKLRTNDFVPPSRKNRSPSPPPVYDAQGKRTNTREQRYRKKLED ERIKLVEIALKTIPYFVPPDDYKRPTKFQDKYYIPVDQYPDVNFVGLLLGPRGRTLRKLQ EDSNCKIAIRGRGSVKEGKNASDLPPGAMNFEDPLHCLIIADSEDKIQKGIKVCQNIVIK AVTSPEGQNDLKRGQLRELAELNGTLREDNRPCPICGLKDHKRYDCPNRKIPNIQGIVCK ICGQTGHFSRDCNSSSQRMSRFDRNATVNNSAPIQSNDVHYNSNTHPIQAPKRSRYDNNS TEPPLKFPASSRYAPSPSPPASHISRQAQNVTPTPPPGLTSSSFSSGVPGIAPPPLQSPP ESEQPKFSLPPPPGMTTVQSSIAPPPGLSGPPGFSNNMGNDINKPTPPGLQGPPGL P40074 D3DM25 AVT6_YEAST Vacuolar amino acid transporter 6 AVT6 YER119C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-448 FUNCTION SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in amino acid efflux from the vacuole to the cytoplasm. Capable of transporting aspartate and glutamate. Requires ATP for function. Vacuole membrane Multi-pass membrane protein Belongs to the amino acid/polyamine transporter 2 family. Amino-acid transport Complete proteome Membrane Phosphoprotein Reference proteome Transmembrane Transmembrane helix Transport Vacuole MVASIRSGVLTLLHTACGAGILAMPYAFKPFGLIPGVIMIVLCGACAMQSLFIQARVAKY VPQGRASFSALTRLINPNLGIVFDLAIAIKCFGVGVSYMIVVGDLMPQIMSVWTRNAWLL NRNVQISLIMLFFVAPLSFLKKLNSLRYASMVAISSVAYLCVLVLLHYVAPSDEILRLKG RISYLLPPQSHDLNVLNTLPIFVFAYTCHHNMFSIINEQRSSRFEHVMKIPLIAISLALI LYIAIGCAGYLTFGDNIIGNIIMLYPQAVSSTIGRIAIVLLVMLAFPLQCHPARASIHQI LQHFAEENVSISATSADEPTVATESSPLIRDSSLDLNEVIEEESIYQPKETPLRGKSFIV ITCSILVASYLVAISVSSLARVLAIVGATGSTSISFILPGLFGYKLIGTEHKTAVPLTTK IFKYTGLLLFIWGLIIMITCLTAALKLN P15703 D6VV59 BGL2_YEAST Glucan 1,3-beta-glucosidase 3.2.1.58 Exo-1,3-beta-glucanase GP29 Soluble cell wall protein 9 BGL2 SCW9 YGR282C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] PARTIAL PROTEIN SEQUENCE NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c PROTEIN SEQUENCE OF 24-34 SUBCELLULAR LOCATION ATCC 96099 / S288c / SEY6210 PROTEIN SEQUENCE OF 24-31 ATCC 38531 / Y41 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase. Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose. Secreted Cell wall Tightly bound to cell wall. This protein strongly binds to glucan and chitin. Present with 45000 molecules/cell in log phase SD medium. Belongs to the glycosyl hydrolase 17 family. Cell wall Cell wall biogenesis/degradation Chitin-binding Complete proteome Direct protein sequencing Glycoprotein Glycosidase Hydrolase Reference proteome Secreted Signal MRFSTTLATAATALFFTASQVSAIGELAFNLGVKNNDGTCKSTSDYETELQALKSYTSTV KVYAASDCNTLQNLGPAAEAEGFTIFVGVWPTDDSHYAAEKAALQTYLPKIKESTVAGFL VGSEALYRNDLTASQLSDKINDVRSVVADISDSDGKSYSGKQVGTVDSWNVLVAGYNSAV IEASDFVMANAFSYWQGQTMQNASYSFFDDIMQALQVIQSTKGSTDITFWVGETGWPTDG TNFESSYPSVDNAKQFWKEGICSMRAWGVNVIVFEAFDEDWKPNTSGTSDVEKHWGVFTS SDNLKYSLDCDFS P40994 D6W2F5 ARF3_YEAST ADP-ribosylation factor 3 ARF3 YOR094W YOR3172W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] INTERACTION WITH RUD3 GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Interacts with RUD3. P25369 LSB5 false 2 Golgi apparatus Present with 1240 molecules/cell in log phase SD medium. Belongs to the small GTPase superfamily. Arf family. Complete proteome ER-Golgi transport Golgi apparatus GTP-binding Lipoprotein Myristate Nucleotide-binding Protein transport Reference proteome Transport MGNSISKVLGKLFGSKEMKILMLGLDKAGKTTILYKLKLNKIKTSTPTVGFNVETVTYKN VKFNMWDVGGQQRLRPLWRHYFPATTALIFVIDSSARNRMEEAKEELYSIIGEKEMENVV LLVWANKQDLKDAMKPQEVSDFLELEKNLKNQPWCVIGSNALSGQGLVEGLSWISNNTNV PKK P38221 D6VQ30 CDS1_YEAST Phosphatidate cytidylyltransferase 2.7.7.41 CDP-diacylglycerol synthase CDP-DAG synthase CDS CDP-diglyceride pyrophosphorylase CDP-diglyceride synthase CDP-DG synthase CTP:phosphatidate cytidylyltransferase CDS1 CDG1 YBR029C YBR0313 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION CATALYTIC ACTIVITY COFACTOR BIOPHYSICOCHEMICAL PROPERTIES ATCC 204508 / S288c SUBCELLULAR LOCATION MUTAGENESIS OF CYS-102 SUBCELLULAR LOCATION Supplies CDP-diacylglycerol, which may play an important role as both a precursor to phosphoinositide biosynthesis in the plasma membrane and as a negative effector of phosphatidylinositol 4-kinase activity, thereby exerting an effect on cell proliferation via a lipid-dependent signal transduction cascade. a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate Mg(2+) 1 mM for CTP 0.5 mM for phosphatidate 4700 nmol/min/mg enzyme Optimum pH is 6.5. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. Homodimer. Endoplasmic reticulum membrane Multi-pass membrane protein Cytoplasmic vesicle Secretory vesicle Exclusively present in the ER, and not in mitochondria. Also associated with post-Golgi apparatus secretory vesicles destined for the plasma membrane. Belongs to the CDS family. Complete proteome Cytoplasmic vesicle Endoplasmic reticulum Lipid biosynthesis Lipid metabolism Magnesium Membrane Nucleotidyltransferase Phospholipid biosynthesis Phospholipid metabolism Reference proteome Transferase Transmembrane Transmembrane helix C Y MSDNPEMKPHGTSKEIVESVTDATSKAIDKLQEELHKDASESVTPVTKESTAATKESRKY NFFIRTVWTFVMISGFFITLASGHAWCIVLILGCQIATFKECIAVTSASGREKNLPLTKT LNWYLLFTTIYYLDGKSLFKFFQATFYEYPVLNFIVTNHKFICYCLYLMGFVLFVCSLRK GFLKFQFGSLCVTHMVLLLVVFQAHLIIKNVLNGLFWFLLPCGLVIVNDIFAYLCGITFG KTKLIEISPKKTLEGFLGAWFFTALASIILTRILSPYTYLTCPVEDLHTNFFSNLTCELN PVFLPQVYRLPPIFFDKVQINSITVKPIYFHALNLATFASLFAPFGGFFASGLKRTFKVK DFGHSIPGHGGITDRVDCQFIMGSFANLYYETFISEHRITVDTVLSTILMNLNDKQIIEL IDILIRFLSKKGIISAKNFEKLADIFNVTKKSLTNHS Q08032 D6VYA3 Q05908 CDC45_YEAST Cell division control protein 45 CDC45 SLD4 YLR103C L8004.11 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION SUBCELLULAR LOCATION NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] INTERACTION WITH MCM10 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-453 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Required for initiation of chromosomal DNA replication. Acts at the origin of replication. Also has a role in minichromosome maintenance. Assembles into a complex with MCM5/CDC46. Interacts with MCM10. P25588 MRC1 false 4 P53135 SLD3 false 13 P53840 TOF1 false 3 Nucleus Present with 1730 molecules/cell in log phase SD medium. Belongs to the CDC45 family. 3D-structure Cell cycle Complete proteome DNA replication Nucleus Phosphoprotein Reference proteome T K MYYGISQFSEAYNKILRNSSSHSSCQLVIFVSCLNIDALCATKMLSLLFKKQLVQSQIVP IFGYSELRRHYSQLDDNINSLLLVGFGGVIDLEAFLEIDPQEYVIDTDEKSGEQSFRRDI YVLDAHRPWNLDNIFGSQIIQCFDDGTVDDTLGEQKEAYYKLLELDEESGDDELSGDEND NNGGDDEATDADEVTDEDEEDEDETISNKRGNSSIGPNDLSKRKQRKKQIHEYEGVLEEY YSQGTTVVNSISAQIYSLLSAIGETNLSNLWLNILGTTSLDIAYAQVYNRLYPLLQDEVK RLTPSSRNSVKTPDTLTLNIQPDYYLFLLRHSSLYDSFYYSNYVNAKLSLWNENGKKRLH KMFARMGIPLSTAQETWLYMDHSIKRELGIIFDKNLDRYGLQDIIRDGFVRTLGYRGSIS ASEFVEALTALLEVGNSTDKDSVKINNDNNDDTDGEEEEDNSAQKLTNLRKRWVSNFWLS WDALDDRKVELLNRGIQLAQDLQRAIFNTGVAILEKKLIKHLRIYRLCVLQDGPDLDLYR NPLTLLRLGNWLIECCAESEDKQLLPMVLASIDENTDTYLVAGLTPRYPRGLDTIHTKKP ILNNFSMAFQQITAETDAKVRIDNFESSIIEIRREDLSPFLEKLTLSGLL P09440 D6VQ83 C1TM_YEAST C-1-tetrahydrofolate synthase, mitochondrial C1-THF synthase Methylenetetrahydrofolate dehydrogenase 1.5.1.5 Methenyltetrahydrofolate cyclohydrolase 3.5.4.9 Formyltetrahydrofolate synthetase 6.3.4.3 MIS1 YBR084W YBR0751 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 35-74 CHARACTERIZATION SUBCELLULAR LOCATION SUBUNIT SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH 5,10-methenyltetrahydrofolate + H2O = (6S)-10-formyltetrahydrofolate + H(+) (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate One-carbon metabolism; tetrahydrofolate interconversion. Homodimer. Mitochondrion This trifunctional enzyme consists of two major domains: an N-terminal part containing the methylene-THF dehydrogenase and cyclohydrolase activities and a larger C-terminal part containing formyl-THF synthetase activity. Present with 11400 molecules/cell in log phase SD medium. In the N-terminal section; belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family. In the C-terminal section; belongs to the formate--tetrahydrofolate ligase family. Amino-acid biosynthesis ATP-binding Complete proteome Direct protein sequencing Histidine biosynthesis Hydrolase Ligase Methionine biosynthesis Mitochondrion Multifunctional enzyme NADP Nucleotide-binding One-carbon metabolism Oxidoreductase Purine biosynthesis Reference proteome Transit peptide MLSRLSLLSNSRAFQQARWRIYRLKVSPTVHASQYHILSGRKLAQSIREKANDEIQAIKL KHPNFKPTLKIIQVGARPDSSTYVRMKLKASKDSNVDCIIEKLPAEITEVELLKKISDIN DDDSIHGLLIQLPLPRHLDETTITNAVDFKKDVDGFHRYNAGELAKKGGKPYFIPCTPYG CMKLLEEAHVKLDGKNAVVLGRSSIVGNPIASLLKNANATVTVCHSHTRNIAEVVSQADI VIAACGIPQYVKSDWIKEGAVVIDVGINYVPDISKKSGQKLVGDVDFDSVKEKTSYITPV PGGVGPMTVAMLVSNVLLAAKRQFVESEKLPVIKPLPLHLESPVPSDIDISRAQSPKHIK QVAEELGIHSHELELYGHYKAKISPNIFKRLESRENGKYVLVAGITPTPLGEGKSTTTMG LVQALSAHLGKPSIANVRQPSLGPTLGVKGGAAGGGYAQVIPMDEFNLHLTGDIHAISAA NNLLAAAIDTRMFHEATQKNDSTFYKRLVPRKKGIRKFTPSMQRRLKRLDIEKEDPDALT PEEVKRFARLNINPDTITIRRVVDINDRMLRQITIGEAATEKGFTRTTGFDITVASELMA ILALSKSLHEMKERIGRMVIGADYDNKPVTVEDIGCTGALTALLRDAIKPNLMQTLEGTP VMVHAGPFANISIGASSVIADLMALKLVGSEKNPLNDKNIHEPGYVVTEAGFDFAMGGER FFDIKCRSSGLVPDAVVLVATVRALKSHGGAPNVKPGQSLPKEYTEENIDFVAKGVSNLV KQIENIKTFGIPVVVAINRFETDSQAEIEVIKKAALNAGASHAVTSNHWMEGGKGAVELA HAVVDATKEPKNFNFLYDVNSSIEDKLTSIVQKMYGGAKIEVSPEAQKKIDTYKKQGFGN LPICIAKTQYSLSHDPSLKGVPRGFTFPIRDVRASIGAGYLYALAAEIQTIPGLSTYAGY MAVEVDDDGEIEGLF Q12291 D6VY64 BMT6_YEAST 25S rRNA (uridine(2843)-N(3))-methyltransferase 2.1.1.312 Base methyltransferase of 25S RNA 6 BMT6 YLR063W L2174 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] FUNCTION CATALYTIC ACTIVITY SUBCELLULAR LOCATION MUTAGENESIS OF GLY-294 S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(3) position of uridine 2843 (m3U2843) in 25S rRNA. S-adenosyl-L-methionine + uridine(2843) in 25S rRNA = H(+) + N(3)-methyluridine(2843) in 25S rRNA + S-adenosyl-L-homocysteine Cytoplasm Nucleus Localizes predominantly to the cytoplasm, with minor localizations in the nucleus (PubMed:24335083). Associates with pre-60S ribosomal particles (PubMed:24335083). Belongs to the class I-like SAM-binding methyltransferase superfamily. Complete proteome Cytoplasm Methyltransferase Nucleus Reference proteome rRNA processing S-adenosyl-L-methionine Transferase G R MLLMRRFAFLTSSVYFKYIPIYSQYHYSSQFPINMNPKKVAQLPVHNKSTLPPQEIIDLF KITFLEELYPKDQDNEKSPLTEQIQAVKSDLYNRDYNAAFNNDSKRIAYCCRWSPSRATS YASVFAHFPELLKIIRCEIDDKDSNVLCIGGGAGGELVALASIFTLSRDFSSKFASALKI DNEVNKKPRNLNIQLVDIADWSTVVEKLTATIKSKWLYGDSEAESFNVNFTHKDCLQMTE PQDIKIYQGLDLITLLFTTNELFTQKKVESIKFLQRLNENCAPGCHLLILESAGSYSHIT INNKKFPIQFLIDTILVGNRKDKGTTGPWSLVSENDSIWYRMDPKLDYSIPLENMRFFYR LYVKN P21595 D6VT34 CP56_YEAST Cytochrome P450-DIT2 1.14.14.- Cytochrome P450 56 DIT2 CYP56 YDR402C D9509.20 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204510 / AB320 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CHARACTERIZATION Involved in spore wall maturation. Thought to catalyze the oxidation of tyrosine residues in the formation of LL-dityrosine a precursor of the spore wall. heme Sporulation. Belongs to the cytochrome P450 family. Complete proteome Heme Iron Metal-binding Monooxygenase Oxidoreductase Reference proteome Sporulation M I MELLKLLCLILFLTLSYVAFAIIVPPLNFPKNIPTIPFYVVFLPVIFPIDQTELYDLYIR ESMEKYGAVKFFFGSRWNILVSRSEYLAQIFKDEDTFAKSGNQKKIPYSALAAYTGDNVI SAYGAVWRNYRNAVTNGLQHFDDAPIFKNAKILCTLIKNRLLEGQTSIPMGPLSQRMALD NISQVALGFDFGALTHEKNAFHEHLIRIKKQIFHPFFLTFPFLDVLPIPSRKKAFKDVVS FRELLVKRVQDELVNNYKFEQTTFAASDLIRAHNNEIIDYKQLTDNIVIILVAGHENPQL LFNSSLYLLAKYSNEWQEKLRKEVNGITDPKGLADLPLLNAFLFEVVRMYPPLSTIINRC TTKTCKLGAEIVIPKGVYVGYNNFGTSHDPKTWGTTADDFKPERWGSDIETIRKNWRMAK NRCAVTGFHGGRRACLGEKLALTEMRISLAEMLKQFRWSLDPEWEEKLTPAGPLCPLNLK LKFNENIME P53867 D6W0W7 ATG4_YEAST Cysteine protease ATG4 3.4.22.- Autophagy-related protein 4 ATG4 APG4 AUT2 YNL223W N1274 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] IDENTIFICATION OF PROBABLE INITIATION SITE FUNCTION FUNCTION FUNCTION INTERACTION WITH ATG8; TUB1 AND TUB2 FUNCTION ACTIVITY REGULATION MUTAGENESIS OF CYS-147 FUNCTION IN ATG8 CLEAVAGE FUNCTION SUBCELLULAR LOCATION FUNCTION NOMENCLATURE SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION IN ATG8 CLEAVAGE INTERACTION WITH ATG8 FUNCTION IN ATG8 CLEAVAGE FUNCTION IN ATG8 CLEAVAGE FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] INDUCTION FUNCTION IN ATG8-PE DECONJUGATION FUNCTION IN ATG8-PE DECONJUGATION Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Cleaves the C-terminal amino acid of ATG8 to reveal a C-terminal glycine. ATG8 ubiquitin-like activity requires the exposure of the glycine at the C-terminus for its conjugation to phosphatidylethanolamine (PE) and its insertion to membranes, which is necessary for autophagy. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Moreover not only conjugation, but also subsequent ATG8-PE deconjugation performed also by ATG4 is an important step required to delipidate ATG8 to release the protein from membranes, which facilitates multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. ATG8 delipidation by ATG4 also recycles ATG8-PE generated on inappropriate membranes to maintain a reservoir of unlipidated ATG8 that is required for autophagosome formation at the PAS. Inhibited by N-ethylmaleimide. Interacts with ATG8, TUB1 and TUB2. P38182 ATG8 false 3 Cytoplasm Nucleus Expression is induced upon starvation, through the action of transcription factors GCN2 and GCN4. Present with 3300 molecules/cell in log phase SD medium. Belongs to the peptidase C54 family. Translation N-terminally shortened. Translation N-terminally shortened. Autophagy Complete proteome Cytoplasm Hydrolase Nucleus Phosphoprotein Protease Protein transport Reference proteome Thiol protease Transport Ubl conjugation pathway C S A MQRWLQLWKMDLVQKVSHGVFEGSSEEPAALMNHDYIVLGEVYPERDEESGAEQCEQDCR YRGEAVSDGFLSSLFGREISSYTKEFLLDVQSRVNFTYRTRFVPIARAPDGPSPLSLNLL VRTNPISTIEDYIANPDCFNTDIGWGCMIRTGQSLLGNALQILHLGRDFRVNGNESLERE SKFVNWFNDTPEAPFSLHNFVSAGTELSDKRPGEWFGPAATARSIQSLIYGFPECGIDDC IVSVSSGDIYENEVEKVFAENPNSRILFLLGVKLGINAVNESYRESICGILSSTQSVGIA GGRPSSSLYFFGYQGNEFLHFDPHIPQPAVEDSFVESCHTSKFGKLQLSEMDPSMLIGIL IKGEKDWQQWKLEVAESAIINVLAKRMDDFDVSCSMDDVESVSSNSMKKDASNNENLGVL EGDYVDIGAIFPHTTNTEDVDEYDCFQDIHCKKQKIVVMGNTHTVNANLTDYEVEGVLVE KETVGIHSPIDEKC P34756 D6VTQ0 FAB1_YEAST 1-phosphatidylinositol 3-phosphate 5-kinase FAB1 Phosphatidylinositol 3-phosphate 5-kinase 2.7.1.150 Type III PIP kinase PIPkin-III FAB1 YFR019W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION SEQUENCE REVISION TO 2275 ATCC 204508 / S288c FUNCTION CATALYTIC ACTIVITY ACTIVITY REGULATION SUBCELLULAR LOCATION ACTIVITY REGULATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX SUBCELLULAR LOCATION MUTAGENESIS OF GLY-864 IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX SUBCELLULAR LOCATION MUTAGENESIS OF CYS-262; THR-1017; CYS-1243 AND ASP-2134 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1953 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-1627; SER-1630 AND SER-1938 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] 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. Hyperosmotic shock-induced increase in the levels of PtdIns(3,5)P2 requires the presence of VAC7, VAC14, and/or FIG4. 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(+) Mg(2+) Mn(2+) Activated by VAC14 and VAC7. VAC14 acts as a specific osmotic response regulator. Component of the PI(3,5)P2 regulatory complex, composed of ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the complex and serves as a scaffold. P42837 FIG4 false 4 Q06708 VAC14 false 9 Vacuole membrane Peripheral membrane protein Endosome membrane Peripheral membrane protein Localization to the vacuole membrane requires VAC14 and FIG4. Present with 149 molecules/cell in log phase SD medium. Acetylation ATP-binding Complete proteome Endosome Kinase Membrane Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Transferase Vacuole Zinc Zinc-finger C S G E T I C A D R R W MSSEEPHASISFPDGSHVRSSSTGTSSVNTIDATLSRPNYIKKPSLHIMSTSTTSTTTDL VTNPILSNISVPKISPPTSSSIATATSTSHVTGTASHSNIKANANTSTSVNKKNLPPTTS GRIPSSTIKRYPSRYKPSHSLQLPIKNDSNFKRSSIYASKSTVTAIPIRNNRPISMQNSY ARTPDSDHDDVGDEVSSIKSASSSLTASLSKSFLFAFYNNRKKDKTSNNGVLSKEYWMKD ESSKECFSCGKTFNTFRRKHHCRICGQIFCSSCTLLIDGDRFGCHAKMRVCYNCYEHADT YEDSSDEENDSTMQLNEPRSRSRSRSSNTNPYSHSHSHLHLISQDNHNGTDLHDPVAATD NPQQQNEVYLLNDDDVQSIMTSGEDSKLFISTPPPPPKMAIPATKQGGSLEISFDSENDR ALHYQDDNPGRHHHLDSVPTRYTIRDMDNISHYDTNSNSTLRPHYNTNNSTITINNLNNT TSNNSNYNNTNSNSNINNPAHSLRRSIFHYVSSNSVNKDSNNSSATPASSAQSSSILDPA NRIIGNYAHRNYKFKFNYNSKGPSQQNDTANGNNDNNNNNNNNNNNNNNNSASGIADNNN IPSNDNGTTFTLDKKKRNPLTKSKSTSAYLEYPLNEEDSSEDEGSMSIYSVLNDDHKTDN PIRSMRNSTKSFQRAQASLQRMRFRRKSKSKHFPNNSKSSIYRDLNFLTNSTPNLLSVVS DDNLYDDSSPLQDKASSSAASRLTDRKFSNSSGSNNNSNSNSNINTDPWKRIASISGFKL KKEKKRELNEVSLLHMHALLKQLLNDQEISNLQEWITLLDGALRKVLRTILNARDLNTLD FRQTYVKIKRISGGSPQNSEYIDGVVFSKALPSKTMPRHLKNPRILLIMFPLEYQKNNNH FLSIESVFRQEREYLDKLVSRLKSLHPDIIYVGANVSGYALELLNDSGIVVQFNMKPQVI ERIAKLTEADIAISVDKLATNIKMGECETFEVKSYIYGNISKTYTFLRGCNPELGGTILL RGDSLENLRKIKQVSEFMVYAIFSLKLESSFFNDNFIQLSTDVYLKRAESKKLQVFEGYF ADFLIKFNNRILTVSPTVDFPIPFLLEKARGLEKKLIERINQYESESDLDRQTQLNMLQG LESTITKKHLGNLIKFLHEMEIENLELEFQKRSRQWEVSYSSSQNLLGTGSHQSITVLYS MVSTKTATPCVGPQIVTIDYFWDSDISIGQFIENVVGTARYPCQQGCNGLYLDHYRSYVH GSGKVDVLIEKFQTRLPKLKDIILTWSYCKKCGTSTPILQISEKTWNHSFGKYLEVMFWS YKDSVTGIGKCPHDFTKDHVKYFGYNDLVVRLEYSDLEVHELITPPRKIKWKPHIDIKLK VELYYKILEKINNFYGSVLSRLERIKLDSMTKDKVLSGQAKIIELKSNATEEQKLMLQDL DTFYADSPCDQHLPLNLVIKSLYDKAVNWNSTFAIFAKSYLPSETDISRITAKQLKKLFY DSSRKDSEDKKSLHDEKAKTRKPEKNELPLEGLKDVEKPKIDSKNTTENRDRTNEPQNAV TITTFKDDTPIIPTSGTSHLTVTPSASSVSSSLTPQTEERPPISRSGTGISMTHDKSTRP NIRKMSSDSSLCGLASLANEYSKNNKVSKLATFFDQMHFDALSKEFELERERERLQLNKD KYQAIRLQTSTPIVEIYKNVKDAVDEPLHSRSSGNNLSSANVKTLEAPVGEHSRANNCNP PNLDQNLETELENSISQWGENILNPSGKTTASTHLNSKPVVKETSENPKSIVRESDNSKS EPLPPVITTTTVNKVESTPQPEKSLLMKTLSNFWADRSAYLWKPLVYPTCPSEHIFTDSD VIIREDEPSSLIAFCLSTSDYRNKMMNLNVQQQQQQQTAEAAPAKTGGNSGGTTQTGDPS VNISPSVSTTSHNKGRDSEISSLVTTKEGLLNTPPIEGARDRTPQESQTHSQANLDTLQE LEKIMTKKTATHLRYQFEEGLTVMSCKIFFTEHFDVFRKICDCQENFIQSLSRCVKWDSN GGKSGSGFLKTLDDRFIIKELSHAELEAFIKFAPSYFEYMAQAMFHDLPTTLAKVFGFYQ IQVKSSISSSKSYKMDVIIMENLFYEKKTTRIFDLKGSMRNRHVEQTGKANEVLLDENMV EYIYESPIHVREYDKKLLRASVWNDTLFLAKMNVMDYSLVIGIDNEGYTLTVGIIDFIRT FTWDKKLESWVKEKGLVGGASVIKQPTVVTPRQYKKRFREAMERYILMVPDPWYREGN Q07897 D6VY05 CMS1_YEAST Protein CMS1 Complementation of MCM10 suppressor protein 1 CMS1 YLR003C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] May play a role in the regulation of DNA replication and cell cycle control. Nucleus Present with 1200 molecules/cell in log phase SD medium. Belongs to the CMS1 family. Complete proteome Nucleus Phosphoprotein Reference proteome MSNPDDLDDGLAYDFDAEHEVIFDAKDGSPPTKKVQKRSIEQDDDDVDDIDGKKEERNSE DDSNRPISKRQKKLQKKSKLIEKKKEESQYIVSQRKALPASSPEKIIEYLTTLIREKNPD LSVLELEELYFKRNDFLSTEKFDAERRLSNFPAFIQKFSVAPKKIVFSMSNIRVADVYRS LNGGKNCVKLFSKSKLKDDIATVERLLTDSSKKSNKNKDSLYFIATPTRMQKIIEATDLL FQGKEKLDIILDASYLDPKDNTILSFENAAVLCQVLKTFLNKKSSVKILLY P18238 D6VQ85 ADT3_YEAST ADP,ATP carrier protein 3 ADP/ATP translocase 3 Adenine nucleotide translocator 3 ANT 3 AAC3 YBR085W YBR0753 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 3-307 IN COMPLEX WITH CARBOXYATRACTYLOSIDE TOPOLOGY Catalyzes the exchange of ADP and ATP across the mitochondrial inner membrane. Homodimer. false 2 Mitochondrion inner membrane Multi-pass membrane protein The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. At least 2 of the odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue. Present with 1080 molecules/cell in log phase SD medium. Belongs to the mitochondrial carrier (TC 2.A.29) family. 3D-structure Complete proteome Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Repeat Transmembrane Transmembrane helix Transport MSSDAKQQETNFAINFLMGGVSAAIAKTAASPIERVKILIQNQDEMIKQGTLDKKYSGIV DCFKRTAKQEGLISFWRGNTANVIRYFPTQALNFAFKDKIKLMFGFKKEEGYGKWFAGNL ASGGAAGALSLLFVYSLDFARTRLAADAKSSKKGGARQFNGLTDVYKKTLKSDGIAGLYR GFMPSVVGIVVYRGLYFGMFDSLKPLVLTGSLDGSFLASFLLGWVVTTGASTCSYPLDTV RRRMMMTSGQAVKYNGAIDCLKKIVASEGVGSLFKGCGANILRSVAGAGVISMYDQLQMI LFGKKFK P38246 D6VQ75 ECM8_YEAST Protein ECM8 Extracellular mutant protein 8 ECM8 YBR076W YBR0722 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION SEQUENCE REVISION TO 74 AND 353 ATCC 204508 / S288c IDENTIFICATION May be involved in cell wall organization and biogenesis. Cell wall biogenesis/degradation Complete proteome Reference proteome MDYGYFFPAQRIEETNGVDFWIDSNAEFTQSKRPDSSTSTLSRVLTDTTNVSNNSGSLKR KTIKNKIFPQRKIFNDSENFDFGKANTDCKHVFKSISKQLIFLPRCFQHHSIRGWMKDRY SEFGYKIKRNQNCPPSACVQALYNTSRSNTEESNPNSLDSLIMYKYMRYSEKKKELMCRF CQGNNWILAENYLKHLFFAHGILSEFKPHTLYHFESKLLKIQGKLNFKIQVLKEPEFSKK ILNSLTVSIIPSPLAYYTQTLNGGFRRIHVKCPHCENWIRLGWCEYDEIIRDSFQDFESL RNLNADYNGMSYIQTRNREDIEGIYENYFTHYIQCDLATFRTKCLYVQVITKSN Q03214 D6VZZ9 ECM5_YEAST Protein ECM5 Extracellular matrix protein 5 ECM5 YMR176W YM8010.06 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] May be involved in cell wall organization and biogenesis. P32561 RPD3 false 5 Nucleus Present with 259 molecules/cell in log phase SD medium. Cell wall biogenesis/degradation Complete proteome Metal-binding Nucleus Reference proteome Zinc Zinc-finger MSGHDSVTKISHILNEPVNEKVMVQNGFHESSKIADIELEIQERPSIKQWESPRSAVIPT SNHNFSPFLYTQFKSRGAAPFAPETIKSVDLVELPEGVPARVFHEKTGLFYQISPHSIPT FILAKKELPDPIKFYELVEDLGSVYGCVKLKIIPDADKFTQLNVDVDRLWFKARKQFFNS NEFQRTKIVDFYAKLYNFHNKIKKSTLTRIPSIDKRTLDLYRLRSCVKLRGGFNAVCEKK LWAQIGRELGYSGRIMSSLSTSLRSAYAKILLDFDIYEEEEQAARNNEKNEDMVESEIFR HSNSRSRDEEEPLHKKAKIHRDVFRAGSINHEFKRMRDIKHIKGFPTYFNSLTEFKLGYT QSTETTLPGYDFTFWENGMEIYDKSKYETKTSPVYNLRQYYEKSLAVFTAIVAKFGSSYP DLFAKHTTLPQKEFERLYFHLLSEHFIDFEIDTGLGLPCSMRSPGNNSSNEKFAIKNILD QWNLDNIPLNELSLLQHLDLDMANFTRTTYDIGMLFSCQGWSVSDHFLPSIDFNHLGSTK LVYSIAPKDMEKFEALIARGKSEWDTIQSRPRYSTSDDELKSFIETDFYKSFLDAEQSAD YSNTGDNSKNSFPEDKIAGNTLHDGSQSDFIFEPNFILANGIKLYKTTQEQGSYIFKFPK AFTCSIGSGFYLSQNAKFAPSSWLRFSSEAAKWTSKMGFLPGLDVNQLLINALLNSNNPV LRKKCRDLISNYVVEEAENSKKLGELIGTVDVVYNKLNYISDISLESTGLSKIVVTHGAL QRNLSLKEFVVLLEKPENGAHSICGIPIRDQSGNLNVCLHSYFDSASLGIALDGLDKPPT SYLLVHNEDFEKKWDVLMTSTFRNRTVPLNIIQYLISHTDSNTEFNRMLRSNFDDSLLLI EKCKKFIKTFVDVSCSVKDVDFGNGFNLRHLPLKFSDNMADNLESLYESVRKCSIEFSEK PTIIRLYHVSRQFPIDNRDIIDGNNLDLLKELYQKSLTIPLKVSYWTKLTRKICRLEWLS VYEHIFIERCDIKNEDPAKYSLPLLYSYFEFGLKYCDSEDIDKLGEVRKLILKYQDMMQK VRVFLKKDPPSKISLSDLEDVLLDIEEYRLPIQSSFFSELDYVIREIENAKKMNDVNILY NTDNIDKIDELIRKNDPKFVKFANQFNGSRLDKRPLASDNSGSVKAKQELKVFKLWNQHL DQIMQKNKFIEILPSIFRCLDLKSDKYIPLESCSKRQTKYCFCRRVEEGTAMVECEICKE WYHVDCISNGELVPPDDPNVLFVCSICTPPCMAVDNIEGVTFELDDLKRILVESLKLSLI PDPPILKNLFDVFAFALNFKNEMEKELFTNGYVNQLSSTHKIKYYLRKLKGSQCGFTNLT DPLRKHCQVKDAEAIKWLTDNGRIIITGIPN P36041 D6VWZ9 EAP1_YEAST Protein EAP1 eIF4E-associated protein 1 EAP1 YKL204W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION FUNCTION INTERACTION WITH EIF4E MUTAGENESIS OF TYR-109 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION MUTAGENESIS OF TYR-109 AND LEU-114 INTERACTION WITH SMY2 AND SYH1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-281; SER-282; SER-327; SER-344 AND SER-387 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-327 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Can regulate translation through binding to eIF4E. Competes with eIF4G and p20 for binding to eIF4E in vivo and inhibits cap-dependent translation in vitro. Plays a role in cell growth and is implicated in the TOR signaling cascade. Functions independently of eIF4E to maintain genetic stability and to attenuate GCN4 translation upon TOR inactivation. Interacts with SMY2, SYH1 and eIF4E. Cytoplasm Present with 3240 molecules/cell in log phase SD medium. 3D-structure ATP-binding Complete proteome Cytoplasm Growth regulation Nucleotide-binding Phosphoprotein Reference proteome Translation regulation Y A L A MELNDPSIISSSQFSGELSDSDTAAATHKSQQAISNLFQKLAKKGREEKPIGSVESSTDS SNISVATSGNNKESNKKKNKKTAMLNFSSLTDPITNYKPMDLQYKTYAYSMNELYHLKPS LASASYEEDPLISELVRSLPKRKFWRLRMGPPDQKHANNHHFNGNNGGGSWKAGYKNGKN DERRMSRTKNMQGGKRRSQQDDEEKKIDQEMLEMDKNLQLGGDVGHSIADFEDWKAKMKE LELKKLSKSKGISNSTAIAPRESASHETPTDLRPVIPRGPSSITDFLNLKRQDKKEESSQ QTPGIPVGQPSLSKTSIEQVNELETNSDLGKSSSSRFSSFFNKSATSLPSLDNNNQVPSS NVSVVNNDGNSTPHQSGSRLMSFFKESRSSTPNAESQLLSASDKDNGKMQTLPQFQQQPQ QMQPMAFTQHPPNNNAFFNGLLNKGKSETSTPPPPPPGLIAHQGPQFPVMGVPPNFPQRM MPPPPGLVQFQKDSKDVNKKEDRQLRQNKNPNGTRNSKGKQEETATPDLPQQQYMPPPPP PGFFPMHPNFPNGPMPPLPQGFPIPPNGMLPVTGQQPQPPYPNMMLQGNFPPNFQQGFGS NSPMPIPSIINANGKNVTNQLPPGLNSKKNIK P38332 D6VQP2 DPH7_YEAST Diphthine methyltransferase 3.1.1.97 Diphthamide biosynthesis protein 7 Endosomal recycling protein 1 Regulator of rDNA transcription protein 2 RRT2 DPH7 ERE1 YBR246W YBR1634 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] GENE NAME FUNCTION FUNCTION FUNCTION SUBCELLULAR LOCATION INTERACTION WITH CAN1 AND RRT10 FUNCTION FUNCTION DISRUPTION PHENOTYPE FUNCTION CATALYTIC ACTIVITY Catalyzes the demethylation of diphthine methyl ester to form diphthine, an intermediate in diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EFT1 and EFT2). Also plays a role in the regulation of the retromer complex and is required for the recycling from endosomes of plasma membrane proteins like CAN1 and MUP1. Identified in a screen for mutants with decreased levels of rDNA transcription. diphthine methyl ester-[translation elongation factor 2] + H2O = diphthine-[translation elongation factor 2] + H(+) + methanol Protein modification; peptidyl-diphthamide biosynthesis. Interacts with CAN1 and RTT10. Cytoplasm Endosome Recruited to endosomes in cells in which increased recycling of internalized plasma membrane proteins occurs. Accumulates diphthine, the last intermediate in the diphthamide biosynthesis pathway. Increases the interaction of DPH5 with elongation factor 2. Present with 2640 molecules/cell in log phase SD medium. Belongs to the DPH7 family. Was originally (PubMed:19965467) thought to be required for the first step of diphthamide biosynthesis but further studies (PubMed:22188241, PubMed:23468660) clearly suggest that it is involved in the third step of diphthamide biosynthesis. Complete proteome Cytoplasm Endosome Hydrolase Reference proteome Repeat WD repeat MDSIQESDVLNAVKTKLPPCCLRIFRNKIILVGTYDLDKSTGYRSGSLDVFTMDLKLLCS NNTYGAILDLKLSPFDDTLICTAHSTGNIMLWRIRCTDKDDFQSNELDIHAIANLQLFEK DVLIASCHFSPLDCKKLLVTNTAGEAATIDIRTLSVQFTASAIAQAYSKLDKIDYEVQGA TEKVIHVESGQFLKPHELECWTAEFGSLQPFQDVVFTGGDDSRIMAHDLRSKEFIWSNNR IHDAGVVSIKCSQPNFRNNKPTSIITGSYDDNIRSLDLRMMGESIFPGANVPTVNKLACD LGGGVWRFVESPIDQEQSHHNGSDRLLVCCMYNGAKVVTMNDNSDEYFQIQHYLKKGHDS MCYGGDWSNSLIATCSFYDNSLQTWIV P38682 D3DM28 GLO3_YEAST ADP-ribosylation factor GTPase-activating protein GLO3 ARF GAP GLO3 GLO3 YER122C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] YAL6B PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-398 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-306; SER-389 AND SER-398 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] GTPase-activating protein for the ADP ribosylation factor (ARF) family. Involved in retrograde vesicular transport from the Golgi to the endoplasmic reticulum. Golgi apparatus Present with 1510 molecules/cell in log phase SD medium. Complete proteome Golgi apparatus GTPase activation Metal-binding Phosphoprotein Protein transport Reference proteome Transport Zinc Zinc-finger S C EAHDKLKTFDNATSISSSSYFGEDKEVDEFGNPINSSGSGAGNFDGRNSNNGFIDFNASADDELQMLRDVVEQGAEKLGSYLRDYLRK GSA MSNDEGETFATEQTTQQVFQKLGSNMENRVCFDCGNKNPTWTSVPFGVMLCIQCSAVHRN MGVHITFVKSSTLDKWTINNLRRFKLGGNHKARDFFLKNNGKQLLNTANVDAKTKYTSPV AKKYKIHLDKKVQKDMELYPSELVLNGQDSSDSPLDTDSDASRSTSKENSVDDFFSNWQK PSSNSSSKLNVNTGSLAPKNNTTGSTPKTTVTKTRSSILTASRKKPVLNSQDKKKHSILS SSRKPTRLTAKKVDKSQAEDLFDQFKKEAQQEKEDEFTNSSSSTKIRQNDYDSQFMNNSK GNNNNSIDDINTQPDEFNDFLNDTSNSFDTTRKEQQDTLTPKFAKLGFGMTMNDANDLAK QQKESQKIAQGPRYTGRIAERYGTQKAISSDQLFGRGSFDEAANREAHDKLKTFDNATSI SSSSYFGEDKEVDEFGNPINSSGSGAGNFDGRNSNNGFIDFNASADDELQMLRDVVEQGA EKLGSYLRDYLRK Q01217 D3DLX4 ARG56_YEAST Protein ARG5,6, mitochondrial N-acetyl-gamma-glutamyl-phosphate reductase 1.2.1.38 N-acetyl-glutamate semialdehyde dehydrogenase NAGSA dehydrogenase Acetylglutamate kinase 2.7.2.8 N-acetyl-L-glutamate 5-phosphotransferase NAG kinase AGK ARG5,6 YER069W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] Sigma 1278B NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEOLYTIC PROCESSING LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate The kinase activity is inhibited by arginine. Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. Mitochondrion The protein precursor is cleaved into the two biologically active enzymes, the kinase and the reductase. Present with 1180 molecules/cell in log phase SD medium. In the N-terminal section; belongs to the acetylglutamate kinase family. In the C-terminal section; belongs to the NAGSA dehydrogenase family. 3D-structure Amino-acid biosynthesis Arginine biosynthesis ATP-binding Complete proteome Kinase Mitochondrion Multifunctional enzyme NADP Nucleotide-binding Oxidoreductase Phosphoprotein Reference proteome Transferase Transit peptide MPSASLLVSTKRLNASKFQKFVSSLNKSTIAGFASVPLRAPPSVAFTRKKVGYSKRYVSS TNGFSATRSTVIQLLNNISTKREVEQYLKYFTSVSQQQFAVIKVGGAIISDNLHELASCL AFLYHVGLYPIVLHGTGPQVNGRLEAQGIEPDYIDGIRITDEHTMAVVRKCFLEQNLKLV TALEQLGVRARPITSGVFTADYLDKDKYKLVGNIKSVTKEPIEASIKAGALPILTSLAET ASGQMLNVNADVAAGELARVFEPLKIVYLNEKGGIINGSTGEKISMINLDEEYDDLMKQS WVKYGTKLKIREIKELLDYLPRSSSVAIINVQDLQKELFTDSGAGTMIRRGYKLVKRSSI GEFPSADALRKALQRDAGISSGKESVASYLRYLENSDFVSYADEPLEAVAIVKKDTNVPT LDKFVCSDAAWLNNVTDNVFNVLRRDFPALQWVVSENDANIAWHFDKSQGSYLKGGKVLF WYGIDDINTISELVENFVKSCDTASTLNSSASSGVFANKKSARSYSTRSTPRPEGVNTNP GRVALIGARGYTGKNLVSLINGHPYLEVAHVSSRELKGQKLQDYTKSEIIYESLQIQDIR KLEEQNAVDFWVMALPNKVCEPFVETIQSVHGKSKIIDLSADHRFVSESDWAYGLPELND RAKIANAAKIANPGCYATGSQLTISPLTKYINGLPTVFGVSGYSGAGTKPSPKNDPKFLN NNLIPYALSDHIHEREISARIGHNVAFMPHVGQWFQGISLTVSIPIKKGSLSIDEIRKLY RNFYEDEKLVHVIDDIPLVKDIEGTHGVVIGGFKLNDAEDRVVVCATIDNLLKGAATQCL QNINLAMGYGEYAGIPENKIIGV P32459 D6VVW3 ALLA_YEAST Ureidoglycolate lyase 4.3.2.3 Degradation of allantoin protein 3 Ureidoglycolatase Ureidoglycolate hydrolase DAL3 YIR032C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c BIOPHYSICOCHEMICAL PROPERTIES FUNCTION CATALYTIC ACTIVITY INDUCTION Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as secondary nitrogen source when primary sources are limiting. (S)-ureidoglycolate = glyoxylate + urea Optimum pH is 7.3. Nitrogen metabolism; (S)-allantoin degradation. Homodimer. Subject to nitrogen catabolite repression. Belongs to the ureidoglycolate lyase family. This enzyme was also named ureidoglycolate hydrolase in the literature. However, this is the recommended name of another enzyme (EC 3.5.1.116) acting on ureidoglycolate. To make the distinction between ammonia- or urea-releasing activities from ureidoglycolate, the use of this ambiguous name is deprecated. Complete proteome Lyase Purine metabolism Reference proteome MVTVVAETLTKESFEEYGTIISPDEEISRMQNLEKGANQGTAIKLLQVSQVENKSTSKVP NWNLFRCFPQPHLNRVFTQGSNQAISHSIKVLEKHPCSTQTFVPMGRTSAEVAYLVVVAK EIGNKPDLSTLRAFTCLGNQAVTYGLGTWHAPMIVLGKEEHLDFSVLIYESLDPDRPEKD CVEEHYSDGDVCIII P53959 D6W1D8 COG6_YEAST Conserved oligomeric Golgi complex subunit 6 COG complex subunit 6 Complexed with DOR1 protein 2 Component of oligomeric Golgi complex 6 Protein SEC37 COG6 COD2 SEC37 TFI2 YNL041C N2675 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBUNIT IDENTIFICATION IN THE COG COMPLEX FUNCTION OF THE COG COMPLEX FUNCTION IDENTIFICATION IN THE COG COMPLEX LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] COMPOSITION OF THE COG COMPLEX INTERACTION WITH COG3 AND COG4 Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events. Component of the conserved oligomeric Golgi (COG or Sec34/Sec35) complex which consists of eight different proteins COG1-COG8. P53079 COG1 false 5 P53271 COG2 false 3 P40094 COG3 false 3 P53951 COG5 false 2 P53195 COG7 false 3 Q04632 COG8 false 5 Golgi apparatus membrane Peripheral membrane protein Present with 1720 molecules/cell in log phase SD medium. Belongs to the COG6 family. Complete proteome Golgi apparatus Membrane Protein transport Reference proteome Transport MDFVVDYQTYAMADTATPELPEPEPRLNLTSDAQSQPTGKLDLQFKLPDLQRYSNNNATL PVDNDGAGSKDLHKKMTHYAMSSIDKIQLSNPSKQLGQNSQDEKLSQQESQNFTNYEPKN LDLSKLVSPSSGSNKNTTNLVLSNKLSKILNNYTLINYQATVQLRKSLKVLEENKERLSL DEQKLMNPEYVGTLARRALRTDLESQLLKEHITVLEEFKPIIRRIKRLSSSVEKIQRTSE KLLSNETNEVPTNNVVLQEIDQYRLKAEQLKLKKKILLSIRDRFTLNQVEDDVITNGTID NIFFEVVKKVINIKDESSFLLTLPNLNAGNALIMGVNEILEKTNKKIFNYLIDFLYSFES SSNLLNDHGTTEQESLNIFRKSLVFLSSDLELFNELLKRVTTLRSKSILDEFLSQFDMNS TTSKPIILSAHDPIRYIGDVLASVHSIIANEADFVKSLFDFQDEDLKDTPISILQQNKTF LKGIDNKLLNDIIQSLSNSCRIRIEQIVRFEENPIINFEIVRLLKLYRVMFERKGIQDDS SIINNLKSLEDISKNRIIGYYEDYMKQTVMAETKNSSDDLLPPEWLSEYMNKLVELFEIY EKTHAAEDEESEDNKLLSSKNLQTIVEQPIKDVLLKQLQTSFPLAKKNEKEKASLLTIEI NCFDLIKSRLQPFEGLFAQDDDSRKITIWVCDKLKEYTKQMLTLQIKFLFENTGLDLYSN LVNMIFPVDSVKDELDYDMYLALRDNSLMELDMVRKNVHDKLNYYLPQALTDVQGNLLFK LTSPMIADEICDECFKKLSLFYNIFRKLLIHLYPNKKDQVFEILNFSTDEFDMLIGIDH P38077 D6VQ39 Q54AF5 Q76MT6 ATPG_YEAST ATP synthase subunit gamma, mitochondrial F-ATPase gamma subunit ATP3 ATP3a ATP3b YBR039W YBR0408 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 34-61; 77-86; 195-207; 220-240 AND 284-290 MUTAGENESIS OF ALA-273 ATCC 201238 / W303-1B D273-10B/A1 NUCLEOTIDE SEQUENCE [GENOMIC DNA] MUTAGENESIS OF THR-297 AND ILE-303 NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES ATP3A AND ATP3B) ATCC 64665 / S288c / DC5 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] 3D-STRUCTURE MODELING X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 34-311 X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) OF 34-311 Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Mitochondrion Mitochondrion inner membrane Peripheral membrane protein Present with 28100 molecules/cell in log phase SD medium. PubMed:12898710 reports two tandemly repeated copies of ATP3 (ATP3a and ATP3b) on the right arm of chromosome II in several laboratory strains, including S288c. This has not been confirmed by the yeast genome sequencing project. Belongs to the ATPase gamma chain family. 3D-structure ATP synthesis CF(1) Complete proteome Direct protein sequencing Hydrogen ion transport Ion transport Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Transit peptide Transport S I S F A V T A I T MLSRIVSNNATRSVMCHQAQVGILYKTNPVRTYATLKEVEMRLKSIKNIEKITKTMKIVA STRLSKAEKAKISAKKMDEAEQLFYKNAETKNLDVEATETGAPKELIVAITSDKGLCGSI HSQLAKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLSINGIGKDAPTFQESALIA DKLLSVMKAGTYPKISIFYNDPVSSLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPR DLFEYTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMINRYSILYNRTRQAVITNEL VDIITGASSLG P40047 D3DLX8 ALDH5_YEAST Aldehyde dehydrogenase 5, mitochondrial 1.2.1.5 ALD5 ALD3 ALDH5 YER073W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION SEQUENCE REVISION TO 411 ATCC 204508 / S288c CHARACTERIZATION BIOPHYSICOCHEMICAL PROPERTIES SUBCELLULAR LOCATION FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 FUNCTION Minor mitochondrial aldehyde dehydrogenase isoform. Plays a role in regulation or biosynthesis of electron transport chain components. Involved in the biosynthesis of acetate during anaerobic growth on glucose. an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Induced by potassium ions. 0.64 mM for NADP (with acetaldehyde as cosubstrate) 3.47 mM for NADP (with propionaldehyde as cosubstrate) 6.43 mM for NAD (with propionaldehyde as cosubstrate) 0.058 mM for acetaldehyde (with NADP as cosubstrate) 0.39 mM for propionaldehyde (with NADP as cosubstrate) 0.83 mM for propionaldehyde (with NAD as cosubstrate) 1.1 umol/min/mg enzyme with acetaldehyde and NADP as substrates 0.45 umol/min/mg enzyme with propionaldehyde and NADP as substrates 0.011 umol/min/mg enzyme with propionaldehyde and NAD as substrates Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. Mitochondrion matrix Present with 23300 molecules/cell in log phase SD medium. Belongs to the aldehyde dehydrogenase family. Complete proteome Mitochondrion NAD NADP Oxidoreductase Reference proteome Transit peptide I T A L AFETKWSIVEPE LLKRSVYCRAG E G MLSRTRAAAPNSRIFTRSLLRLYSQAPLRVPITLPNGFTYEQPTGLFINGEFVASKQKKT FDVINPSNEEKITTVYKAMEDDVDEAVAAAKKAFETKWSIVEPEVRAKALFNLADLVEKH QETLAAIESMDNGKSLFCARGDVALVSKYLRSCGGWADKIYGNVIDTGKNHFTYSIKEPL GVCGQIIPWNFPLLMWSWKIGPALATGNTVVLKPAETTPLSALFASQLCQEAGIPAGVVN ILPGSGRVVGERLSAHPDVKKIAFTGSTATGRHIMKVAADTVKKVTLELGGKSPNIVFAD ADLDKAVKNIAFGIFYNSGEVCCAGSRIYIQDTVYEEVLQKLKDYTESLKVGDPFDEEVF QGAQTSDKQLHKILDYVDVAKSEGARLVTGGARHGSKGYFVKPTVFADVKEDMRIVKEEV FGPIVTVSKFSTVDEVIAMANDSQYGLAAGIHTNDINKAVDVSKRVKAGTVWINTYNNFH QNVPFGGFGQSGIGREMGEAALSNYTQTKSVRIAIDKPIR Q01802 D6VXI2 AATM_YEAST Aspartate aminotransferase, mitochondrial 2.6.1.1 Transaminase A AAT1 YKL106W YKL461 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ENZYME ACTIVITY NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol (By similarity). 2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate pyridoxal 5'-phosphate Homodimer. Mitochondrion matrix In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes. Present with 2910 molecules/cell in log phase SD medium. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Aminotransferase Complete proteome Mitochondrion Pyridoxal phosphate Reference proteome Transferase Transit peptide V A Y S MLRTRLTNCSLWRPYYTSSLSRVPRAPPDKVLGLSEHFKKVKNVNKIDLTVGIYKDGWGK VTTFPSVAKAQKLIESHLELNKNLSYLPITGSKEFQENVMKFLFKESCPQFGPFYLAHDR ISFVQTLSGTGALAVAAKFLALFISRDIWIPDPSWANHKNIFQNNGFENIYRYSYYKDGQ IDIDGWIEQLKTFAYNNQQENNKNPPCIILHACCHNPTGLDPTKEQWEKIIDTIYELKMV PIVDMAYQGLESGNLLKDAYLLRLCLNVNKYPNWSNGIFLCQSFAKNMGLYGERVGSLSV ITPATANNGKFNPLQQKNSLQQNIDSQLKKIVRGMYSSPPGYGSRVVNVVLSDFKLKQQW FKDVDFMVQRLHHVRQEMFDRLGWPDLVNFAQQHGMFYYTRFSPKQVEILRNNYFVYLTG DGRLSLSGVNDSNVDYLCESLEAVSKMDKLA P80235 D6VPN4 CACM_YEAST Putative mitochondrial carnitine O-acetyltransferase 2.3.1.7 YAT1 YAR035W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] DL-1 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 Involved in the transfer of acetyl-CoA into mitochondria. May also be involved in the metabolism of acetate and of ethanol. (R)-carnitine + acetyl-CoA = CoA + O-acetyl-(R)-carnitine Mitochondrion inner membrane Peripheral membrane protein Intermembrane side By ethanol and by acetate. Repressed by glucose, and to a lesser extent, by galactose. Derepressed by glycerol. Belongs to the carnitine/choline acetyltransferase family. Acyltransferase Complete proteome Fatty acid metabolism Lipid metabolism Membrane Mitochondrion Mitochondrion inner membrane Phosphoprotein Reference proteome Transferase Transport P T S SS SF AS A T T A MPNLKRLPIPPLQDTLNRYLARVEPLQDERQNRRTRRTVLSAENLDALNTLHERLLEYDA RLAESNPESSYIEQFWYDAYLLYDATVVLNVNPYFQLQDDPTIKDTPETAAQGPYGAHTV QVRRAARLTTSILKFIRQIRHGTLRTDTVRGKTPLSMDQYERLFGSSRIPPGPGEPSCHL QTDATSHHVVAMYRGQFYWFDVLDTRNEPIFATPEQLEWNLYSIIMDAESAGSGSAPFGV FTTESRRVWSNIRDYLFHADDCTNWRNLKLIDSALFVVCLDDVAFAADQQDELTRSMLCG TSTINLDPHQHQPPLNVQTGTCLNRWYDKLQLIVTKNGKAGINFEHTGVDGHTVLRLATD IYTDSILSFARGVTKNVVDIFSDDDGKPSSSSLASAAHSANLITIPRKLEWRTDNFLQSS LHFAETRISDLISQYEFVNLDFSNYGASHIKTVFKCSPDAFVQQVFQVAYFALYGRFETV YEPAMTKAFQNGRTEAIRSVTGQSKLFVKSLLDQDASDATKIQLLHDACTAHSQITRECS QGLGQDRHLYALYCLWNQWYKDKLELPPIFRDKSWTTMQNNVLSTSNCGNPCLKSFGFGP VTANGFGIGYIIRDHSVSVVVSSRHRQTARFASLMEKSLLEIDRIFKRQQARAAKPAART TASANTKSEDMKYLLSGYDYFDVSVSG Q01532 D6W0V4 BLH1_YEAST Cysteine proteinase 1, mitochondrial 3.4.22.40 Bleomycin hydrolase BLM hydrolase Homocysteine-thiolactonase HTLase Hcy-thiolactonase Leucine aminopeptidase 3 Y3 LAP3 BLH1 GAL6 YCP1 YNL239W N1118 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] BIOPHYSICOCHEMICAL PROPERTIES ACTIVITY REGULATION NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 228-250 AND 367-387 NUCLEOTIDE SEQUENCE [GENOMIC DNA] BIOPHYSICOCHEMICAL PROPERTIES ACTIVITY REGULATION NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58 MASS SPECTROMETRY MUTAGENESIS OF CYS-102 AND 271-LYS--LYS-274 PROTEIN SEQUENCE OF 228-251 AND 367-387 PROTEIN SEQUENCE OF C-TERMINUS X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 30-483 SUBUNIT DNA-BINDING BIOPHYSICOCHEMICAL PROPERTIES DNA-BINDING SUBCELLULAR LOCATION FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 FUNCTION MUTAGENESIS OF HIS-398 ALTERNATIVE INITIATION IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 30-483 OF MUTANT ALA-102 MUTAGENESIS OF GLY-479 The normal physiological role of the enzyme is unknown, but it is not essential for the viability of yeast cells. Has aminopeptidase activity, shortening substrate peptides sequentially by 1 amino acid. Has bleomycin hydrolase activity, which can protect the cell from the toxic effects of bleomycin. Has homocysteine-thiolactonase activity, protecting the cell against homocysteine toxicity. Acts as a repressor in the GAL4 regulatory system, but this does not require either the peptidase or nucleic acid-binding activities. Inactivates bleomycin B2 (a cytotoxic glycometallopeptide) by hydrolysis of a carboxyamide bond of beta-aminoalanine, but also shows general aminopeptidase activity. The specificity varies somewhat with source, but amino acid arylamides of Met, Leu and Ala are preferred. Inhibited by E64, a specific inhibitor of cysteine proteases, N-ethylmaleimide, iodacetamide, and mercury and zinc ions. 12.8 uM for arginine-4-methyl-7-coumarylamide 0.33 mM for glutamine-beta-naphthylamide 228 uM for lysine-4-methyl-7-coumarylamide 2.56 umol/h/mg enzyme for arginine-4-methyl-7-coumarylamide 370 nmol/min/mg enzyme for glutamine-beta-naphthylamide N-terminal acetylation of lysine-4-methyl-7-coumarylamide (Ac-Lys-AMC) reduces the catalytic efficiency 50-fold towards this substrate. Optimum pH is 7.5. Homohexamer. Binds to nucleic acids. Binds single-stranded DNA and RNA with higher affinity than double-stranded DNA. Isoform Cytoplasmic Cytoplasm Isoform Mitochondrial Mitochondrion Q01532-1 Mitochondrial Q01532-2 Cytoplasmic Produced by alternative initiation at Met-30 of isoform Mitochondrial. The N-terminus of isoform Cytoplasmic is blocked. Present with 521 molecules/cell in log phase SD medium. Belongs to the peptidase C1 family. 3D-structure Alternative initiation Complete proteome Cytoplasm Direct protein sequencing DNA-binding Hydrolase Mitochondrion Protease Reference proteome Thiol protease Transit peptide C A KDKK ADAA H A G A I M MLPTSVSRSLYLKTFRSHLLRAPQIVLKRMSSSIDISKINSWNKEFQSDLTHQLATTVLK NYNADDALLNKTRLQKQDNRVFNTVVSTDSTPVTNQKSSGRCWLFAATNQLRLNVLSELN LKEFELSQAYLFFYDKLEKANYFLDQIVSSADQDIDSRLVQYLLAAPTEDGGQYSMFLNL VKKYGLIPKDLYGDLPYSTTASRKWNSLLTTKLREFAETLRTALKERSADDSIIVTLREQ MQREIFRLMSLFMDIPPVQPNEQFTWEYVDKDKKIHTIKSTPLEFASKYAKLDPSTPVSL INDPRHPYGKLIKIDRLGNVLGGDAVIYLNVDNETLSKLVVKRLQNNKAVFFGSHTPKFM DKKTGVMDIELWNYPAIGYNLPQQKASRIRYHESLMTHAMLITGCHVDETSKLPLRYRVE NSWGKDSGKDGLYVMTQKYFEEYCFQIVVDINELPKELASKFTSGKEEPIVLPIWDPMGA LAK P38731 D3DKS9 ARN1_YEAST Siderophore iron transporter ARN1 Ferrichrome permease ARN1 YHL040C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A Involved in the transport of siderophore ferrichrome and so has a role in iron homeostasis. Cell membrane Multi-pass membrane protein Endosome membrane Multi-pass membrane protein Belongs to the major facilitator superfamily. Cell membrane Complete proteome Endosome Ion transport Iron Iron transport Membrane Reference proteome Transmembrane Transmembrane helix Transport MESVHSRDPVKEEKKHVFMGMEHELNPETHNDSNSDSYGLPQLSEKYNALRQNRSLIIQQ TEIIGSAYNKWYLQAILLLSAFICGYGYGLDGNIRYIYTGYATSSYSEHSLLSTINVINA VVSAASQIIYARLSDVFGRLYLFISAVILYVVGTIIQSQAYDVQRYAAGAIFYNAGYVGV ILILLIILSDFSSLKWRLLYQFVPTWPFIINTWIAGNITSRANPVVNWSWDVGMWAFIFP LSCVPIVLCMLHMQWRARKTPEWHALKGQKSYYQEHGFIKILKQLFWMLDVVGVLLMGCS LGCILVPLTLAGGVKTTWNDSRLIGPFVLGFVLIPILWIWEYRFARDPILPYRLVKDRAV WSSMGISFLIDFIYYMAADYLYTVMIVAVNESVKSATRIATLSSFVSTVASPFFALLVTR CTRLKPFIMFGCALWMVAMGLLYHFRGGSQSHSGIIGALCVWGVGTTLFTYPVTVSVQSA VSHENMATVTALNYTLYRIGSAVGSAVSGAIWTQTLYKQILKRMGDVALATTAYESPYTF IETYTWGTPQRNALMNAYKYVQRLETIVALVFCVPLIAFSLCLRDPKLTDTVAVEYIEDG EYVDTKDNDPILDWFEKLPSKFTFKRE Q06697 D6VZ54 CDC73_YEAST Cell division control protein 73 RNA polymerase-associated protein CDC73 CDC73 YLR418C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBUNIT SUBCELLULAR LOCATION SUBUNIT IDENTIFICATION IN THE PAF1 COMPLEX INTERACTION WITH POB3 AND SPT16 FUNCTION SUBCELLULAR LOCATION FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-150 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. Component of the PAF1 complex which consists of at least CDC73, CTR9, LEO1, PAF1 and RTF1. Interacts with FACT subunits POB3 and SPT16. P38351 PAF1 false 8 P04050 RPO21 false 17 P53064 RTF1 false 9 Q00772 SLT2 false 2 P27692 SPT5 false 6 Nucleus Nucleoplasm Belongs to the CDC73 family. 3D-structure Activator Complete proteome Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation MANSLDRLREHLKNGDKLVLKNNEGQSTDDITKATMVETLSSDGSTQDSFPLNEETEIEI DGSLVQLRIIVHCWMNKDSSAADYLADCQNKQLTNVSFLQRTDLINWLSGNTESSQYLKA PGQKGETSDKVDIENKTLAGELSTVKSTTSASLENDSEVSDPVVVETMKHERILVDHNSA LRGAKPINFGYLIKDAELKLVQSIKGSLRGSKLPPGHKGAHGRISKTNGSSGGPRKDPII LIPSAASSILTVANIKQFLLESKYVNPRNLPSVPNGLVNIEKNFERISRPIRFIIVDNTR MFTKPEYWDRVVAIFTTGHTWQFNNYQWNSPQELFQRCKGYYFHFAGDSVPQHVQQWNVE KVELDKNKRFKDVEVVRYFWHSLEKELISRGYR P00830 D6VWU0 ATPB_YEAST ATP synthase subunit beta, mitochondrial 7.1.2.2 ATP2 YJR121W J2041 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ERRATUM SEQUENCE REVISION NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 24657 / D273-10B NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-507 PROTEIN SEQUENCE OF 371-379 AND 390-398 ATCC 38531 / Y41 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-112; THR-237 AND SER-373 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 3D-STRUCTURE MODELING Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. Q02888 INA17 false 2 Mitochondrion Mitochondrion inner membrane Peripheral membrane protein. Present with 164000 molecules/cell in log phase SD medium. Belongs to the ATPase alpha/beta chains family. 3D-structure ATP synthesis ATP-binding CF(1) Complete proteome Direct protein sequencing Hydrogen ion transport Ion transport Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Phosphoprotein Reference proteome Transit peptide Translocase Transport Q M T A REMKET HEMEDS G E FI Y APATT SPSTS TT SS DTVAS RTRCL A R A R A R MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQ SELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPV GRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPY ARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVI NLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSE VSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFA HLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDI IAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEG KYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN P38770 D3DKY3 BRL1_YEAST Nucleus export protein BRL1 BRR6-like protein 1 BRL1 YHR036W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION SUBCELLULAR LOCATION INTERACTION WITH BRR6 TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in mRNA and protein export from nucleus. Interacts with BRR6. Nucleus membrane Multi-pass membrane protein Present with 1280 molecules/cell in log phase SD medium. Belongs to the BRL1/BRR6 family. Complete proteome Membrane mRNA transport Nucleus Protein transport Reference proteome Transmembrane Transmembrane helix Transport MESFENLSIRDSFTSGMEHVDEELGGLSDLSISKQGPTLSPQLINRFMPHFPSSPSPLRN TLDFSAAKADEEEDDRMEIDEVDDTSFEEEYNNEPIETHTEATENAVVEEIEATPEERQK QEKNESQDQSVEEVENIVSPHRSTVIKALLSPTDLGVAAATKVEGVVPLPPSANQDDNES SNNNAEGEDIIRNEEVEDEIKSSLGNHKSSQYANAFDSEIIKRELRSRSKYQPIQVSFNT HNYFYSDKDGIKTYSLTKPNHNKIDEFYDQNEAFKLPKPWSPNSHPASRASYALMSYLQL FLNAITTVVIFSFILSFIIALQKDLKSTWEQRKHELQYESRICQEQYLTNRCNQTPGLPA LGEQCAIWKQCMDRNNDIFFRARSTLSAKLFGDIINSFIDPLNWKTLFVIFCGVITWCFS SNFLLGFVRAKSYYGNGIKTYPLPSSPKSPTSEETHSSMTASGEDSHLLKQ P25300 D6VR48 Q06729 BUD5_YEAST Bud site selection protein 5 BUD5 YCR038C YCR38C YCR526 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c SEQUENCE REVISION TO 110; 401; 481 AND N-TERMINUS GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-642 SP1 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-642 ATCC 96604 / S288c / FY1679 FUNCTION FUNCTION SUBCELLULAR LOCATION FUNCTION INTERACTION WITH GSP1 SUBCELLULAR LOCATION INTERACTION WITH AXL2 SUBCELLULAR LOCATION INTERACTION WITH AXL1 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] GDP-GTP exchange factor (GEF) for the small GTPase BUD1/RSR1. Regulates the activity of BUD1 together with BUD2 which is a GTPase-activating protein (GAP) of BUD1. Required to produce both the axial and bipolar patterns of bud site selection. Determines the orientation of division axis. Overexpression can suppress mutations in PRP20 which is the GEF for GSP1. May be a cytoplasmic GEF for GSP1. Might also act on the Ras-like protein CDC42. Appears to bind to Ras proteins but not to activate them. Interacts with AXL2, BEM1, GSP1 and in haploid cells with AXL1. P38928 AXL2 false 2 P32835 GSP1 false 2 Bud neck Cytoplasm Cell cortex In haploid cells, forms double rings that encircle the mother-bud neck and split upon cytokinesis, each progeny cell inheriting BUD5 at the axial division remnant. In diploid cells, localizes to the poles of the cell. Present with 2110 molecules/cell in log phase SD medium. Complete proteome Cytoplasm Guanine-nucleotide releasing factor Reference proteome R P V D L P S A MSPKNKYVYICVEYIYIYFAKIHKQSTLSSDTTKMFVLIDNVLAYLLEQDDLFVTARFAI QGQIVSRRVNKIHISNITDVLLQQFISHTLPYNDNIVPKKILDSMRTAVRQLLEATACVS RECPLVKRSQDIKRARKRLLSDWYRLGADANMDAVLLVVNSAWRFLAVWRPFVNSIQHAT QELYQNIAHYLLHGNVNIQRVTALIQLVMGQDDLLFSMDDVLQEVFRIQLYLNKMLPHNS HKWQKPSPFDSANLLLNFRDWTTDNALLQELLLSYPTINKNKHKNHSVPRLIQIWVESYW QDSETTLKDILNFWYSHLAEYYEYQELFADIVQLFINKKRTRQLKIHYIGLTDKEIEENK PPLDYENLFLQYEIDKTNANDELCGATDLSDLLFQWKQGELLEVEAFALNVSPWSLAKTL TLLESSLYLDIETIEFTRHFKHNDTTIDSVFTLSNQLSSYVLETTLQQTHTISYWLQVAL SCLYLRNLNSLASIITSLQNHSIERLSLPIDVKSDHLFQRLKVVVHPNNNYNVYRRTIKH IFHSQLPCVPFTSLLIRDITFIRDGNDTFTKDGNNVNMQKFNQITKIVAFAQYLQQKQYE DIHCSNTTARSLLGAMIKVHTLYNDNKDRAYQVSIAKVPRLT P0CX13 D6VQU7 P38363 COS3_YEAST Protein COS3 COS3 YML132W YM4987.03 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A Membrane Multi-pass membrane protein Belongs to the DUP/COS family. Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MKENELKNEKSVDVLSFKQLESQKIVLPQDLFRSSFTWFCYEIYKSLAFRIWMLLWLPLS VWWKLSNNCIYPLIVSLLVLFLGPIFVLVICGLSRKRSLSKQLIQFCKEITENTPSSDPH DWEVVAANLNSYLYENNVWNTKYFFFNAMVCQEAFRTTLLEPFSLKKDKAAKVKSFKDSV PYIEEALGVYFTEVEKQWKLFNTEKSWSPVGLEDAKLPKEAYRFKLTWFLKRISNIFMLI PFLNFLCCIYVSRGMCLLLRTLYLGWILFMLVQGFQNIRVLIMSMEHKMQFLSTIINEQE SGANGWDEIARKMNRYLFEKKAWKNEEFFFDGIDCEWFFNHFFYRVLSAKKSMWPLPLNV ELWPYIKEAQLSRSEVLLV P43568 D6VTK1 CAK1_YEAST Serine/threonine-protein kinase CAK1 2.7.11.22 CDK-activating kinase CAK1 CIV1 YFL029C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] P00546 CDC28 false 3 Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. ATP-binding Complete proteome Kinase Nucleotide-binding Reference proteome Serine/threonine-protein kinase Transferase MKLDSIDITHCQLVKSTRTARIYRSDTYAIKCLALDFDIPPHNAKFEVSILNKLGNKCKH ILPLLESKATDNNDLLLLFPFEEMNLYEFMQMHYKRDRRKKNPYYDLLNPSIPIVADPPV QKYTNQLDVNRYSLSFFRQMVEGIAFLHENKIIHRDIKPQNIMLTNNTSTVSPKLYIIDF GISYDMANNSQTSAEPMDSKVTDISTGIYKAPEVLFGVKCYDGGVDVWSLLIIISQWFQR ETSRMGHVPAMIDDGSDDMNSDGSDFRLICSIFEKLGIPSIQKWEEVAQHGSVDAFVGMF GADGDGKYVLDQEKDVQISIVERNMPRLDEIADVKVKQKFINCILGMVSFSPNERWSCQR ILQELEKP P29465 D6VQ25 CHS3_YEAST Chitin synthase 3 2.4.1.16 Chitin-UDP acetyl-glucosaminyl transferase 3 Class-IV chitin synthase 3 CHS3 CAL1 CSD2 DIT101 KIT2 YBR023C YBR0305 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-1165 FUNCTION FUNCTION FUNCTION SUBCELLULAR LOCATION SUBCELLULAR LOCATION CATALYTIC ACTIVITY GLYCOSYLATION MUTAGENESIS OF SER-991; ARG-993; ARG-994; ARG-995 AND SER-999 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-136 IDENTIFICATION BY MASS SPECTROMETRY SUB592 SUBCELLULAR LOCATION SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A SUBCELLULAR LOCATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND THR-538 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Appears to be responsible for the synthesis of the majority of the chitin found in the cell wall periphery. It is involved in the synthesis of the chitin ring that forms in the cell wall just before bud emergence. This ring remains at the base of the bud as the bud grows and ultimately forms part of the bud scar marking the division site on the mother cell. Also catalyzes the synthesis of chitin laid down during mating and spore cell-wall synthesis. [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP Seems to interact with BNI4 and SKT5 which link CHS3 to septins. Cell membrane Multi-pass membrane protein Bud neck Cytoplasmic vesicle membrane Multi-pass membrane protein Localizes to a ring on the surface of cells about to undergo bud emergence and in the mother-bud neck of small-budded cells (PubMed:8909536). Delocalized throughout the plasma membrane during heat shock (PubMed:12928491). Also localizes to intracellular membrane-bound particles called chitosomes, proposed to act as a reservoir for regulated transport of chitin synthase enzymes to the division septum (PubMed:8970154, PubMed:12928491). Glycosylated. Palmitoylated by PFA4; required for proper export from the ER. Present with 1510 molecules/cell in log phase SD medium. Belongs to the chitin synthase family. Class IV subfamily. 3D-structure Cell membrane Cell wall biogenesis/degradation Complete proteome Cytoplasmic vesicle Glycoprotein Glycosyltransferase Isopeptide bond Membrane Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Ubl conjugation S A R A R A R A S A F L MTGLNGDDPDDYYLNLNQDEESLLRSRHSVGSGAPHRQGSLVRPERSRLNNPDNPHFYYA QKTQEQMNHLDVLPSSTGVNPNATRRSGSLRSKGSVRSKFSGRETDSYLLQDMNTTDKKA SVKISDEGVAEDEFDKDGDVDNFEESSTQPINKSIKPLRKETNDTLSFWQMYCYFITFWA PAPILAFCGMPKKERQMAWREKVALISVILYIGAIVAFLTFGFTKTVCSSSKLRLKNNEV STEFVVINGKAYELDTSSRSGIQDVEVDSDTLYGPWSDAGKDASFLFQNVNGNCHNLITP KSNSSIPHDDDNNLAWYFPCKLKNQDGSSKPNFTVENYAGWNCHTSKEDRDAFYGLKSKA DVYFTWDGIKNSSRNLIVYNGDVLDLDLLDWLEKDDVDYPVVFDDLKTSNLQGYDLSLVL SNGHERKIARCLSEIIKVGEVDSKTVGCIASDVVLYVSLVFILSVVIIKFIIACYFRWTV ARKQGAYIVDNKTMDKHTNDIEDWSNNIQTKAPLKEVDPHLRPKKYSKKSLGHKRASTFD LLKKHSSKMFQFNESVIDLDTSMSSSLQSSGSYRGMTTMTTQNAWKLSNENKAVHSRNPS TLLPTSSMFWNKATSSPVPGSSLIQSLDSTIIHPDIVQQPPLDFMPYGFPLIHTICFVTC YSEDEEGLRTTLDSLSTTDYPNSHKLLMVVCDGLIKGSGNDKTTPEIALGMMDDFVTPPD EVKPYSYVAVASGSKRHNMAKIYAGFYKYDDSTIPPENQQRVPIITIVKCGTPAEQGAAK PGNRGKRDSQIILMSFLEKITFDERMTQLEFQLLKNIWQITGLMADFYETVLMVDADTKV FPDALTHMVAEMVKDPLIMGLCGETKIANKAQSWVTAIQVFEYYISHHQAKAFESVFGSV TCLPGCFSMYRIKSPKGSDGYWVPVLANPDIVERYSDNVTNTLHKKNLLLLGEDRFLSSL MLKTFPKRKQVFVPKAACKTIAPDKFKVLLSQRRRWINSTVHNLFELVLIRDLCGTFCFS MQFVIGIELIGTMVLPLAICFTIYVIIFAIVSKPTPVITLVLLAIILGLPGLIVVITATR WSYLWWMCVYICALPIWNFVLPSYAYWKFDDFSWGDTRTIAGGNKKAQDENEGEFDHSKI KMRTWREFEREDILNRKEESDSFVA P32462 D6W0R4 ERG24_YEAST Delta(14)-sterol reductase 1.3.1.70 C-14 sterol reductase Sterol C14-reductase ERG24 YNL280C N0593 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-5alpha-cholesta-8,24-dien-3beta-ol + NADP(+) = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + H(+) + NADPH Inhibited by the morpholine antifungal drug fenpropimorph. Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 2/6. Membrane Multi-pass membrane protein Present with 1600 molecules/cell in log phase SD medium. Belongs to the ERG4/ERG24 family. Complete proteome Lipid biosynthesis Lipid metabolism Membrane NADP Oxidoreductase Reference proteome Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism Transmembrane Transmembrane helix L S MVSALNPRTTEFEFGGLIGALGISIGLPVFTIILNQMIRPDYFIKGFFQNFDIVELWNGI KPLRYYLGNRELWTVYCLWYGILAVLDVILPGRVMKGVQLRDGSKLSYKINGIAMSTTLV LVLAIRWKLTDGQLPELQYLYENHVSLCIISILFSFFLATYCYVASFIPLIFKKNGNGKR EKILALGGNSGNIIYDWFIGRELNPRLGPLDIKMFSELRPGMLLWLLINLSCLHHHYLKT GKINDALVLVNFLQGFYIFDGVLNEEGVLTMMDITTDGFGFMLAFGDLSLVPFTYSLQAR YLSVSPVELGWVKVVGILAIMFLGFHIFHSANKQKSEFRQGKLENLKSIQTKRGTKLLCD GWWAKSQHINYFGDWLISLSWCLATWFQTPLTYYYSLYFATLLLHRQQRDEHKCRLKYGE NWEEYERKVPYKIIPYVY P35195 D6VQ01 ECM15_YEAST UPF0045 protein ECM15 Extracellular mutant protein 15 ECM15 YBL001C YBL0105 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) Homotetramer. Cytoplasm Nucleus Present with 1900 molecules/cell in log phase SD medium. Belongs to the UPF0045 family. 3D-structure Complete proteome Cytoplasm Nucleus Reference proteome MPKIFCLADVCMVPIGTDSASISDFVALIEKKIRESPLKSTLHSAGTTIEGPWDDVMGLI GEIHEYGHEKGYVRVHTDIRVGTRTDKHQTAQDKIDVVLKKISQ P38167 D6VPQ2 ECM21_YEAST Protein ECM21 Extracellular mutant protein 21 ECM21 YBL101C YBL0814 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-577; LYS-651; LYS-712; LYS-794; LYS-807 AND LYS-1024 IDENTIFICATION BY MASS SPECTROMETRY SUB592 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-577 IDENTIFICATION BY MASS SPECTROMETRY PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-527 AND SER-775 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-286 AND SER-550 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-115; SER-775 AND SER-1035 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-191 AND LYS-794 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] May be involved in cell wall organization and biogenesis. P39940 RSP5 false 2 Cytoplasm Present with 799 molecules/cell in log phase SD medium. Belongs to the CSR2 family. Cell wall biogenesis/degradation Complete proteome Cytoplasm Isopeptide bond Phosphoprotein Reference proteome Ubl conjugation PSGY HPDT MPFITSRPVAKNSSHSLSETDLNQSKGQPFQPSPTKKLGSMQQRRRSSTIRHALSSLLGG ANVHSPAVLNNTTKGGNNNGNIRSSNTDAQLLGKKQNKQPPPNARRHSTTAIQGSISDSA TTTPRSSTSDTNRRTSGRLSVDQEPRISGGRYSQIEEDSTVLDFDDDHNSSAVVSSDLSS TSLTRLANSKKFNEQFLIEYLTARGLLGPKTVLSNEYLKISISTSGESVFLPTISSNDDE YLSRLNGLNDGTDDAEADFFMDGIDQQEGNTPSLATTAAATESGGSINENRDTLLRENNS GDHPGSGSELNTRSVEIDSSMVSYSIAVIVSVKKPTRFTDMQLELCSRVKVFWNTGVPPT KTFNEEFYNAASMKWNLNDENFDLFVPLSISPDDQMIENNSNDRQMRLFKNIPTEERLYL DKTKTKASLLNAIDVNKTHLYQPGDYVFLVPVVFSNHIPETIYLPSARVSYRLRLATKAI NRKGFYRQDSNSPQPIVSPDSSSSLSSTTSSLKLTETESAQAHRRISNTLFSKVKNHLHM SSHQLKNEESGEEDIFAEYPIKVIRTPPPVAVSTANKPIYINRVWTDSLSYEISFAQKYV SLNSEVPIKIKLAPICKNVCVKRIHVSITERVTFVSKGYEYEYDQTDPVAKDPYNPYYLD FASKRRKERSVSLFEIRTKEKGTRALREEIVENSFNDNLLSYSPFDDDSDSKGNPKERLG ITEPIIIETKLKFPKYEDLDKRTAKIIPPYGIDAYTSIPNPEHAVANGPSHRRPSVIGFL SGHKGSKSHEENEKPVYDPKFHQTIIKSNSGLPVKTHTRLNTPKRGLYLDSLHFSNVYCR HKLEIMLRISKPDPECPSKLRHYEVLIDTPIFLVSEQCNSGNMELPTYDMATMEGKGNQV PLSMNSDFFGNTCPPPPTFEEAISVPASPIVSPMGSPNIMASYDPDLLSIQQLNLSRTTS VSGPSGYSDDAGVPNVNRNSISNANAMNGSISNSAFVSGNSGQGVARARATSVNDRSRFN NLDKLLSTPSPVNRSHNSSPTNGLSQANGTVRIPNATTENSKDKQNEFFKKGYTLANVKD DEEQEGIVSSSSADSLLSHGNEPPRYDEIVPLMSDEE Q01649 D6W023 CIK1_YEAST Spindle pole body-associated protein CIK1 Chromosome instability and karyogamy protein 1 CIK1 YMR198W YM9646.11 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION INTERACTION WITH KAR3 SUBCELLULAR LOCATION INDUCTION FUNCTION SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] A developmentally regulated protein important for microtubule functions. Targets KAR3 to the cytoplasmic microtubules during mating. Essential for KAR3 function during prophase of meiosis I. Required for interhomolog recombination, synapsis of homologous chromosomes and establishment of a meiosis I spindle. Interacts with KAR3. Nucleus Cytoplasm Cytoskeleton Microtubule organizing center Spindle pole body By alpha factor. Present with 98 molecules/cell in log phase SD medium. Coiled coil Complete proteome Cytoplasm Cytoskeleton Microtubule Nucleus Reference proteome MNNSKIPKLSFHSDPNNVTRDFPKTKRQKVQKREMDMILTPNNNKLNILHSSGSGIRRCY TDDTSATYTKKLTFGGDPKIIERVKNNERKVRKDIDSLLNAISEIEKESVRIHARELPAI TLELDAKVKACRELQNEIDGLSTEMDLKDNQCDLQRKNVELSSKNIVSMHAVKVQEFEND LEEELSNAKREWTYKLMEVENLKPDERLTDEMRQLKTEFEEVNRKLFILQNENENECKNY KKELDKKFEIFKKVKNDARIELDGEQERLSKVLKDLQDTHGELKENIKTCRDEFNDFEKR IGEAEVNFHSMELAVVPLKKKLASTSQALTQVQEEKKQVEGEANNWKKKYVNELEKVQQE LYTRQNLATSIEEIKGYTRCFAYANERQMPDEFHINYVDRCICENSGEKRVQVFDRVVLE EIHKDHKRLYNECIPFLEKYISKLINCSIIVVSQQPTAPMKKTLLKQLIEQYGENYKMTL NILHLDGSIKHSDVGLDNPTEIRDLSQDEECMNILTLDTKLGKDEESHSMNIYIGSMSTV QLNRELDDAPSVLSHILTKTKQCFVFKINAGENIEKALALAGKLKRTITLPQLD P40353 D6W370 Q08901 ATF1_YEAST Alcohol O-acetyltransferase 1 AATase 1 2.3.1.84 3.1.2.20 ATF1 YOR377W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] PARTIAL PROTEIN SEQUENCE Kyokai No.7 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PARTIAL PROTEIN SEQUENCE FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES ACTIVITY REGULATION INDUCTION FUNCTION INDUCTION INDUCTION FUNCTION BIOTECHNOLOGY FUNCTION DISRUPTION PHENOTYPE INDUCTION FUNCTION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION FUNCTION BIOTECHNOLOGY FUNCTION BIOTECHNOLOGY FUNCTION FUNCTION FUNCTION BIOTECHNOLOGY BIOTECHNOLOGY BIOTECHNOLOGY SUBCELLULAR LOCATION DOMAIN BIOTECHNOLOGY BIOTECHNOLOGY BIOTECHNOLOGY SUBCELLULAR LOCATION BIOTECHNOLOGY FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES MUTAGENESIS OF HIS-191 Major alcohol O-acetyltransferase that uses acetyl-CoA to synthesize acetate esters from various alcohols, producing ethyl acetate, isoamyl acetate, isobutyl acetate, butyl acetate, hexyl acetate, heptyl acetate and octyl acetate (PubMed:7764365, PubMed:9758847, PubMed:10653746, PubMed:12937998, PubMed:16845703, PubMed:18597084, PubMed:17891501, PubMed:25306884, PubMed:28160314). The alcohol acyltransferase activity is promiscuous with regard to alcohol but relatively specific for acetyl-CoA since ATF1 does not use any other acyl-CoAs (C3, C4, C5, C6, C8, C10, C12) (PubMed:28160314). Acts also as an efficient thioesterase in vitro with specificity towards medium-chain-length acyl-CoAs (PubMed:28160314). In natural environments, the production of aromatic volatile metabolites promotes dispersal through insect vectors (PubMed:25310977). acetyl-CoA + an aliphatic alcohol = an acetyl ester + CoA an acyl-CoA + H2O = a fatty acid + CoA + H(+) Found to be inhibited by cadmium, copper, zinc and mercurium divalent cations and sulfhydryl reagents (PubMed:7764365). Inhibited by the addition of unsaturated fatty acids to the culture (PubMed:7764365). 0.19 mM for acetyl-CoA (for acetyltransferase activity) 29.8 mM for isoamyl alcohol (for acetyltransferase activity) 61 uM for acetyl-CoA (for thioesterase activity) 25 uM for butyryl-CoA (for thioesterase activity) 12 uM for hexanoyl-CoA (for thioesterase activity) 3 uM for octanoyl-CoA (for thioesterase activity) Optimum pH is 8. Optimum temperature is 25 degrees Celsius. Lipid droplet Endoplasmic reticulum membrane Peripheral membrane protein Traffics to lipid droplets during the stationary phase (PubMed:25093817). Expression is repressed both by aeration and by unsaturated fatty acids (PubMed:9055409, PubMed:9675816). Also repressed by heat and ethanol stress (PubMed:14654433). Rapid induction by glucose depends on the cAMP/PKA signaling pathway (PubMed:14654433). Long-term expression requires both carbon and nitrogen sources (PubMed:14654433). The activation of transcription is dependent on RAP1, and the ROX1-TUP1p-SSN6 hypoxic repressor complex is responsible for repression by oxygen (PubMed:10487921). The putative ROX1-binding sequence in the ATF1 promoter is 5'-CCTATTGTTTT-3' and the RAP1-binding sequence is 5'-AACCCAACAAA-3' (PubMed:10487921). Segments of the N- and C-terminal domains (residues 24-41 and 508-525, respectively) are predicted to be amphipathic helices and are essential for endoplasmic reticulum and lipid dropplet association (PubMed:25093817). Reduces levels of isoamyl acetate production during fermentation to about 16% of those produced by the wild-type strain and causes a 40% reduction of ethyl acetate formation (PubMed:12957907). Understanding the biochemistry of the volatile esters is of considerable importance in industrial agriculture, winemaking and brewing. ATF1 could profoundly affect the flavor profiles of wines and distillates deficient in aroma, thereby paving the way for the production of products maintaining a fruitier character for longer periods after bottling (PubMed:10653746, PubMed:16845703, PubMed:18597084, PubMed:25306884, PubMed:28176138). The most important acetate esters from the perspective of fermented foods and beverages are probably ethyl acetate (fruity, solvent aroma), isobutyl acetate (sweet, fruit), isoamyl acetate (banana) and 2-phenylethyl acetate (rose). In addition, the enzymes responsible for ester synthesis are targets for the metabolic engineering of cellular factories intended to produce insect pheromones for use in pest control, but also for the production of fragrances, industrial solvents, fine chemicals, pharmaceuticals and renewable biofuels (PubMed:25281839, PubMed:24609358, PubMed:26205521, PubMed:26801935). Present with 1990 molecules/cell in log phase SD medium. Belongs to the ATF1 alcohol acetyltransferase family. Acyltransferase Complete proteome Direct protein sequencing Endoplasmic reticulum Hydrolase Lipid droplet Membrane Reference proteome Transferase H A T I N K MNEIDEKNQAPVQQECLKEMIQNGHARRMGSVEDLYVALNRQNLYRNFCTYGELSDYCTR DQLTLALREICLKNPTLLHIVLPTRWPNHENYYRSSEYYSRPHPVHDYISVLQELKLSGV VLNEQPEYSAVMKQILEEFKNSKGSYTAKIFKLTTTLTIPYFGPTGPSWRLICLPEEHTE KWKKFIFVSNHCMSDGRSSIHFFHDLRDELNNIKTPPKKLDYIFKYEEDYQLLRKLPEPI EKVIDFRPPYLFIPKSLLSGFIYNHLRFSSKGVCMRMDDVEKTDDVVTEIINISPTEFQA IKANIKSNIQGKCTITPFLHVCWFVSLHKWGKFFKPLNFEWLTDIFIPADCRSQLPDDDE MRQMYRYGANVGFIDFTPWISEFDMNDNKENFWPLIEHYHEVISEALRNKKHLHGLGFNI QGFVQKYVNIDKVMCDRAIGKRRGGTLLSNVGLFNQLEEPDAKYSICDLAFGQFQGSWHQ AFSLGVCSTNVKGMNIVVASTKNVVGSQESLEELCSIYKALLLGP P23293 D6W4G2 BUR1_YEAST Serine/threonine-protein kinase BUR1 2.7.11.22 2.7.11.23 Bypass UAS requirement protein 1 Suppressor of GPA1-Vall50 mutation protein 1 SGV1 BUR1 YPR161C P9584.8 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION INTERACTION WITH BUR2 FUNCTION INTERACTION WITH RBP1 FUNCTION PHOSPHORYLATION AT THR-240 MUTAGENESIS OF THR-240 FUNCTION FUNCTION MUTAGENESIS OF GLU-107; ASP-213 AND THR-240 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION FUNCTION IN PHOSPHORYLATION OF UBC2 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] YAL6B PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND THR-405 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-634 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Serine/threonine-protein kinase component of the BUR kinase complex involved in transcription regulation. This complex phosphorylates 'Ser-120' of the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B, the localization of the PAF1 complex to the chromatin, and the silencing of telomeric-associated genes. Also required for histone H3 'Lys-4' trimethylation. May phosphorylate the 'Ser-5' of the RBP1 carboxy-terminal domain (CTD) repeats. Necessary for the recovery from pheromone-induced growth arrest in the cell cycle G1 phase. The kinase activity of the complex requires the presence of BUR2. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] [DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase] Belongs to the BUR kinase complex composed of SGV1/BUR1 and BUR2. Interacts with BUR2 and RBP1. Q05949 BUR2 false 6 Nucleus Present with 2070 molecules/cell in log phase SD medium. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. ATP-binding Complete proteome Kinase Nucleotide-binding Nucleus Phosphoprotein Reference proteome Serine/threonine-protein kinase Transferase E Q D N T A D E MSDNGSPAVLPKTEFNKYKIGKVKSTPAIQRDAKTNLTYIKLRKRSSEKVYGCTVFQNHY REDEKLGQGTFGEVYKGIHLETQRQVAMKKIIVSVEKDLFPITAQREITILKRLNHKNII KLIEMVYDHSPDITNAASSNLHKSFYMILPYMVADLSGVLHNPRINLEMCDIKNMMLQIL EGLNYIHCAKFMHRDIKTANILIDHNGVLKLADFGLARLYYGCPPNLKYPGGAGSGAKYT SVVVTRWYRAPELVLGDKQYTTAVDIWGVGCVFAEFFEKKPILQGKTDIDQGHVIFKLLG TPTEEDWAVARYLPGAELTTTNYKPTLRERFGKYLSETGLDFLGQLLALDPYKRLTAMSA KHHPWFKEDPLPSEKITLPTEESHEADIKRYKEEMHQSLSQRVPTAPRGHIVEKGESPVV KNLGAIPRGPKKDDASFLPPSKNVLAKPPPSKIRELHQNPRPYHVNSGYAKTAIPPPAAP AGVNRYGPNNSSRNNRFSGNSTAPNNSRNPVNRFHPETNVSSKYNKVPLPLGPQSRYQGN SNESRYKNSPNDSRYHNPRYVNKPETNFNRQPQKYSRQESNAPINKNYNPSNGSRNMAGD HHQGSRPSHPQFPISPSQGQHQLTSKPIEKKNGSFKDERAKPDESKEFQNSDIADLY P27680 D6W1X2 COQ3_YEAST Ubiquinone biosynthesis O-methyltransferase, mitochondrial 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase DHHB methyltransferase DHHB-MT DHHB-MTase 3-demethylubiquinol 3-O-methyltransferase 2.1.1.64 3-demethylubiquinone-6 3-O-methyltransferase Hexaprenyldihydroxybenzoate methyltransferase Polyprenyldihydroxybenzoate methyltransferase 2.1.1.114 COQ3 YOL096C HRF316 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] INDUCTION D273-10B/A1 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION CATALYTIC ACTIVITY SUBCELLULAR LOCATION PATHWAY IDENTIFICATION OF PROBABLE INITIATION SITE SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 INTERACTION WITH COQ4 SUBUNIT SUBUNIT O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. Catalyzes the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate (DHHB) to 3-methoxy-4-hydroxy-5-hexaprenylbenzoate (HMHB) and the methylation of 2-hexaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinol (3-demethylubiquinol-6) to ubiquinol-6. 3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine Regulated in response to catabolite repression. Cofactor biosynthesis; ubiquinone biosynthesis. Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9 (PubMed:15792955, PubMed:24406904). Interacts directly with COQ4 (PubMed:15792955). Mitochondrion inner membrane Peripheral membrane protein Matrix side Present with 259 molecules/cell in log phase SD medium. Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family. Translation N-terminally shortened. Translation N-terminally shortened. Translation N-terminally shortened. Translation N-terminally shortened. Complete proteome Membrane Methyltransferase Mitochondrion Mitochondrion inner membrane Reference proteome S-adenosyl-L-methionine Transferase Transit peptide Ubiquinone biosynthesis MLLRSRFLKVIHVRKQLSACSRFAIQTQTRCKSTDASEDEVKHFQELAPTWWDTDGSQRI LHKMNLTRLDFVQRTVRNQVKIQNPEIFVPGFNYKEFLPEYVCDNIQREMQESIETNLDK RPEVSVLDVGCGGGILSESLARLKWVKNVQGIDLTRDCIMVAKEHAKKDPMLEGKINYEC KALEDVTGQFDIITCMEMLEHVDMPSEILRHCWSRLNPEKGILFLSTINRDLISWFTTIF MGENVLKIVPKGTHHLSKYINSKEILAWFNDNYSGQFRLLDLKGTMYLPYQGWVEHDCSD VGNYFMAIQRLN Q06680 D6VSV8 CND3_YEAST Condensin complex subunit 3 CAPG homolog YCG1 YCS5 YDR325W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c SEQUENCE REVISION GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; BRN1 AND YCS4 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-981 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933 AND SER-1008 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRN1, YCS4 and YCG1/YCS5. P38989 SMC2 false 3 Q12267 SMC4 false 2 Nucleus Cytoplasm Chromosome In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. Present with 1920 molecules/cell in log phase SD medium. Belongs to the CND3 (condensin subunit 3) family. 3D-structure Cell cycle Cell division Chromosome Complete proteome Cytoplasm DNA condensation Mitosis Nucleus Phosphoprotein Reference proteome Repeat MQDPDGIDINTKIFNSVAEVFQKAQGSYAGHRKHIAVLKKIQSKAVEQGYEDAFNFWFDK LVTKILPLKKNEIIGDRIVKLVAAFIASLERELILAKKQNYKLTNDEEGIFSRFVDQFIR HVLRGVESPDKNVRFRVLQLLAVIMDNIGEIDESLFNLLILSLNKRIYDREPTVRIQAVF CLTKFQDEEQTEHLTELSDNEENFEATRTLVASIQNDPSAEVRRAAMLNLINDNNTRPYI LERARDVNIVNRRLVYSRILKSMGRKCFDDIEPHIFDQLIEWGLEDRELSVRNACKRLIA HDWLNALDGDLIELLEKLDVSRSSVCVKAIEALFQSRPDILSKIKFPESIWKDFTVEIAF LFRAIYLYCLDNNITEMLEENFPEASKLSEHLNHYILLRYHHNDISNDSQSHFDYNTLEF IIEQLSIAAERYDYSDEVGRRSMLTVVRNMLALTTLSEPLIKIGIRVMKSLSINEKDFVT MAIEIINDIRDDDIEKQEQEEKIKSKKINRRNETSVDEEDENGTHNDEVNEDEEDDNISS FHSAVENLVQGNGNVSESDIINNLPPEKEASSATIVLCLTRSSYMLELVNTPLTENILIA SLMDTLITPAVRNTAPNIRELGVKNLGLCCLLDVKLAIDNMYILGMCVSKGNASLKYIAL QVIVDIFSVHGNTVVDGEGKVDSISLHKIFYKVLKNNGLPECQVIAAEGLCKLFLADVFT DDDLFETLVLSYFSPINSSNEALVQAFAFCIPVYCFSHPAHQQRMSRTAADILLRLCVLW DDLQSSVIPEVDREAMLKPNIIFQQLLFWTDPRNLVNQTGSTKKDTVQLTFLIDVLKIYA QIEKKEIKKMIITNINAIFLSSEQDYSTLKELLEYSDDIAENDNLDNVSKNALDKLRNNL NSLIEEINERSETQTKDENNTANDQYSSILGNSFNKSSNDTIEHAADITDGNNTELTKTT VNISAVDNTTEQSNSRKRTRSEAEQIDTSKNLENMSIQDTSTVAKNVSFVLPDEKSDAMS IDEEDKDSESFSEVC P47129 D6VWQ2 ACF4_YEAST Assembly-complementing factor 4 ACF4 YJR083C J1857 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION PREDICTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-74; SER-78; SER-165 AND SER-288 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-74; SER-165 AND SER-288 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-78; SER-165 AND SER-288 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] May be involved in actin cytoskeleton organization and biogenesis. P43603 LSB3 false 4 P39743 RVS167 false 5 P32793 YSC84 false 4 Present with 1140 molecules/cell in log phase SD medium. Complete proteome Phosphoprotein Reference proteome MSEDQRVISQPIELHKLSIVDKHSQGQQQQPHQKQHEVQPESKSPRVTTPLKPKRLAIPI SSPQRSTTNQSPVSDHASPISTDQDLIYKLAAKHREINELSFKLEVAQKELKQLELQFKD TLPRNGQQKLGNQNPSEYLSTFTKRIQQTFVDVNNSPNMLKGKKSINDFFSKPNNNVNSN INNTLPNRKPNPPPNRSQRMQNIAPSRSSESTPTSGPPLLPPRNTMKNANTTATAGENTP FLQRILNKFNQMNMEEDEFDDLLEKRKSKKDHYYIKENLGYEYDEVRSEDEDDEEFEPMG DIPVHLFKR P47001 D6VW29 CIS3_YEAST Cell wall mannoprotein CIS3 Covalently-linked cell wall protein 5/11 Protein with internal repeats 4 Soluble cell wall protein 8 CIS3 CCW11 CCW5 PIR4 SCW8 YJL158C J0561 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c PROTEIN SEQUENCE OF 22-47 AND 65-89 CLEAVAGE BY KEX2 SUBCELLULAR LOCATION PROTEIN SEQUENCE OF 65-118 GLYCOSYLATION AT SER-105; SER-106; SER-107; SER-109; THR-111; SER-112; THR-113; THR-116; SER-117 AND SER-118 PROTEIN SEQUENCE OF 65-77 GLYCOSYLATION SUBCELLULAR LOCATION PROTEIN SEQUENCE OF 65-77 MUTAGENESIS OF CYS-130; CYS-197; 208-GLN--CYS-227 AND CYS-227 SUBCELLULAR LOCATION PROTEIN SEQUENCE OF 65-77 GLYCOSYLATION AT SER-68 AND THR-78 MUTAGENESIS OF ASP-65; SER-68; GLN-69; ASP-72; GLN-74; GLN-76; THR-78; SER-79 AND THR-82 CELL WALL ATTACHMENT SITE IDENTIFICATION BY MASS SPECTROMETRY PROTEIN SEQUENCE OF 65-75 SUBCELLULAR LOCATION ATCC 96099 / S288c / SEY6210 INDUCTION FUNCTION FUNCTION INDUCTION SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] INDUCTION GLYCOSYLATION [LARGE SCALE ANALYSIS] Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents. Secreted Cell wall Covalently attached to the cell wall. Localizes predominantly on the surface of growing buds. Positively regulated by signaling through MPK1 in response to cell wall perturbation. The PIR1/2/3 repeat is required for the covalent linkage to the cell wall. Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensitive ester linkage between the gamma-carboxyl group of glutamic acid, arising from Gln-74 within the PIR1/2/3 repeat, and hydroxyl groups of glucoses of beta-1,3-glucan chains. Extensively O-mannosylated. Also N-glycosylated. Present with 12500 molecules/cell in log phase SD medium. Belongs to the PIR protein family. Cell wall Cell wall biogenesis/degradation Cleavage on pair of basic residues Complete proteome Direct protein sequencing Glycoprotein Reference proteome Repeat Secreted Signal D N S A Q A D N Q A Q A T A S A T A C S C S QNVAEQCSAIHLEAVSLVDC LDC AA SS S T S E MQFKNVALAASVAALSATASAEGYTPGEPWSTLTPTGSISCGAAEYTTTFGIAVQAITSS KAKRDVISQIGDGQVQATSAATAQATDSQAQATTTATPTSSEKISSSASKTSTNATSSSC ATPSLKDSSCKNSGTLELTLKDGVLTDAKGRIGSIVANRQFQFDGPPPQAGAIYAAGWSI TEDGYLALGDSDVFYQCLSGNFYNLYDQNVAEQCSAIHLEAVSLVDC Q05955 D6VYM7 ADY4_YEAST Accumulates dyads protein 4 ADY4 YLR227C L8083.11 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION FUNCTION SUBCELLULAR LOCATION DEVELOPMENTAL STAGE INTERACTION WITH CNM67; SPO21 AND NUD1 Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. May be required to stabilize the outer plaque of the spindle pole body (SPB). Interacts with CNM67, SPO21/MPC70 and NUD1. Cytoplasm Cytoskeleton Microtubule organizing center Spindle pole body Localizes to the meiotic outer plaque of the SPB, at the end of the meiotic spindles. Meiosis-specific. Cell cycle Cell division Complete proteome Cytoplasm Cytoskeleton Meiosis Reference proteome Sporulation MNKDVDYQTFKKSLRKEFKKAVKTILNLQAYNGDLIRDFLALYIPYHVVFYNLSIMKKGS PLRIQTNNLLKEALAKILNFNLAMGPKHIIKIMKKDKADPETMNKLKLVLYIKLFQGVFG HVDKNYNLAFQSFRWCLQFIAYSKRTRLFASIADEQIGAFYELCELFISMLCCHCFLIDL KENEALVGNNLKNFIKRQNPNYSHGFDLNEETKSLQWHWSLDEVDVIEALYCVAFDAMDK ITLKFSKVNENFVFSQFFQYCAEIEEMLAILRGKIWECECDVFGPRIGLLVDSNHMNETI QKNILSITFKLKNDPQIICCLNKILEGLLLSSGVQFKVIQFFYVLKLYYMQDNEYTFEAS SEMDKLTIECLCIIENIIDACDNPDEVTDYQLPKVLLTAMEGKLLVAEKISEDNDCSESL DDYHPRTYQFRHPRIIIDKMKTKLKQKLRFDSPKDPETDDHWIEYWKYCYQDNIGNLPDI LSRIYQTFTDPSN P0CZ17 D6VYF3 P11163 Q12268 Q6Q5K8 Q6Q5K9 ASP21_YEAST L-asparaginase 2-1 3.5.1.1 L-asparaginase II L-asparagine amidohydrolase II ASP II ASP3-1 YLR155C L9632.6 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 26-41 AND 56-71 VARIANT 26-GLU--ALA-55 DEL NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c BIOPHYSICOCHEMICAL PROPERTIES INDUCTION BIOPHYSICOCHEMICAL PROPERTIES H2O + L-asparagine = L-aspartate + NH4(+) 0.27 mM for L-asparagine 0.27 mM for D-asparagine 0.27 mM for N-acetyl-L-asparagine 0.07 mM for N-carbamyl-L-asparagine 0.06 mM for N-isoleucyl-L-asparagine 0.06 mM for N-glycyl-L-asparagine 0.06 mM for N-valyl-L-asparagine 0.2 mM for N-methionyl-L-asparagine 0.4 mM for N-glycyl-D-asparagine 42 umol/min/mg enzyme for L-asparagine 60 umol/min/mg enzyme for D-asparagine 167 umol/min/mg enzyme for N-acetyl-L-asparagine 79 umol/min/mg enzyme for N-carbamyl-L-asparagine 67 umol/min/mg enzyme for N-isoleucyl-L-asparagine 135 umol/min/mg enzyme for N-glycyl-L-asparagine 56 umol/min/mg enzyme for N-valyl-L-asparagine 92 umol/min/mg enzyme for N-methionyl-L-asparagine 8 umol/min/mg enzyme for N-glycyl-D-asparagine Does not act on isoasparagine, L-aspartate diamide, beta-alanine amide and L-glutamine. Optimum pH is 6.8. Active from pH 5.5 to pH 7.5. Stable from pH 3.5 to pH 10.5. Secreted Periplasm Subject to nitrogen catabolite repression (NCR). Not found in cells grown on rich nitrogen sources like ammonia, glutamine or glutamate, but is found in cells that have been subjected to nitrogen starvation or have been grown on a poor nitrogen source such as proline. Yeast contains 2 L-asparaginase isoenzymes: cytoplasmic L-asparaginase I, and cell wall L-asparaginase II. There are 4 copies for L-asparaginase 2 in yeast. The 4 identical copies ASP3-1, ASP3-2, ASP3-3 and ASP3-4 are arranged in tandem repeats located near a ribosomal DNA cluster. Belongs to the asparaginase 1 family. Complete proteome Direct protein sequencing Glycoprotein Hydrolase Periplasm Reference proteome Secreted Signal S P MRSLNTLLLSLFVAMSSGAPLLKIREEKNSSLPSIKIFGTGGTIASKGSTSATTAGYSVG LTVNDLIEAVPSLAEKANLDYLQVSNVGSNSLNYTHLIPLYHGISEALASDDYAGAVVTH GTDTMEETAFFLDLTINSEKPVCIAGAMRPATATSADGPMNLYQAVSIAASEKSLGRGTM ITLNDRIASGFWTTKMNANSLDTFRADEQGYLGYFSNDDVEFYYPPVKPNGWQFFDISNL TDPSEIPEVIILYSYQGLNPELIVKAVKDLGAKGIVLAGSGAGSWTATGSIVNEQLYEEY GIPIVHSRRTADGTVPPDDAPEYAIGSGYLNPQKSRILLQLCLYSGYGMDQIRSVFSGVY GG Q12438 D6VRX8 GLRX6_YEAST Monothiol glutaredoxin-6 GRX6 YDL010W D2890 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 70-82; 85-102; 144-175; 181-193 AND 208-219 IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Vacuole Present with 1643 molecules/cell in log phase SD medium. Belongs to the glutaredoxin family. Monothiol subfamily. 2Fe-2S 3D-structure Complete proteome Direct protein sequencing Iron Iron-sulfur Metal-binding Reference proteome Signal Vacuole MIPSNKRNARILSITTLLLLLVFFVAQNANFLTVEIKEETSKAFSTNMDNMAGGSSREYA AMPTSTTNKGSSEVDEEINEIKQKVGLQQPIASVDDSLSAIKNDKGSRITKAFNVQKEYS LILDLSPIIIFSKSTCSYSKGMKELLENEYQFIPNYYIIELDKHGHGEELQEYIKLVTGR GTVPNLLVNGVSRGGNEEIKKLHTQGKLLESLQVWSDGKFSVEQREKPSNN Q06551 D6VYP4 Q6B217 ERFB_YEAST Palmitoyltransferase ERF2 2.3.1.225 DHHC cysteine-rich domain-containing protein ERF2 Ras protein acyltransferase ERF2 YLR246W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c MUTAGENESIS OF LYS-173; ARG-182; CYS-189; ASP-200 AND PHE-218 SUBCELLULAR LOCATION FUNCTION MUTAGENESIS OF CYS-189; HIS-201 AND CYS-203 INTERACTION WITH SHR5 INTERACTION WITH SHR5 SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A The ERF2-SHR5 complex is a palmitoyltransferase specific for Ras proteins. Palmitoylates RAS2, which is required for its proper plasma membrane localization. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Interacts with SHR5. P41912 SHR5 false 2 Endoplasmic reticulum membrane Multi-pass membrane protein The DHHC domain is required for palmitoyltransferase activity. Autopalmitoylated. Belongs to the DHHC palmitoyltransferase family. ERF2/ZDHHC9 subfamily. Acyltransferase Complete proteome Endoplasmic reticulum Lipoprotein Membrane Palmitate Reference proteome Transferase Transmembrane Transmembrane helix K E R Q C S D A H A C S F S R M MALVSRRSTRSESTSITKEEHTGEGSLTKLFFRWLVTLEGDQDINDGKGYISLPNVSNYI FFLGGRFRTVKGAKPLWLGVLLAIVCPMVLFSIFEAHKLWHTQNGYKVLVIFFYYFWVIT LASFIRTATSDPGVLPRNIHLSQLRNNYQIPQEYYNLITLPTHSSISKDITIKYCPSCRI WRPPRSSHCSTCNVCVMVHDHHCIWVNNCIGKRNYRFFLIFLLGAILSSVILLTNCAIHI ARESGGPRDCPVAILLLCYAGLTLWYPAILFTYHIFMAGNQQTTREFLKGIGSKKNPVFH RVVKEENIYNKGSFLKNMGHLMLEPRGPSFVSARKPHEAGDWRFMDLSPAHSFEKIQKI P15315 D6VTY6 CUP2_YEAST Transcriptional activator protein CUP2 Copper-fist transcription factor CUP2 ACE1 YGL166W G1810 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33 ATCC 96604 / S288c / FY1679 CHARACTERIZATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Trans-acting regulatory protein that activates transcription of the CUP1 gene (metallothionein) in response to copper ions. Binds to the CUP1 UAS sequence 5'-GCTTCTTTTCCGCTGA-3'. Binds DNA only in presence of copper or silver. Copper seems to alter the conformation of the protein. Nucleus Present with 1760 molecules/cell in log phase SD medium. Activator Complete proteome Copper DNA-binding Metal-binding Nucleus Reference proteome Transcription Transcription regulation Zinc MVVINGVKYACETCIRGHRAAQCTHTDGPLQMIRRKGRPSTTCGHCKELRRTKNFNPSGG CMCASARRPAVGSKEDETRCRCDEGEPCKCHTKRKSSRKSKGGSCHRRANDEAAHVNGLG IADLDVLLGLNGRSSDVDMTTTLPSLKPPLQNGEIKADSIDNLDLASLDPLEQSPSISME PVSINETGSAYTTTNTALNDIDIPFSINELNELYKQVSSHNSHSQ P36033 D6VWY3 FRE2_YEAST Ferric/cupric reductase transmembrane component 2 1.16.1.9 Ferric-chelate reductase 2 FRE2 YKL220C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CHARACTERIZATION SUBCELLULAR LOCATION ATCC 204508 / S288c INDUCTION FUNCTION INDUCTION INDUCTION INDUCTION ERRATUM INDUCTION FUNCTION INDUCTION BY AFT1 AND AFT2 TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake. 2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH FAD heme Cell membrane Multi-pass membrane protein By transcription factors AFT1 and AFT2 upon iron deprivation. Belongs to the ferric reductase (FRE) family. Cell membrane Complete proteome Copper Copper transport Electron transport FAD Flavoprotein Glycoprotein Heme Ion transport Iron Iron transport Membrane Metal-binding NADP Oxidoreductase Reference proteome Signal Transmembrane Transmembrane helix Transport MHWTSILSAILLFCLSGARASPAKTVIRNKVPLLVTNACTRIFQKVTWEYTSKSKRSSPV CSYEPAFQSMLYCIYETLDEKGYSNKTLEKTFSTIKKNCASYSDALQNMTNSEFYDVLNN GTRHMTPYVKGSANLTYPVEMDTQLRKAYYHALHGFYANLDVGNIYGGIICAYFVAIMAF AGVLHCMNYTPFKTVLLKQKLVGYVRGYLTLPTIGSKHASDFSYFRIFTGYLPTRLEGII ILGYLVLHTVFLAYGYEYDPENIIFKSRRVQVARYVADRSGVLAFAHFPLIVLFAGRNNF LEYISGVKYTSFIMFHKWLGRMMFLDAMIHGSAYTSYTVANKTWATSKNRLYWQFGVAAL CLAGTMVFFSFAVFRKYFYEAFLFLHIVLGAMFFYACWEHVVSLSGIEWIYTAIAIWIVD RIIRIIKASYFGFPKASLQLIGDDLIRLTVKKPARPWRAKPGQYVFVSFLHPLYFWQSHP FTVLDSVSKNGELVIILKEKKGVTRLVKKYVCRNGGKTSMRLAIEGPYGSSSPVNNYNNV LLLTGGTGLPGPIAHAIKLGKTSAAAGKQSVKLVIAVRGFDVLEAYKPELMCLENLNVQL HIYNTMEVPSLTPSDSLDISQQDEKADEKGTVVATTLEKSANPLGFDGVVFHCGRPNVKE LLHEAAELSGSLSVVCCGPPIFVDKVRNETAKIVLDKSAKAIEYFEEYQCW P41912 D6W1V7 ERFD_YEAST Ras modification protein ERF4 Hyperactive Ras suppressor protein 5 SHR5 ERF4 YOL110W HRC237 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION SP1 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION INTERACTION WITH ERF2 FUNCTION MUTAGENESIS OF SER-128; VAL-148 AND LEU-204 INTERACTION WITH ERF2 SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] The ERF2-SHR5 complex is a palmitoyltransferase specific for Ras proteins. Palmitoylates RAS2, which is required for its proper plasma membrane localization. Interacts with ERF2. Q06551 ERF2 false 2 Endoplasmic reticulum membrane Peripheral membrane protein Present with 937 molecules/cell in log phase SD medium. Belongs to the ERF4 family. Complete proteome Endoplasmic reticulum Membrane Reference proteome S P V K L P MCDSHQKEEDNANTSERALFFNYHEFSYSFYEDLGSEDAKPTEHDEDHKLCITHFPNVYA ARGSAEFQVTRVVRVPRRFDESRSSLETPQFSTQLPGSEPAAIVGDDGTSFVRCGRYDIG DHVFGCSSVSPLSEYLSAAELAEVVHRVNGFLLREEGEVFGWRNLSGLLLDMLTGGLWSW VLGPLLSRPVFQESLALEQYVAQLNSPGGLLHERGVRLVLPRRSGCLSLDFVVPRPK P81449 D6VSV5 ATPJ_YEAST ATP synthase subunit e, mitochondrial ATPase subunit e Translocase of the inner membrane protein 11 TIM11 ATP21 YDR322C-A YDR322BC Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c IDENTIFICATION PROTEIN SEQUENCE OF 2-14 CLEAVAGE OF INITIATOR METHIONINE ACETYLATION AT SER-2 ATCC 208353 / W303-1A IDENTIFICATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k. Mitochondrion Mitochondrion inner membrane Present with 4590 molecules/cell in log phase SD medium. Belongs to the ATPase e subunit family. Acetylation ATP synthesis CF(0) Complete proteome Direct protein sequencing Hydrogen ion transport Ion transport Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Transport MSTVNVLRYSALGLGLFFGFRNDMILKCNAKKKEEQAQYEEKLKLVEEAKKEYAKLHPVV TPKDVPANASFNLEDPNIDFERVILNAVESLKEAST Q04930 D6VSK5 CRF1_YEAST Transcription factor CRF1 Corepressor with FHL1 protein 1 CRF1 YDR223W YD9934.08 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PHOSPHORYLATION BY CDC28 FUNCTION SUBCELLULAR LOCATION INTERACTION WITH FHL1 PHOSPHORYLATION BY YAK1 FUNCTION Transcription factor, corepressor with FHL1 of ribosomal protein genes. May be involved in the blocking of the spread of silencing. Interacts with FHL1 to form a repressor complex. The formation of the CRF1-FHL1 complex is inhibited by the TOR pathway. Cytoplasm Nucleus The nuclear location is negatively regulated by the TOR pathway. Phosphorylated by CDC28 and YAK1. Complete proteome Cytoplasm Nucleus Phosphoprotein Reference proteome Repressor Transcription Transcription regulation MLLSAPVNSTVRRKPHSPNKKKPKETGTAASFSSSSSTVVLSSNNDGSFDALWDPSISKA SDFESSYISAKRLKPESSNRQKKKNSYKYSREENTNEVEEKTSLGSSSKTEADNIFNDQL TSAGNTTYVSNKRDVNFGANSAVVLLGLPTSKSESHRQYHSPSASTTNEDEEDIGVDILV DNHIDSCETVSINNNRGITHQYPETESDVDFDEAVILTPMDGTDKGVKNPRPLEKKYSSS CFEDRTPLNLDDGHFSECNHFSTLDVSSFFHLNEHVHKIDEVELDGPDRTFSLDNVAINT RKKDIDCLYNSSREDLSNLTCSSEGPRNDSYDSDYNIDEVTYRDDESTDEDESLPTPDRK RKKIGHKACEILDSKRIGIKVPKLYVWSLSDKPFSVIDGLCTKSLYPLSDDINTPESLSS CSSSVSSRENQKGDATFDNDAMIADLLNIGGLEVEKASNGHIELIGE P19516 D6W3N5 COX11_YEAST Cytochrome c oxidase assembly protein COX11, mitochondrial COX11 YPL132W LPI13W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-300 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-300 ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I. Mitochondrion inner membrane Single-pass membrane protein Intermembrane side Intrinsic component of the inner-membrane. Belongs to the COX11/CtaG family. Complete proteome Copper Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Transit peptide Transmembrane Transmembrane helix WLAPHALA MVGTSCAS T S MIRICPIVRSKVPLLGTFLRSDSWLAPHALALRRAICKNVALRSYSVNSEQPKHTFDISK LTRNEIQQLRELKRARERKFKDRTVAFYFSSVAVLFLGLAYAAVPLYRAICARTGFGGIP ITDRRKFTDDKLIPVDTEKRIRISFTSEVSQILPWKFVPQQREVYVLPGETALAFYKAKN YSDKDIIGMATYSIAPGEAAQYFNKIQCFCFEEQKLAAGEEIDMPVFFFIDPDFASDPAM RNIDDIILHYTFFRAHYGDGTAVSDSKKEPEMNADEKAASLANAAILSPEVIDTRKDNSN P47039 D6VWC2 BNA3_YEAST Probable kynurenine--oxoglutarate transaminase BNA3 2.6.1.7 Biosynthesis of nicotinic acid protein 3 Kynurenine aminotransferase BNA3 YJL060W J1138 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) SUBUNIT IDENTIFICATION AS KYNURENINE AMINOTRANSFERASE Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). 2-oxoglutarate + L-kynurenine = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate pyridoxal 5'-phosphate Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2. Homodimer. Cytoplasm Mitochondrion Present with 1600 molecules/cell in log phase SD medium. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. 3D-structure Aminotransferase Complete proteome Cytoplasm Mitochondrion Pyridoxal phosphate Reference proteome Transferase MKQRFIRQFTNLMSTSRPKVVANKYFTSNTAKDVWSLTNEAAAKAANNSKNQGRELINLG QGFFSYSPPQFAIKEAQKALDIPMVNQYSPTRGRPSLINSLIKLYSPIYNTELKAENVTV TTGANEGILSCLMGLLNAGDEVIVFEPFFDQYIPNIELCGGKVVYVPINPPKELDQRNTR GEEWTIDFEQFEKAITSKTKAVIINTPHNPIGKVFTREELTTLGNICVKHNVVIISDEVY EHLYFTDSFTRIATLSPEIGQLTLTVGSAGKSFAATGWRIGWVLSLNAELLSYAAKAHTR ICFASPSPLQEACANSINDALKIGYFEKMRQEYINKFKIFTSIFDELGLPYTAPEGTYFV LVDFSKVKIPEDYPYPEEILNKGKDFRISHWLINELGVVAIPPTEFYIKEHEKAAENLLR FAVCKDDAYLENAVERLKLLKDYL P32629 D3DLL3 ANP1_YEAST Mannan polymerase II complex ANP1 subunit M-Pol II subunit ANP1 Aminonitrophenyl propanediol resistance protein ANP1 GEM3 YEL036C SYGP-ORF28 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] B-6441 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 1-10 SUBCELLULAR LOCATION SUBUNIT PROTEIN SEQUENCE OF 1-5 SUBCELLULAR LOCATION CHARACTERIZATION ACTIVITY OF M-POL II COMPLEX SUBUNIT SUBCELLULAR LOCATION SUBCELLULAR LOCATION Involved in the organization of the secretory pathway. Required to maintain a functional Golgi apparatus. The M-Pol II complex possesses alpha-1,6-mannosyltransferase activity and is probably involved in the elongation of the mannan backbone of N-linked glycans on cell wall and periplasmic proteins. Component of the M-Pol II complex composed of ANP1, MNN9, MNN10, MNN11 and HOC1. P47124 HOC1 false 2 P50108 MNN10 false 3 P46985 MNN11 false 3 P39107 MNN9 false 6 Endoplasmic reticulum membrane Single-pass type II membrane protein Golgi apparatus membrane Single-pass type II membrane protein Cis-Golgi (PubMed:9430634). Recycles between endoplasmic reticulum and Golgi (PubMed:11095735). Belongs to the ANP1/MMN9/VAN1 family. Complete proteome Direct protein sequencing Endoplasmic reticulum Golgi apparatus Membrane Reference proteome Signal-anchor Transmembrane Transmembrane helix HHDKD QSGQGN F L PQGKPLDDNDKNKKKHPKEVPLDFDPDRN RRGNLLMTTTRTRKNILKKFH MKYNNRKLSFNPTTVSIAGTLLTVFFLTRLVLSFFSISLFQLVTFQGIFKPYVPDFKNTP SVEFYDLRNYQGNKDGWQQGDRILFCVPLRDASEHLPMFFNHLNTMTYPHNLIDLSFLVS DSSDNTMGVLLSNLQMAQSQQDKSKRFGNIEIYEKDFGQIIGQSFSDRHGFGAQGPRRKL MARARNWLGSVALKPYHSWVYWRDVDVETIPTTIMEDLMHHDKDVIVPNVWRPLPDWLGN IQPYDLNSWKESEGGLQLADSLDEDAVIVEGYPEYATWRPHLAYMRDPNGNPEDEMELDG IGGVSILAKAKVFRTGSHFPAFSFEKHAETEAFGRLSRRMNYNVIGLPHYVIWHIYEPSS DDLKHMAWMAEEEKRKLEEERIREFYNKIWEIGFEDVRDQWNEERDSILKNIDSTLNNKV TVDWSEEGDGSELVDSKGDFVSPNNQQQQQQQQQQQQQQQQQQQQQQLDGNPQGKPLDDN DKNKKKHPKEVPLDFDPDRN Q12380 D6W3M0 ATG5_YEAST Autophagy protein 5 ATG5 APG5 YPL149W P2601 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION FUNCTION CONJUGATION TO ATG12 MUTAGENESIS OF LYS-149 ATCC 26109 / X2180 FUNCTION INTERACTION WITH ATG12 AND ATG16 FUNCTION SUBCELLULAR LOCATION FUNCTION IDENTIFICATION IN A COMPLEX WITH ATG12 AND ATG16 NOMENCLATURE CONJUGATION TO ATG12 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION SUBCELLULAR LOCATION FUNCTION CONJUGATION TO ATG12 INTERACTION WITH ATG16 FUNCTION CRYSTALLIZATION OF THE ATG5-ATG16 COMPLEX SUBCELLULAR LOCATION FUNCTION FUNCTION OF THE ATG12-ATG5 CONJUGATE INTERACTION WITH ATG3 SUBCELLULAR LOCATION FUNCTION CONJUGATION TO ATG12 FUNCTION OF THE ATG12-ATG5 CONJUGATE CRYSTALLIZATION OF THE ATG12-ATG5 CONJUGATE BOUND TO ATG16 FUNCTION CONJUGATION TO ATG12 SUBCELLULAR LOCATION FUNCTION OF THE ATG5-ATG12/ATG16 COMPLEX FUNCTION SUBCELLULAR LOCATION FUNCTION OF THE ATG12-ATG5 CONJUGATE INTERACTION WITH ATG3 X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH ATG16 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-284 IN CONJUGATION WITH ATG12 Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes. ATG12-ATG5 rearranges the ATG3 catalytic center and enhances its E2 activity. Plays a role in the regulation of filamentous growth and chronological longevity. Conjugated with ATG12. The ATG5-ATG12 conjugate forms a complex with several units of ATG16. The ATG12-ATG5 conjugate associates also with ATG3. P38316 ATG12 false 9 Q03818 ATG16 false 4 Preautophagosomal structure membrane Peripheral membrane protein Localizes to the isolation membrane (IM), a membrane sac which is generated from the pre-autophagosomal structure (PAS). Ultimately, the IM expands to become a mature autophagosome. Localizes also to a dot at the junction between the IM and the vacuolar membrane, termed the vacuole-IM contact site (VICS). Correct localization to the PAS requires ATG21. Conjugated to ATG12; which is essential for autophagy. Conjugation with ATG12 involves ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme. Present with 606 molecules/cell in log phase SD medium. Small amount of ATG5-ATG12 conjugate is enough to perform normal autophagy. Belongs to the ATG5 family. 3D-structure Autophagy Complete proteome Hydrolase Isopeptide bond Membrane Protein transport Reference proteome Transport Ubl conjugation K R MNDIKQLLWNGELNVLVSIDPSFLMKGSPREIAVLRIRVPRETYLVNYMPLIWNKIKSFL SFDPLTDSEKYFWFEHNKTPIPWNYPVGVLFDCLAGKSATFTTSFENQVKDVLTFLRIHL VMGDSLPPTIIPIASSKTQAEKFWFHQWKQVCFILNGSSKAIMSLSVNEARKFWGSVITR NFQDFIEISNKISSSRPRHIPLIIQTSRTSGTFRISQPTISMTGVNPTLKDIEGDILDVK EGINGNDVMVICQGIEIPWHMLLYDLYSKLRSFDGFLYITLVPIKGGDKASSEL P32190 D3DKT6 GLPK_YEAST Glycerol kinase GK Glycerokinase 2.7.1.30 ATP:glycerol 3-phosphotransferase GUT1 YHL032C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. Belongs to the FGGY kinase family. ATP-binding Complete proteome Glycerol metabolism Kinase Nucleotide-binding Reference proteome Transferase MFPSLFRLVVFSKRYIFRSSQRLYTSLKQEQSRMSKIMEDLRSDYVPLIASIDVGTTSSR CILFNRWGQDVSKHQIEYSTSASKGKIGVSGLRRPSTAPARETPNAGDIKTSGKPIFSAE GYAIQETKFLKIEELDLDFHNEPTLKFPKPGWVECHPQKLLVNVVQCLASSLLSLQTINS ERVANGLPPYKVICMGIANMRETTILWSRRTGKPIVNYGIVWNDTRTIKIVRDKWQNTSV DRQLQLRQKTGLPLLSTYFSCSKLRWFLDNEPLCTKAYEENDLMFGTVDTWLIYQLTKQK AFVSDVTNASRTGFMNLSTLKYDNELLEFWGIDKNLIHMPEIVSSSQYYGDFGIPDWIME KLHDSPKTVLRDLVKRNLPIQGCLGDQSASMVGQLAYKPGAAKCTYGTGCFLLYNTGTKK LISQHGALTTLAFWFPHLQEYGGQKPELSKPHFALEGSVAVAGAVVQWLRDNLRLIDKSE DVGPIASTVPDSGGVVFVPAFSGLFAPYWDPDARATIMGMSQFTTASHIARAAVEGVCFQ ARAILKAMSSDAFGEGSKDRDFLEEISDVTYEKSPLSVLAVDGGMSRSNEVMQIQADILG PCVKVRRSPTAECTALGAAIAANMAFKDVNERPLWKDLHDVKKWVFYNGMEKNEQISPEA HPNLKIFRSESDDAERRKHWKYWEVAVERSKGWLKDIEGEHEQVLENFQ P38823 D3DL65 Q66GT1 DMA1_YEAST E3 ubiquitin-protein ligase DMA1 2.3.2.27 Checkpoint forkhead associated with RING domains-containing protein 1 Defective in mitotic arrest protein 1 RING-type E3 ubiquitin transferase DMA1 DMA1 CHF1 YHR115C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION INTERACTION WITH CDC123 MUTAGENESIS OF GLY-192; SER-220; HIS-223; CYS-345 AND HIS-350 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION FUNCTION CATALYTIC ACTIVITY IDENTIFICATION BY MASS SPECTROMETRY UBIQUITINATION AT LYS-150; LYS-204; LYS-217; LYS-237; LYS-240; LYS-260; LYS-300; LYS-306; LYS-313 AND LYS-317 FUNCTION CATALYTIC ACTIVITY INDUCTION INTERACTION WITH PCL1 E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjonction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugationg enzymes (PubMed:18202552). Involved in nutritional control of the cell cycle (PubMed:15319434). Targets the G1 cyclin PCL1 for destruction (PubMed:23264631). Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck (PubMed:15146058). 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. Interacts with CDC123 (PubMed:15319434). Interacts with PCL1 (PubMed:23264631). Cytoplasm Protein levels are regulated by nutrient status, being high under good nutrient conditions. UBC4-dependent autoubiquitination occurs at Lys-150, Lys-204, Lys-217, Lys-237, Lys-240, Lys-260, Lys-300, Lys-306, Lys-313 and Lys-317. UBC4-dependent autoubiquitination is responsible for DMA2 turnover. UBC13/MMS2-dependent autoubiquitination occurs at Lys-237 and Lys-306. Lys-204 and Lys-306 are also ubiquitinated in trans by DMA2 E3 ligase in association with UBC4. Present with 2790 molecules/cell in log phase SD medium. Belongs to the DMA1 family. Cell cycle Cell division Complete proteome Cytoplasm Isopeptide bond Metal-binding Mitosis Reference proteome Transferase Ubl conjugation Ubl conjugation pathway Zinc Zinc-finger G E S A H L C S H A MSTNTVPSSPPNQTPPAASGIATSHDHTKFNNPIRLPISISLTINDTPNNNSNNNSVSNG LGILPSRTATSLVVANNGSANGNVGATAAAAATVETNTAPAVNTTKSIRHFIYPPNQVNQ TEFSLDIHLPPNTSLPERIDQSTLKRRMDKHGLFSIRLTPFIDTSSTSVANQGLFFDPII RTAGAGSQIIIGRYTERVREAISKIPDQYHPVVFKSKVISRTHGCFKVDDQGNWFLKDVK SSSGTFLNHQRLSSASTTSKDYLLHDGDIIQLGMDFRGGTEEIYRCVKMKIELNKSWKLK ANAFNKEALSRIKNLQKLTTGLEQEDCSICLNKIKPCQAIFISPCAHSWHFHCVRRLVIM NYPQFMCPNCRTNCDLETTLESESESEFENEDEDEPDIEMDIDMEINNNLGVRLVD P20081 D6W147 FKBP_YEAST FK506-binding protein 1 FKBP Peptidyl-prolyl cis-trans isomerase PPIase 5.2.1.8 Rapamycin-binding protein FPR1 FKB1 RBP1 YNL135C N1213 N1845 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [MRNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c PROTEIN SEQUENCE OF 67-100 INTERACTION WITH HMO1 INTERACTION WITH FAP1 MUTAGENESIS OF PHE-43; ASP-44; ASP-48; ARG-49; PHE-94 AND PHE-106 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0) Interacts with HMO1. Interacts with FAP1. P43573 BUD27 false 2 P10869 HOM3 false 3 Q9FR53 TOR true 3 P35169 TOR1 false 4 P32600 TOR2 false 3 Cytoplasm Mitochondrion Binds to the immunosuppressant drug FK506 and also mediates the sensitivity to rapamycin. Rapamycin disrupts interaction with FAP1. Present with 43300 molecules/cell in log phase SD medium. Belongs to the FKBP-type PPIase family. FKBP1 subfamily. 3D-structure Acetylation Complete proteome Cytoplasm Direct protein sequencing Isomerase Mitochondrion Phosphoprotein Reference proteome Rotamase F Y D V D V R I F V F Y MSEVIEGNVKIDRISPGDGATFPKTGDLVTIHYTGTLENGQKFDSSVDRGSPFQCNIGVG QVIKGWDVGIPKLSVGEKARLTIPGPYAYGPRGFPGLIPPNSTLVFDVELLKVN P53720 D6W1J0 DUS2_YEAST tRNA-dihydrouridine(20) synthase [NAD(P)+] 1.3.1.91 Protein SMM1 tRNA-dihydrouridine synthase 2 SMM1 DUS2 YNR015W N2065 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] R100 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION GLYCOSYLATION [LARGE SCALE ANALYSIS] Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U20 in cytoplasmic tRNAs. 5,6-dihydrouridine(20) in tRNA + NADP(+) = H(+) + NADPH + uridine(20) in tRNA 5,6-dihydrouridine(20) in tRNA + NAD(+) = H(+) + NADH + uridine(20) in tRNA FMN Monomer. Cytoplasm Nucleus N-glycosylated. Present with 2650 molecules/cell in log phase SD medium. Belongs to the Dus family. Dus2 subfamily. Complete proteome Cytoplasm Flavoprotein FMN Glycoprotein NAD NADP Nucleus Oxidoreductase Reference proteome tRNA processing MVTYAGKLVLAPMVRAGELPTRLMALAHGADLVWSPEIIDKKLIQCVRKENTALQTVDYV VPSKVQTRPETLVFRTYPKLESSKLIFQIGSASPALATQAALKVINDVSGIDINAGCPKH FSIHSGMGSALLRTPDTLCLILKELVKNVGNPHSKPISVKIRLLDTKQDTLQLVKRLCAT GITNLTVHCRKTEMRNREQPITDYIAEIYEICQANNVSLIVNGAIRDRSHFHDLQANHWK NTNIGGMIAECAERDPTVFDHTSKPSEDGPSWVVACREFIQWATKFDNHIGNTKYMLSRI VPGKSVFFQYFARCKSPEEVSFVLKQLNDDGSAQTDPSEYLENCRAQEKALKNANAIAKQ KRKQTDHIGSDTKKQKVVPLPTDI Q04399 D6VTC8 GMC1_YEAST Putative multicopper oxidase GMC1 1.-.-.- Grand meiotic recombination cluster protein 1 GMC1 YDR506C D9719.12 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION Could be an iron transport multicopper oxidase, which is required for Fe(2+) high affinity uptake. May be required to oxidize Fe(2+) and release it from the transporter. Essential component of copper-dependent iron transport (By similarity). Involved in meiotic prophase and synaptonemal complex (SC) assembly. Cu cation Binds 4 Cu cations per monomer. Present with 589 molecules/cell in log phase SD medium. Belongs to the multicopper oxidase family. Complete proteome Copper Ion transport Iron Iron transport Meiosis Metal-binding Oxidoreductase Reference proteome Repeat Transport MKVILLKPVQLPMLLLILLKFIMAAKEGKIHVLEFNASSEYTLDKRRVISINGYSATFGP EIRVKSGDTLNLKLTNWICSEEEASKDSDVWKDYCSTALHFHGVVPLANEFDGIPGLTQP TIGYGESYWYNFTIDQSTCGTFWYHSHSSVQYGDGMRGVLIVECDDYDNHVANTINSVRD IETLDDGVVTMKKDKHTKELTDYEVQERIITLSDWYTNWNLDILNDKVLSSTGGTDPKFD GSLINGKSSDGETIKIGFNTEYLLLRIVNSGMSGTQVFHLDGFQLIVLEADGIMIKPFIV QTINLAVGQRYTILVKLKSDTSFIRMINGCNKMMGYITKQWWFYKEGAHLDLPKNPNDVS IEHLPGFTKAELYRDIEPTQEENKKLRTKADPVAVFEFDYAYYKDESTKQKYGTGMYKVN ERTFSEYVKDPVRFGFNETYDIVINSLDHMRHPWHMHGHHFQIISLGNKGDGPFHKDVQE GKAWSRYQNDLRHLARTGKAPMVRDSINIAGNSYAVLRINTEMPGKWLLHCHVEWHMMKG LGIVFEVPTTTEDSTKQATTAVLSYPTKEPDPNTVVHTAALEQNKSKVIAVYILIMCAVD AIFYWLLM P38737 D3DKT8 ECM29_YEAST Proteasome component ECM29 Extracellular mutant protein 29 ECM29 YHL030W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION FUNCTION IDENTIFICATION BY MASS SPECTROMETRY IDENTIFICATION IN PROTEASOME COMPLEX SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Stabilizes the proteasome holoenzyme, probably by tethering the 20S proteolytic core particle and the 19S regulatory particle. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Component of the proteasome. ECM29 binds to both proteasome 19S and 20S particles. Cytoplasm Nucleus Present with 2950 molecules/cell in log phase SD medium. Belongs to the ECM29 family. Acetylation Complete proteome Cytoplasm Nucleus Phosphoprotein Proteasome Reference proteome Repeat MSISSDEAKEKQLVEKAELRLAIADSPQKFETNLQTFLPPLLLKLASPHASVRTAVFSAL KNLISRINTLPQVQLPVRALIVQAKEPNLAAQQDSTNVRLYSLLLASKGIDRLSLQDRQQ LLPLVVSNISCLTGTVAARMFHILLKLILEWVAPQESSHEQEEFVQFLQLDNDGFSFLMR QFTRFFLLVPSKQVQVSQQPLSRGYTCPGLSLTDVAFFTYDAGVTFNKEQLNKFKKAIFQ FVCRGMAATQTIEQSPRMIELMEFLCVVSTDSTNLSDDAAQFMKRFPMPYENEEFITFLQ TLYIGNTANGRPPVKAILQEKILSILNRSHFATTKAECISLICSIGLHSSEYKLRSLTLS FIRHVAKLNYKNLNPASSSPSSTDFSTCIVSLIRNNLHAEGWPKLQLGPQTPAFNTAILQ RQLQYETLGDILKRDFELVSDLSYIEFLFESLKNDLPQFRSSIQESLLSLVGHLSILPQQ SKLKLKNLLRKNLSIDEQQREDNNDAVNSIMALKFVSIKFTNAAFPFHDPEARLFNIWGT VRTNRFDIIEESFKGLQPFWFRVNNASINTSATVKTSDLLGSHLSETEFPPFREFLQVLI DQLDSEAASITRKSLNNAVRFSKQCLISNAIYGKKTMVIQDEDWSVRIDKALELDDTVVS RVNEMVQGMNDDIFIRYLTLLSNEFTATNSKGEQIAIFPYQDPIFGSVLLTLLNFVSNNV LRRLEILVPDLYHLVIMKFQSLSDNDLAVCATIIGIISTAIADSTHVKRITKIAQSQTMA ETYVASYVVPRLYLKDQTNHIESDSILNLLNILTTHLSHPGTNKDMILKLVCQVTKFGLL LQVSAQERKDFLKKVMDTIQDKLINDVTAIQTWSYLSLYSTDLENSSLFQEKLLETNVSK QNDFLFSVGESLSVVAGKWSSKYLIKQIDIPNFNVEIMQQKFPATNVTTILDEIFSGCDS TKPSLRKASCIWLLSYIQYLGHLPEVSSKCNDIHLRFMRFLADRDEFIQDSAARGLSLVY EIGGSDLKESMVKGLLKSFTESTAGSASTSATGISGSVSEETELFEPGVLNTGDGSISTY KDILNLASEVGDPALVYKFMSLAKSSALWSSRKGIAFGLGAIMSKSSLEELLLKDQQTAK KLIPKLYRYRFDPFQAVSRSMTDIWNTLIPESSLTISLYFNDILDELLCGMANKEWRVRE ASTSALLQLIQSQPQEKFSEKMLKIWTMAFRTMDDIKDSVREVGTKFTTVLAKILARSID VEKGVNPTKSKEILDNILPFLWGPHGLNSDAEEVRNFALTTLIDLVKHSPGAIKPFTPKL IYDFITLFSSIEPQVINYLALNAANYNIDANVIDTQRKNGVTNSPLFQTIEKLINNSDDC MMEEIINVVIKASRKSVGLPSKVASSLVIIILVKRYSIEMKPYSGKLLKVCLTMFEDRNE SVNIAFAISMGYLFKVSALDKCIKYSEKLITKYFEPTSTENNKKVVGTAIDSILNYAKSE FDNVASVFMPLIFIACNDEDKDLETLYNKIWTEASSSGAGTVKLYLPEILNVLCVNIKSN DFSIRKTCAKSVIQLCGGINDSIPYPQIVKLFDISREALSGRSWDGKEHIVAALVSLTEK FSQTVADNNDLQESINHVMYTEVSRKSMKYVKKILPLYARYINVNPQEETITFLIEKAKE MIRLLGSESDDSEGSIKQTSDESTIKRIKPNTEITQKSSKENIENEEYVINLLKVSVDIC NNSKSRYPMNLLEFIIDEIAYLFHNDRIIHTWRTQLAASEIGISIVGRFSTISSADFIQN VGRLWDQTFPINCNKETIENVKLQMIKFGGLIIQKIPSLQNNIEENLRLLNSIDSTSRIE LELKNIGL P28003 D6VPI4 FUN19_YEAST SWIRM domain-containing protein FUN19 FUN19 YAL034C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c SEQUENCE REVISION GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION OF PROBABLE INITIATION SITE PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-194; SER-207 AND SER-211 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] FUN19 is a non-essential gene. Complete proteome Phosphoprotein Reference proteome T S L S MGLYSPESEKSQLNMNYIGKDDSQSIFRRLNQNLKASNNNNDSNKNGLNMSDYSNNSPYG RSYDVRINQNSQNNGNGCFSGSIDSLVDEHIIPSPPLSPKLESKISHNGSPRMASSVLVG STPKGAVENVLFVKPVWPNGLSRKRYRYATYGFLSQYKIFSNLAQPYSKNIINRYNNLAY NARHKYSKYNDDMTPPPLPSSSSRLPSPLASPNLNRQARYNMRKQALYNNNLGKFESDTE WIPRKRKVYSPQRRTMTTSPHRAKKFSPSASTPHTNIASIEAIHDAPQYIPNVSWKKLPD YSPPLSTLPTDSNKSLKIEWKGSPMDLSTDPLRNELHPAELVLAQTLRLPCDLYLDSKRR LFLEKVYRLKKGLPFRRTDAQKACRIDVNKASRLFQAFEKVGWLQDSNFTKYL P09201 D6VZ13 F16P_YEAST Fructose-1,6-bisphosphatase FBPase 3.1.3.11 D-fructose-1,6-bisphosphate 1-phosphohydrolase FBP1 YLR377C L8039.18 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c PROTEIN SEQUENCE OF 2-16; 83-97; 256-280; 289-306 AND 327-346 PROTEASOMAL DEGRADATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PROTEASOMAL DEGRADATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION PROTEASOMAL DEGRADATION DOMAIN PROTEASOMAL DEGRADATION MUTAGENESIS OF PRO-2 beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate Mg(2+) Binds 3 Mg(2+) ions per subunit. Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate (By similarity). Carbohydrate biosynthesis; gluconeogenesis. Homotetramer. The Pro/N-degron targets the protein for proteasomal degradation when cells are shifted to glucose-containing growth medium. Ubiquitinated (PubMed:22645139). Targeted for proteasomal degradation when cells are shifted to glucose-containing growth medium (PubMed:12686616, PubMed:18508925, PubMed:22645139, PubMed:28126757). Present with 589 molecules/cell in log phase SD medium. Belongs to the FBPase class 1 family. Allosteric enzyme Carbohydrate metabolism Complete proteome Direct protein sequencing Hydrolase Magnesium Metal-binding Phosphoprotein Reference proteome Ubl conjugation P S C D MPTLVNGPRRDSTEGFDTDIITLPRFIIEHQKQFKNATGDFTLVLNALQFAFKFVSHTIR RAELVNLVGLAGASNFTGDQQKKLDVLGDEIFINAMRASGIIKVLVSEEQEDLIVFPTNT GSYAVCCDPIDGSSNLDAGVSVGTIASIFRLLPDSSGTINDVLRCGKEMVAACYAMYGSS THLVLTLGDGVDGFTLDTNLGEFILTHPNLRIPPQKAIYSINEGNTLYWNETIRTFIEKV KQPQADNNNKPFSARYVGSMVADVHRTFLYGGLFAYPCDKKSPNGKLRLLYEAFPMAFLM EQAGGKAVNDRGERILDLVPSHIHDKSSIWLGSSGEIDKFLDHIGKSQ P60010 D6VTJ1 P02579 Q9P3X6 Q9P3X7 ACT_YEAST Actin ACT1 ABY1 END7 YFL039C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-58 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-57 NUCLEOTIDE SEQUENCE [GENOMIC DNA] Carlsbergensis NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-358 ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632 CBS 1907 ACETYLATION AT MET-1 PROTEIN SEQUENCE OF N-TERMINUS PROTEIN SEQUENCE OF 19-25 ATCC 38531 / Y41 MUTAGENESIS INTERACTION WITH YIH1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] INTERACTION WITH YIH1 IDENTIFICATION BY MASS-SPECTROMETRY LACK OF METHYLATION AT HIS-73 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-191 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] SUBUNIT MUTAGENESIS OF ARG-183 AND ARG-335 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (Probable). Treatments with Lantrunculin A, the microbial peptide Chondramide or the microbial metabolite Chivazole F inhibit actin polymerization (PubMed:28796488). Each actin can bind to 4 others. Interacts with YIH1 (via C-terminus); this interaction occurs in a GCN1-independent manner (PubMed:15126500, PubMed:21239490). Component of the INO80 complex. Component of the SWR1 complex. Component of the NuA4 complex. false 6 P46680 AIP1 false 3 Q03048 COF1 false 3 Q06440 CRN1 false 3 P0A6F5 groL true 5 P02829 HSP82 false 2 Q12446 LAS17 false 4 P07274 PFY1 false 4 P39743 RVS167 false 4 P32599 SAC6 false 4 P17555 SRV2 false 7 P12612 TCP1 false 3 Cytoplasm Cytoskeleton Belongs to the actin family. 3D-structure Acetylation ATP-binding Complete proteome Cytoplasm Cytoskeleton Direct protein sequencing Isopeptide bond Nucleotide-binding Reference proteome Ubl conjugation Y F R K R K I L G S MDSEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGIMVGMGQKDSYVGDEAQS KRGILTLRYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPMNPKSNREKMT QIMFETFNVPAFYVSIQAVLSLYSSGRTTGIVLDSGDGVTHVVPIYAGFSLPHAILRIDL AGRDLTDYLMKILSERGYSFSTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSSIEKSY ELPDGQVITIGNERFRAPEALFHPSVLGLESAGIDQTTYNSIMKCDVDVRKELYGNIVMS GGTTMFPGIAERMQKEITALAPSSMKVKIIAPPERKYSVWIGGSILASLTTFQQMWISKQ EYDESGPSIVHHKCF Q06338 D6VSY9 BCP1_YEAST Protein BCP1 BCP1 YDR361C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION BY THE PHO85-PCL1 KINASE COMPLEX PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND THR-209 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND THR-209 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in nuclear export of the lipid kinase MSS4 and of the 60S ribosomal subunit. May also play a role in directing MSS4 to the plasma membrane. Plays a role in actin cytoskeleton organization and vesicular transport. Cytoplasm Nucleus Phosphorylated by the PHO85-PCL1 kinase complex. Present with 4590 molecules/cell in log phase SD medium. Belongs to the BCP1 family. Complete proteome Cytoplasm Nucleus Phosphoprotein Protein transport Reference proteome Transport MVQAIKLNDLKNRKRKNVEEENGSDESEIDISSTDSENEEEQNGEEEIVNIDFDFFGGNP EVDFHALKNLLRQLFGPQESTRIQLSSLADLILGSPTTTIKTDGKESDPYCFLSFVDFKA NHLSDYVKYLQKVDMRLSTFFKTMIDSGNKNCALVLSERLINMPPEVVPPLYKITLEDVA TALGDDKHYDFYIIVTRKYEVNFDTDDDTDSGKRNKNKDERSKKRVKADEVDYFHEEDRF FEKYAKIHFESEAKKGVISSYMILDHEGLVKSIDELETEISTW P53286 D6VUS2 BTN2_YEAST Protein BTN2 Batten disease protein 2 BTN2 YGR142W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION FUNCTION INTERACTION WITH RHB1 SUBCELLULAR LOCATION INTERACTION WITH YIF1 FUNCTION INTERACTION WITH IST2 FUNCTION SUBCELLULAR LOCATION INTERACTION WITH TDA3 V-SNARE binding protein that facilitates specific protein retrieval from a late endosome to the Golgi. Modulates the rate of arginine uptake. Involved in pH homeostasis. Required for the correct localization of IST2. May be involved in ion homeostasis together with IST2. Interacts with RHB1, IST2, TDA3 and YIF1. P38250 IST2 false 2 P25378 RHB1 false 2 P53845 YIF1 false 2 Cytoplasm Late endosome Coiled coil Complete proteome Cytoplasm Endosome Reference proteome MFSIFNSPCVFEQLPSFSQPLHSRYFDCSSPVSYYPECKRRKAIKANLRAPKKSDANCSE PLRYALAETPNGYTLSLSKRIPYELFSKYVNEKLGELKENHYRPTYHVVQDFFGNQYYVE DEADEDALLRSALKDLDFRAIGKKIAKDLFQDYEIELNHRGDELSILSKKDKIFKEFSLD QVFEDVFVIGCGVENIDDGSREKYALLKIGLVKHEEEISEGGINEPKMPIIESKIDESHD DVNMSESLKEEEAEKAKEPLTKEDQIKKWIEEERLMQEESRKSEQEKAAKEDEERQKKEK EARLKARKESLINKQKTKRSQQKKLQNSKSLPISEIEASNKNNNSNSGSAESDNESINSD SDTTLDFSVSGNTLKKHASPLLEDVEDEEVDRYNESLSRSPKGNSIIEEI P14724 D6VTR9 CDC26_YEAST Anaphase-promoting complex subunit CDC26 Cell division control protein 26 CDC26 HIT3 SCD26 YFR036W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-54 P-28-24C SUBUNIT SUBUNIT SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. Protein modification; protein ubiquitination. The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. CDC26 is required to tether the essential subunits APC9, CDC27 and CDC16 to the complex. Nucleus Belongs to the CDC26 family. Was originally thought to be a suppressor of CDC26. Cell cycle Cell division Complete proteome Mitosis Nucleus Phosphoprotein Reference proteome Ubl conjugation pathway S F IREE TARNNSISAYAHAHAHAHASTFTFTYKISSL MIRRAPTTLQLSHDDVTSLIDDLNEQKLKQQLNIEKTKYFQGKNGGSLHSNTDFQDTSQN IEDNNNDNDNDIDEDDDMSSYNDKAASVAHTRVLNSLHLSTDSNTAHETSNANDNHNPFY IREE P38903 D6W281 2A5D_YEAST Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform PP2A, B subunit, B' delta isoform Protein RTS1 Protein SCS1 RTS1 SCS1 YOR014W OR26.04 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] SUBCELLULAR LOCATION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBUNIT PHOSPHORYLATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Multicopy suppressor of ROX3 and HSP60. PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory 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. Cytoplasm Nucleus Present with 300 molecules/cell in log phase SD medium. Belongs to the phosphatase 2A regulatory subunit B family. Complete proteome Cytoplasm Nucleus Phosphoprotein Reference proteome T S L F A R MMRGFKQRLIKKTTGSSSSSSSKKKDKEKEKEKSSTTSSTSKKPASASSSSHGTTHSSAS STGSKSTTEKGKQSGSVPSQGKHHSSSTSKTKTATTPSSSSSSSRSSSVSRSGSSSTKKT SSRKGQEQSKQSQQPSQSQKQGSSSSSAAIMNPTPVLTVTKDDKSTSGEDHAHPTLLGAV SAVPSSPISNASGTAVSSDVENGNSNNNNMNINTSNTQDANHASSQSIDIPRSSHSFERL PTPTKLNPDTDLELIKTPQRHSSSRFEPSRYTPLTKLPNFNEVSPEERIPLFIAKVDQCN TMFDFNDPSFDIQGKEIKRSTLDELIEFLVTNRFTYTNEMYAHVVNMFKINLFRPIPPPV NPVGDIYDPDEDEPVNELAWPHMQAVYEFFLRFVESPDFNHQIAKQYIDQDFILKLLELF DSEDIRERDCLKTTLHRIYGKFLSLRSFIRRSMNNIFLQFIYETEKFNGVAELLEILGSI INGFALPLKEEHKVFLVRILIPLHKVRCLSLYHPQLAYCIVQFLEKDPLLTEEVVMGLLR YWPKINSTKEIMFLNEIEDIFEVIEPLEFIKVEVPLFVQLAKCISSPHFQVAEKVLSYWN NEYFLNLCIENAEVILPIIFPALYELTSQLELDTANGEDSISDPYMLVEQAINSGSWNRA IHAMAFKALKIFLETNPVLYENCNALYLSSVKETQQRKVQREENWSKLEEYVKNLRINND KDQYTIKNPELRNSFNTASENNTLNEENENDCDSEIQ P16661 D6VQA9 ALG1_YEAST Chitobiosyldiphosphodolichol beta-mannosyltransferase 2.4.1.142 Asparagine-linked glycosylation protein 1 Beta-1,4-mannosyltransferase GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase GDP-mannose-dolichol diphosphochitobiose mannosyltransferase ALG1 YBR110W YBR0906 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] OLIGOMERIZATION INTERACTION WITH ALG2 AND ALG11 MUTAGENESIS OF GLU-278; GLY-310; HIS-356; ASP-363 AND ASP-370 Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER. GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + GDP + H(+) Protein modification; protein glycosylation. Homodimer. Interacts with ALG2 and ALG11. P53954 ALG11 false 2 P43636 ALG2 false 2 Endoplasmic reticulum membrane Single-pass type II membrane protein Present with 1890 molecules/cell in log phase SD medium. Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 33 subfamily. Complete proteome Endoplasmic reticulum Glycoprotein Glycosyltransferase Membrane Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix E K G D H Q D A D A MFLEIPRWLLALIILYLSIPLVVYYVIPYLFYGNKSTKKRIIIFVLGDVGHSPRICYHAI SFSKLGWQVELCGYVEDTLPKIISSDPNITVHHMSNLKRKGGGTSVIFMVKKVLFQVLSI FKLLWELRGSDYILVQNPPSIPILPIAVLYKLTGCKLIIDWHNLAYSILQLKFKGNFYHP LVLISYMVEMIFSKFADYNLTVTEAMRKYLIQSFHLNPKRCAVLYDRPASQFQPLAGDIS RQKALTTKAFIKNYIRDDFDTEKGDKIIVTSTSFTPDEDIGILLGALKIYENSYVKFDSS LPKILCFITGKGPLKEKYMKQVEEYDWKRCQIEFVWLSAEDYPKLLQLCDYGVSLHTSSS GLDLPMKILDMFGSGLPVIAMNYPVLDELVQHNVNGLKFVDRRELHESLIFAMKDADLYQ KLKKNVTQEAENRWQSNWERTMRDLKLIH P0CX12 D6VQU7 P38363 COS2_YEAST Protein COS2 COS2 YBR302C YBR2121 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A Membrane Multi-pass membrane protein Belongs to the DUP/COS family. Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MKENELKNEKSVDVLSFKQLESQKIVLPQDLFRSSFTWFCYEIYKSLAFRIWMLLWLPLS VWWKLSNNCIYPLIVSLLVLFLGPIFVLVICGLSRKRSLSKQLIQFCKEITENTPSSDPH DWEVVAANLNSYLYENNVWNTKYFFFNAMVCQEAFRTTLLEPFSLKKDKAAKVKSFKDSV PYIEEALGVYFTEVEKQWKLFNTEKSWSPVGLEDAKLPKEAYRFKLTWFLKRISNIFMLI PFLNFLCCIYVSRGMCLLLRTLYLGWILFMLVQGFQNIRVLIMSMEHKMQFLSTIINEQE SGANGWDEIARKMNRYLFEKKAWKNEEFFFDGIDCEWFFNHFFYRVLSAKKSMWPLPLNV ELWPYIKEAQLSRSEVLLV P08566 D6VSB3 ARO1_YEAST Pentafunctional AROM polypeptide 3-dehydroquinate synthase DHQS 4.2.3.4 3-phosphoshikimate 1-carboxyvinyltransferase 2.5.1.19 5-enolpyruvylshikimate-3-phosphate synthase EPSP synthase EPSPS Shikimate kinase SK 2.7.1.71 3-dehydroquinate dehydratase 3-dehydroquinase 4.2.1.10 Shikimate dehydrogenase 1.1.1.25 ARO1 AROM YDR127W YD9302.02 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 AND 1557-1588 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate 3-dehydroquinate = 3-dehydroshikimate + H2O NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH ATP + shikimate = 3-phosphoshikimate + ADP + H(+) 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate Zn(2+) Binds 2 Zn(2+) ions per subunit. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. Homodimer. P15108 HSC82 false 3 Cytoplasm Present with 6420 molecules/cell in log phase SD medium. In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family. In the 2nd section; belongs to the EPSP synthase family. In the 3rd section; belongs to the shikimate kinase family. In the 4th section; belongs to the type-I 3-dehydroquinase family. In the C-terminal section; belongs to the shikimate dehydrogenase family. Amino-acid biosynthesis Aromatic amino acid biosynthesis ATP-binding Complete proteome Cytoplasm Kinase Lyase Metal-binding Multifunctional enzyme NADP Nucleotide-binding Oxidoreductase Reference proteome Transferase Zinc MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFK ASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVA STFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAK REFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDI EAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVS IGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKM SIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVI PPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVE GHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTSSQKYIVLTGNARMQQRPIAPLVD SLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTL ALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSAT YPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKP LKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKF GVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERD EVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAG KTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYG DDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIR EVWNRREGWYKECSNFSFFAPHCSAEAEFQALRRSFSKYIATITGVREIEIPSGRSAFVC LTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRT MKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDF QGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTS KGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSR SPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDEL TDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRA ALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVP ADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQML VHQGVAQFEKWTGFKGPFKAIFDAVTKE P43542 D6VTG8 COS4_YEAST Protein COS4 COS4 YFL062W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c Membrane Multi-pass membrane protein Belongs to the DUP/COS family. Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MKENELKNEKSVDVLSFKQLESQKIVLPQDLFRSSFTWFCYEIYKSLAFRIWMLLWLPLS VWWKLSNNWIYPLMVSLLVLFWGPVFVLVIFRLSRKRSLSKQLTQFCKEITKSTPSSDPH DWEVVAANLNSYLYENKAWNIRYFFFNAMGCQEAFRTTLLEPFSLKKDEAAKVKSFKDSV PYIEEALGVYFREVEKQWKLFNSEKSWSPVGLEDAKLPKEAYRFKLTWFLKRISNIFMLI PFLNFLCCIYVSRGMCLLLRTLYLGWILFMLVQGFQNIRVLIMSMEHKMQFLSTIINEQE SGANGWDEIARKMNRYLFEKKVWKNEEFFFDGIDCEWFFSHFFYRVLSAKKSMRALSLNV ELWPYIKEAQLSCSEESLA P25373 D6VQY0 GLRX1_YEAST Glutaredoxin-1 Glutathione-dependent oxidoreductase 1 GRX1 YCL035C YCL35C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION INDUCTION INDUCTION FUNCTION BIOPHYSICOCHEMICAL PROPERTIES FUNCTION BIOPHYSICOCHEMICAL PROPERTIES LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION BIOPHYSICOCHEMICAL PROPERTIES MUTAGENESIS OF CYS-30 FUNCTION BIOPHYSICOCHEMICAL PROPERTIES MUTAGENESIS OF ASP-89 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE GLUTATHIONYLATION AT CYS-27 MUTAGENESIS OF CYS-30 X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE GLUTATHIONYLATION AT CYS-27 DISULFIDE BOND Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2. 0.88 mM for H(2)O(2) 0.52 mM for cumene hydroperoxide 0.37 mM for tert-butyl hydroperoxide 4.2 mM for 1-chloro-2,4-dinitrobenzene 1.3 mM for 1,2-dichloro-4-nitrobenzene 6.2 mM for reduced glutathione 110 umol/min/mg enzyme for H(2)O(2) 32.5 umol/min/mg enzyme for cumene hydroperoxide 7.5 umol/min/mg enzyme for tert-butyl hydroperoxide P34230 PXA2 false 2 Cytoplasm In response to heat shock and osmotic stress. Present with 3030 molecules/cell in log phase SD medium. Belongs to the glutaredoxin family. 3D-structure Complete proteome Cytoplasm Disulfide bond Electron transport Glutathionylation Isopeptide bond Redox-active center Reference proteome Transport Ubl conjugation C S D S MVSQETIKHVKDLIAENEIFVASKTYCPYCHAALNTLFEKLKVPRSKVLVLQLNDMKEGA DIQAALYEINGQRTVPNIYINGKHIGGNDDLQELRETGELEELLEPILAN Q06156 D6VYR9 CND1_YEAST Condensin complex subunit 1 XCAP-D2 homolog YCS4 LOC7 YLR272C L8479.14 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; BRN1 AND YCG1 FUNCTION SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRN1, YCS4 and YCG1/YCS5. Nucleus Chromosome Nuclear throughout the cell cycle. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. At anaphase, it is enriched at rDNA. Dissociation from chromosomes is observed in late telophase. Present with 2540 molecules/cell in log phase SD medium. Belongs to the CND1 (condensin subunit 1) family. Cell cycle Cell division Chromosome Complete proteome DNA condensation Mitosis Nucleus Phosphoprotein Reference proteome Repeat MSGFSLSEYLTKFQTTDRESYPRLQDPSRELNVIIDQLAVSPEQIDASPDSLEALIDLCH DFPHLTPKLQTQLSYLISSSLSNLSKDIKANLSSNVNFTEIGGLIPQWKRHLEEYGYLIQ VLLTFLQDELHKVSSQSTNLNRSAKNSKNDSANVELFKRDCNQMENLLESITKLLEINLS KIFQTTPEKDLFIGLFTRPLFVLLEIEPVTKVSSLKMFIQRILAMCVKNHGQSSSIQSSL MTNLTYFLHLSVFNAELLKLLNDEYNYPQLTEDILKEISTRVFNAKDTTGPKAISNFLIK LSELSPGIMLRQMNLVITLLNNSSITLRCSVVEACGNIVAELAQDPQTMEHYKQQIAVLI ELLEERFQDSNPYVRTKAIQGCSKICDLSSKFNKSKAKFTSLAVRSLQDRSSLVRRNSVK LLSKLLLKHPFKAIHGSQLRLSEWEEYLKGSESQLNSTLKKVESQETLNDTIERSLIEEE VEQDEGQCRTELEGSFNKSAELSRIENEVENINATNTSVLMKLKLMIVYYKDAISFIKEI HKSIELISNLLFSKNRNEVLESMDFLVLADAFDIELSEFGIKKMLHLVWMKGTNDEGTSI SVHLIECYKQLFLTAPDSCNMQEKAAHIAKNLINLSIGASIADLASLEQLLGMMYEQKLI DQHVINILWAIYNSASKASMQKEQNVNNRDSEKGFSKEQIHGSIIILGMLSLADNEIALK GLESLLNIGLGAVGLKDLTLCRYSCLALERMVPKRSTIITKAINQELEDVAVKKLYAIII NYTKDNEYYPMCEQALSALFTISSKPDILATDLIREKTMMTFGKPEEEDSILSLEQSSRV VSLSQLLFIVGQVAIKTLVYLEKCEAEFKKRKIEAETRNGKVKNQGADVTNTTQDNGGDK ELEMIGGTNEDDFTDAIQFVKENELLFGEKSILGKFCPIVEEIVSNSSRFSDPMLQRTAT LCLEKLMCLSSKYCEKSLPLLITVMEKSPDPTIRSNAVLGLGDMAVCFNNLVDENTDYLY RRLHDENLMVQRTCLMTVTFLILAGQVKVKGQLGEMAKCLDNPDQGISDMCRLFFTELAS KDNAIYNGFIDIFSNLSSDDLLGKESFKKIIKFLLTFIDKERHQKQLNEKLVGRLRKCET QKQWDDIAFVLNNLPYKNEDVTALLEQGFKVVSAKE P38170 D6VPQ8 Q6Q5G8 CND2_YEAST Condensin complex subunit 2 Barren homolog CAPH homolog BRN1 YBL097W YBL0830 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] S288c / FY1678 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION SEQUENCE REVISION TO 517 ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-754 ATCC 204508 / S288c IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC2; SMC4; YCG1 AND YCS4 FUNCTION FUNCTION SUBCELLULAR LOCATION INTERACTION WITH SMC2 IDENTIFICATION OF FRAMESHIFT LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-548 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase. Component of the condensin complex, which contains the SMC2 and SMC4 heterodimer, and three non SMC subunits that probably regulate the complex: BRN1, YCS4 and YCG1/YCS5. P38989 SMC2 false 2 Nucleus Cytoplasm Chromosome In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. Present with 704 molecules/cell in log phase SD medium. Belongs to the CND2 (condensin subunit 2) family. 3D-structure Cell cycle Cell division Chromosome Complete proteome Cytoplasm DNA condensation Mitosis Nucleus Phosphoprotein Reference proteome G A MTTQLRYENNDDDERVEYNLFTNRSTMMANFEEWIKMATDNKINSRNSWNFALIDYFYDL DVLKDGENNINFQKASATLDGCIKIYSSRVDSVTTETGKLLSGLAQRKTNGASNGDDSNG GNGEGLGGDSDEANIEIDPLTGMPISNDPDVNNTRRRVYNRVLETTLVEFETIKMKELDQ ELIIDPLFKKALVDFDEGGAKSLLLNTLNIDNTARVIFDASIKDTQNVGQGKLQRKEEEL IERDSLVDDENEPSQSLISTRNDSTVNDSVISAPSMEDEILSLGMDFIKFDQIAVCEISG SIEQLRNVVEDINQAKDFIENVNNRFDNFLTEEELQAAVPDNAEDDSDGFDMGMQQELCY PDENHDNTSHDEQDDDNVNSTTGSIFEKDLMAYFDENLNRNWRGREHWKVRNFKKANLVN KESDLLEETRTTIGDTTDKNTTDDKSMDTKKKHKQKKVLEIDFFKTDDSFEDKVFASKGR TKIDMPIKNRKNDTHYLLPDDFHFSTDRITRLFIKPGQKMSLFSHRKHTRGDVSSGLFEK STVSANHSNNDIPTIADEHFWADNYERKEQEEKEKEQSKEVGDVVGGALDNPFEDDMDGV DFNQAFEGTDDNEEASVKLDLQDDEDHKFPIRENKVTYSRVSKKVDVRRLKKNVWRSINN LIQEHDSRKNREQSSNDSETHTEDESTKELKFSDIIQGISKMYSDDTLKDISTSFCFICL LHLANEHGLQITHTENYNDLIVNYEDLATTQAAS P38111 D6VQD2 Q02580 ATR_YEAST Serine/threonine-protein kinase MEC1 2.7.11.1 ATR homolog DNA-damage checkpoint kinase MEC1 Mitosis entry checkpoint protein 1 MEC1 ESR1 SAD3 YBR136W YBR1012 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION INDUCTION NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION PHOSPHORYLATION OF RPA2 INTERACTION WITH LCD1 PHOSPHORYLATION OF LCD1 INTERACTION WITH LCD1 FUNCTION IDENTIFICATION AS A KINASE FUNCTION MUTAGENESIS OF ASP-2224 AND ASN-2229 FUNCTION INTERACTION WITH LCD1 PHOSPHORYLATION OF LCD1 MUTAGENESIS OF VAL-225; SER-552; LEU-781; PHE-1179; ASN-1700; ASP-2224 AND ASP-2243 FUNCTION FUNCTION FUNCTION FUNCTION PHOSPHORYLATION OF RTT107 FUNCTION PHOSPHORYLATION OF SLX4 FUNCTION OF THE MEC1-LCD1 COMPLEX PHOSPHORYLATION OF LCD1 AND RAD53 FUNCTION INTERACTION WITH LCD1; RFA1 AND RFA2 MUTAGENESIS OF 2360-MET--ILE-2362 AND 2367-PHE-TRP-2368 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited in complex with protein LCD1 by the single-strand-binding protein complex RPA to DNA lesions in order to initiate the DNA repair by homologous recombination, after the MRX-complex and TEL1 are displaced. Phosphorylates LCD1 and RPA2, a subunit of RPA, involved in DNA replication, repair and recombination. Phosphorylates RAD9, CHK1 and RAD53, which leads to the activation of the CHK1 and RAD53 kinases involved in DNA damage repair cascade. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, also involved in the regulation of DNA damage response mechanism. Phosphorylates also SLX4 and RTT107 which are proteins involved in genome stability. Required for cell growth and meiotic recombination. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Interacts with LCD1, which is required for localization MEC1 to the RPA complex. Interacts directly with the RPA subunits RFA1 and RFA2. P47027 DPB11 false 3 Q04377 LCD1 false 10 Nucleus Localizes to nuclear DNA repair foci in response to DNA double strand breaks. The recruitment to DNA lesion sites requires its interaction with LCD1 and the presence of the RPA complex on DNA. Induced during meiosis. Belongs to the PI3/PI4-kinase family. ATM subfamily. 3D-structure ATP-binding Chromatin regulator Complete proteome DNA damage DNA repair Kinase Meiosis Nucleotide-binding Nucleus Reference proteome Serine/threonine-protein kinase Transferase V G S P L S F S N S D A N K D E MYI AAA FW AA N D S P K Q L G MESHVKYLDELILAIKDLNSGVDSKVQIKKVPTDPSSSQEYAKSLKILNTLIRNLKDQRR NNIMKNDTIFSKTVSALALLLEYNPFLLVMKDSNGNFEIQRLIDDFLNISVLNYDNYHRI WFMRRKLGSWCKACVEFYGKPAKFQLTAHFENTMNLYEQALTEVLLGKTELLKFYDTLKG LYILLYWFTSEYSTFGNSIAFLDSSLGFTKFDFNFQRLIRIVLYVFDSCELAALEYAEIQ LKYISLVVDYVCNRTISTALDAPALVCCEQLKFVLTTMHHFLDNKYGLLDNDPTMAKGIL RLYSLCISNDFSKCFVDHFPIDQWADFSQSEHFPFTQLTNKALSIVYFDLKRRSLPVEAL KYDNKFNIWVYQSEPDSSLKNVTSPFDDRYKQLEKLRLLVLKKFNKTERGTLLKYRVNQL SPGFFQRAGNDFKLILNEASVSIQTCFKTNNITRLTSWTVILGRLACLESEKFSGTLPNS TKDMDNWYVCHLCDIEKTGNPFVRINPNRPEAAGKSEIFRILHSNFLSHPNIDEFSESLL SGILFSLHRIFSHFQPPKLTDGNGQINKSFKLVQKCFMNSNRYLRLLSTRIIPLFNISDS HNSEDEHTATLIKFLQSQKLPVVKENLVIAWTQLTLTTSNDVFDTLLLKLIDIFNSDDYS LRIMMTLQIKNMAKILKKTPYQLLSPILPVLLRQLGKNLVERKVGFQNLIELLGYSSKTI LDIFQRYIIPYAIIQYKSDVLSEIAKIMCDGDTSLINQMKVNLLKKNSRQIFAVALVKHG LFSLDILETLFLNRAPTFDKGYITAYLPDYKTLAEITKLYKNSVTKDASDSENANMILCS LRFLITNFEKDKRHGSKYKNINNWTDDQEQAFQKKLQDNILGIFQVFSSDIHDVEGRTTY YEKLRVINGISFLIIYAPKKSIISALAQISICLQTGLGLKEVRYEAFRCWHLLVRHLNDE ELSTVIDSLIAFILQKWSEFNGKLRNIVYSILDTLIKEKSDLILKLKPYTTLALVGKPEL GILARDGQFARMVNKIRSTTDLIPIFANNLKSSNKYVINQNLDDIEVYLRRKQTERSIDF TPKKVGQTSDITLVLGALLDTSHKFRNLDKDLCEKCAKCISMIGVLDVTKHEFKRTTYSE NEVYDLNDSVQTIKFLIWVINDILVPAFWQSENPSKQLFVALVIQESLKYCGLSSESWDM NHKELYPNEAKLWEKFNSVSKTTIYPLLSSLYLAQSWKEYVPLKYPSNNFKEGYKIWVKR FTLDLLKTGTTENHPLHVFSSLIREDDGSLSNFLLPYISLDIIIKAEKGTPYADILNGII IEFDSIFTCNLEGMNNLQVDSLRMCYESIFRVFEYCKKWATEFKQNYSKLHGTFIIKDTK TTNMLLRIDEFLRTTPSDLLAQRSLETDSFERSALYLEQCYRQNPHDKNQNGQLLKNLQI TYEEIGDIDSLDGVLRTFATGNLVSKIEELQYSENWKLAQDCFNVLGKFSDDPKTTTRML KSMYDHQLYSQIISNSSFHSSDGKISLSPDVKEWYSIGLEAANLEGNVQTLKNWVEQIES LRNIDDREVLLQYNIAKALIAISNEDPLRTQKYIHNSFRLIGTNFITSSKETTLLKKQNL LMKLHSLYDLSFLSSAKDKFEYKSNTTILDYRMERIGADFVPNHYILSMRKSFDQLKMNE QADADLGKTFFTLAQLARNNARLDIASESLMHCLERRLPQAELEFAEILWKQGENDRALK IVQEIHEKYQENSSVNARDRAAVLLKFTEWLDLSNNSASEQIIKQYQDIFQIDSKWDKPY YSIGLYYSRLLERKKAEGYITNGRFEYRAISYFLLAFEKNTAKVRENLPKVITFWLDIAA ASISEAPGNRKEMLSKATEDICSHVEEALQHCPTYIWYFVLTQLLSRLLHSHQSSAQIIM HILLSLAVEYPSHILWYITALVNSNSSKRVLRGKHILEKYRQHSQNPHDLVSSALDLTKA LTRVCLQDVKSITSRSGKSLEKDFKFDMNVAPSAMVVPVRKNLDIISPLESNSMRGYQPF RPVVSIIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCKKEDVRQDNQYMQFATTMDFL LSKDIASRKRSLGINIYSVLSLREDCGILEMVPNVVTLRSILSTKYESLKIKYSLKSLHD RWQHTAVDGKLEFYMEQVDKFPPILYQWFLENFPDPINWFNARNTYARSYAVMAMVGHIL GLGDRHCENILLDIQTGKVLHVDFDCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGT FKKSSEVTLALMRKNEVALMNVIETIMYDRNMDHSIQKALKVLRNKIRGIDPQDGLVLSV AGQTETLIQEATSEDNLSKMYIGWLPFW Q08058 D6W259 COQ10_YEAST Coenzyme Q-binding protein COQ10, mitochondrial COQ10 YOL008W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION INTERACTION WITH COENZYME Q SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY Required for the function of coenzyme Q in the respiratory chain. May serve as a chaperone or may be involved in the transport of Q6 from its site of synthesis to the catalytic sites of the respiratory complexes. Interacts with coenzyme Q. Mitochondrion inner membrane Peripheral membrane protein Matrix side Belongs to the COQ10 family. Complete proteome Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Transit peptide MVLIIRPSQTLILFRKAMLKPIGRYPLKRNFFGLSGTNHTIREQRYVLRKAINAPPSTVY AAVSEVAQYKEFIPYCVDSFVDKRNPVDNKPLIAGLRVGFKQYDEEFICNVTCKDTDHTY TVVAETISHNLFHLLISKWTIMPHPNRPNAAMVELLLRFKFKSRIYNSVSLIFAKTVTEL VMNAFAKRAYHLVRLAMLKPSSKEGSP Q12471 D6W1T3 6P22_YEAST 6-phosphofructo-2-kinase 2 6PF-2-K 2 2.7.1.105 Phosphofructokinase 2 II PFK27 YOL136C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] WA-1A NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-55 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Synthesis of fructose 2,6-bisphosphate. ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate + H(+) By glucose and fructose, but not by galactose or maltose. ATP-binding Complete proteome Isopeptide bond Kinase Nucleotide-binding Reference proteome Transferase Ubl conjugation MGGSSDSDSHDGYLTSEYNSSNSLFSLNTGNSYSSASLDRATLDCQDSVFFDNHKSSLLS TEVPRFISNDPLHLPITLNYKRDNADPTYTNGKVNKFMIVLIGLPATGKSTISSHLIQCL KNNPLTNSLRCKVFNAGKIRRQISCATISKPLLLSNTSSEDLFNPKNNDKKETYARITLQ KLFHEINNDECDVGIFDATNSTIERRRFIFEEVCSFNTDELSSFNLVPIILQVSCFNRSF IKYNIHNKSFNEDYLDKPYELAIKDFAKRLKHYYSQFTPFSLDEFNQIHRYISQHEEIDT SLFFFNVINAGVVEPHSLNQSHYPSTCGKQIRDTIMVIENFINHYSQMFGFEYIEAVKLF FESFGNSSEETLTTLDSVVNDKFFDDLQSLIESNGFA P40433 D6VVI0 6P21_YEAST 6-phosphofructo-2-kinase 1 6PF-2-K 1 2.7.1.105 Phosphofructokinase 2 I PFK26 YIL107C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c PARTIAL PROTEIN SEQUENCE LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] YAL6B PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-644; SER-652 AND SER-667 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Synthesis of fructose 2,6-bisphosphate. ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate + H(+) Phosphorylation results in the activation of the kinase activity. P11484 SSB1 false 2 Present with 1710 molecules/cell in log phase SD medium. ATP-binding Complete proteome Direct protein sequencing Kinase Nucleotide-binding Phosphoprotein Reference proteome Transferase A R G E MFKPVDFSETSPVPPDIDLAPTQSPHHVAPSQDSSYDLLSRSSDDKIDAEKGPHDELSKH LPLFQKRPLSDTPISSNWNSPGITEENTPSDSPENSATNLKSLHRLHINDETQLKNAKIP TNDTTDYMPPSDGANEVTRIDLKDIKSPTRHHKRRPTTIDVPGLTKSKTSPDGLISKEDS GSKLVIVMVGLPATGKSFITNKLSRFLNYSLYYCKVFNVGNTRRKFAKEHGLKDQDSKFF EPKNADSTRLRDKWAMDTLDELLDYLLEGSGSVGIFDATNTSRERRKNVLARIRKRSPHL KVLFLESVCSDHALVQKNIRLKLFGPDYKGKDPESSLKDFKSRLANYLKAYEPIEDDENL QYIKMIDVGKKVIAYNIQGFLASQTVYYLLNFNLADRQIWITRSGESEDNVSGRIGGNSH LTPRGLRFAKSLPKFIARQREIFYQNLMQQKKNNENTDGNIYNDFFVWTSMRARTIGTAQ YFNEDDYPIKQMKMLDELSAGDYDGMTYPEIKNNFPEEFEKRQKDKLRYRYPGIGGESYM DVINRLRPVITELERIEDNVLIITHRVVARALLGYFMNLSMGIIANLDVPLHCVYCLEPK PYGITWSLWEYDEASDSFSKVPQTDLNTTRVKEVGLVYNERRYSVIPTAPPSARSSFASD FLSRKRSNPTSASSSQSELSEQPKNSVSAQTGSNNTTLIGSNFNIKNENGDSRIPLSAPL MATNTSNNILDGGGTSISIHRPRVVPNQNNVNPLLANNNKAASNVPNVKKSAATPRQIFE IDKVDEKLSMLKNKSFLLHGKDYPNNADNNDNEDIRAKTMNRSQSHV P32943 D6VUP0 CGS6_YEAST S-phase entry cyclin-6 CLB6 YGR109C G5970 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] K1107 NUCLEOTIDE SEQUENCE [GENOMIC DNA] SEQUENCE REVISION TO C-TERMINUS NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c Involved in G1/S and or S phase progression. Interacts with CDC28. P00546 CDC28 false 3 Maximally expressed just before cell cycle start. Belongs to the cyclin family. Cyclin AB subfamily. Cell cycle Cell division Complete proteome Cyclin Reference proteome T S P S I M F L MNCIPSPISERKIQINNEDCIGKENAFHTIPRESSINLTPHSTNEKKVLSEVNSNKIDSL QLPRGKLQRDSTHLEKTRKRQLSNDSTDPIEPKTVKKIKCHQWKNLDSIEMDDPFMVAEY TDSIFSHLYEKEIQMLPTHNYLMDTQSPYHLKSSMRALLIDWLVEVHEKFHCLPETLFLA INLLDRFLSQNVVKLNKLQLLCITCLFIACKFEEVKLPKITNFAYVTDGAATVEGIRKAE LFVLSSLGYNISLPNPLNFIRRISKADNYCIETRNMAKFIMEYSICCNKFIHLKPSYLAA MSMYIARKIKNENSKWDETFIHYSGGIDIESDPAFKDFISELVEDIAVPDTNLDSLRLKY KKPKHGMVYFKVFDWCKQKR Q3E823 D6W3H9 COA2_YEAST Cytochrome c oxidase assembly factor 2 COA2 YPL189C-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c GENOME REANNOTATION FUNCTION INTERACTION WITH SHY1 SUBCELLULAR LOCATION Required for efficient assembly of cytochrome c oxidase in the mitochondrial inner membrane. Seems to be involved in the SHY1-mediated step of cytochrome c oxidase maturation. May aid in stabilizing an early COX1 intermediate containing the nuclear subunits COX5A and COX6. Mitochondrion inner membrane Peripheral membrane protein Matrix side Mitochondrial matrix soluble protein partially associated with the inner membrane. Belongs to the COA2 family. Complete proteome Membrane Mitochondrion Mitochondrion inner membrane Reference proteome MRAVTRNKIVNNLYFSTFLIAFASVAIGSVLPCPAHSVDSDSPAVQQHKLQLAHEQELKR KDALSKKI P36170 D6VXG3 FLO10_YEAST Flocculation protein FLO10 Flocculin-10 FLO10 YKR102W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c REVIEW FUNCTION FUNCTION REPEATS Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, glucose, maltose and sucrose. Also involved in cell-substrate adhesion, haploid invasive growth and diploid pseudohyphae formation. Secreted Cell wall Membrane Lipid-anchor GPI-anchor The number of the intragenic tandem repeats varies between different S.cerevisiae strains. There is a linear correlation between protein size and the extend of adhesion: the more repeats, the stronger the adhesion properties and the greater the fraction of flocculating cells (By similarity). Extensively O-glycosylated. The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity). Belongs to the flocculin family. Cell wall Complete proteome Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Repeat Secreted Signal MPVAARYIFLTGLFLLSVANVALGTTEACLPAGEKKNGMTINFYQYSLKDSSTYSNPSYM AYGYADAEKLGSVSGQTKLSIDYSIPCNGASDTCACSDDDATEYSASQVVPVKRGVKLCS DNTTLSSKTEKRENDDCDQGAAYWSSDLFGFYTTPTNVTVEMTGYFLPPKTGTYTFGFAT VDDSAILSVGGNVAFECCKQEQPPITSTDFTINGIKPWNADAPTDIKGSTYMYAGYYYPI KIVYSNAVSWGTLPVSVVLPDGTEVNDDFEGYVFSFDDNATQAHCSVPNPAEHARTCVSS ATSSWSSSEVCTECTETESTSYVTPYVTSSSWSSSEVCTECTETESTSTSTPYVTSSSSS SSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYVTSS SWSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYV TSSSSSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTST PYVTSSSWSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTS TSTPYATSSTGTATSFTASTSNTMTSLVQTDTTVSFSLSSTVSEHTNAPTSSVESNASTF ISSNKGSVKSYVTSSIHSITPMYPSNQTVTSSSVVSTPITSESSESSASVTILPSTITSE FKPSTMKTKVVSISSSPTNLITSYDTTSKDSTVGSSTSSVSLISSISLPSSYSASSEQIF HSSIVSSNGQALTSFSSTKVSSSESSESHRTSPTTSSESGIKSSGVEIESTSTSSFSFHE TSTASTSVQISSQFVTPSSPISTVAPRSTGLNSQTESTNSSKETMSSENSASVMPSSSAT SPKTGKVTSDETSSGFSRDRTTVYRMTSETPSTNEQTTLITVSSCESNSCSNTVSSAVVS TATTTINGITTEYTTWCPLSATELTTVSKLESEEKTTLITVTSCESGVCSETASPAIVST ATATVNDVVTVYSTWSPQATNKLAVSSDIENSASKASFVSEAAETKSISRNNNFVPTSGT TSIETHTTTTSNASENSDNVSASEAVSSKSVTNPVLISVSQQPRGTPASSMIGSSTASLE MSSYLGIANHLLTNSGISIFIASLLLAIV P32898 D6VT59 Q04068 CYM1_YEAST Mitochondrial presequence protease 3.4.24.- Cytosolic metalloprotease 1 Metalloprotease of 112 kDa CYM1 MOP112 YDR430C D9461.18 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-166 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION FUNCTION SUBCELLULAR LOCATION MUTAGENESIS OF HIS-84; GLU-87 AND HIS-88 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ATP-independent protease that degrades mitochondrial transit peptides after their cleavage both in intermembrane space and in matrix. Also degrades other unstructured peptides (By similarity). Zn(2+) Binds 1 zinc ion per subunit. Homodimer. Mitochondrion intermembrane space May also be present in the mitochondrial matrix. Present with 6140 molecules/cell in log phase SD medium. Belongs to the peptidase M16 family. PreP subfamily. Complete proteome Hydrolase Metal-binding Metalloprotease Mitochondrion Phosphoprotein Protease Reference proteome Zinc H Y E Q H Y MLRFQRFASSYAQAQAVRKYPVGGIFHGYEVRRILPVPELRLTAVDLVHSQTGAEHLHID RDDKNNVFSIAFKTNPPDSTGVPHILEHTTLCGSVKYPVRDPFFKMLNKSLANFMNAMTG PDYTFFPFSTTNPQDFANLRGVYLDSTLNPLLKQEDFDQEGWRLEHKNITDPESNIVFKG VVYNEMKGQISNANYYFWSKFQQSIYPSLNNSGGDPMKITDLRYGDLLDFHHKNYHPSNA KTFTYGNLPLVDTLKQLNEQFSGYGKRARKDKLLMPIDLKKDIDVKLLGQIDTMLPPEKQ TKASMTWICGAPQDTYDTFLLKVLGNLLMDGHSSVMYQKLIESGIGLEFSVNSGVEPTTA VNLLTVGIQGVSDIEIFKDTVNNIFQNLLETEHPFDRKRIDAIIEQLELSKKDQKADFGL QLLYSILPGWTNKIDPFESLLFEDVLQRFRGDLETKGDTLFQDLIRKYIVHKPCFTFSIQ GSEEFSKSLDDEEQTRLREKITALDEQDKKNIFKRGILLQEKQNEKEDLSCLPTLQIKDI PRAGDKYSIEQKNNTMSRITDTNGITYVRGKRLLNDIIPFELFPYLPLFAESLTNLGTTT ESFSEIEDQIKLHTGGISTHVEVTSDPNTTEPRLIFGFDGWSLNSKTDHIFEFWSKILLE TDFHKNSDKLKVLIRLLASSNTSSVADAGHAFARGYSAAHYRSSGAINETLNGIEQLQFI NRLHSLLDNEETFQREVVDKLTELQKYIVDTNNMNFFITSDSDVQAKTVESQISKFMERL PHGSCLPNGPKTSDYPLIGSKCKHTLIKFPFQVHYTSQALLGVPYTHKDGSALQVMSNML TFKHLHREVREKGGAYGGGASYSALAGIFSFYSYRDPQPLKSLETFKNSGRYILNDAKWG VTDLDEAKLTIFQQVDAPKSPKGEGVTYFMSGVTDDMKQARREQLLDVSLLDVHRVAEKY LLNKEGVSTVIGPGIEGKTVSPNWEVKEL Q08955 D6W3G9 CSM4_YEAST Chromosome segregation in meiosis protein 4 CSM4 YPL200W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION FUNCTION INTERACTION WITH MPS3 Involved in chromosome segregation during meiosis. Involved in meiotic telomere clustering (bouquet formation) and telomere-led rapid prophase movements. Interacts with MPS3. P47069 MPS3 false 2 Endoplasmic reticulum membrane Single-pass membrane protein Nucleus membrane Single-pass membrane protein Chromosome partition Complete proteome Endoplasmic reticulum Meiosis Membrane Nucleus Reference proteome Sporulation Transmembrane Transmembrane helix MMDGSITRKVTSTLSNQLATWKWKLQLSLLERKLATINNDYFLLQWELLFITNEVMKWKE MIAFLESQLFCTTQNFVAQETHDRETFQSLVDDYNKQLSENNLIISVLKSRPQLSSFPIY LSDEVCSHLKFVIAELNSLIIVFFISLVFLWVSIEV Q12013 D6W2A0 AKR2_YEAST Probable palmitoyltransferase AKR2 2.3.1.225 Ankyrin repeat-containing protein AKR2 AKR2 YOR034C OR26.25 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION IDENTIFICATION OF PROBABLE INITIATION SITE LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A May be involved in constitutive endocytosis of a-factor receptor STE3. hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein] Membrane Multi-pass membrane protein The DHHC domain is required for palmitoyltransferase activity. Present with 815 molecules/cell in log phase SD medium. Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily. It is uncertain whether Met-1 or Met-4 is the initiator. Acyltransferase ANK repeat Complete proteome Glycoprotein Lipoprotein Membrane Palmitate Reference proteome Repeat Transferase Transmembrane Transmembrane helix MTSMSIIDDENVKKTSNGAAVVTDVAQHAVSDSDNNKAQLLGDGSNTEYVVDIFIEAAKD GDLKVVKDVVESGAVDINNDRIDELSGLHWACINNRFSVAKFLLLRGANPNQAAGPGGAT ALHWAARYGNIYIVDLLLKHGADPTLKDEQGLNIMHFSVYSSNILLVVYVLYFVVNNNDN VDIDSKDNNNRTPLLWAAYQGDFLTVELLLKFGSTVAWTDNRGFNALHCALVGGDQRVIC DLILSGANFYERNNQKQDCFDLAEGMGTKSLFEQALQHHGYDRLGNQKDKLFKKSSHAQF TIFLSPFLLMVYIYLISLVLSPVLAIMLSLLVTVVMVNTLKKFVLPCLPRKNTYKVSLTR TPFFSGLFLSTFCFLIYIWTKKLYPYSVSDYTMKNVQFLVTSFLTVVLFLRLVRSDPGCL KTDDSLTSIQETIKQLIDLGKFDRENFCVETLERKPLRSKYSFFSGALVARYDHYCPWIY NDVGLKNHKLFVFFAVTVQYHMFLFMWLCLAYFKKTNYIYEQVEEYARCALLKNETLCKG SNYDPSTFFLFIWISVNFIWLGAMLIVQFFQILKGITTPELFILIKEEHKAKFINLIPFE NSIYTSESKGVEDSDMIPEGPSATTITHTISIDGLEPRNRRRAILSACFSMMGINQWLVT IKEIVGITHILHGQVPQQHHSSLLRSFLVTNHWKTNLTDFWLNSDVTAPLWQRFFYSSDT SKAMLGGTEVDYYELYEYPAREGEVLRPN Q00684 D6VTQ8 Q05180 Q05673 CDC14_YEAST Tyrosine-protein phosphatase CDC14 3.1.3.48 CDC14 OAF3 YFR028C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-421 FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES FUNCTION INTERACTION WITH SIC1 FUNCTION IN DEPHOSPHORYLATION OF CDH1; SIC1 AND SWI5 FUNCTION SUBUNIT FUNCTION SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION FUNCTION FUNCTION CATALYTIC ACTIVITY FUNCTION IN DEPHOSPHORYLATION OF SWI6 SUBCELLULAR LOCATION SUBCELLULAR LOCATION INTERACTION WITH CRM1 FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 FUNCTION IN DEPHOSPHORYLATION OF DBP2; SIC1 AND SLD2 FUNCTION IN DEPHOSPHORYLATION OF ASE1 SUBCELLULAR LOCATION INTERACTION WITH CDC5 SUBCELLULAR LOCATION FUNCTION INTERACTION WITH TOF2 FUNCTION IN DEPHOSPHORYLATION OF ACM1 SUBCELLULAR LOCATION INTERACTION WITH UTP7 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION FUNCTION FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] FUNCTION IN DEPHOSPHORYLATION OF INCENP FUNCTION IN DEPHOSPHORYLATION OF DSN1 FUNCTION SUBCELLULAR LOCATION SUBCELLULAR LOCATION FUNCTION IN DEPHOSPHORYLATION OF ORC2; ORC6; CDC6 AND MCM3 FUNCTION FUNCTION MUTAGENESIS OF ALA-280 MUTAGENESIS OF ASP-253 AND CYS-283 INTERACTION WITH BNI1; BNR1 AND KAR9 FUNCTION IN DEPHOSPHORYLATION OF BNI1; BNR1 AND KAR9 SUBCELLULAR LOCATION SUBCELLULAR LOCATION FUNCTION FUNCTION SUBCELLULAR LOCATION FUNCTION SUBCELLULAR LOCATION FUNCTION IN DEPHOSPHORYLATION OF INN1 FUNCTION IN DEPHOSPHORYLATION OF CHS2 FUNCTION SUBCELLULAR LOCATION Protein phosphatase which antagonizes mitotic cyclin-dependent kinase CDC28, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Inhibits transcription of ribosomal genes (rDNA) during anaphase and controls segregation of nucleolus by facilitating condensin targeting to rDNA chromatin in anaphase. Dephosphorylates SIC1, a CDC28 inhibitor, and SWI5, a transcription factor for SIC1, and induces degradation of mitotic cyclins, likely by dephosphorylating the activator of mitotic cyclin degradation, CDH1. Dephosphorylates the microtubule bundling factor ASE1 which is required to define a centered and focused mitotic spindle midzone that can drive continuous spindle elongation. Dephosphorylates the anaphase-promoting complex inhibitor ACM1, leading to its degradation. Facilitates INN1-CYK3 complex formation which promotes cytokinesis through the dephosphorylation of CDC28-phosphosphorylated INN1. Reverts also the inhibitory CDC28 phosphorylation of CHS2 for endoplasmic reticulum export, ensuring that septum formation is contingent upon chromosome separation and exit from mitosis. Additional substrates for CDC14 are the formins BNI1 and BNR1, as well as CDC6, DBP2, DSN1, INCENP, KAR9, MCM3, ORC2, ORC6, SLD2, and SWI6. Activity is inhibited by interaction with NET1 which sequesters it to the nucleolus. H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate 4 mM for p-nitrophenyl phosphate Optimum pH is 6.9. Component of the RENT (regulator of nucleolar silencing and telophase) complex which is composed of at least NET1, CDC14 and SIR2. Interacts with CDC5, CRM1, SIC1, TOF2 and UTP7. P35734 ASK1 false 2 Q01389 BCK1 false 4 P38041 BOI1 false 2 P53894 CBK1 false 5 P32562 CDC5 false 2 P38147 CHK1 false 2 P15790 CKA1 false 3 P19454 CKA2 false 3 P24870 CLB3 false 2 Q03898 FIN1 false 2 P53233 FMP48 false 2 P38785 GIC1 false 2 Q12329 HSP42 false 2 P21965 MCK1 false 2 Q02196 MET14 false 2 P47035 NET1 false 13 P38826 ORC6 false 2 P39940 RSP5 false 2 P38990 SAK1 false 2 P38634 SIC1 false 2 P06700 SIR2 false 5 P38283 SLI15 false 2 P06782 SNF1 false 2 P06784 STE7 false 2 P32944 SWE1 false 3 Q02208 TOF2 false 8 Q03785 VHS1 false 2 Nucleus Nucleolus Cytoplasm Bud neck Sequestered in the nucleolus for most of the cell cycle by the nucleolar proteins NET1 and TOF2, and is released into the nucleus and cytoplasm during anaphase. CDC55 maintains CDC14 sequestration in the nucleolus during early meiosis, which is essential for the assembly of the meiosis I spindle. In anaphase, the CDC14 early anaphase release (FEAR) network (including CDC5, ESP1, and SLK19), and the mitotic exit network (including the DBF2-MOB1 complex) coordinately trigger the release of CDC14 from the nucleolus. Present with 8550 molecules/cell in log phase SD medium. Belongs to the protein-tyrosine phosphatase family. Non-receptor class CDC14 subfamily. 3D-structure Cell cycle Cell division Complete proteome Cytoplasm Hydrolase Meiosis Mitosis Nucleus Phosphoprotein Protein phosphatase Reference proteome D A A V C S A P MRRSVYLDNTIEFLRGRVYLGAYDYTPEDTDELVFFTVEDAIFYNSFHLDFGPMNIGHLY RFAVIFHEILNDPENANKAVVFYSSASTRQRANAACMLCCYMILVQAWTPHQVLQPLAQV DPPFMPFRDAGYSNADFEITIQDVVYGVWRAKEKGLIDLHSFNLESYEKYEHVEFGDFNV LTPDFIAFASPQEDHPKGYLATKSSHLNQPFKSVLNFFANNNVQLVVRLNSHLYNKKHFE DIGIQHLDLIFEDGTCPDLSIVKNFVGAAETIIKRGGKIAVHCKAGLGRTGCLIGAHLIY TYGFTANECIGFLRFIRPGMVVGPQQHWLYLHQNDFREWKYTTRISLKPSEAIGGLYPLI SLEEYRLQKKKLKDDKRVAQNNIEGELRDLTMTPPSNGHGALSARNSSQPSTANNGSNSF KSSAVPQTSPGQPRKGQNGSNTIEDINNNRNPTSHANRKVVIESNNSDDESMQDTNGTSN HYPKVSRKKNDISSASSSRMEDNEPSATNINNAADDTILRQLLPKNRRVTSGRRTTSAAG GIRKISGSIKK P38179 D6VPS1 ALG3_YEAST Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase 2.4.1.258 Asparagine-linked glycosylation protein 3 Dol-P-Man-dependent alpha(1-3)-mannosyltransferase Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase HM-1 killer toxin resistance protein ALG3 RHK1 YBL082C YBL0720 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-406 FUNCTION CHARACTERIZATION VARIANT ALG3-1 FUNCTION CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-Dol. Sensitive to H.mrakii HM-1 killer toxin. alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + dolichyl beta-D-mannosyl phosphate = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + dolichyl phosphate + H(+) Protein modification; protein glycosylation. Endoplasmic reticulum membrane Multi-pass membrane protein Belongs to the glycosyltransferase 58 family. Complete proteome Endoplasmic reticulum Glycosyltransferase Membrane Reference proteome Transferase Transmembrane Transmembrane helix A V G R LGAIVASRCHQR FRGYRGQQVPSA S Q MEGEQSPQGEKSLQRKQFVRPPLDLWQDLKDGVRYVIFDCRANLIVMPLLILFESMLCKI IIKKVAYTEIDYKAYMEQIEMIQLDGMLDYSQVSGGTGPLVYPAGHVLIYKMMYWLTEGM DHVERGQVFFRYLYLLTLALQMACYYLLHLPPWCVVLACLSKRLHSIYVLRLFNDCFTTL FMVVTVLGAIVASRCHQRPKLKKSLALVISATYSMAVSIKMNALLYFPAMMISLFILNDA NVILTLLDLVAMIAWQVAVAVPFLRSFPQQYLHCAFNFGRKFMYQWSINWQMMDEEAFND KRFHLALLISHLIALTTLFVTRYPRILPDLWSSLCHPLRKNAVLNANPAKTIPFVLIASN FIGVLFSRSLHYQFLSWYHWTLPILIFWSGMPFFVGPIWYVLHEWCWNSYPPNSQASTLL LALNTVLLLLLALTQLSGSVALAKSHLRTTSSMEKKLN P21592 D6W3J6 COX10_YEAST Protoheme IX farnesyltransferase, mitochondrial 2.5.1.- Heme O synthase COX10 YPL172C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30 RZ49-1 FUNCTION Converts protoheme IX and farnesyl diphosphate to heme O. Mitochondrion membrane Multi-pass membrane protein Belongs to the UbiA prenyltransferase family. Complete proteome Heme biosynthesis Membrane Mitochondrion Reference proteome Transferase Transit peptide Transmembrane Transmembrane helix MSYFPRTYAHLMRNVLAHNKGNIYLQIGTQLHDTQIKIRFNGVRYISRNHGGKQQHINTA PIEFTPNFGYGDRTSNCNKKVESTAMKTLRCTDDISTSSGSEATTDASTQLPFNVKLVDP MVRKSKRPSHAISEGLNMKTLKKKVIMPYLQLTKPRLTILVMLSAICSYALSPYPASVNE LLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQAFEFAALIGTLGV SILYFGVNPTVAILGASNIALYGWAYTSMKRKHIINTWLGALVGMVPPLMGWAAASPLSH PGSWCLAGLLFAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNPLLNARVSLRYSILMFPLC FGLSYFNITDWYYQIDSGLINAWLTFWAFKFYWQQRINYSAKTLKDNVKFNKGLSVANIY ARKTFMASVLHLPAILILAIIHKKGRWDWIYPGEAKRPQERF P38356 D6VQT5 BSD2_YEAST Metal homeostatis protein BSD2 Bypass SOD defects protein 2 BSD2 YBR290W YBR2037 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION DISRUPTION PHENOTYPE MUTAGENESIS OF PRO-149 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION DISRUPTION PHENOTYPE FUNCTION DISRUPTION PHENOTYPE SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-312 IDENTIFICATION BY MASS SPECTROMETRY SUB592 TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-312 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Required for homeostasis of heavy metal ions such as cadmium, cobalt and copper. Controls metal ion transport and prevents metal hyperaccumulation by negatively regulating the SMF1 and SMF2 metal transport systems. Under manganese-replete conditions facilitates trafficking of SMF1 and SMF2 metal transporters to the vacuole where they are degraded. Endoplasmic reticulum Vacuole Membrane Multi-pass membrane protein Increased accumulation of copper, cadmium and cobalt ions and enhanced sensitivity to the toxic effects of copper and cadmium. Exhibits no additional sensitivity to manganese. SMF1 fails to enter the vacuole and is stabilized. Reverses the aerobic defects of yeast strains lacking superoxide dismutase (SOD). Concomitant deletion of SMF1 completely abolishes the ability of BSD2 deletion to suppress SOD deficiency and reverses the increased sensitivity to cadmium and copper. However cobalt ion hyperaccumulation is not suppressed. Present with 3070 molecules/cell in log phase SD medium. Belongs to the BSD2 family. Complete proteome Endoplasmic reticulum Isopeptide bond Membrane Reference proteome Stress response Transmembrane Transmembrane helix Transport Ubl conjugation Vacuole P S MPEQELLIGQEMNTLHAGSSTDGINVGNAGRTRDTQTGVEGETEIGSDEEDSIEDEGSSS GGNSTTERLVPHQLREQAARHIGKIGRHFNILDRLFKKRTQQSSDIQQGAMFDGVFSNLS AKPDTTETEGNNEQDIPPTYDEAAADMAPSYYGMDLNNSDIYYDEICIEGLPVGNIANLL WNIIVSTSFQFIGFLITYILHTSHAAKQGSRFGLGLTFIGYGYSMIPNDVTSKVGKNKSL NRMELEDPNEFDDVRLNSQSTTQDKFESHLNHGLDEEKQNIPWLAVFVAFLGLFITLKSI YDYIQVKKLEKKYLNQSQNQA P47041 D6VWC4 BIT61_YEAST Target of rapamycin complex 2 subunit BIT61 TORC2 subunit BIT61 61 kDa binding partner of TOR2 protein BIT61 YJL058C J1141 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION IDENTIFICATION IN TORC2 IDENTIFICATION BY MASS SPECTROMETRY INTERACTION WITH SLM1 AND SLM2 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-58; SER-59; SER-139 AND SER-144 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway. The target of rapamycin complex 2 (TORC2) is composed of at least AVO1, AVO2, BIT61, LST8, TOR2 and TSC11. TORC2 likely forms a homodimer. Contrary to TORC1, TORC2 does not bind to and is not sensitive to FKBP-rapamycin. P32600 TOR2 false 2 Cell membrane Peripheral membrane protein Cytoplasmic side Vacuole membrane Peripheral membrane protein Cytoplasmic side Present with 1960 molecules/cell in log phase SD medium. Belongs to the BIT61 family. Cell membrane Complete proteome Membrane Phosphoprotein Reference proteome Vacuole MTAEDILLRERTSTTTQRPVNSEQYLNVQLATAPVKNFQTTSEISRQTLVDTSNDDVYSI KNLKGSRNPISPSVSNVGFQSIFHTVDHPRSKVSVASNHSLRSNDNASAATSKSGSSQIG ESHSVDTVECSNNLSKKLSSDAISITQKSLHSTPSGRYMKGKASGFFNRRNRAHTTISSD PASFLTDSSTLHNSSHSFRNVIKNFFQNKSHRHIGQDAIEPAIPNSLSKFLHSSYGRHKS PSQFIHTNAGQLVDSGTSVYSLNVNPSGVNPNTIVEDPLSGTDPASPNPVSMLHDLLRNL PSLEANYKHFNSQELTTLTNNIWNIFCSNVAELFRTQRIWKLRAKIENFNEVLEFYCILK TDPRVTHSGMNRIISDLKEFLVSSLYNLENQIVFNYSNEDTINNALKRLGVIWRIFYQEV YYDLAAVLLPLDQSIREDGNSTVLKSGNESRTHINGNYSIGFLLLMCFRDSIVLPCYENF VNSNDGISKSFQLYIFNQEEESNVTETDKLTLLQCFGILSTIQSNDRNQRIIEELLAGIR MSI Q12287 D6VXZ3 COX17_YEAST Cytochrome c oxidase copper chaperone COX17 YLL009C L1343 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 24657 / D273-10B NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 2-6 CHARACTERIZATION SUBCELLULAR LOCATION CHARACTERIZATION IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] STRUCTURE BY NMR Copper chaperone for cytochrome c oxidase (COX). Binds two copper ions and deliver them to the Cu(A) site of COX. Mitochondrion intermembrane space Belongs to the COX17 family. 3D-structure Chaperone Complete proteome Copper Direct protein sequencing Disulfide bond Metal-binding Mitochondrion Reference proteome MTETDKKQEQENHAECEDKPKPCCVCKPEKEERDTCILFNGQDSEKCKEFIEKYKECMKG YGFEVPSAN P00410 A0A0A7NYF9 COX2_YEAST Cytochrome c oxidase subunit 2 1.9.3.1 Cytochrome c oxidase polypeptide II COX2 OXI1 Q0250 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] DS200/A1 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 24657 / D273-10B NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 96604 / S288c / FY1679 GENOME REANNOTATION ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-132 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-200 ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632 POST-TRANSLATIONAL CLEAVAGE COMPOSITION OF THE CYTOCHROME C OXIDASE COMPLEX POST-TRANSLATIONAL CLEAVAGE BY IMP1 Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1. 4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] + 2 H2O Cu cation Binds a copper A center. Cytochrome c oxidase is composed of 11 subunits: one copy each of COX1, COX2, COX3, COX4, COX5A or COX5B, COX6, COX7, COX9, COX12, COX13 and two copies of COX8. Q04935 COX20 false 3 Mitochondrion inner membrane Multi-pass membrane protein The N-terminal sequence of COX2 is processed by IMP1. Belongs to the cytochrome c oxidase subunit 2 family. 3D-structure Complete proteome Copper Electron transport Membrane Metal-binding Mitochondrion Mitochondrion inner membrane Oxidoreductase Reference proteome Respiratory chain Transmembrane Transmembrane helix Transport Y N MLDLLRLQLTTFIMNDVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYT IVMTYSKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILLYLCDEVISPAMTIKAI GYQWYWKYEYSDFINDSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVT AADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGACSELCGTGHANMPIKIEAVS LPKFLEWLNEQ Q04052 D6VT51 ARO80_YEAST Transcriptional activator ARO80 ARO80 YDR421W D9461.10 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CHARACTERIZATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 Transcription activator required for the expression of genes involved in the catabolism of aromatic amino acids such as the aromatic aminotransferase II ARO9 and the phenylpyruvate decarboxylase ARO10. Nucleus Present with 319 molecules/cell in log phase SD medium. Branched-chain amino acid catabolism Complete proteome DNA-binding Metal-binding Nucleus Phenylalanine catabolism Reference proteome Transcription Transcription regulation Tryptophan catabolism Tyrosine catabolism Zinc MSAKKRPSGNAAFELPKRRRTYQACISCRSRKVKCDLGPVDNPHDPPCARCKRELKKCIF SSNKGTSNDLPPNSINAISLPSLGKSKQEIQNDSTSPILSDVPLSRKGISSEKSFKSEGM KWKLELSSMQNALEFLAQAAGTVAKEGAKEIIKEKSTTPKPLKSSLDATNKSATDEGLKR LSKSDSTNTLYENTADMLNHTLNTNRKTSQLMEEIGKVRPPPTRKIDDFDYIGPDSLLTK EEAIELIEAFFLTMHPFFPNIPLQLHDPKELAEYPILFCAILTVSARYHPFDTLGLDNGE DGMRHIEVHDKLWVYCQKLISQTIWAEASTRSIGTVLAFIIFTEWNPRSIHYKWSDYAND PELNNVNARGSKNISTRKDEEGLTGVGAIRRSDRMSWMLTGSAVRLAQDMGFIENSSKVF IVTHISETTSAMNMNQRSLLAESFSVLNLNLGKIENDGNESNEDYLGNEKFYLNEILPDE ESKLRWKRVFENSENDHDNEKNFLTDWEREFLNDEYVLYYSNKKDDTNLAQNHIPPFPLR FSFAQRAKIEIIRILSIAYETIYCEKNKRKLATTDQRHNLSVLSVFSPLIEGWLSNYREL LVPLSDVPFSLADRKNKKQIFDNIDRINGESIITDFNYCQLYIFSLALQVDGKTSRLNMN EIVTSARYVELAYRSAKEILSSAKRVSRQGMLKYMPVRWVIRIIRSIAFIVKCYLTLTGS ELATNPDARNILKLSAISVDETFDIIRDTAVTLKEATPDELHLCQRYAAILMYLCTEMKL RKKSYLERPPLLRDGTTPLESNRESSLEGQDLTKKPIFSKRIGYNKTETTFEPSERPLTE EINSNSQNSNDTSSKGIVDPFVEQNNDITTALLNNELFQGPSLSDEVTDWFGASEDIGLE FVEPWTELIEQRYMQCGDGDNNNFENLYNLFVNSNNINNDINNSRPITRK Q06705 D6VZ15 Q6B265 CSR1_YEAST Phosphatidylinositol transfer protein CSR1 CHS5 SPA2 rescue protein 1 SEC14 homolog protein 2 CSR1 SFH2 YLR380W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION FUNCTION PHOSPHATIDYLINOSITOL-BINDING SUBCELLULAR LOCATION FUNCTION FUNCTION SUBCELLULAR LOCATION FUNCTION INTERACTION WITH TSA2 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] YAL6B FUNCTION FUNCTION Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Activates SPO14/PLD1 (phospholipase D1) by stimulating phosphoinositide synthesis via the STT4 PtdIns 4-kinase. Modulates ArfGAP function through effects on SPO14 activity. Inhibits phosphatidylcholine degradation by PLB1 (phospholipase B1). May also regulate post-Golgi membrane-trafficking events and have a role resistance to oxidative stress. Forms a complex with 2 TSA2 subunits. Binds phosphatidylinositol (PtdIns). Cytoplasm Endosome Present with 9600 molecules/cell in log phase SD medium. Belongs to the PITP family. Acetylation Complete proteome Cytoplasm Endosome Lipid degradation Lipid metabolism Lipid transport Phospholipid degradation Phospholipid metabolism Phosphoprotein Reference proteome Transport Q H MSFDRQLTEDQEVVLKQIWTHLFHLWQVPVDGTHIFPNNSLHSSSTPAKKKKSSWFSKLQ SSDHTQDSSEAAEAAHLYEKGKIHKALANLDPQTTKKQFWHDIKNETPDATILKFIRARK WNADKTIAMLGHDLYWRKDTINKIINGGERAVYENNETGVIKNLELQKATIQGYDNDMRP VILVRPRLHHSSDQTEQELEKFSLLVIEQSKLFFKENYPASTTILFDLNGFSMSNMDYAP VKFLITCFEAHYPESLGHLLIHKAPWIFNPIWNIIKNWLDPVVASKIVFTKNIDELHKFI QPQYIPRYLGGENDNDLDHYTPPDGSLDVHLKDTETRAMIEKEREELVEQFLTVTAQWIE HQPLNDPAYIQLQEKRVQLSTALCENYSKLDPYIRSRSVYDYNGSLKV P53309 D6VV22 AP18B_YEAST Clathrin coat assembly protein AP180B YAP1802 YGR241C G8610 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION INTERACTION WITH CHC1; CLC1 AND PAN1 FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-449 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-282 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in endocytosis and clathrin cage assembly. Interacts with PAN1 and the clathrin heavy and light chains CHC1 and CLC1. Bud Bud neck Cell membrane Peripheral membrane protein Cytoplasmic side Cytoplasm Present with 6800 molecules/cell in log phase SD medium. Belongs to the AP180 family. Cell membrane Complete proteome Cytoplasm Endocytosis Isopeptide bond Membrane Phosphoprotein Reference proteome Ubl conjugation MSSLYTKLVKGATKIKMAPPKQKYVDPILSGTSSARGLQEITHALDIRLSDTAWTIVYKA LIVLHLMIQQGEKDVTLRHYSHNLDVFQLRKISHTTKWSSNDMRALQRYDEYLKTRCEEY GRLGMDHLRDNYSSLKLGSKNQLSMDEELDHVESLEIQINALIRNKYSVSDLENHLLLYA FQLLVQDLLGLYNALNEGVITLLESFFELSIEHAKRTLDLYKDFVDMTEYVVRYLKIGKA VGLKIPVIKHITTKLINSLEEHLREETKRQRGEPSEPQQDRKPSTAISSTSSHNNNSNDK NKSIAQKKLEQIREQKRLLEQQLQNQQLLISPTVPQDAYNPFGSQQQDLNNDTFSFEPTQ PQMTAQVPQPTANPFLIPQQQQQALQLTSASTMPQPSEIQITPNLNNQQTGMYASNLQYT PNFTGSGFGGYTTTENNAIMTGTLDPTKTGSNNPFSLENIAREQQQQNFQNSPNPFTLQQ AQTTPILAHSQTGNPFQAQNVVTSPMGTYMTNPVAGQLQYASTGAQQQPQMMQGQQTGYV MVPTAFVPINQQQQQQQHQQENPNLIDI P38818 D3DL59 Q66R84 CTM1_YEAST Cytochrome c lysine N-methyltransferase 1 2.1.1.59 CTM1 YHR109W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION ENZYME ACTIVITY SUBCELLULAR LOCATION DOMAIN Methyltransferase which mediates trimethylation of 'Lys-78' of cytochrome c (CYC1). L-lysyl-[cytochrome c] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[cytochrome c] + S-adenosyl-L-homocysteine Cytoplasm Cytosol The SET-like region, although related with the SET domain is not detected by any prediction method. Present with 2940 molecules/cell in log phase SD medium. Belongs to the class V-like SAM-binding methyltransferase superfamily. Complete proteome Cytoplasm Methyltransferase Reference proteome S-adenosyl-L-methionine Transferase K R MEEVFRFYSNSRNIFIHKSLSLKPSTIDDPKSGYGLFVEPSKFKNDELKSETIQLLRIPK RCTFNINTLLALLGDEDEFSSKEEFQRTNDKIKIALREIMAHPNFSVFLTETNLLIIYFM IFQTIRSRYEIPENIQYYLENVLMSIEVETAMDSIENLATDYGHYPQIFGLRETLNLFKE LFHDVLNLSDIKHLYSAIISRCLEIPERADTKSEEFTVHSTLVPIVDFANHEGTQKNAYF DIDPSNNDVLLLLDTKAVQSELTKPIEVFISYSPTEDLFSMLVTYGFTPDFRGNSQFWTV SFDRCFLRNYDGPDKTTNLRLFYKWMHINPVVPLVKYEHNGKTRWFLNDTTPEFDMLLLP FIPSIDDGKIARWAYDSTCHLMFTKIHCLINPEANEHALMIAENYRSLIKEKESNGDDFI NLPPLAWSLRYKDTENDCVRQRHICSEDAVAVLKQEEMQDSTKTKSQFTSFFRKFLEFRR SKIIRPTSDSKVASILYQQELEIIADLAKAIDSSSTIFFSDLNVTLDTEPERLPPLRFLD DYIEISADKQEPSPICEDLSYYTPSRFTDFFQEEVSQYAAFFQDD P37020 D6VWL1 GEF1_YEAST Anion/proton exchange transporter GEF1 CLC protein GEF1 ClC-A ClC-Y1 Voltage-gated chloride channel GEF1 N-terminal GEF1 C-terminal GEF1 CLCY1 YJR040W J1616 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION FUNCTION SUBCELLULAR LOCATION FUNCTION CLEAVAGE BY KEX2 SUBCELLULAR LOCATION INTERACTION WITH GET3 TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A FUNCTION Anion/proton exchange transporter involved in iron and copper cation homeostasis. Involved in intracellular iron metabolism during growth on fermentable and non fermentable carbon sources. Required for proper copper-loading and maturation of multicopper oxidase FET3. Important for adjusting intracellular compartment pH to more alkaline pH under iron limitation. May also transport chloride ions through the plasma membrane. Homodimer (By similarity). Interacts with GET3. Q12154 GET3 false 6 Golgi apparatus membrane Multi-pass membrane protein Endosome membrane Multi-pass membrane protein Prevacuolar compartment membrane Multi-pass membrane protein Proteolytically processed in the secretory pathway by protease KEX2 within the first extracellular loop. However, both the N- and C-terminal products of the cleavage reaction are required for assembly of a functional channel. Belongs to the chloride channel (TC 2.A.49) family. Was originally thought to be a voltage-gated ClC-type chloride channel. CBS domain Chloride Chloride channel Complete proteome Endosome Golgi apparatus Ion channel Ion transport Membrane Reference proteome Repeat Transmembrane Transmembrane helix Transport G R F L S T I L T I MPTTYVPINQPIGDGEDVIDTNRFTNIPETQNFDQFVTIDKIAEENRPLSVDSDREFLNS KYRHYREVIWDRAKTFITLSSTAIVIGCIAGFLQVFTETLVNWKTGHCQRNWLLNKSFCC NGVVNEVTSTSNLLLKRQEFECEAQGLWIAWKGHVSPFIIFMLLSVLFALISTLLVKYVA PMATGSGISEIKVWVSGFEYNKEFLGFLTLVIKSVALPLAISSGLSVGKEGPSVHYATCC GYLLTKWLLRDTLTYSSQYEYITAASGAGVAVAFGAPIGGVLFGLEEIASANRFNSSTLW KSYYVALVAITTLKYIDPFRNGRVILFNVTYDRDWKVQEIPIFIALGIFGGLYGKYISKW NINFIHFRKMYLSSWPVQEVLFLATLTALISYFNEFLKLDMTESMGILFHECVKNDNTST FSHRLCQLDENTHAFEFLKIFTSLCFATVIRALLVVVSYGARVPAGIFVPSMAVGATFGR AVSLLVERFISGPSVITPGAYAFLGAAATLSGITNLTLTVVVIMFELTGAFMYIIPLMIV VAITRIILSTSGISGGIADQMIMVNGFPYLEDEQDEEEEETLEKYTAEQLMSSKLITINE TIYLSELESLLYDSASEYSVHGFPITKDEDKFEKEKRCIGYVLKRHLASKIMMQSVNSTK AQTTLVYFNKSNEELGHRENCIGFKDIMNESPISVKKAVPVTLLFRMFKELGCKTIIVEE SGILKGLVTAKDILRFKRIKYREVHGAKFTYNEALDRRCWSVIHFIIKRFTTNRNGNVI P43550 D6VTH7 DAK2_YEAST Dihydroxyacetone kinase 2 DHA kinase 2 2.7.1.28 2.7.1.29 Glycerone kinase 2 Triokinase 2 Triose kinase 2 DAK2 YFL053W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde. ATP + dihydroxyacetone = ADP + dihydroxyacetone phosphate + H(+) ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate + H(+) Polyol metabolism; glycerol fermentation; glycerone phosphate from glycerol (oxidative route): step 2/2. Belongs to the dihydroxyacetone kinase (DAK) family. ATP-binding Complete proteome Glycerol metabolism Kinase Nucleotide-binding Reference proteome Transferase MSHKQFKSDGNIVTPYLLGLARSNPGLTVIKHDRVVFRTASAPNSGNPPKVSLVSGGGSG HEPTHAGFVGEGALDAIAAGAIFASPSTKQIYSAIKAVESPKGTLIIVKNYTGDIIHFGL AAERAKAAGMKVELVAVGDDVSVGKKKGSLVGRRGLGATVLVHKIAGAAASHGLELAEVA EVAQSVVDNSVTIAASLDHCTVPGHKPEAILGENEYEIGMGIHNESGTYKSSPLPSISEL VSQMLPLLLDEDEDRSYVKFEPKEDVVLMVNNMGGMSNLELGYAAEVISEQLIDKYQIVP KRTITGAFITALNGPGFGITLMNASKAGGDILKYFDYPTTASGWNQMYHSAKDWEVLAKG QVPTAPSLKTLRNEKGSGVKADYDTFAKILLAGIAKINEVEPKVTWYDTIAGDGDCGTTL VSGGEALEEAIKNHTLRLEDAALGIEDIAYMVEDSMGGTSGGLYSIYLSALAQGVRDSGD KELTAETFKKASNVALDALYKYTRARPGYRTLIDALQPFVEALKAGKGPRAAAQAAYDGA EKTRKMDALVGRASYVAKEELRKLDSEGGLPDPGAVGLAALLDGFVTAAGY P21623 D6VT35 DIT1_YEAST Spore wall maturation protein DIT1 DIT1 YDR403W D9509.21 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204510 / AB320 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CHARACTERIZATION Involved in spore wall maturation. Catalyzes a two step reaction that leads to the LL-dityrosine containing precursor of the spore wall. Sporulation. Complete proteome Reference proteome Sporulation F S MTFTSNLPSSSEQSISPPASSFSSSTDTLKDIDIPHNGADLSTYSKFLALYCRSDKCDDF YSLEEKQNCKFGDQWLDFINTIHNLDFSESEVSGRVSERILPASLANKFTNNLGVAIKIS EYTRDDERQIRGCVTTVENENSFNNWFVYHILDQSQLSLSEHPIVTKEVKYHELFADFFE KNLKNTIVNDQWNFGGRDYFIERSRYFTDRYLRIECILPAFPCKSSNEQKVYGSVPDKGE ELALKRLIKATQDLVKIYPPGMKIWIVSDGHVFSDCIGVDDDVVSTYTTKLHELYKRVAI PGVDAIGFCGLNDLFFSGAASKVFDPKWVSDVEVAHYTGTQICPKSDLSRQILMKGCDTD AGRLRKQIAIEGHPRLHLYRGFSRFMMEDLSLLEHFQSYSRKKFKKIISMIAFNMIKRND AYSNLVELIFPHHLRISIHAHTNSGPKFGIKVISNEQCSIVSSLEDLDEPKFEDFLHIPT PWHNCVVKVEDEKEKYFLTKSKVVKEALEKGMYDGVWKDTRFDIGEGGHFVIKKIS Q12748 D6VZ16 Q7LHY6 CENPI_YEAST Inner kinetochore subunit CTF3 CENP-I homolog Chromosome loss protein 3 Chromosome transmission fidelity protein 3 Constitutive centromere-associated network protein CTF3 CTF3 CHL3 YLR381W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 538-733 AB1-4A/8/55 IDENTIFICATION BY MASS SPECTROMETRY COMPONENT OF CTF19 COMPLEX INTERACTION WITH CTF19; MCM16 AND MCM22 SUBCELLULAR LOCATION INTERACTION WITH CHL4 AND CTF19 SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION IN CCAN SUBUNIT ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Component of the central kinetochore, which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle-microtubule attachments and proper chromosome segregation. Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly. Component of the heterotrimeric kinetochore subcomplex CTF3, which consists of CTF3, MCM16 and MCM22 (PubMed:11782448). The CTF3 subcomplex is part of a larger constitutive centromere-associated network (CCAN) (also known as central kinetochore CTF19 complex in yeast), which is composed of at least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (PubMed:12408861, PubMed:22561346). Interacts with CTF19 (PubMed:11782448, PubMed:12589047). Interacts with CHL4 (PubMed:12589047). Q02732 CTF19 false 3 Q12262 MCM16 false 3 P47167 MCM22 false 2 Nucleus Chromosome Centromere Kinetochore Associated with kinetochores. Present with 319 molecules/cell in log phase SD medium. Belongs to the CENP-I/CTF3 family. 3D-structure Acetylation Cell cycle Cell division Centromere Chromosome Complete proteome Kinetochore Meiosis Mitosis Nucleus Reference proteome MSLILDDIILSLTNANERTPPQALKTTLSLLYEKSKQYGLSSPQLQALVRLLCETSIIDT VTKVYIVENCFLPDGYLTKELLLEIINHLGTPTVFSRYRIQTPPVLQSALCKWLVHVYFL FPVHSEREHNISSSIWLHLWQFSFLQKWITPLVIWQATTPVDVKPWKLSIIKRCAMHPGY RDAPGSATLILQRFQCLVGASSQITESIITINCNRKTLKSHRNLKLDAHFLSILKRILSR AHPANFPADTVQNTIDMYLSEIHQLGADSIYPLRLQSLPEYVPSDSTVSLWDVTSLEQLA QNWPQLHIPNDVDYMMKPSLNSNVLLPRKVMSRDSLKHLYSSIILIKNSRDESSSPYEWC IWQLKRCFAHQIETPQEVIPIIISVSSMDNKLSSRIIQTFCNLKYLKLDELTLKKVCGGI LPLWKPELISGTREFFVKFMASIFMWSTRDGHDNNCTFSETCFYVLQMITNWVLDDKLIA LGLTLLHDMQSLLTLDKIFNNATSNRFSTMAFISSLDILTQLSKQTKSDYAIQYLIVGPD IMNKVFSSDDPLLLSAACRYLVATKNKLMQYPSTNKFVRMQNQYIMDLTNYLYRNKVLSS KSLFGVSPDFFKQILENLYIPTADFKNAKFFTITGIPALSYICIIILRRLETAENTKIKF TSGIINEETFNNFFRVHHDEIGQHGWIKGVNNIHDLRVKILMHLSNTANPYRDIAAFLFT YLKSLSKYSVQNS P39970 D3DLU6 ACA1_YEAST ATF/CREB activator 1 ACA1 YER045C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION FUNCTION FUNCTION FUNCTION INDUCTION Transcriptional activator of promoters containing ATF/CREB sites. Can independently stimulate transcription through ATF/CREB sites. Important for a variety of biological functions including growth on non-optimal carbon sources. Regulates the expression of COS8. Has efficient silencing blocking activities. Nucleus By nitrogen limitation. Belongs to the bZIP family. This ORF was incorrectly assigned as MEI4. Complete proteome DNA-binding Nucleus Reference proteome Transcription Transcription regulation MDYKHNFATSPDSFLDGRQNPLLYTDFLSSNKELIYKQPSGPGLVDSAYNFHHQNSLHDR SVQENLGPMFQPFGVDISHLPITNPPIFQSSLPAFDQPVYKRRISISNGQISQLGEDLET VENLYNCQPPILSSKAQQNPNPQQVANPSAAIYPSFSSNELQNVPQPHEQATVIPEAAPQ TGSKNIYAAMTPYDSNIKLNIPAVAATCDIPSATPSIPSGDSTMNQAYINMQLRLQAQMQ TKAWKNAQLNVHPCTPASNSSVSSSSSCQNINDHNIENQSVHSSISHGVNHHTVNNSCQN AELNISSSLPYESKCPDVNLTHANSKPQYKDATSALKNNINSEKDVHTAPFSSMHTTATF QIKQEARPQKIENNTAGLKDGAKAWKRARLLERNRIAASKCRQRKKMSQLQLQREFDQIS KENTMMKKKIENYEKLVQKMKKISRLHMQECTINGGNNSYQSLQNKDSDVNGFLKMIEEM IRSSSLYDE Q2V2Q1 D6VQV8 ADF1_YEAST Antisense of depressing factor protein 1 ADF1 YCL058W-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c GENOME REANNOTATION IDENTIFICATION OF PROBABLE INITIATION SITE FUNCTION SUBCELLULAR LOCATION Transcriptional repressor which negatively regulates transcription of FYV5 by binding to the promoter on the sense strand. Nucleus Encoded by the antisense strand of the FYV5 gene. Belongs to the ADF1 family. Complete proteome Nucleus Reference proteome Transcription Transcription regulation MGKCSMKKKGVGKNVGVGKKVQKKRSISTAERKRTKLQVEKLNKSSETMIPTLLREASTQ EPAKLKAETTLKAEELIKDQEKDSKVREQIRTEKSKTNDSMLKQIEMISGFSL P16639 D6VUC0 ATE1_YEAST Arginyl-tRNA--protein transferase 1 Arginyltransferase 1 R-transferase 1 2.3.2.8 Arginine-tRNA--protein transferase 1 ATE1 YGL017W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 46191 / IL125-2B NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity). an N-terminal L-alpha-aminoacyl-[protein] + L-arginyl-tRNA(Arg) = H(+) + N-terminal L-arginyl-L-amino acid-[protein] + tRNA(Arg) Cytoplasm Present with 2030 molecules/cell in log phase SD medium. Belongs to the R-transferase family. Acyltransferase Complete proteome Cytoplasm Reference proteome Transferase Ubl conjugation pathway T S Y I MSDRFVIWAPSMHNEPAAKCGYCHGNKGGNMDQLFALDSWAHRYMNKMDVVKIENCTIGS FVEHMDVATYDRMCNMGFRRSGKFLYKVDPLRNCCRLYTIRTAPQELNMTKELKKCISRF ATRITSEDYCPAAVASSDFVGKIVNAEMNSKTFYTRFEPALYSEEKYHLFVKYQEKVHQD YNNSPKSFKRFLCDTPFGPEAVLGTQESWEQLNNWQRMKPGEKLKHMGPVHECYYYEGKL IAITVSDILPSGISSVYFIWDPDYSKWSLGKLSALRDLAIIQRTNLQYYYLGYYIEDCPK MNYKANYGAEVLDVCHSKYIPLKPIQDMISRGKLFVIGEEETKVTKELYLVDSETGRGEG FPTDNVVKYKNIAEEIYGVGGCAFKSANESALELKELYGIPYEEEDLDTIYHLKEHNGHA PNGIPNVVPGLLPLWELLDIMQSGKITDLEGRLFLFEIETEGIRPLINFYSEPPNVKKRI CDVIRLFGFETCMKAVILYSEQM Q06549 D6VYP3 CDD_YEAST Cytidine deaminase CDA 3.5.4.5 Cytidine aminohydrolase CDD1 YLR245C L9672.13 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] CHARACTERIZATION ATCC 28383 / FL100 / VTT C-80102 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS SUBUNIT This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. cytidine + H(+) + H2O = NH4(+) + uridine 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+) Zn(2+) Homodimer. false 4 Present with 3120 molecules/cell in log phase SD medium. Belongs to the cytidine and deoxycytidylate deaminase family. 3D-structure Complete proteome Hydrolase Metal-binding Reference proteome Zinc MKVGGIEDRQLEALKRAALKACELSYSPYSHFRVGCSILTNNDVIFTGANVENASYSNCI CAERSAMIQVLMAGHRSGWKCMVICGDSEDQCVSPCGVCRQFINEFVVKDFPIVMLNSTG SRSKVMTMGELLPMAFGPSHLN P19414 D6VYU7 ACON_YEAST Aconitate hydratase, mitochondrial Aconitase 4.2.1.3 Citrate hydro-lyase ACO1 GLU1 YLR304C L8003.22 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION DISRUPTION PHENOTYPE CATALYTIC ACTIVITY ATCC 44774 / DBY747 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 17-23 SUBCELLULAR LOCATION DISRUPTION PHENOTYPE LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION SUBUNIT PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-409 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 FUNCTION SUBUNIT DISRUPTION PHENOTYPE SUBCELLULAR LOCATION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION FUNCTION INDUCTION MUTAGENESIS OF ARG-604 FUNCTION Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Can also provide minor contributions to the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. Plays also an essential role in mtDNA maintenance. May directly protect mtDNA from accumulation of point mutations and ssDNA breaks as a component of mitochondrial nucleoids, or by preventing accumulation of iron citrate thereby alleviating its detrimental effects in mitochondria. citrate = isocitrate [4Fe-4S] cluster Binds 1 [4Fe-4S] cluster per subunit. Subject to catabolite regulation. Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. Monomer. Binds to mitochondrial DNA (mtDNA) and identified as component of mitochondrial nucleoids. Mitochondrion Cytoplasm Mainly mitochondrial, small amounts are also detected in the cytosol with a ratio of 94:6. Highly induced in the absence of glutamate. Induction is further increased when both glutamate and lysine are missing. Essential for growth on nonfermentable carbon sources and for biosynthesis of glutamate. Causes a dramatic increase in cellular citrate levels. The fermenting yeast S.cerevisiae has 2 aconitases, ACO1 essential for the citric acid cycle, and ACO2 specifically and exclusively contributing to lysine biosynthesis. In contrast, in respiring filamentous fungi the ACO2 homologs (acoB) seem enzymatically inactive and the ACO1 homolog (acoA) is solely responsible for these functions. Present with 96700 molecules/cell in log phase SD medium. Belongs to the aconitase/IPM isomerase family. 4Fe-4S Complete proteome Cytoplasm Direct protein sequencing Iron Iron-sulfur Lyase Metal-binding Mitochondrion Phosphoprotein Reference proteome Transit peptide Tricarboxylic acid cycle R K DGLPQRGYDAGENTYQAPPADRS RWFASKEVMMLVRTLTKLHLQTVA MLSARSAIKRPIVRGLATVSNLTRDSKVNQNLLEDHSFINYKQNVETLDIVRKRLNRPFT YAEKILYGHLDDPHGQDIQRGVSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPVTV HCDHLIQAQVGGEKDLKRAIDLNKEVYDFLASATAKYNMGFWKPGSGIIHQIVLENYAFP GALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSP KDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMI EYLEATGRGKIADFAKLYHKDLLSADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSK MKEVAVANNWPLDVRVGLIGSCTNSSYEDMSRSASIVKDAAAHGLKSKTIFTVTPGSEQI RATIERDGQLETFKEFGGIVLANACGPCIGQWDRRDIKKGDKNTIVSSYNRNFTSRNDGN PQTHAFVASPELVTAFAIAGDLRFNPLTDKLKDKDGNEFMLKPPHGDGLPQRGYDAGENT YQAPPADRSTVEVKVSPTSDRLQLLKPFKPWDGKDAKDMPILIKAVGKTTTDHISMAGPW LKYRGHLENISNNYMIGAINAENKKANCVKNVYTGEYKGVPDTARDYRDQGIKWVVIGDE NFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDKINPDDR IDILGLAELAPGKPVTMRVHPKNGKPWDAVLTHTFNDEQIEWFKYGSALNKIKADEKK P53933 D6W186 APP1_YEAST Phosphatidate phosphatase APP1 PAP 3.1.3.4 Actin patch protein 1 APP1 YNL094W N2219 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] INTERACTION WITH ABP1 GLYCOSYLATION [LARGE SCALE ANALYSIS] FUNCTION CATALYTIC ACTIVITY ACTIVITY REGULATION MUTAGENESIS OF ASP-281 Mg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. May play a role in vesicular trafficking through its PAP activity at cortical actin patches. a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate Mg(2+) Inhibited by N-ethylmaleimide. Interacts with ABP1. P15891 ABP1 false 11 P47068 BBC1 false 3 P38822 BZZ1 false 14 Q05080 HOF1 false 2 P53281 LSB1 false 4 P43603 LSB3 false 8 Q04439 MYO5 false 2 P80667 PEX13 false 2 Q06449 PIN3 false 4 P39743 RVS167 false 9 P32790 SLA1 false 4 P32793 YSC84 false 6 Cytoplasm Cytoskeleton Actin patch Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity. N-glycosylated. Present with 2289 molecules/cell in log phase SD medium. Translation N-terminally extended. Complete proteome Cytoplasm Cytoskeleton Glycoprotein Hydrolase Lipid metabolism Reference proteome D E MNSQGYDESSSSTAATSGPTSGDPRMGKKQRFMNLIRTTKDVYIPNLTSSISQKTMDGIR STTNSFEGYNDLPMELPHNTTITYFPTYTTTNLVDPDGLSAPRKDFETTVRCAVSYPGNP TSRRNRWLLSLCKQYLRTGTAEADVAPVVPPHLEEDSGDLNDSQSSIESSLSSKSENRYS HMGIQEEDVLNERIQGFLSKKVPNTPVVVDLLPKDKLRGDTASFFGTTDSYGNLLIKAET DFLPSKINITLDTPIEGHADPISETFPANYVSPYGIGLISDIDDTIKHTGVTGDRRSMFR NVFIHDVQSWVIDGVPLWYKTLHDVADVDFFYVSNSPIQTFTLLKQYICANFPPGPIFLK QYSGNFFSTIMTSSANRKIQPIANILKDFPKKKFILVGDSGEHDLEAYTTTALQFPNQIL AIYIRCCSNSMSDVPSHDEEVMNEVNNIIELQQRPMQMTKSTVRTRRRPPPPPIPSTQKP SLTEEQTESIRMSRRNKDENNAKRVAPPPLPNRQLPNLDANTYYVPSSQNDYGMYGAFMD KKADEWKRRVMDSIQKLSNQDTTLMFFSDPALSLEDSIRRIREKYSN P38877 D3DLD9 CTF8_YEAST Chromosome transmission fidelity protein 8 CTF8 YHR191C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION IDENTIFICATION IN THE CTF18-RFC COMPLEX SUBCELLULAR LOCATION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c IDENTIFICATION IN THE CTF18-RFC COMPLEX FUNCTION OF THE CTF18-RFC COMPLEX Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. P49956 CTF18 false 4 P25559 DCC1 false 2 P40348 RFC2 false 2 P38629 RFC3 false 2 P40339 RFC4 false 2 P38251 RFC5 false 2 Nucleus Associates with chromatin. Belongs to the CTF8 family. 3D-structure Cell cycle Complete proteome DNA replication DNA-binding Nucleus Reference proteome MPSVDIDASQWQKLTQSREKQTTVITPLGMMMLEIQGELELPKDFASLARRDSPNEGRFS EQDGETLIRFGSLQIDGERATLFVGKKQRLLGKVTKLDVPMGIMHFNSKDNKVELVDVMK YKVIFKDRPLPIM Q07732 D6VRB7 ADY3_YEAST Accumulates dyads protein 3 ADY3 YDL239C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION SEQUENCE REVISION TO 569 ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY FUNCTION SUBCELLULAR LOCATION PHOSPHORYLATION COMPOSITION OF A SPB COMPLEX INTERACTION WITH SSP1; NUD1; CNM67 AND MPC54 FUNCTION SUBCELLULAR LOCATION INTERACTION WITH SPO21; NUD1 AND CNM67 Involved in the pathway that organizes the prospore membrane (PSM) during sporulation. Mediates the assembly of the DON1 ring structure at the leading edge of PSM during meiosis II. May constitute a physical link between SSP1-containing PSM precursors and the spindle pole body (SPB) and may facilitate the recruitment of other factors that are required to promote spore wall formation. Interacts directly with SSP1. Probable component of a SPB complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67. Q08550 MPC54 false 3 Q12411 SPO21 false 5 P38871 SSP1 false 3 Prospore membrane Cytoplasm Cytoskeleton Microtubule organizing center Spindle pole body Localizes to the leading edge, which cover the ring-shape opening of the PSMs during meiosis II. Colocalizes with DON1 to dots in the cytoplasm and at the SPB. Its localization to the PSMs but not to the SPBs depends on SSP1. Meiosis-specific. Expressed from 3 to 9 hours after induction of sporulation. Not expressed during mitosis. Phosphorylated. Cell cycle Cell division Coiled coil Complete proteome Cytoplasm Cytoskeleton Meiosis Membrane Phosphoprotein Reference proteome Sporulation E G MNHWLAFLNKPESLKEQNSDCDQQGEMRHVTDGTLTKSPESKPFRERRSQTWIDSEVPTS TEKSNVQESISSDIISKLSNRRSRRNRSESWAGSEASSPSGNISTLENATEKNTLKSPNK FLQRGGLPTVGIGSQALSPAGKPSTLGNVSPGKFTTYKVHNSIEVNRFSSTPTKLLTNPH KVAAISNDEHYVVSNESLEENIEVAHLENVFRSSKTPDEEQSEYMKLGEIRLSSSSYGGS ISKENSLPKVLDELQSQNEEIKALRQKLEEKDDRIQELEELNSMNDAKLQRIEDLQKEFH NERKAASKRLNIVQDRFRKEIKKIREEKITDFQNKNASKKEKNEVTSAKTKCKAFSQRNI LVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILKSNLQLSQDENKKLHDN GSFYEKRLNDVYSYMQNLSLFEKDLGKFILEEMKCGHSPSMFQNGFAKLYPDFQDIKNLE NMEQYKQLKGKIELLEKNDRIRLEKIISVFKLINERLHFMQQQHSHKIKYLQKEALTKEQ QFRLEKRRWHDILNLKEENFQKLKSELKEKLILSEKIQKNAEDKLNDYMNEHQEIVEKLQ NQALIASRWSTQIQESENTHKKITDELAGKQSEILKLEETILSLKEDVFQEKLNLKKLYG DPSTELNFETVGKSFPHITKEKYDSLGLDILTDLTYVQSQNLIKNLLIVLDIPLKTFLKI VPTIVIQLRCELTLLTKFANDLNLKVFGKQLDFKSRRKVAMNEFLNNHDIAEVKHPLEYD LQALFKYFFS P38872 D3DLD3 ADY1_YEAST Prospore formation at selected spindle poles protein 1 Accumulates dyads protein 1 PFS1 ADY1 YHR185C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required to localize MPC54 to all four spindle pole bodies, and localize DON1 and SPO14 to four prospore membranes. P40555 NAS2 false 3 Nucleus Cytoplasm Cytoskeleton Microtubule organizing center Spindle pole body Nuclear in mononucleate meiotic cells. May not be localized to the spindle pole body or prospore membrane. Complete proteome Cytoplasm Cytoskeleton Nucleus Reference proteome Sporulation MNQGYTQLSAPELKETKTSKLNKMNNFRSSPIAEIINKIPPDCGKIQNTTFPEFNPALRR RQHEQWPAYEKPIRVTDSMSPQLSSINCLPNLYPHGTLPLPNPYLSYLNHIEKVNCQDVK FSNWSVLHNSNNGFEIPTYFSPRTTQNMPCSEKVESWLERLPIFVGFDGYLFTNCFDYEY MLDWEETEFTFEKTSCMETDYSKALTDTDIIYIQEKKIEALIRNQYLKEYEFSQKDF P53838 D6W0R9 BOR1_YEAST Boron transporter 1 BOR1 YNL275W N0626 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION TOPOLOGY LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION FUNCTION SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A FUNCTION FUNCTION SUBCELLULAR LOCATION Functions in boric acid/borate export across the plasma membrane, and thereby protects yeast cells from boron toxicity. Involved in the trafficking of proteins to the vacuole. Cell membrane Multi-pass membrane protein Vacuole membrane Multi-pass membrane protein Present with 195 molecules/cell in log phase SD medium. Belongs to the anion exchanger (TC 2.A.31) family. Anion exchange Cell membrane Complete proteome Ion transport Membrane Reference proteome Transmembrane Transmembrane helix Transport Vacuole MSNESTRVTVSRGCTASDECAQALERTNDELDRESSVSESRSDEESHEKLSRRRFPTLGI GIWLDLKDRIPYYKSDWVDAFNYRVIPSIVDTYFNNLLPAIAFAQDMFDRTDNSYGVNEV LLSSAMAGIVFGVLGGQPLCIVGVTGPISIFNYTVYEIIKPLNTSYFGFMFWICMWSMIF HLVLAFTNAVCLLQYVTTFPCDIFGLFINVVYIQKGIQILTRQFSAKSGEKSVQDGFASV VVALVMTAFGLFFKLFHYYPLFSHRIRTFISDYSTALSVLFWSSFTHFGGYLHDVKFKKL PITKAFFPTSKVNRPQNTWLAYEPIPVKDVFIALPFGIFLTILFYFDHNVSSLMAQRHQY KLKKPSSFHYDFALLGLTTCISGVLGIPAPNGLIPQAPLHTETLLVRDSNQKVISCVEQR FTNTFQGLMILGTMTRPLLVCLGEIPQAVLSGLFFIMGINGLMTNSIIQRLVFLFSDPNR RDNTSPLMKVSKKSMLIFLSFSLTGFAGEFAITNTIAAIGFPLVLLLSVLVSFSFAYIFP TEELKILDTNVAQKFTIKNLLLENIRDAKFCDKHED P50084 D6VV10 BNS1_YEAST Protein BNS1 BNS1 YGR230W G8558 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION FUNCTION FUNCTION FUNCTION Component of the FEAR (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase and is required for the efficient segregation of telomeric and nucleolar regions. Although BNS1 can partially compensate for a lack of SPO12 function when overexpressed, it does not appear to play any role in controlling meiotic nuclear division. Cell cycle Complete proteome Reference proteome MSYGGSASQDIVTKLIRKIQNTSVSCTRRDENLDSFNQHLKMSLKVAHNTKTFAKHCLHR QVFKNTYRKRKAVEDQRKNLNTQLRQKFASPSDNLLSPCSRKLNDHKSKLFSAKSQPKTL EFVRGKQNIPRKPNVDI P38195 D6VPV5 ECM13_YEAST Protein ECM13 Extracellular mutant protein 13 ECM13 YBL043W YBL0405 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c IDENTIFICATION May be involved in cell wall organization and biogenesis. Cell wall biogenesis/degradation Complete proteome Reference proteome MNSTTPSIQDQYILASKVRSKLAKCVSVTTKNKDYNLRVLVGHANLLDKITENVETHNAA TNALAGDPFSKGPENLSIEHIELSNANASKNDVGKEENAEKTIESEDYCDFYSSDEDPDA DTLSSTDSEDDDDYEDYDFEYDYSGGDYNKKIDMYFSFHTAPNYQYLTHTNSHSEQTDEL AESTPRYNALPATASTTEEEQDTETLDAVSLHSSAPIFRVLSRRVNGQEDDSENESSSDV DDGSVPLTRFHSCPITA P52892 D6VS97 Q66RF8 ALAT_YEAST Probable alanine aminotransferase 2.6.1.2 Glutamate pyruvate transaminase GPT Glutamic--alanine transaminase Glutamic--pyruvic transaminase ALT2 YDR111C YD9727.07C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] 2-oxoglutarate + L-alanine = L-glutamate + pyruvate pyridoxal 5'-phosphate Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1. Homodimer. Cytoplasm Nucleus Present with 3480 molecules/cell in log phase SD medium. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily. Aminotransferase Complete proteome Cytoplasm Nucleus Pyridoxal phosphate Reference proteome Transferase K E MTMTHQQDLKGVFTAKDLDFKPAGKITKKDLNTGVTKAEYAVRGAIPTRADELKEELKKN PEVLPFDDIINANIGNPQQLDQKPLTFTRQVLAILEYPEILRVGHNELASLNLFSRDALE RAERLLNDIGGSIGAYSHSQGVPGIRQTVADFITRRDGGEPATPEDIYLTTGASSAATSL LSLLCKDSQTGLLIPIPQYPLYTASASLFNAQVLPYYLDEESNWSTNSDEIEKVVQDALK KQIRPSVLIVINPGNPTGAVLSEETIARICLIAAKYGITIISDEVYQENIFNDVKFHSMK KVLRKLQHLYPGKFDNVQLASLHSISKGFMDECGQRGGYMEIIGFSQEIRDALFKLMSIS ICSVVTGQAVVDLMVKPPQPGDESYEQDHDERLKIFHEMRTRANLLYETFKELEGIECQK PQGAMYLFPRLVLPKKALCESERLGIEPDEFYCTSLLESTGICTVPGSGFGQRPGTYHVR TTFLAPGTKWIQDWKEFHQDFFSKYRN Q08683 D6W2V0 APC5_YEAST Anaphase-promoting complex subunit 5 APC5 RMC1 YOR249C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 519-527 AND 626-632 SUBUNIT IDENTIFICATION BY MASS SPECTROMETRY SUBUNIT INTERACTION WITH MND2 AND SWM1 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication. Protein modification; protein ubiquitination. The APC/C is composed of at least 13 subunits that stay tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5, APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1. APC5 directly interacts with MND2 and SWM1. Q04601 APC4 false 7 P40577 MND2 false 4 Q12379 SWM1 false 4 Nucleus Present with 259 molecules/cell in log phase SD medium. Belongs to the APC5 family. Cell cycle Cell division Complete proteome Direct protein sequencing Mitosis Nucleus Reference proteome Ubl conjugation pathway MSKYGPLGITNFITPYDLCILILIHAHCSQDNGISVPTAVFLRLISPTRPSLEWNPLLKD NSNLRSSSIVPPPVLPILDNIIRILLDDKDGNKIALTLMGYLEAINGLDSINRLMMDLEK NCLVNNYRSMKMRTTSTRRQMTRASFLGTFLSTCIRKYQIGDFEMRETIWINLQNFKTVF KHTPLWLRFKDNVHIQKVKNCLLANDEISVEDQQMVEFFQHFNNGNDADSKTMNEENYGT LISIQHLQSIVNRQIVNWLDNTEFNLMGQEETSSTYEEQSGLVFDLLDTLSLNDATKFPL IFILKYLEAIKENSYQTALDSLHNYFDYKSTGNSQNYFHISLLSLATFHSSFNECDAAIN SFEEATRIARENKDMETLNLIMIWIINFIEVHPEYANRFYITVEQIIKYLKNSSDVEDAN IFSNAYKFETLLSMVKESKTAEVSSSLLKFMAITLQNVPSQNFDLFQSLVSYEVKFWKEL GYESISDVYEKFLSKTSSSSLRNYDSSIINQDIKVAFKALEEDDFLKVKQYLLKSESLEL DYDQKINLKYLRVKYLVKIGDYDLSMRLINQYVKECCEEVADSNWRFKFEIESINVLLLS DVGIRSLPKIIKLIDEYKEIGNPLRCVILLLKLCEVLIQVGKSMEAECLISCNLSTILEF PFVRKKTDELLESLSVEEDRDVQMT Q12406 D6W444 ARP7_YEAST Actin-related protein 7 Actin-like protein ARP7 Chromatin structure-remodeling complex protein ARP7 SWI/SNF complex component ARP7 ARP7 SWP61 YPR034W YP9367.14 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 184-196; 217-232 AND 289-297 FUNCTION IDENTIFICATION IN THE RSC AND SWI/SNF COMPLEXES MUTAGENESIS OF ALA-19; SER-33; GLY-396 AND GLU-411 FUNCTION OF THE RSC COMPLEX COMPOSITION OF THE RSC COMPLEX GENE NAME FUNCTION OF THE RSC COMPLEX FUNCTION OF THE RSC COMPLEX COMPOSITION OF THE RSC COMPLEX FUNCTION OF THE RSC COMPLEX FUNCTION OF THE RSC COMPLEX FUNCTION HETERODIMERIC COMPLEX FORMATION WITH ARP9 WITHIN THE RSC COMPLEX MUTAGENESIS OF ALA-19; SER-33 AND GLU-411 FUNCTION OF THE RSC COMPLEX SUBCELLULAR LOCATION INTERACTION OF THE RSC COMPLEX WITH HISTONES LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX ELECTRON MICROSCOPY OF THE SWI/SNF COMPLEX INTERACTION WITH NPL6 Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. This subunit is involved in transcriptional regulation. Heterodimer of ARP7 and ARP9 functions with HMG box proteins to facilitate proper chromatin architecture. Heterodimer formation is necessary for assembly into RSC complex. Part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Forms a heterodimer with ARP9. Interacts with NPL6. Component of the two forms of the RSC complex composed of at least either RSC1 or RSC2, and ARP7, ARP9, LDB7, NPL6, RSC3, RSC30, RSC4, RSC58, RSC6, RSC8, RSC9, SFH1, STH1, HTL1 and probably RTT102. The complexes interact with histone and histone variant components of centromeric chromatin. Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29. Q05123 ARP9 false 5 Nucleus Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1. Present with 1360 molecules/cell in log phase SD medium. Belongs to the actin family. 3D-structure Chromatin regulator Complete proteome Direct protein sequencing Nucleus Reference proteome Transcription Transcription regulation A P S F G V E K MTLNRKCVVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEGGEAEFIFGTYNMIDAAAE KRNGDEVYTLVDSQGLPYNWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMAIL ERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVTPIIDGIVVKNAVV RSKFGGDFLDFQVHERLAPLIKEENDMENMADEQKRSTDVWYEASTWIQQFKSTMLQVSE KDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFKPLNKTLT LDLKECYQFAEYLFKPQLISDKFSPEDGLGPLMAKSVKKAGASINSMKANTSTNPNGLGT SHINTNVGDNNSTASSSNISPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQYK LTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYETLKRDRKQSQATNATN P39960 D3DM62 BEM2_YEAST GTPase-activating protein BEM2/IPL2 Bud emergence protein 2 BEM2 IPL2 SUP9 YER155C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CHARACTERIZATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1012; SER-1016 AND SER-1046 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1012; SER-1046 AND SER-1054 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-283 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-283; THR-1038 AND SER-1128 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-27 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] GTPase-activating protein (GAP) for RHO1 and RHO2. Involved in the control of cellular morphogenesis. Required for proper bud site selection and bud emergence. P27637 BUD14 false 3 Present with 1230 molecules/cell in log phase SD medium. Complete proteome GTPase activation Isopeptide bond Phosphoprotein Reference proteome Ubl conjugation MKGLLWSKNRKSSTASASSSSTSTSHKTTTASTASSSSPSSSSQTIRNSTSGASPYMHSH HHHGQGHSHHRGEDNNRDKRKSSVFPPSKQYTSTSSSQVNLGMYHSDTNTRSSRSIASTL KDDSPSVCSEDEISNSSSQKSNAQDETPIAYKKSAHSKDSLLPSRSSSLSPPQSRCSTGT TLEKSLNTSGISNSSGTNNNNSNNNNDNEQKQRNVIHLNSENYDTTVFKTGWVNKSHGQT VATNYNSSMTAPSSSSSSSSQNLRNDAYSRNRESRFYGNDGSSLKNDDSSSTTATNSGND VASARSSMAIDPQMLVPDYRLYRAQLKGCVLNLYKSGLNSNIKFFDPTLPASNSSIANEN HQQKKQQTNNQAQAEALHQKQSFGQMGEPITLDLKYLSEVYPHPDLRQDSDGKIISGTIE SLCHTVLFYPGPKQSDVPNEKSLSKTHRAVINLLLMFPLLDHFIKFLKVFNQFGLSFTKN KSRLTNNSTQFYNISPAVDDSMTQRLALTAKTILDVFPGFLLDEPMLKTIISLLDTISLH NDEISNNLKIKIANKHNELMKLTAFTRSLPMATSSTHELEIILDPSHFLSLDITTLADEV HHINLKFDKVWAPKFDYSLLYDSKFINRRIVSLNPLVFNNDQNIHFLGRLLISHLFPTNP EFSKKVTPKVRAELLDKWVQIGCRFEHLGDMVSWLAVATIICSIPVLRSSSWKYVPDQSL KTIFKDWVPTIIQLERRQRTSKSTSSVFILAPPNLDDDFTRANVISYFGDLLIHADDLPS DTKFKYLEKKINRTKNAFHKWQQRLQAIDSTRHKTNSTENVRDNDSPNNVVYQLWKFHLS QPPLNIEGIMKLSVQHEPPIIDQKAYSTIGSQRSALVTGSYLPILFNELFPNYSLFPKNT LVGAASDAKLPPPRSSARLSKSLSISEPIPIASNSHTMGSLTDDAMSSKNDNNKVTGVGK IDGPVIKEMSSKQSNKQRLLKSVRDVFNIDMDVFHISDELVFKSVYDNDGKSRPASMVIE TPKRFSQHSSMLINNPATPNQKMRDSLDTTGRLSKTLENMDFFNNIGQVSDSLKESIIRV VLKSSSLEKIFDLLVLTSNIFSKLVDTKDLENYYYHQRQRGHSTRGLSDDNIGLLDYAFV KLTMDNDIFTETFFNTYKSFTTTTTVLENMAKRYVGAKSCSVSISKILDRSDDSKMKINE DTNLVSSSLYDQNFPVWDMKVTDDENINLIYMAKIQIGAAEAILHLVKNHYSDFTDDLCN NSTLLDIIKIMEQEVSTEWPTRIANSKLQKSLPENFVIETENLLTTLTDLFHGIKSAYQK QLYRPIGVNRTQKRITDILNSFNTFSFTDLNNIIDDPSFSDDMIRSFQKLHSTNYEDILE WIYQLDNFISKKFNLVSKKDWIVLFQELELLSKESLVSFFNYPLHFKSSKLINPGYLQLH EFEISNLFTWISTLILKDDNGTESLFFEKLPQSIKLLIKLHTSLTTFFVMEISNVNKSSS ERLTTCKVILQILNYIRWKNGSLDLFDSEEDESPHAICPHIPAFIETAIAHAIISPESRN YELSWIKASEKLSDPTKGTQNLRSISNVLEKIDDIHIKRFIEIDDVFSKNCKNLCPCPGW FISRLLEISQFVPNMSITNSKLINFDKRRFVNNIISNVLDLIPNEREFPLDIEMSDENPS KRTTFGRILFNNFEDVNKVYRKKTKKVSESEAISERFQEQGVFNEILVNEIEKIKREARK LEVLLDQEKILKNSAALHQAVPKKNRKSVIISGTHSDNDHSYNINKNTGQTPSLGSVMES NNSARNRRDSRASFSTNRSSVVSNSSHNGVSKKIGGFFRRPFSIGGFNTSSSNYSLNSIL SQEVSSNKSILPSILPEVDSMQLHDLKPSYSLKTFEIKSIMEIINHRNIPAYYYAFKIVM QNGHEYLIQTASSSDLTEWIKMIKASKRFSFHSKKYKGKTHNKIFGVPLEDVCERENTLI PTIVVKLLEEIELRGLDEVGLYRIPGSIGSINALKNAFDEEGATDNSFTLEDDRWFEVNA IAGCFKMYLRELPDSLFSHAMVNDFTDLAIKYKAHAMVNEEYKRMMNELLQKLPTCYYQT LKRIVFHLNKVHQHVVNNKMDASNLAIVFSMSFINQEDLANSMGSRLGAVQTILQDFIKN PNDYFKQ P53109 D6VTZ1 AIM14_YEAST Probable metalloreductase AIM14 1.16.1.- Altered inheritance of mitochondria protein 14 AIM14 YGL160W G1837 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c COPURIFICATION WITH RIBOSOMAL COMPLEXES IDENTIFICATION BY MASS SPECTROMETRY TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A DISRUPTION PHENOTYPE IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Probable cell surface metalloreductase. May be involved in iron or copper homeostasis (By similarity). Interacts with ribosomes. Membrane Multi-pass membrane protein Increases frequency of mitochondrial genome loss. Belongs to the ferric reductase (FRE) family. AIM14 subfamily. Complete proteome Electron transport FAD Flavoprotein Ion transport Membrane NADP Oxidoreductase Reference proteome Transmembrane Transmembrane helix Transport MKESPLITLVKRHSETHFANIKYGYYVLIISLVYLIGLALLRAFGRRTPSRSSSAFKNKI IYRLYDIDPAIHLGILFFAVLIPFYYHYSLTTQSTVYLKRLGRLSYALIPLNLFLTLRPN WFLRKNCTYTDFIPFHKWFSRIITVIGLLHGIFFIIKWAIDDNVSLKQKLILKTFNFAGF IISILVLFLLICSIGPMRRYNYRLFYIVHNLVNVAFILLTPIHSRPGVKFPFLLLNCTLL FIHIINRIVFAKSLMILNKNANYSKTNLVHVRLPRAILPDYFEPGSHIRISPYRRINPLY WLLPSHPYTIASLAEDNSIDLIIKETSTAEPGSQIESLRSNPKSFHLDQEKTYTLINSYP PSVPEECYSQGTNIAIICGGSGISFALPLFRHFFNKENVKYLKMIWLIKDYSEYELVLDY LKTNGLTFEKKLSNNKRISVFISGEYTAETRLDEITTNIDDENSEYEMGSFNNEDEDLSI SNFNSENADSNDNTPETSHSPTKENGSMIEVKSKHSFTLSNELKSFNNESAQVNQNETWL FSCGPPSLLQLSKKYCNDERINFVCETYGL P38772 D3DKY8 BCD1_YEAST Box C/D snoRNA protein 1 BCD1 YHR040W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis. Nucleus Present with 2800 molecules/cell in log phase SD medium. Belongs to the BCD1 family. 3D-structure Complete proteome Metal-binding Nucleus Phosphoprotein Reference proteome Ribosome biogenesis Zinc Zinc-finger MAVLCGVCGIKEFKYKCPRCLVQTCSLECSKKHKTRDNCSGQTHDPKEYISSEALKQADD DKHERNAYVQRDYNYLTQLKRMVHVQKMDARMKNKRVLGPVGGHNSNFKKRRYDIDEDDR DSTECQRIIRRGVNCLMLPKGMQRSSQNRSKWDKTMDLFVWSVEWILCPMQEKGEKKELF KHVSHRIKETDFLVQGMGKNVFQKCCEFYRLAGTSSCIEGEDGSETKEERTQILQKSGLK FYTKTFPYNTTHIMDSKKLVELAIHEKCIGELLKNTTVIEFPTIFVAMTEADLPEGYEVL HQEPRPLEHTSTLNKFIDNAREEEDAEEDSQPTEEPVQKETQDASDSDSDSDDDYNPGLS MDFLTA P38892 D3DLF8 Q6Q5R3 CRG1_YEAST Probable S-adenosylmethionine-dependent methyltransferase CRG1 2.1.1.- Cantharidin resistance protein 1 CRG1 YHR209W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] INDUCTION FUNCTION Probable S-adenosylmethionine-dependent methyltransferase which mediates cantharidin resistance. Cytoplasm By cell wall perturbation. Present with 4380 molecules/cell in log phase SD medium. Belongs to the methyltransferase superfamily. Complete proteome Cytoplasm Methyltransferase Reference proteome S-adenosyl-L-methionine Transferase Y C MPKTSYLNKNFESAHYNNVRPSYPLSLVNEIMKFHKGTRKSLVDIGCGTGKATFVVEPYF KEVIGIDPSSAMLSIAEKETNERRLDKKIRFINAPGEDLSSIRPESVDMVISAEAIHWCN LERLFQQVSSILRSDGTFAFWFYIQPEFVDFPEALNVYYKYGWSKDYMGKYLNDNQREIL LNYGGEKLRSLLSDRFGDIEVTIYSPSDPNASTVTAENSQFLWRAAITLNQFKEFVKSWS IYTSWARDNPSKPDIADIFINELKEICHCEDLNVPLKIEWSTFYYLCRKRE P29311 D3DM86 Q06854 BMH1_YEAST Protein BMH1 BMH1 YER177W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 26109 / X2180 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c ACETYLATION AT SER-2 INTERACTION WITH FIN1 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-76 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in growth regulation. Interacts with FIN1. Q96B36 AKT1S1 true 3 P32356 NTH1 false 7 Present with 158000 molecules/cell in log phase SD medium. Belongs to the 14-3-3 family. 3D-structure Acetylation Complete proteome Isopeptide bond Phosphoprotein Reference proteome Ubl conjugation A R GEAPK VKHQSKYSDKSKEKLLKKRKKKERGCNNL MSTSREDSVYLAKLAEQAERYEEMVENMKTVASSGQELSVEERNLLSVAYKNVIGARRAS WRIVSSIEQKEESKEKSEHQVELICSYRSKIETELTKISDDILSVLDSHLIPSATTGESK VFYYKMKGDYHRYLAEFSSGDAREKATNASLEAYKTASEIATTELPPTHPIRLGLALNFS VFYYEIQNSPDKACHLAKQAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMSES GQAEDQQQQQQHQQQQPPAAAEGEAPK P25656 D6VR94 CDC50_YEAST Cell division control protein 50 CDC50 YCR094W YCR94W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] INTERACTION WITH DRS2 TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A Required for polarized cell growth. Interacts with DRS2. Might function as an essential subunit for this protein. P39524 DRS2 false 6 Late endosome membrane Multi-pass membrane protein Present with 589 molecules/cell in log phase SD medium. Belongs to the CDC50/LEM3 family. Complete proteome Endosome Glycoprotein Membrane Reference proteome Transmembrane Transmembrane helix MVSLFKRGKAPPLTKEGPTSKKPPNTAFRQQRLKAWQPILSPQSVLPLLIFVACIFTPIG IGLIVSATKVQDLTIDYSHCDTKASTTAFEDIPKKYIKYHFKSKVENKPQWRLTENENGE QSCELQFEIPNDIKKSIFIYYKITNFYQNHRRYVQSFDTKQILGEPIKKDDLDTSCSPIR SREDKIIYPCGLIANSMFNDTFSQVLSGIDDTEDYNLTNKHISWSIDRHRFKTTKYNASD IVPPPNWMKKYPDGYTDENLPDIHTWEEFQVWMRTAAFPKFYKLTLKNESASLPKGKYQM NIELNYPISLFGGTKSFVLTTNGAIGGRNMSLGVLYLIVAGLCALFGIIFLVKLIFQPRA MGDHTYLNFDDEENEDYEDVHAENTTLREIL P13090 D6W0G8 ATR1_YEAST Aminotriazole resistance protein ATR1 SNQ1 YML116W YM8339.03 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c CHARACTERIZATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Putative component of the machinery responsible for pumping aminotriazole (and possibly other toxic compounds) out of the cell. Probable ATP-dependent export permease. Appears to confer resistance only to aminotriazole. Membrane Multi-pass membrane protein Deletion of the C-terminal 34 residues abolishes ATR1 activity, while deletion of the C-terminal 23 residues have a minor effect. Present with 1720 molecules/cell in log phase SD medium. Belongs to the major facilitator superfamily. Complete proteome Glycoprotein Membrane Reference proteome Transmembrane Transmembrane helix Transport ARAAAEYDCTVA QELLQNTIALWLSGKRY MGNQSLVVLTESKGEYENETELPVKKSSRDNNIGESLTATAFTQSEDEMVDSNQKWQNPN YFKYAWQEYLFIFTCMISQLLNQAGTTQTLSIMNILSDSFGSEGNSKSWLMASFPLVSGS FILISGRLGDIYGLKKMLLVGYVLVIIWSLICGITKYSGSDTFFIISRAFQGLGIAFVLP NVLGIIGNIYVGGTFRKNIVISFVGAMAPIGATLGCLFAGLIGTEDPKQWPWAFYAYSIA AFINFVLSIYAIPSTIPTNIHHFSMDWIGSVLGVIGLILLNFVWNQAPISGWNQAYIIVI LIISVIFLVVFIIYEIRFAKTPLLPRAVIKDRHMIQIMLALFFGWGSFGIFTFYYFQFQL NIRQYTALWAGGTYFMFLIWGIIAALLVGFTIKNVSPSVFLFFSMVAFNVGSIMASVTPV HETYFRTQLGTMIILSFGMDLSFPASSIIFSDNLPMEYQGMAGSLVNTVVNYSMSLCLGM GATVETQVNSDGKHLLKGYRGAQYLGIGLASLACMISGLYMVESFIKGRRARAAAEYDCT VA Q3E7A9 D6W019 CMC4_YEAST Cx9C motif-containing protein 4, mitochondrial CMC4 YMR194C-B Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c GENOME REANNOTATION ATCC 204511 / S288c / AB972 DOMAIN SUBCELLULAR LOCATION DOMAIN IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] Mitochondrion intermembrane space Imported into the mitochondria via the mitochondrial MIA40-ERV1 machinery. The twin Cx9C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system and the subsequent transfer of disulfide bonds by dithiol/disulfide exchange reactions to the newly imported protein. Belongs to the CMC4 family. Complete proteome Disulfide bond Mitochondrion Reference proteome Repeat MSNPCQKEACAIQDCLLSHQYDDAKCAKVIDQLYICCSKFYNDNGKDSRSPCCPLPSLLE LKMKQRKLTPGDS P41810 D6VSL9 Q03779 COPB_YEAST Coatomer subunit beta Beta-coat protein Beta-COP SEC26 YDR238C YD8419.05C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 353-362; 496-514; 645-655 AND 934-942 FUNCTION PTM DISRUPTION PHENOTYPE RSY255 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBUNIT IDENTIFICATION BY MASS SPECTROMETRY FUNCTION MUTAGENESIS OF 334-ASP--ASP-336 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-540 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] 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. Required for mitochondrial morphology. Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. The complex interacts with ARF1 and PAB1. Q04651 ERV41 false 3 Cytoplasm 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. The N-terminus is blocked. Causes a block in ER to Golgi transport. Exhibits exaggerated ER structures displaying interconnected networks of ER cisternae. Cells arrest at all stages of the vegetative cycle. Present with 26000 molecules/cell in log phase SD medium. Complete proteome Cytoplasm Cytoplasmic vesicle Direct protein sequencing ER-Golgi transport Golgi apparatus Membrane Phosphoprotein Protein transport Reference proteome Repeat Transport DLD NAN D E MTSLSSQPAYTLVFDPSPSMETYSSTDFQKALEKGSDEQKIDTMKSILVTMLEGNPMPEL LMHIIRFVMPSKNKELKKLLYFYWEIVPKLAEDGKLRHEMILVCNAIQHDLQHPNEYIRG NTLRFLTKLREAELLEQMVPSVLACLEYRHAYVRKYAILAVFSIFKVSEHLLPDAKEIIN SFIVAETDPICKRNAFIGLAELDRENALHYLENNIADIENLDPLLQAVFVQFIRQDANRT PALKAQYIELLMELLSTTTSDEVIFETALALTVLSANPNVLVPAVNKLIDLAVKVSDNNI KLIVLDRIQDINANNVGALEELTLDILRVLNAEDLDVRSKALDISMDLATSRNAEDVVQL LKKELQTTVNNPDQDKAMQYRQLLIKTIRTVAVNFVEMAASVVSLLLDFIGDLNSVAASG IIAFIKEVIEKYPQLRANILENMVQTLDKVRSAKAYRGALWIMGEYAEGESEIQHCWKHI RNSVGEVPILQSEIKKLTQNQEHTEENEVDATAKPTGPVILPDGTYATESAFDVKTSQKS VTDEERDSRPPIRRFVLSGDFYTAAILANTIIKLVLKFENVSKNKTVINALKAEALLILV SIVRVGQSSLVEKKIDEDSLERVMTSISILLDEVNPEEKKEEVKLLEVAFLDTTKSSFKR QIEIAKKNKHKRALKDSCKNIEPIDTPISFRQFAGVDSTNVQKDSIEEDLQLAMKGDAIH ATSSSSISKLKKIVPLCGFSDPVYAEACITNNQFDVVLDVLLVNQTKETLKNLHVQFATL GDLKIIDTPQKTNVIPHGFHKFTVTVKVSSADTGVIFGNIIYDGAHGEDARYVILNDVHV DIMDYIKPATADDEHFRTMWNAFEWENKISVKSQLPTLHAYLRELVKGTNMGILTPSESL GEDDCRFLSCNLYAKSSFGEDALANLCIEKDSKTNDVIGYVRIRSKGQGLALSLGDRVAL IAKKTNKLALTHV Q99186 D6W205 AP2M_YEAST AP-2 complex subunit mu Adaptin medium chain APM4 Clathrin assembly protein complex 2 mu medium chain Clathrin coat assembly protein AP50 Clathrin coat-associated protein AP50 Mu2-adaptin Plasma membrane adaptor AP-2 50 kDa protein APM4 AMP1 YOL062C O1210 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 90843 / S288c / FY73 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBUNIT LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-180 AND SER-181 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit APL3 and beta-type subunit APL1), a medium chain (mu-type subunit APM4) and a small adaptin (sigma-type subunit APS2). Membrane Clathrin-coated pit Cytoplasmic vesicle Clathrin-coated vesicle membrane Present with 3410 molecules/cell in log phase SD medium. Belongs to the adaptor complexes medium subunit family. Coated pit Complete proteome Cytoplasmic vesicle Endocytosis Membrane Phosphoprotein Protein transport Reference proteome Transport MISGVLVYSSRGELVLNKFFKNSLKRSISDIFRVQVINNLDVRSPVLTLGSTTFHHIRSR HGDNLWLVTITRSNANSAAIWEFLYKLDAVMNAYRLDREEALKEEFMIVHEMLDIMLGGN GIPIDTELNSVIAQMSVKPVRNMGGLLDSPDGNDVLSSSSSPTSSAGELHFPKFLTKRSS SFLGQGDSTSDFYDNNKITWRPKGIIHKKDEVFLYVNERINILVSRDGSILKSYVDGTID ITTHLSGTPICRFGLNDSLGMQSEDEKKWLAQQQRHSGSDFGNKNFIPKAAAGSVLLEDC KFHECVSLDKFNRNHIIEFVPPDGSMELMKYHVRDNINLPFKVTPIVTHSTRDNEIDYRI TLKSLFPGKLSAKDVVLHIPVPPSTVDCKISVSNGHCKFVPEENAMIWRFNKYNGLTENT LSAVTVSTSDTTQLNLQQWTRPPISLEFEVMMFSNSGLVVRYFTISGKDSKHRAVKWIKY ISKAGSYEVRY Q05790 D6VYL4 CRR1_YEAST Probable glycosidase CRR1 3.2.-.- CRH-related protein 1 CRR1 YLR213C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c INDUCTION FUNCTION DEVELOPMENTAL STAGE DEVELOPMENTAL STAGE SUBCELLULAR LOCATION FUNCTION FUNCTION Spore specific glycosidase involved in spore wall assembly during sporulation. May be involved in copper import. Spore wall Spore wall envelope. Expressed in spores. Expression is increased in low copper conditions, probably through the transcription regulation by the copper regulon transcription factor MAC1. Belongs to the glycosyl hydrolase 16 family. CRR1 subfamily. Complete proteome Glycosidase Hydrolase Reference proteome Signal Sporulation MRISILQLVPVVGYIGFALGELYKPKNSISCSPNNPCPAEWPCCSPYNECGAGPICVGGC NVRSSFDEESCAPIPALVASQKLEFVSTPKVPKFIVNYQPKPPIREGNGPNKANTKVGVV EGELNSKRIIHYAKFLVTPDSKEAEKMLEDFDFTHSGYTSIEASSGNIVLAMPKKTTGSL ITSTRSFLYGKASVRMKTARSRGVVTAFDLTSAIGDEIDFEWLGGDLMTAQSNYYSQGHL DYTRMQRFPVGADTWATYHTYEIDWDPDRIIWYVDGKIARTVLKKDTWDPISKEYRYPQT PMRLEIAVWPGGSETNGPGTINWAGGLIDWENSPDIIEKGQFTAHVEQITVTPYQNKFTE QVQFCIKAKKKAPTFSQKDLSRVVVSYNRQDRLNHHDEGSLKWDCFVTPKINDWLSSWKR SK Q08957 D6W3G7 AFT2_YEAST Iron-regulated transcriptional activator AFT2 Activator of iron transcription protein 2 AFT2 YPL202C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION FUNCTION FUNCTION FUNCTION FUNCTION Transcription factor required for iron homeostasis and resistance to oxidative stress. With RCS1, activates the gene expression in response to low-iron conditions, also called iron regulon. Nucleus The transcription activation by RCS1 and AST2 depends on the mitochondrial iron-sulfur protein biosynthesis pathway. 3D-structure Activator Complete proteome Iron Nucleus Reference proteome Transcription Transcription regulation MKAKSMKSIISVPISVSKTGKMKLTASPDNLASMMSKDQNKLIHLDPVPSFEDRHEIKPW LQKIFYPQGIDIVIERSDSSKVTFKCRSVRSKVGLNPKSKGSSSRSHACPFRIRAAYSVR LQKWNVVVMNNIHSHELRFDLITKTDDYKKFKENLRQKNDEKAIKTFDELEYKASLNLPL VTPIISCDCGLTKEIEAFNNIFLPLSNPPLTSKKNLLKTNKNSVSKIKSRQMDNSKPRPR LKTKLDADLHDTGFLDNFKTRNSCVKIEKEDSLTNLNEIDFTNMFCNDNFIQNYNQGLME LLTEPTPGPSSSSCILPSTPTRPLSQSKMDIALSESTTSSPNFMETDAPYGDEIIKVSKD TKSNAPTADTDIATNLGKERNENFGMLNYNYEALLHFNDEHFNELNSIDPALISKY P53314 D6VV27 CPD1_YEAST 2',3'-cyclic-nucleotide 3'-phosphodiesterase CPDase 3.1.4.37 CPD1 YGR247W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION BIOPHYSICOCHEMICAL PROPERTIES FUNCTION BIOPHYSICOCHEMICAL PROPERTIES MUTAGENESIS OF HIS-39; THR-41; HIS-150 AND SER-152 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Involved in the metabolism of ADP-ribose 1',2'-cyclic phosphate which is produced as a consequence of tRNA splicing. a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-phosphate + H(+) 4.97 mM for adenosine 1',2'-cyclic phosphate 14.29 mM for guanosine 1',2'-cyclic phosphate 12.18 mM for cytidine 1',2'-cyclic phosphate 8.91 mM for uridine 1',2'-cyclic phosphate 0.37 mM for ADP-ribose 1',2'-cyclic phosphate 0.33 mM for ribose 1,3-cyclic phosphate 353 umol/min/mg enzyme toward adenosine 1',2'-cyclic phosphate 390 umol/min/mg enzyme toward guanosine 1',2'-cyclic phosphate 598 umol/min/mg enzyme toward cytidine 1',2'-cyclic phosphate 296 umol/min/mg enzyme toward uridine 1',2'-cyclic phosphate 61 umol/min/mg enzyme toward ADP-ribose 1',2'-cyclic phosphate 0.02 umol/min/mg enzyme toward ribose 1,3-cyclic phosphate Golgi apparatus Present with 1520 molecules/cell in log phase SD medium. Belongs to the 2H phosphoesterase superfamily. CPD1 family. Complete proteome Golgi apparatus Hydrolase Reference proteome H A T A H A S A MAIALWYCPPQGSVAYETLQMLIFSFQTLFPDSPVFEPHVTVTSHLVCNSKDDVNKILTS CVAAIQSIRSHQTAKKGRKGQVSHAVAAPLVSFNGCSVGKQYFKKIVLECNKNKILYGVA QVMREMYVEIDPETRSSRAATWVHEEFHPHVSLLYSDIHPVSQASLRVVQQRIEDALDVQ LVPREKRKGSGNADGSNEVQMRWDFDVSSSLSWNIPGTFKVVNCVGPVQEWEVLGRVDV P48360 D6VT08 P32840 ADRO_YEAST Probable NADPH:adrenodoxin oxidoreductase, mitochondrial AR Adrenodoxin reductase 1.18.1.6 Ferredoxin--NADP(+) reductase Ferredoxin reductase ARH1 YDR376W D9481.5 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] FL200 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64 FUNCTION SUBCELLULAR LOCATION DISRUPTION PHENOTYPE LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Acts as an electron transfer protein. Essential for viability. H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized [adrenodoxin] FAD Mitochondrion inner membrane Peripheral membrane protein Lethality in aerobic growth conditions and also during fermentation. Present with 1600 molecules/cell in log phase SD medium. Belongs to the ferredoxin--NADP reductase type 1 family. Complete proteome Electron transport FAD Flavoprotein Membrane Mitochondrion Mitochondrion inner membrane NADP Oxidoreductase Reference proteome Transit peptide Transport H Y G S MSFVQIRHISSQINRKTVSIVGSGPSGFYTAYHLLKKSPIPLNVTIWEKLPVPFGLSRYG VAPDHPEVKNCEETFTTCAEEFSSPTNQKHKFSFVGGITIGKEILLKELLDNQDAVILSY GCTGDRKLNIPGELGTKGVFSSREFVNWYNGHPDFAKDKRFTDFDWSKVSKVGIIGNGNV ALDITRVLISNQIDEIWENTDISSLALNLLRRAPVKDVKLIARRDFVHSKFTNKELRELW ELEKYGIRGRIDPKFFQKEMFDPSKYDRAFNRRVEMCSEYLKPFNERSKKNYKKAPPPSS GYDKFWELDYLKTPLKINRDDFGAINSLSLCNNRLNEDNSLQPLKDVNNIMTYKVDLLIT SLGYAGVPMPEFSKLSIGFDKDHIANKQGRVLTSSGEIFPHLYASGWIRKGSQGVIASTM QDAFEVGDRVIQDLVVSGALSLENSIDLSNIKHTTWKDWERINKKELLRGKKEHKTRSKF LTFEELWNGVEGI P40558 D6VVS7 CFD1_YEAST Cytosolic Fe-S cluster assembly factor CFD1 Cytosolic Fe-S cluster-deficient protein 1 Ribosomal export protein 19 CFD1 DRE3 RIX19 YIL003W YIA3W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 FUNCTION INTERACTION WITH NBP35 EPR SPECTROSCOPY OF IRON-SULFUR CLUSTER PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] FUNCTION SUBUNIT MUTAGENESIS OF CYS-182; CYS-201; CYS-204 AND CYS-207 Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35. Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export. [4Fe-4S] cluster Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer. Heterotetramer of 2 NBP35 and 2 CFD1 chains. P52920 NBP35 false 9 Cytoplasm Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily. 4Fe-4S ATP-binding Complete proteome Cytoplasm Iron Iron-sulfur Metal-binding Nucleotide-binding Phosphoprotein Reference proteome K A T A C A C A C A C A MEEQEIGVPAASLAGIKHIILILSGKGGVGKSSVTTQTALTLCSMGFKVGVLDIDLTGPS LPRMFGLENESIYQGPEGWQPVKVETNSTGSLSVISLGFLLGDRGNSVIWRGPKKTSMIK QFISDVAWGELDYLLIDTPPGTSDEHISIAEELRYSKPDGGIVVTTPQSVATADVKKEIN FCKKVDLKILGIIENMSGFVCPHCAECTNIFSSGGGKRLSEQFSVPYLGNVPIDPKFVEM IENQVSSKKTLVEMYRESSLCPIFEEIMKKLRKQDTTTPVVDKHEQPQIESPK P46989 D6VW11 Q86ZR9 ATG27_YEAST Autophagy-related protein 27 Enhancer of VPS34 missorting protein 1 ATG27 ETF1 YJL178C J0490 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-103 ATCC 204511 / S288c / AB972 FUNCTION SUBCELLULAR LOCATION MUTAGENESIS OF 188-LYS--LYS-193 NOMENCLATURE SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION IDENTIFICATION IN THE ATG9-ATG23-ATG27 COMPLEX FUNCTION FUNCTION SUBCELLULAR LOCATION TOPOLOGY SUBCELLULAR LOCATION FUNCTION Effector of VPS34 phosphatidylinositol 3-phosphate kinase signaling. Regulates the cytoplasm to vacuole transport (Cvt) vesicle formation. Plays a role in ATG protein retrieval from the pre-autophagosomal structure (PAS) and is especially required for autophagy-dependent cycling of ATG9. Forms a complex with ATG9 and ATG23. Cytoplasmic vesicle membrane Single-pass type I membrane protein Golgi apparatus membrane Single-pass type I membrane protein Mitochondrion membrane Single-pass membrane protein Preautophagosomal structure membrane Single-pass type I membrane protein Cycles among the pre-autophagosomal structure (PAS), mitochondria and Golgi. Present with 8970 molecules/cell in log phase SD medium. Belongs to the ATG27 family. Autophagy Complete proteome Cytoplasmic vesicle Golgi apparatus Membrane Mitochondrion Protein transport Reference proteome Signal Transmembrane Transmembrane helix Transport KKPAKK AAPAAA MVSKTWICGFISIITVVQALSCEKHDVLKKYQVGKFSSLTSTERDTPPSTTIEKWWINVC EEHNVEPPEECKKNDMLCGLTDVILPGKDAITTQIIDFDKNIGFNVEETESALTLTLKGA TWGANSFDAKLEFQCNDNMKQDELTSHTWADKSIQLTLKGPSGCLKSKDDDKKNGDGDNG KDGDSEGKKPAKKAGGTSWFTWLFLYALLFTLIYLMVVSFLNTRGGSFQDFRAEFIQRST QFLTSLPEFCKEVVSRILGRSTAQRGGYSAV P36107 D6VXT3 Q92324 AUR1_YEAST Inositol phosphorylceramide synthase catalytic subunit AUR1 IPC synthase catalytic subunit AUR1 2.-.-.- Aureobasidin A resistance protein Phosphatidylinositol:ceramide phosphoinositol transferase AUR1 YKL004W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] MUTAGENESIS OF PHE-158 AR9-4A NUCLEOTIDE SEQUENCE [GENOMIC DNA] MUTAGENESIS OF LEU-137 AND HIS-157 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION TOPOLOGY MUTAGENESIS OF HIS-294 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-395 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] FUNCTION BIOPHYSICOCHEMICAL PROPERTIES ACTIVITY REGULATION FUNCTION SUBCELLULAR LOCATION INTERACTION WITH KEI1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Catalytic component of the inositol phosphorylceramide synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis. Inhibited by aureobasidin A (AbA), khafrefungin and rustmicin. 555 uM for phosphatidylinositol 3.0 uM for C(6)-NBD-ceramide 824 pmol/min/mg enzyme for phosphatidylinositol 367 pmol/min/mg enzyme for C(6)-NBD-ceramide Component of the inositol phosphorylceramide synthase complex composed of at least AUR1 and KEI1. Q06346 KEI1 false 2 Golgi apparatus Golgi stack membrane Multi-pass membrane protein Present with 4170 molecules/cell in log phase SD medium. Belongs to the AUR1 family. Complete proteome Glycoprotein Golgi apparatus Lipid metabolism Membrane Phosphoprotein Reference proteome Sphingolipid metabolism Transferase Transmembrane Transmembrane helix L F H Y F Y H A MANPFSRWFLSERPPNCHVADLETSLDPHQTLLKVQKYKPALSDWVHYIFLGSIMLFVFI TNPAPWIFKILFYCFLGTLFIIPATSQFFFNALPILTWVALYFTSSYFPDDRRPPITVKV LPAVETILYGDNLSDILATSTNSFLDILAWLPYGLFHFGAPFVVAAILFVFGPPTVLQGY AFAFGYMNLFGVIMQNVFPAAPPWYKILYGLQSANYDMHGSPGGLARIDKLLGINMYTTA FSNSSVIFGAFPSLHSGCATMEALFFCYCFPKLKPLFIAYVCWLWWSTMYLTHHYFVDLM AGSVLSYVIFQYTKYTHLPIVDTSLFCRWSYTSIEKYDISKSDPLAADSNDIESVPLSNL ELDFDLNMTDEPSVSPSLFDGSTSVSRSSATSITSLGVKRA P24870 D6VRJ5 CG23_YEAST G2/mitotic-specific cyclin-3 CLB3 YDL155W D1539 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-383 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the CDC2 protein kinase to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. Q00684 CDC14 false 2 P20486 CKS1 false 4 Present with 892 molecules/cell in log phase SD medium. Belongs to the cyclin family. Cyclin AB subfamily. Cell cycle Cell division Complete proteome Cyclin Mitosis Reference proteome D R MHHNSQSLSSGHIRSPEDENVAPIGNLKHRTGSLSHISSAHPRVALSDVTNIVATNSSNN SISKPKVAPIKERLDSAAIIEEERLDANSVAQRKEADHNDLLTDREQEEPVEDDGESEED EEEDQEPLLLQHYASDTLVWEHAFRTYYRTTLDPNDDDVYDVVMVAELSNEIFEYMRKLE DLYKPNPYYMDKQPELRWSFRSTLIDWIVQVHEKFQLLPETLYLCINIIDRYLCKEVVPV NKFQLVGAASLFIAAKYEEINCPTIKDFVYMSENCYSRNDLLDAERTILNGLEFELGWPG PMSFLRRISKADDYEHDTRTLAKYLLESTIMDHRLVSAQPSWLAAGAYFLSKIILGQNQW SLAHVYYSNYTQEQILPLATIILENCRYASKRHNAIWRKYSSRRYLHSSQIVAKWIALAE HRVERSN Q12092 D6W3K2 ATG29_YEAST Autophagy-related protein 29 ATG29 YPL166W P2540 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION SUBCELLULAR LOCATION FUNCTION FUNCTION SUBCELLULAR LOCATION INTERACTION WITH ATG1 AND ATG17 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] INTERACTION WITH ATG17 AND ATG31 IDENTIFICATION IN THE ATG17-ATG29-ATG31 COMPLEX INTERACTION WITH THE ATG1-ATG13 COMPLEX FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND SER-188 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Plays a role in autophagy. Functions at the preautophagosomal structure (PAS) in order to form normal autophagosomes under starvation conditions. Plays also a role in mitophagy and regulation of filamentous growth. Forms a stable complex with ATG17 and ATG31. Interacts directly with ATG31. The ATG17-ATG29-ATG31 complex interacts with the ATG1-ATG13 complex. Note=The interaction with the ATG1-ATG13 complex is induced by starvation. Preautophagosomal structure Localizes also to other perivacuolar punctate structures. Present with 752 molecules/cell in log phase SD medium. Belongs to the ATG29 family. Autophagy Complete proteome Phosphoprotein Protein transport Reference proteome Transport MIMNSTNTVVYIKVKGRRPQGFLDPPKFEWNGTKERQLWTMVSNLNYSQDQIDWQNLSKI FETPEFFLKKRTYKLFAEHLELLQLQLEKKRDLEKYSNDQVNEGMSDLIHKYTPTLQNDN LLNVSASPLTTERQDSEEVETEVTNEALQHLQTSKILNIHKKTSDSENKPNDKLDKDGIN KEMECGSSDDDLSSSLSVSKSALEEALMDRLQF Q03981 D6VSG1 CSN9_YEAST COP9 signalosome complex subunit 9 CSN9 YDR179C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION OF THE COP9 SIGNALOSOME COMPLEX INTERACTION WITH CSN12 AND CSI1 IDENTIFICATION IN THE COP9 SIGNALOSOME COMPLEX FUNCTION OF THE COP9 SIGNALOSOME COMPLEX INTERACTION WITH RRI1/CSN5 IDENTIFICATION BY MASS SPECTROMETRY INTERACTION WITH CSN12; CSI1 AND RPN5 IDENTIFICATION IN THE COP9 SIGNALOSOME COMPLEX SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Component of the COP9 signalosome (CSN) complex that acts as a regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes. The CSN complex is involved in the regulation of the mating pheromone response. Component of a COP9 signalosome-like (CSN) complex, composed of at least RRI1/CSN5, CSN9, RRI2/CSN10, PCI8/CSN11, CSN12 and CSI1. In the complex, it probably interacts directly with CSN12 and CSI1. Interacts also with RPN5. Q04368 CSI1 false 5 Q12250 RPN5 false 5 Cytoplasm Nucleus Present with 358 molecules/cell in log phase SD medium. Complete proteome Cytoplasm Nucleus Reference proteome Signalosome MVMREETIKSLEDPYKYHYKEEWLNTKDPDEQQLFEIFAFGNIKDLPENIILTSLMRSKL EKLTLVTLSEIYNELSYELIKEECQIEDDGIIESHLIQLQNIFKAEMDSVSKSMKFSRRF DCRDVYCHEKELTIIKNPRVTKEYLVQNLRSWETKLKQNILE P47158 D6VWU1 CAF17_YEAST Putative transferase CAF17, mitochondrial 2.1.-.- 57 kDa iron-sulfur cluster assembly factor for biotin synthase- and aconitase-like mitochondrial proteins CCR4-associated factor 17 IBA57 CAF17 YJR122W J2043 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c INDUCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] INTERACTION WITH CCR4 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY FUNCTION SUBCELLULAR LOCATION INTERACTION WITH ISA1 AND ISA2 Required for lysine and glutamate prototrophy and mitochondrial genome maintenance. Has a role in the maturation of mitochondrial aconitase-type and radical-SAM Fe/S proteins biotin synthase and lipoic acid synthase. Interacts with CCR4, ISA1 and ISA2. Mitochondrion matrix Up-regulated during calcium shortage. Present with 2960 molecules/cell in log phase SD medium. Belongs to the GcvT family. CAF17 subfamily. Complete proteome Mitochondrion Reference proteome Transferase Transit peptide MFISRRCRIKGFTLKNLLWFRSSSTRFVSTESPDASAITKPDGIFNYSLLENRTYIRIRG PDTVKFLNGLVTSKLLPHFIKKNLTTVEENEVPTEEGTTKVDPIIPVPEFDARLGNWGLY NEKGIQGPYISRFGLYSAFLNGKGKLITDTIIYPTPVTVSEQISNYPEYLLELHGNVVDK ILHVLQTHKLANKIKFEKIDHSSLKTWDVEVQFPNLPKDIENPWFDNLLDPMALPKNSID ANNFAVNVLNSLFNSDPRILGIYVERRTESMSRHYSTFPQSFRVVTSEQVDDLSKLFNFN VFDFPFQVNKKASVQVREIRFQKGLIDSTEDYISETLLPLELNFDFFPNTISTNKGCYVG QELTARTYATGILRKRLVPVKLDNYQLLDTDPERKYAEFHIDNVVEKSLAENEPTLNPFT NKPPERTKRKQRPAGLLISNEGLYGVALLRTEHFSAAFSSDEPVEFYITTTKGENIKITP QKPFWFSDWKNNNGPHK P00331 D6W0D0 ADH2_YEAST Alcohol dehydrogenase 2 1.1.1.1 Alcohol dehydrogenase II YADH-2 ADH2 ADR2 YMR303C YM9952.05C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 193-207 AND 227-234 ATCC 204508 / S288c ACETYLATION AT SER-2 REVIEW LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic alcohols. a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH a secondary alcohol + NAD(+) = a ketone + H(+) + NADH Zn(2+) Binds 2 Zn(2+) ions per subunit. Homotetramer. Cytoplasm Repressed by glucose. Present with 1620 molecules/cell in log phase SD medium. Belongs to the zinc-containing alcohol dehydrogenase family. Acetylation Complete proteome Cytoplasm Direct protein sequencing Isopeptide bond Metal-binding NAD Oxidoreductase Phosphoprotein Reference proteome Ubl conjugation Zinc N H P A V K MSIPETQKAIIFYESNGKLEHKDIPVPKPKPNELLINVKYSGVCHTDLHAWHGDWPLPTK LPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGY THDGSFQEYATADAVQAAHIPQGTDLAEVAPILCAGITVYKALKSANLRAGHWAAISGAA GGLGSLAVQYAKAMGYRVLGIDGGPGKEELFTSLGGEVFIDFTKEKDIVSAVVKATNGGA HGIINVSVSEAAIEASTRYCRANGTVVLVGLPAGAKCSSDVFNHVVKSISIVGSYVGNRA DTREALDFFARGLVKSPIKVVGLSSLPEIYEKMEKGQIAGRYVVDTSK Q05902 D6VYU3 ECM38_YEAST Glutathione hydrolase proenzyme 3.4.19.13 CIK1 suppressor protein 2 Extracellular mutant protein 38 Gamma-glutamyltransferase 2.3.2.2 Gamma-glutamyltranspeptidase Gamma-GT Glutathione hydrolase heavy chain Glutathione hydrolase light chain ECM38 CIS2 YLR299W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CATALYTIC ACTIVITY INDUCTION CATALYTIC ACTIVITY SUBCELLULAR LOCATION INDUCTION SUBCELLULAR LOCATION ACTIVITY REGULATION IDENTIFICATION INDUCTION FUNCTION SUBCELLULAR LOCATION INDUCTION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] VARIANTS ARG-171 AND ASP-494 ATCC 76625 / YPH499 Catalyzes the transfer of the gamma-glutamyl moiety of glutathione (GSH) and other gamma-glutamyl compounds to amino acids and peptides. Major GSH-degrading enzyme, catalyzing the hydrolytic release of L-glutamate from GSH. Plays a role in the turnover of the vacuolar GSH, serving as an alternative nitrogen source during nitrogen starvation. an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide] glutathione + H2O = L-cysteinylglycine + L-glutamate an S-substituted glutathione + H2O = an S-substitued L-cysteinylglycine + L-glutamate Activity is decreased by glutathione and ammonium ion. Sulfur metabolism; glutathione metabolism. Heterodimer composed of a light and a heavy chain. The active site is located in the light chain. Vacuole membrane Single-pass type II membrane protein Induced upon nitrogen starvation. Repressed by ammonium ions. 6-diazo-5-oxo-L-norleucine and L-azaserine are irreversible inhibitors whereas serine-borate is a reversible inhibitor. Cleaved by autocatalysis into a large and a small subunit. Present with 672 molecules/cell in log phase SD medium. Belongs to the gamma-glutamyltransferase family. Acyltransferase Complete proteome Glycoprotein Hydrolase Membrane Protease Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix Vacuole H R G D MLLCNRKVPKTLNTCFILHIFTLLTLGVLVSGMPSKMVSFASQETLQRINNLLRGSANRD VDIIAEYLKKDDDDDGGDKDHHNIDIDPLPRRPSLTPDRQLLKVGLHGAISSDLEVCSNL TINEVLLKFPGSNAADAAVTQALCKGMVNFFNSGIGGGGYVVFSGKDDEDHLSIDFREKA PMDSHKFMFENCSLCSKIGGLAVGVPGELMGLYRLFKERGSGQVDWRDLIEPVAKLGSVG WQIGEALGATLELYEDVFLTLKEDWSFVLNSTHDGVLKEGDWIKRPALSNMLMELAKNGS VAPFYDPDHWIAKSMIDTVAKYNGIMNLQDVSSYDVHVTKPLSMKIRKGANFIPDNDMTV LTSSGSSSGAALLAALRIMDNFQNQEGGDYEKETTYHLLESMKWMASARSRLGDFEGEAL PKHIEEVLDPEWALKAVKSIKRNSQDGNFKTLENWTLYDPAYDINNPHGTAHFSIVDSHG NAVSLTTTINLLFGSLVHDPKTGVIFNNEMDDFAQFNKSNSFELAPSIYNFPEPGKRPLS STAPTIVLSELGIPDLVVGASGGSRITTSVLQTIVRTYWYNMPILETIAYPRIHHQLLPD RIELESFPMIGKAVLSTLKEMGYTMKEVFPKSVVNAIRNVRGEWHAVSDYWRKRGISSVY Q06497 D6W4C5 ANT1_YEAST Peroxisomal adenine nucleotide transporter 1 ANT1 YPR128C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY FUNCTION SUBCELLULAR LOCATION INDUCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION FUNCTION Adenine nucleotide transporter involved in the uniport of ATP and adenine nucleotide hetero-exchange transport between the cytosol and the peroxisomal lumen. This transport is accompanied by a proton transport from the peroxisomal lumen to the cytosol. Transport of ATP into the peroxisome is required for beta-oxidation of medium-chain fatty acids. Required for growth on medium-chain fatty acids, pH gradient formation in peroxisomes and for normal peroxisome proliferation. Peroxisome membrane Multi-pass membrane protein Induced by oleic acid, through its ORE-like (oleate responsive element) promoter element and the PIP2-OAF1 transcription factors. Present with 2250 molecules/cell in log phase SD medium. Belongs to the mitochondrial carrier (TC 2.A.29) family. Complete proteome Hydrogen ion transport Ion transport Membrane Peroxisome Reference proteome Repeat Transmembrane Transmembrane helix Transport MLTLESALTGAVASAMANIAVYPLDLSKTIIQSQVSPSSSEDSNEGKVLPNRRYKNVVDC MINIFKEKGILGLYQGMTVTTVATFVQNFVYFFWYTFIRKSYMKHKLLGLQSLKNRDGPI TPSTIEELVLGVAAASISQLFTSPMAVVATRQQTVHSAESAKFTNVIKDIYRENNGDITA FWKGLRTGLALTINPSITYASFQRLKEVFFHDHSNDAGSLSAVQNFILGVLSKMISTLVT QPLIVAKAMLQSAGSKFTTFQEALLYLYKNEGLKSLWKGVLPQLTKGVIVQGLLFAFRGE LTKSLKRLIFLYSSFFLKHNGQRKLAST P48582 D6W3T3 Q02823 BRO1_YEAST Vacuolar-sorting protein BRO1 Amino acid sensor-independent protein 6 BCK1-like resistance to osmotic shock protein 1 BRO domain-containing protein 1 Nitrogen permease inactivating protein 3 Vacuolar protein-sorting-associated protein 31 BRO1 ASI6 LPF2 NPI3 VPS31 YPL084W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION FUNCTION FUNCTION SUBCELLULAR LOCATION FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION SUBCELLULAR LOCATION INTERACTION WITH DOA4 INTERACTION WITH DOA4 AND SNF7 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-740 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. Acts as an adapter that recruits the DOA4 deubiquitinase to the endosomes, leading to deubiquitination of cargo proteins prior to the lumenal sequestration. Its association to the endosomes depends on SNF7 and its dissociation requires VPS4. Interacts functionally with the Pkc1p-mitogen-activated protein kinase pathway. Interacts with DOA4 and SNF7. P32571 DOA4 false 15 Q08003 RFU1 false 2 P39929 SNF7 false 3 Cytoplasm Endosome The coiled-coil domain is essential for MVB sorting. The BRO1 domain may be involved in the binding to SNF7. Present with 10200 molecules/cell in log phase SD medium. 3D-structure Coiled coil Complete proteome Cytoplasm Endosome Phosphoprotein Protein transport Reference proteome Transport C Y MKPYLFDLKLKDTEKLDWKKGLSSYLKKSYGSSQWRTFYDEKATSELDHLRNNANGELAP SSLSEQNLKYYSFLEHLYFRLGSKGSRLKMDFTWYDAEYSSAQKGLKYTQHTLAFEKSCT LFNIAVIFTQIARENINEDYKNSIANLTKAFSCFEYLSENFLNSPSVDLQSENTRFLANI CHAEAQELFVLKLLNDQISSKQYTLISKLSRATCNLFQKCHDFMKEIDDDVAIYGEPKWK TTVTCKLHFYKSLSAYYHGLHLEEENRVGEAIAFLDFSMQQLISSLPFKTWLVEFIDFDG FKETLEKKQKELIKDNDFIYHESVPAVVQVDSIKALDAIKSPTWEKILEPYMQDVANKCD SLYRGIIPLDVYEKESIYSEEKATLLRKQVEETETANLEYSSFIEFTNLPRLLSDLEKQF SDGNIFSNTDTQGQLMRDQIQTWCKFIQTNEFRDIEEQMNKIVFKRKQILEILSALPNDQ KENVTKLKSSLVAASNSDEKLFACVKPHIVEINLLNDNGKIWKKFDEFNRNTPPQPSLLD IDDTKNDKILELLKQVKGHAEDLRTLKEERSRNLSELRDEINNDDITKLLIINKGKSDVE LKDLFEVELEKFEPLSTRIEATIYKQSSMIDDIKAKLDEIFHLSNFKDKSSGEEKFLEDR KNFFDKLQEAVKSFSIFASDLPKGIEFYDSLFNMSRDLAERVRVAKQTEDSTANSPAPPL PPLDSKASVVGGPPLLPQKSAAFQSLSRQGLNLGDQFQNLKISAGSDLPQGPGIPPRTYE ASPYAATPTMAAPPVPPKQSQEDMYDLRRRKAVENEERELQENPTSFYNRPSVFDENMYS KYSS P37898 D3DKZ5 AAP1_YEAST Alanine/arginine aminopeptidase 3.4.11.- AAP1 YHR047C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-652 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Positive effector of glycogen accumulation. May be involved in nutrient-sensing. Zn(2+) Binds 1 zinc ion per subunit. Present with 77000 molecules/cell in log phase SD medium. Belongs to the peptidase M1 family. Aminopeptidase Complete proteome Hydrolase Metal-binding Metalloprotease Protease Reference proteome Zinc V E MSREVLPNNVTPLHYDITLEPNFRAFTFEGSLKIDLQINDHSINSVQINYLEIDFHSARI EGVNAIEVNKNENQQKATLVFPNGTFENLGPSAKLEIIFSGILNDQMAGFYRAKYTDKVT GETKYMATTQMEATDARRAFPCFDEPNLKATFAVTLVSESFLTHLSNMDVRNETIKEGKK YTTFNTTPKMSTYLVAFIVADLRYVESNNFRIPVRVYSTPGDEKFGQFAANLAARTLRFF EDTFNIEYPLPKMDMVAVHEFSAGAMENWGLVTYRVIDLLLDIENSSLDRIQRVAEVIQH ELAHQWFGNLVTMDWWEGLWLNEGFATWMSWYSCNKFQPEWKVWEQYVTDNLQRALNLDS LRSSHPIEVPVNNADEINQIFDAISYSKGSSLLRMISKWLGEETFIKGVSQYLNKFKYGN AKTGDLWDALADASGKDVCSVMNIWTKRVGFPVLSVKEHKNKITLTQHRYLSTGDVKEEE DTTIYPILLALKDSTGIDNTLVLNEKSATFELKNEEFFKINGDQSGIFITSYSDERWAKL SKQANLLSVEDRVGLVADAKALSASGYTSTTNFLNLISNWKNEDSFVVWEQIINSLSALK STWVFEPEDILNALDKFTLDLVLNKLSELGWNIGEDDSFAIQRLKVTLFSAACTSGNEKM QSIAVEMFEEYANGNKQAIPALFKAVVFNTVARLGGENNYEKIFNIYQNPVSSEEKIIAL RALGRFEDKELLERTLSYLLDGTVLNQDFYIPMQGIRVHKKGIERLWAWMQEHWDEIAKR LQPGSPVLGGVLTLGLTNFTSFEALEKISAFYSRKVTKGFDQTLAQALDTIRSKAQWVSR DREIVATYLREHEYDQ P53318 D6VV35 Q05674 Q05675 COQ6_YEAST Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial 1.14.13.- Ubiquinone C4-deaminase 3.5.-.- COQ6 YGR255C G9165 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] SUBCELLULAR LOCATION COFACTOR PATHWAY NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION IN COQ ENZYME COMPLEX INTERACTION WITH COQ9 FUNCTION CATALYTIC ACTIVITY MUTAGENESIS OF GLY-202; GLY-386 AND ASN-388 SUBUNIT FUNCTION CATALYTIC ACTIVITY FUNCTION COFACTOR MUTAGENESIS OF GLY-248 AND LEU-382 FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-hexaprenyl-4-hydroxybenzoic acid (HHB) to 3-hexaprenyl-4,5-dihydroxybenzoic acid (DHHB). The electrons required for the hydroxylation reaction may be funneled indirectly from NADPH via ferredoxin (YAH1) and ferredoxin reductase (ARH1) to COQ6 (By similarity) (PubMed:21944752). Can also convert 3-hexaprenyl-4-aminobenzoic acid (HAB), a COQ2-prenylated pABA, to DHHB in a too step process. HAB is first hydroxylated at C5 to yield 3-hexaprenyl-4-amino-5-hydroxybenzoic acid (HHAB) which is further deaminated at C4 by COQ6 to produce DHHB (PubMed:26260787). 4-hydroxy-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] 4-amino-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 4-amino-5-hydroxy-3-all-trans-hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] 4-amino-5-hydroxy-3-all-trans-hexaprenylbenzoate + 5 H(+) + O2 + 4 reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate + H2O + NH4(+) + 4 oxidized [2Fe-2S]-[ferredoxin] FAD Cofactor biosynthesis; ubiquinone biosynthesis. Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. Mitochondrion inner membrane Peripheral membrane protein Matrix side Present with 2940 molecules/cell in log phase SD medium. Belongs to the UbiH/COQ6 family. Based on current literature, utilization of para-aminobenzoic acid (pABA) involving C4-deamination seems not to occur in bacteria, plants and mammals where only C5 hydroxylation of HHB has been shown, even if human COQ6 is able to perform the deamination reaction in the absence of COQ9. Complete proteome FAD Flavoprotein Hydrolase Membrane Mitochondrion Mitochondrion inner membrane Monooxygenase Oxidoreductase Reference proteome Transit peptide Ubiquinone biosynthesis G A G R L E G A N D V I K R K E MFFSKVMLTRRILVRGLATAKSSAPKLTDVLIVGGGPAGLTLAASIKNSPQLKDLKTTLV DMVDLKDKLSDFYNSPPDYFTNRIVSVTPRSIHFLENNAGATLMHDRIQSYDGLYVTDGC SKATLDLARDSMLCMIEIINIQASLYNRISQYDSKKDSIDIIDNTKVVNIKHSDPNDPLS WPLVTLSNGEVYKTRLLVGADGFNSPTRRFSQIPSRGWMYNAYGVVASMKLEYPPFKLRG WQRFLPTGPIAHLPMPENNATLVWSSSERLSRLLLSLPPESFTALINAAFVLEDADMNYY YRTLEDGSMDTDKLIEDIKFRTEEIYATLKDESDIDEIYPPRVVSIIDKTRARFPLKLTH ADRYCTDRVALVGDAAHTTHPLAGQGLNMGQTDVHGLVYALEKAMERGLDIGSSLSLEPF WAERYPSNNVLLGMADKLFKLYHTNFPPVVALRTFGLNLTNKIGPVKNMIIDTLGGNEK P46963 D6W0H2 Q6LBS6 CTK3_YEAST CTD kinase subunit gamma CTDK-I gamma subunit CTD kinase 32 kDa subunit CTD kinase subunit 3 CTK3 YML112W YM8339.07 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 146-173 CTD KINASE ACTIVITY SUBUNIT DISRUPTION PHENOTYPE NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-262 FUNCTION IN RNA POLYMERASE II TRANSCRIPTION CTK1 ACTIVATION INTERACTION WITH CTK1 AND CTK2 UBIQUITINATION MUTAGENESIS OF 247-TYR--TYR-296 FUNCTION DISRUPTION PHENOTYPE FUNCTION IN H3 METHYLATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION OF THE CTDK-I COMPLEX FUNCTION IN RNA POLYMERASE I TRANSCRIPTION SUBCELLULAR LOCATION FUNCTION IN ADAPTATION TO ALTERNATIVE CARBON SOURCES FUNCTION IN THE INTEGRITY OF RDNA IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Gamma subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase I transcription and RNA polymerase II transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA 3'-end processing and SET2 mediated H3K36 methylation. Together with CTK2, required for CTK1 CTD kinase activation. Required for DNA damage induced transcription. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus. CTDK-I consists of three subunits, CTK1, CTK2 and CTK3 (also called alpha, beta and gamma). Interacts with CTK1. Heterodimerization with CTK2 is required to protect this subunit from degradation. Q03957 CTK1 false 7 P46962 CTK2 false 10 Nucleus Nucleolus Cytoplasm Ubiquitinated. Ubiquitination leads to degradation by the 26S proteasome pathway. Null mutants are viable, but grow more slowly than wild-type cells at 30 degrees Celsius. They are cold-sensitive, failing to grow at 12 degrees Celsius. They display flocculent growth in liquid media and they show abnormal cell morphologies, for example, a significant fraction of the cells are greatly enlarged. Deletion mutant is sensitive to the DNA synthesis inhibitor hydroxyurea (HU) and UV irradiation. Present with 2640 molecules/cell in log phase SD medium. Belongs to the CTK3 family. Complete proteome Cytoplasm Direct protein sequencing DNA damage mRNA processing Nucleus Phosphoprotein Reference proteome Transcription Ubl conjugation N T M MLM L V T I I M MDSLEARLQFIQVLKNLQKTLHKTRDSITSSSTTTPPSSQQKLNNDPIQFYLRNYRHHYE DFHQCLFDTTMKMDPLDRLDVVIYYVRIIRNLYPHSHSNTNVTKVLNEVLLMDIDLVFEL CLPCQDWKSLTNQATCKELFLDLSKLIHYDATSVTHTPSDTTLIDATTWYSVKTERTTKD YKESLQRTESLLKDRDLKKLAFFQQFNSDTTAINPDLQTQPTNANILLHRMEADRELHKR SKETSWYIERPSNDILDESEFKSLWTHFETTDSGFDKDDYKNIKALNDIAKASYIY P49089 D6W4E2 ASNS1_YEAST Asparagine synthetase [glutamine-hydrolyzing] 1 6.3.5.4 Glutamine-dependent asparagine synthetase 1 ASN1 YPR145W P9659.3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-509 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate + H(+) + L-asparagine + L-glutamate Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1. Amino-acid biosynthesis Asparagine biosynthesis ATP-binding Complete proteome Glutamine amidotransferase Ligase Nucleotide-binding Phosphoprotein Reference proteome MCGIFAAFRHEDVHRYKPKALQLSKRIRHRGPDWSGNAIKNSTIFVHERLAIVGVESGAQ PITSSDGEYMLCVNGEIYNHIQLREECADYEFGTLSDCEPIIPMYLKHDIDAPKYLDGMF AWTLYDAKQDRIVAARDPIGITTLYMGRSSASPKTVYFASELKCLTDDCDTITAFPPGHV YDSKTDKITRYFTPDWLDEKRIPSTPIDYMAIRHSLEKAVRKRLMAEVPYGVLLSGGLDS SLIASIAARETAKATNDVEPSTYDSKARHLAGIDDDGKLHTAGWTSLHSFAIGLPNAPDL QAARKVAKFIGSIHHEHTFTLQEGLDALDDVIYHLETYDVTTIRASTPMFLLSRKIKAQG VKMVLSGEGSDEIFGGYLYFAQAPSAAEFHTESVQRVKNLHLADCLRANKSTMAWGLEAR VPFLDREFLQLCMNIDPNEKMIKPKEGRIEKYILRKAFDTTGEPDAKPYLPEEILWRQKE QFSDGVGYSWIDGLKDTAEAVISDEMFASPKAEWGSDIPTTKEAFWYRLKFDALFPQKTV ADTVMRWIPKADWGCAEDPSGRYAQIHEKHIE P05759 D6VYH3 P04838 P14800 P61864 Q6LA96 RS31_YEAST Ubiquitin-40S ribosomal protein S31 Ubiquitin 40S ribosomal protein S31 CEP76 S37 Small ribosomal subunit protein eS31 YS24 RPS31 RPS37 UBI3 YLR167W L9470.14 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PARTIAL PROTEIN SEQUENCE OF 77-95 IDENTIFICATION OF PROTEIN (S31) MUTAGENESIS OF LYS-29; LYS-48 AND LYS-63 MUTAGENESIS OF LYSINE RESIDUES IN UBIQUITIN NOMENCLATURE SUBUNIT (S31) PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] NOMENCLATURE X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME SUBUNIT SUBCELLULAR LOCATION Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). 40S ribosomal protein S31: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). Ubiquitin Cytoplasm Nucleus 40S ribosomal protein S31 Cytoplasm Ubiquitin is encoded by several different genes. UBI1 and UBI2 genes code for a single copy of ubiquitin fused to the ribosomal proteins eL40. UBI3 is a polyprotein with one copy of ubiquitin fused to ribosomal protein eS31. UBI4 is a polyprotein containing 5 exact head to tail repeats of ubiquitin. In the N-terminal section; belongs to the ubiquitin family. In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family. 3D-structure Complete proteome Cytoplasm Direct protein sequencing Isopeptide bond Metal-binding Nucleus Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein Zinc Zinc-finger K R K R K R MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGGGKKRKKKVYTTPKKIKHKHKKVKLAVLSYYKVDAEGKVTKLRRE CSNPTCGAGVFLANHKDRLYCGKCHSVYKVNA P07263 D6W443 Q12095 SYH_YEAST Histidine--tRNA ligase, mitochondrial 6.1.1.21 Histidyl-tRNA synthetase HisRS HTS1 YPR033C YP9367.13C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION ALTERNATIVE INITIATION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION ALTERNATIVE INITIATION SUBCELLULAR LOCATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] DISRUPTION PHENOTYPE MUTAGENESIS OF 198-LEU--LYS-207; LEU-198 AND VAL-381 Catalyzes the aminoacylation of histidyl-tRNA in both the cytoplasm and the mitochondrion. ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His) Isoform Cytoplasmic Cytoplasm Isoform Mitochondrial Mitochondrion P07263-1 Mitochondrial P07263-2 Cytoplasmic Produced by alternative initiation at Met-21 of isoform Mitochondrial. Lethal. Present with 26800 molecules/cell in log phase SD medium. Belongs to the class-II aminoacyl-tRNA synthetase family. Alternative initiation Aminoacyl-tRNA synthetase ATP-binding Complete proteome Cytoplasm Ligase Mitochondrion Nucleotide-binding Protein biosynthesis Reference proteome Transit peptide L V V L AAE TTK MLSRSLNKVVTSIKSSSIIRMSSATAAATSAPTANAANALKASKAPKKGKLQVSLKTPKG TKDWADSDMVIREAIFSTLSGLFKKHGGVTIDTPVFELREILAGKYGEDSKLIYNLEDQG GELCSLRYDLTVPFARYVAMNNIQSIKRYHIAKVYRRDQPAMTKGRMREFYQCDFDVAGT FESMVPDSECLSILVEGLTSLGIKDFKIKLNHRKILDGIFQIAGVKDEDVRKISSAVDKL DKSPWEAVKKEMTEEKGQSEETADKIGEYVKLNGSLKEIHAVLSADANITSNEKAKQGLD DIATLMKYTEAFDIDSFISFDLSLARGLDYYTGLIYEVVTSASAPPENASELKKKAKSAE DASEFVGVGSIAAGGRYDNLVNMFSEASGKKSTQIPCVGISFGVERIFSLIKQRINSSTT IKPTATQVFVMAFGGGKDWTGYLPERMKVTKQLWDAGIEAEYVYKAKANPRKQFDAAEKA GCHIAVILGKEEYLEGKLRVKRLGQEFADDDGELVSAADIVPIVQEKLSQIHEDGLNEVT RLIKGL Q12034 D6VTD6 E9P8Z6 SLF1_YEAST Protein SLF1 SLF1 YDR515W D9719.20 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Regulates the copper-dependent mineralization of copper sulfide complexes on the cell surface in cells cultured in medium containing copper salts. Present with 861 molecules/cell in log phase SD medium. Complete proteome Copper Reference proteome RNA-binding N S MSSQNLNDNPKNTSSAAEDKKKQTSSLKLAPIPTTSPWKSSSPDSNTVIPVEELRDISKT AKPSKNGSGSIKLTSNTKWTPITPSVIISGSKDTNSKSGKNSKNSKTNKKMKKRGKYNND INKKDFNGQTNSTSEISNVSNLESKPLDANAKVNIHSSSGATANGNIKRITNNNNSTNGR QSRNYQNRNGKTRYNNNSRHSQAANNAISFPNNYQARPEYIPNASHWLNNNSRNSYKQLS YFRQQQYYNNINYQQQLQTPYYYSMEPIFKSIESIKNQIEFYFSEENLKTDEFLRSKFKK ANDGFIPMSLIGKFYRMVNLSLGGDPNLILASMREVLQHKETNHLEIALGSIEGAQKNMA DDFNPLENYFIRRENWAEYAMESNFDENDDETEKYNIEKLLGPNDLDNYSYMGYPNFFPS NENGKKSQSYDQGEISRQFEQNLQIND P39939 A2TBN5 D3DM37 Q6B2E8 RS26B_YEAST 40S ribosomal protein S26-B Small ribosomal subunit protein eS26-B RPS26B YER131W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [MRNA] OF 1-88 ATCC 201390 / BY4743 NOMENCLATURE SUBUNIT INTERACTION WITH TSR2 INTERACTION WITH TSR2 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBUNIT SUBCELLULAR LOCATION NOMENCLATURE Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). eS26 interacts with eS1 forming part of the mRNA exit tunnel (PubMed:9559554, PubMed:22096102). eS26 interacts with TSR2 (PubMed:10688190, PubMed:12837249). Cytoplasm Present with 503000 molecules/cell in log phase SD medium. There are 2 genes for eS26 in yeast. Belongs to the eukaryotic ribosomal protein eS26 family. 3D-structure Complete proteome Cytoplasm Reference proteome Ribonucleoprotein Ribosomal protein S P MPKKRASNGRNKKGRGHVKPVRCVNCSKSIPKDKAIKRMAIRNIVEAAAVRDLSEASVYP EYALPKTYNKLHYCVSCAIHARIVRVRSREDRKNRAPPQRPRFNRDNKVSPAAAAKKAL P0C0W1 D6VW01 P04648 RS22A_YEAST 40S ribosomal protein S22-A RP50 S24 Small ribosomal subunit protein uS8-A YP58 YS22 RPS22A RPS24 RPS24A YJL190C J0355 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 2-44 NOMENCLATURE SUBUNIT CLEAVAGE OF INITIATOR METHIONINE LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] NOMENCLATURE 3D-STRUCTURE MODELING OF 4-130 ELECTRON MICROSCOPY 3D-STRUCTURE MODELING ELECTRON MICROSCOPY X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME SUBUNIT SUBCELLULAR LOCATION Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). Cytoplasm Present with 40400 molecules/cell in log phase SD medium. There are 2 genes for uS8 in yeast. Belongs to the universal ribosomal protein uS8 family. 3D-structure Complete proteome Cytoplasm Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein MTRSSVLADALNAINNAEKTGKRQVLIRPSSKVIIKFLQVMQKHGYIGEFEYIDDHRSGK IVVQLNGRLNKCGVISPRFNVKIGDIEKWTANLLPARQFGYVILTTSAGIMDHEEARRKH VSGKILGFVY Q06102 D6W4A5 YTH1_YEAST mRNA 3'-end-processing protein YTH1 Yeast 30 kDa homolog 1 YTH1 YPR107C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c IDENTIFICATION IN THE CPF COMPLEX INTERACTION WITH FIP1 RNA-BINDING MUTAGENESIS OF CYS-67; TRP-70; CYS-75; ASP-79; CYS-81 AND HIS-142 INTERACTION WITH FIP1 IDENTIFICATION IN THE CPF COMPLEX SUBCELLULAR LOCATION IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION INTERACTION WITH FIP1 AND YSH1 RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of at least PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. Interacts with FIP1 and YSH1. P45976 FIP1 false 5 Q06224 YSH1 false 4 Nucleus Present with 3690 molecules/cell in log phase SD medium. Belongs to the CPSF4/YTH1 family. 3D-structure Complete proteome Metal-binding mRNA processing Nucleus Reference proteome Repeat RNA-binding Zinc Zinc-finger C S W A C S D A C S H N MSLIHPDTAKYPFKFEPFLRQEYSFSLDPDRPICEFYNSREGPKSCPRGPLCPKKHVLPI FQNKIVCRHWLRGLCKKNDQCEYLHEYNLRKMPECVFFSKNGYCTQSPDCQYLHIDPASK IPKCENYEMGFCPLGSSCPRRHIKKVFCQRYMTGFCPLGKDECDMEHPQFIIPDEGSKLR IKRDDEINTRKMDEEKERRLNAIINGEV Q12025 D6VS42 YD056_YEAST Uncharacterized protein YDR056C YDR056C D4219 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Endoplasmic reticulum Present with 1600 molecules/cell in log phase SD medium. Complete proteome Endoplasmic reticulum Glycoprotein Reference proteome Signal MLVRLLRVILLASMVFCADILQLSYSDDAKDAIPLGTFEIDSTSDGNVTVTTVNIQDVEV SGEYCLNAQIEGKLDMPCFSYMKLRTPLKYDLIVDVDEDNEVKQVSLSYDETNDAITATV RYPEAGPTAPVTKLKKKTKTYADKKASKNKDGSTAQFEEDEEVKEVSWFQKNWKMLLLGL LIYNFVAGSAKKQQQGGAGADQKTE Q07963 D6VY26 UBR2_YEAST E3 ubiquitin-protein ligase UBR2 2.3.2.27 RING-type E3 ubiquitin transferase UBR2 Ubiquitin-protein ligase E3 component N-recognin-1 homolog UBR2 YLR024C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c INTERACTION WITH UBC2 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-709 SUB592 INTERACTION WITH UBC2 AND RPN4 FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1222 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 FUNCTION INTERACTION WITH MUB1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1218 AND SER-1222 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] E3 ubiquitin-protein ligase which probably functions outside the N-end rule pathway, since it lacks the residues essential for the degradation of N-end rule substrates. Mediates RPN4 ubiquitination and subsequent degradation. 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. Interacts with MUB1, RPN4 and UBC2. Q03162 MUB1 false 2 P06104 RAD6 false 6 Q03465 RPN4 false 2 Cytoplasm The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif. Present with 49 molecules/cell in log phase SD medium. Deletion produces no detectable phenotype. Belongs to the UBR1 family. Complete proteome Cytoplasm Isopeptide bond Metal-binding Phosphoprotein Reference proteome Transferase Ubl conjugation Ubl conjugation pathway Zinc Zinc-finger MEDSDLSITNIRDFLTELPKLAKCEYSETTSYLLWKTLNLRLKHSDNDINWRSLVSILNS EAWENEKYRDILNGRKWRTLEFENDHHSVGNMHIGTACTRLCFPSETIYYCFTCSTNPLY EICELCFDKEKHVNHSYVAKVVMRPEGRICHCGDPFAFNDPSDAFKCKNELNNIPISNDN SNVTDDENVISLLNYVLDFLIDVTVSYKEEAEAHSSERKASSLMHPNQNSITDDIMEKHE CEPLVNDENFVFFDNNWSNTRKEAHMEWAIQIEEEECNVHYMDLASTITRILNTPVEYAI SITKALEDSHDVVTVLQSENFFEIDQIAKEFQKENIVVHVRKADDIFKRKLTDDLTDWLY SLCFKAATSLQNKYALRISMLDVWYSHFSKMRVSPTNTNPDFSKINLLGGFLISNEDSDE SWFKPWSLENIEDERISKILTNYNERLIRAHSPNTVSHFYNFYGSRFQYIIINSINILSK KSKFKMLKIMASLFSLRDESRKFLAAQYIDVYLSVLYDAVASDAKECQVTLMSILGQYTF QDPSIANMTISSGFIERTIRFAFTLMAFNPEDLMSYLPISLYNGFKLPTETIRNRRTIIC FKDLCTIMSANTVPEELLSNEAIFNAIIESFSEFSNVLPLKRETKEHVEVENFDFSAFYF FFSSILIMTDGYTRSISLVKDAAFRKQIVLKLLDVAQTREFESLTNSRKAISPDNASTNE NDSNKATLSTVRETICNYVAETINFQVGVNTQYFFNPMSYLFKFVIQWSQCGRYEPIPAS LTNYINLFEVFQDKQKALYISESALSTLVLIGQINVGFWVRNGTPITHQARMYTKYSMRE FTYISDIFNVQFSMAMCNPDELMVTYLSRWGLKHWANGVPMYDYPDTETTVAVVNECILL LIQLLTEVRSLVMKSSKEGFERTFKSEIIHALCFDTCSYAQIVNCIPEHITKHPSFDIYL EKYANYTSPVSLTDNGIFVLKEKYKDEIDPYYIGLSSSRRYDVEKNIRLNMANLKKMKYE DTFVPAKKVKDLLKNTLFSGLYSISSVNTFGLFLKNTLDHIIKYDYDNLLPRVVHLIHLC VVNNLNEFMGILWHEYAIVDTEFCHYHSIGSILYYCLLKDNFSESHGKIREIFRYLMETA PHVNVNSYLREQTTSYTPGILWPTKEDKSHKDKEFERKKHLARLRKKKLMKKLAQQQMKF MENNSVDTSDISTPRTTSPSLSPTRINAENSSNTINSCCDDDCVFCKMPKDDDVFVYFSY QERNICDHGIDFTNPTDVNRINSLFSGKQTKDSAIQENPQDDDGTRLKFTSCEPVLRACG HGSHTKCLSGHMKSIRGIQNQTTKNIPLSYGSGLIYCPVCNSLSNSFLPKTNDIDKRTSS QFFMCIEKRSEAEENLDPMSSICIKAAMILGDLQGKKVTTIEDAYKVVNSVFINTISNTE LRLRSHKKEGKIVNMERISSQCILTLHLVCELKSFIYKKFVNSKTFSSEISRKIWNWNEF LIKGNNVNLLLYMSQNFDNIDGGKTPQPPNLCIYEMFKRRFHQLLLLLARDMMRVNFYKD CRNKIKISSNGSEEPSTSFSYLFNTFKKYVDLFKPDDVRFDFTSLEKIKDFICSLLLESL SIFCRRTFLLFNIQYDDDGDGDNNNNRSNNFMDVKQREIELIFRYFKLPNLTHFLKDFFY NELTQNIERYNDGNDNLRIQQVIYDMVQNINTRAYPSPEHIQLIELPLNLSKFSLDNDEI SNKCDKYEIAVCLLCGQKCHIQKSIALQGYLQGECTDHMRNGCEITSAYGVFLMTGTNAI YLSYGKRGTFYAAPYLSKYGETNEDYKFGTPVYLNRARYANLANEIVFGNMIPHIVFRLT DGSADLGGWETM P0CF16 D6VZH2 Q03665 Q04257 Q04263 Q6B2L5 Q6WV03 U5071_YEAST UPF0507 protein YML003W YML003W YM9571.16 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-290 CONFIRMATION OF FRAMESHIFT ATCC 204511 / S288c / AB972 Belongs to the UPF0507 family. This is a truncated version of an UPF0507 family protein. Strain S288c has a frameshift in position 286, which disrupts the gene coding for this protein and produces two ORFs YML003W and YML002W. A contiguous sequence for a S.cerevisiae UPF0507 family protein can be found in strain YJM789 (AC A6ZM60). Complete proteome Reference proteome MSVYHLPTLLNPLVNAIFNCPEPERSPLKKLFANLKTRRFILLAPPSEYLLNYHDVKSKL PLHDLCYNAEFINSYILLMTENSYINTNSRDSHYETLDGKTVVIQWKNNVIHALNGFHIR RRLKILETKILPNFNDYFEGAADFIILFIDQPLNCEFVPNDYLQCFHNYEKIPKNAHAMP NLSIDSFQQERSSFENILHIHPARLTQLGQLFSSYRTLAPGDDPSRSIFESIVQQAFDGM KSDSLFKNFSNLYDLIHDYFELNLYDDIWSRLTTHFKGHEVDTEKINIFQ P39989 A0A1S0T060 YEC8_YEAST Uncharacterized protein YEL028W YEL028W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c Complete proteome Reference proteome Signal MKITITSLLFFLVMIVELASAGTLLHNGANLPSLRDNTTLTDARNVLKYLQVLGFPSNKI AATDTVGTFIIFSNRTEANTTAMTKTVSYCYRNYGHSFYFTHYKYDYFPSGISYMAKLGD ATVNHTDLPHFRNNKRLTTQELNAFQHPIVEFQ P38835 D3DL79 YHT1_YEAST PH domain-containing protein YHR131C YHR131C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c SEQUENCE REVISION TO N-TERMINUS GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION OF FRAMESHIFT SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] P39940 RSP5 false 3 Cytoplasm Present with 172 molecules/cell in log phase SD medium. Complete proteome Cytoplasm Reference proteome MALPIEGKLSMANNRIERLKSPSSSSTCSMDEVLITSSNNSSSICLETMRQLPREGVSGQ INIIKETAASSSSHAALFIKQDLYEHIDPLPAYPPSYDLVNPNKEVRFPIFGDTAPCPKS SLPPLYAPAVYELTLISLKLERLSPYEISSNRSWRNFIIEINSTQLNFYHIDESLTKHIR NYSSGETKSEKEDRIHSDLVHRSDQSQHLHHRLFTLPTRSASEFKKADQERISYRVKRDR SRYLTDEALYKSFTLQNARFGIPTDYTKKSFVLRMSCESEQFLLRFSHIDDMIDWSMYLS IGISVSLDLEVREYPDYRIVPRRRRRRRRRRRRRRHTHRSESSMGSFSQRFIRSNSRPDL IQRYSTGSSTNNNTTIRERSNTFTAGLLDHYCTGLSKTPTEALISSAASGESSDNSTLGS TRSLSGCSASRSIASRSLKFKIKNFFRPKNSSRTEKLHRLRSNSSNLNSVIETEEDDEHH ESSGGDHPEPGVPVNTTIKVERPMHRNRAISMPQRQSLRRAISEEVVPIKFPNSTVGESV HSPSPIEHLSVDGCEIMLQSQNAVMKEELRSVASNLVANERDEASIRPKPQSSSIYLSGL APNGESATDLSQSSRSLCLTNRDAEINDDESATETDEDENDGETDEYAGDDTNDDTDDSN IGYAYGSESDYSCLIEERIRNRRRASSTLSCFSNIPYGTDDIKWKPAIKEISRRRYLRDS LKCIKPFLDSNDCLGKVIYIPVSGPTFETSNKIHFSNRQSLQKQKNHFLKGFIVGPTALI ELNCKNKNAIVGTTKDAEDHGEDDGDGDDGEDDDDDDDDDDDDDDDEDDDDDDDDDDDDD DDDDDGQITA Q12235 D6VXV3 YCT1_YEAST High affinity cysteine transporter YCT1 YLL055W L0578 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c INDUCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A FUNCTION BIOPHYSICOCHEMICAL PROPERTIES SUBCELLULAR LOCATION INDUCTION IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] INDUCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500 AND SER-501 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] INDUCTION High affinity cysteine-specific transporter. Major contributor to cysteine transport when cysteine, at low concentrations, is provided as the sole sulfur source. 55.4 uM for cysteine 22.4 nmol/min/mg enzyme for cysteine transport Cell membrane Multi-pass membrane protein Endoplasmic reticulum membrane Multi-pass membrane protein Induced under nitrogen starvation conditions, co-regulated by GCN4 and GLN3. Regulated by the MET4-based sulfur regulatory network. Expression is maximum in nonrepressing sulfur conditions and considerably repressed in the presence of organic sulfur. Induced by chromate. Belongs to the major facilitator superfamily. Allantoate permease family. Amino-acid transport Cell membrane Coiled coil Complete proteome Endoplasmic reticulum Glycoprotein Membrane Phosphoprotein Reference proteome Transmembrane Transmembrane helix Transport MSKVDVKIGADSISSSDEILVPSRLADVTLAFMEENDAAVPEITPEQEKKLKRKLFLTIF TFVSAINLLLYMDKATLSYDSILGFFEDTGLTQNTYNTVNTLFYVGFAIGQFPGQYLAQK LPLGKFLGGLLATWTILIFLSCTAYNFSGVVALRFFLGLTESVVIPILITTMGMFFDASE RAAAQPFFFAACMGSPIPTGFIAYGVLHITNPSISLWKIFTIIIGGLTFIMTVVVILWFP NNPADVKFFSIQERVWIIRRVQASTGSSIEQKVFKKSQFREAMKDYITWLFGLFFLLQQL ANNLPYQQNLLFEGMGGVDALGSTLVSVAGAGFAVVCAFIATLMLAKWKNISALTAIFWT LPALVGSIAAAALPWDNKIGILANICMAGQIFGIPFIIALSWASSSASGYTKKLTRSSVS LFAMGIANIISPQIWREKDSPRFLPAWIVQIVLSFSLAPAILLLIHFILKRRNNQRLKNY DENLQNYLDRIQLIESENPSSIEEGKVVTHENNLAVFDLTDLENETFIYPL Q12130 A0A1S0T095 YL112_YEAST Uncharacterized protein YLR112W YLR112W L2928 L9354.3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 90840 / EAY235 / FY23 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c Complete proteome Reference proteome MGGRSAQPRRFSFACRILHPAVAHDAMAGSRYILRAPASIIRLAQHGWLHCCLHFFLFPA MNDVCFVAKGSALYLFTVEIIVFGSPSLRHNVLSFFYFALPWFKRQCRLKVNFNRLKEIR GIAQVVRKAFFISKTLPCI P36036 D6VWY9 YRA2_YEAST RNA annealing protein YRA2 YRA2 YKL214C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION ASSOCIATION WITH MRNPS SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION INTERACTION WITH YRA1 IDENTIFICATION BY MASS SPECTROMETRY ASSOCIATION WITH MRNPS DNA-BINDING ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in export of poly(A) mRNAs from the nucleus. Recruited to the coding sequences as well as poly-A sites of active genes. Associates with mRNPs. Interacts with YRA1. Nucleus Present with 1310 molecules/cell in log phase SD medium. Belongs to the YRA1 family. Acetylation Complete proteome DNA-binding mRNA transport Nucleus Reference proteome RNA-binding Transport MDKAFDEIIGNSHTDSSSNHKVTRYRRRDLRNELGPRLGFAPSDAASRSKDRLYREREEP PLPKRIRISKIPLDVSDYTLDDMIKEFGSPIFSKIFDNKEDRTCIYEFEDPEVLEKIVER YNGHELHNAKIEVEIYQPQRKHSRMNAHNRRKQTAQEHGRGRPGSHYRQKPNRVSKKNKG REKNNTPTSVEALDAELDAYMKG Q05016 D6W051 YM71_YEAST NADP-dependent 3-hydroxy acid dehydrogenase L-allo-threonine dehydrogenase 1.1.1.381 YMR226C YM9959.08C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 1-14 FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES SUBSTRATE SPECIFICITY SUBUNIT SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH NADP NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. L-allo-threonine + NADP(+) = aminoacetone + CO2 + NADPH 0.5 mM for NADP(+) (at pH 9 and at 30 degrees Celsius) 95 mM for L-serine (at pH 9 and at 30 degrees Celsius) 71 mM for D-serine (at pH 9 and at 30 degrees Celsius) 7 mM for D-threonine (at pH 9 and at 30 degrees Celsius) 3 mM for L-allo-threonine (at pH 9 and at 30 degrees Celsius) 36 mM for L-3-hydroxyisobutyrate (at pH 9 and at 30 degrees Celsius) 57 mM for D-3-hydroxyisobutyrate (at pH 9 and at 30 degrees Celsius) 95 mM for L-3-hydroxybutyrate (at pH 9 and at 30 degrees Celsius) The highest catalytic efficiency was observed with L-allo-threonine. Optimum pH is about 8.5 for the oxidation of L-serine. Stable from pH 7.5 to 10.5. Stable up to 40 degrees Celsius. Homotetramer. P39009 DUN1 false 2 Cytoplasm Nucleus Present with 3210 molecules/cell in log phase SD medium. Belongs to the short-chain dehydrogenases/reductases (SDR) family. 3D-structure Complete proteome Cytoplasm Direct protein sequencing NADP Nucleus Oxidoreductase Phosphoprotein Reference proteome MSQGRKAAERLAKKTVLITGASAGIGKATALEYLEASNGDMKLILAARRLEKLEELKKTI DQEFPNAKVHVAQLDITQAEKIKPFIENLPQEFKDIDILVNNAGKALGSDRVGQIATEDI QDVFDTNVTALINITQAVLPIFQAKNSGDIVNLGSIAGRDAYPTGSIYCASKFAVGAFTD SLRKELINTKIRVILIAPGLVETEFSLVRYRGNEEQAKNVYKDTTPLMADDVADLIVYAT SRKQNTVIADTLIFPTNQASPHHIFRG Q12351 D6W280 YO012_YEAST Uncharacterized protein YOR012W YOR012W OR26.02 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c Complete proteome Reference proteome MVASSINEESSLAVNLTSDVEKASKTLFKAFEKSYANDYLMKKFFHIPITEKVSRARINA MIHYYTTCYHDLDGEIAEANDFDAVAIWSRPGCHLPATLSDDESFNKIFFSRLDCEEARS HASGNGLLLPLCHRKRS P40207 D6VZV7 YM17_YEAST Uncharacterized protein YMR134W YMR134W YM9375.03 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] P46956 PHO86 false 3 Membrane Single-pass membrane protein Present with 2950 molecules/cell in log phase SD medium. Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MSLKDRYLNLELKLINKLQELPYVHQFIHDRISGRITLFLIVVGTLAFFNELYITIEMSL LQKNTSEELERGRIDESLKLHRMLVSDEYHGKEYKDEKSGIVIEEFEDRDKFFAKPVFVS ELDVECNVIVDGKELLSTPLKFHVEFSPEDYENEKRPEFGTTLRVLRLRLYHYFKDCEIY RDIIKNEGGEGARKFTISNGVKIYNHKDELLPLNIDDVQLCFLKIDTGNTIKCEFIL Q08909 D6W378 YO385_YEAST Uncharacterized protein YOR385W YOR385W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Cytoplasm Present with 504 molecules/cell in log phase SD medium. Complete proteome Cytoplasm Reference proteome MRGFSGQPLSDDDNYRIEKTQRNTIPERLHFSRERNMPIASIFGTRGYFVFSSEQSYDKF KQTNFNISTLDADGVGVPLFHIVQSYNVIGKITRSSPDFYIYKYVLQGVQDPPLYSDCKV ICQDKVFRLCKILYCEIYAHQGFFETKYDFFYPSKTQPVKKYQIIKQSNMRDLYSTLDGM RFRWHVKFYSDHFRLMFLDEDRLNYSNSNQKERQKPDQGKSKAPDFVIGHYTRTFSDILP RSTSKCSNLIIGEHSKPDSLGITTVPDLTQEFACQGALIHYLLHIERERK P38749 D3DKQ4 YAP3_YEAST AP-1-like transcription factor YAP3 YAP3 YHL009C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION ISOLATION OF YAP FAMILY PROTEINS FUNCTION MULTIDRUG RESISTANCE FUNCTION MULTIDRUG RESISTANCE FUNCTION INTERACTION WITH PDR5 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Transcription activator involved in the regulation of genes expressed in response to environmental changes. When overexpressed it activates transcription of the multidrug resistance ABC transporter PDR5, thus conferring resistance to the fungicide fluconazole (FCZ) and cycloheximide. When overexpressed, it also confers, independent of PDR5, increased resistance to 4-nitroquinoline-N-oxide (4-NQO) (By similarity). Preferentially binds 5'-TTACTAA-3'. Homodimer (By similarity). Interacts with the C-terminal, cytoplasmic tail of the multidrug resistance ABC transporter PDR5. Cytoplasm Nucleus One of 8 closely related fungi-specific YAP proteins (YAP1 to YAP8), which all seem to be transcription activators of the environmental stress response and metabolism control pathways and to have similar but not identical DNA binding specificities. Present with 1700 molecules/cell in log phase SD medium. Belongs to the bZIP family. YAP subfamily. Activator Complete proteome Cytoplasm DNA-binding Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation MTPSNMDDNTSGFMKFINPQCQEEDCCIRNSLFQEDSKCIKQQPDLLSEQTAPFPILEDQ CPALNLDRSNNDLLLQNNISFPKGSDLQAIQLTPISGDYSTYVMADNNNNDNDSYSNTNY FSKNNGISPSSRSPSVAHNENVPDDSKAKKKAQNRAAQKAFRERKEARMKELQDKLLESE RNRQSLLKEIEELRKANTEINAENRLLLRSGNENFSKDIEDDTNYKYSFPTKDEFFTSMV LESKLNHKGKYSLKDNEIMKRNTQYTDEAGRHVLTVPATWEYLYKLSEERDFDVTYVMSK LQGQECCHTHGPAYPRSLIDFLVEEATLNE Q12303 D6VYB9 YPS3_YEAST Aspartic proteinase yapsin-3 3.4.23.- YPS3 YLR121C L2964 L9233.10 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 90840 / EAY235 / FY23 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 48-68 FUNCTION SUBCELLULAR LOCATION PROTEOLYTIC PROCESSING INDUCTION SUBCELLULAR LOCATION FUNCTION Cleaves proteins C-terminally to mono- and paired-basic residues. Required for cell wall integrity. Cell membrane Lipid-anchor GPI-anchor GPI-anchored plasma membrane protein (GPI-PMP). Positively regulated in response to cell wall perturbation. Can also be processed to start at Phe-54. Belongs to the peptidase A1 family. Aspartyl protease Cell membrane Cleavage on pair of basic residues Complete proteome Direct protein sequencing Glycoprotein GPI-anchor Hydrolase Lipoprotein Membrane Protease Reference proteome Signal Zymogen MKLQLAAVATLAVLTSPAFGRVLPDGKYVKIPFTKKKNGDNGELSKRSNGHEKFVLANEQ SFYSVELAIGTPSQNLTVLLDTGSADLWVPGKGNPYCGSVMDCDQYGVFDKTKSSTFKAN KSSPFYAAYGDGTYAEGAFGQDKLKYNELDLSGLSFAVANESNSTFGVLGIGLSTLEVTY SGKVAIMDKRSYEYDNFPLFLKHSGAIDATAYSLFLNDESQSSGSILFGAVDHSKYEGQL YTIPLVNLYKSQGYQHPVAFDVTLQGLGLQTDKRNITLTTTKLPALLDSGTTLTYLPSQA VALLAKSLNASYSKTLGYYEYTCPSSDNKTSVAFDFGGFRINAPLSDFTMQTSVGTCVLA IIPQAGNATAILGDSFLRNAYVVYDLDNYEISLAQAKYGTGKENVEVIKSTVPSAIRAPS YNNTWSNYASATSGGNIFTTVRTFNGTSTATTTRSTTTKKTNSTTTAKSTHKSKRALQRA ATNSASSIRSTLGLLLVPSLLILSVFFS P25303 D6W039 SCJ1_YEAST DnaJ-related protein SCJ1 J protein SCJ1 SCJ1 YMR214W YM8261.08 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION IDENTIFICATION OF PROBABLE INITIATION SITE FUNCTION FUNCTION IDENTIFICATION OF PROBABLE INITIATION SITE LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Regulates protein folding in the endoplasmic reticulum lumen. Probably acts as a J-protein for the Hsp70-type chaperone KAR2 by stimulating its ATP-dependent reaction cycle and initiating folding reactions. Also involved in the endoplasmic reticulum-associated degradation (ERAD) process. Cooperates with KAR2 and another J-protein JEM1 to facilitate the export of ERAD substrates to the cytoplasm by maintaining them in a translocation-competent state and preventing their aggregation in the endoplasmic reticulum lumen. Endoplasmic reticulum lumen Present with 8260 molecules/cell in log phase SD medium. Chaperone Complete proteome Endoplasmic reticulum Metal-binding Protein transport Reference proteome Repeat Signal Transport Zinc Zinc-finger MIPKLYIHLILSLLLLPLILAQDYYAILEIDKDATEKEIKSAYRQLSKKYHPDKNAGSEE AHQKFIEVGEAYDVLSDPEKKKIYDQFGADAVKNGGGGGGPGGPGAGGFHDPFDIFERMF QGGHGGPGGGFGQRQRQRGPMIKVQEKLSLKQFYSGSSIEFTLNLNDECDACHGSGSADG KLAQCPDCQGRGVIIQVLRMGIMTQQIQQMCGRCGGTGQIIKNECKTCHGKKVTKKNKFF HVDVPPGAPRNYMDTRVGEAEKGPDFDAGDLVIEFKEKDTENMGYRRRGDNLYRTEVLSA AEALYGGWQRTIEFLDENKPVKLSRPAHVVVSNGEVEVVKGFGMPKGSKGYGDLYIDYVV VMPKTFKSGQNMLKDEL Q05776 D6VYJ6 UPS1_YEAST Protein UPS1, mitochondrial Unprocessed MGM1 protein 1 UPS1 YLR193C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION SUBUNIT SUBCELLULAR LOCATION DISRUPTION PHENOTYPE FUNCTION SUBCELLULAR LOCATION FUNCTION SUBCELLULAR LOCATION SUBCELLULAR LOCATION FUNCTION INTERACTION MDM35 SUBCELLULAR LOCATION INTERACTION WITH MDM35 FUNCTION INTERACTION WITH MDM35 MUTAGENESIS OF ARG-54 X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-170 IN COMPLEX WITH PHOSPHATIDIC ACID AND MDM35 INTERACTION WITH MDM35 FUNCTION MUTAGENESIS OF PHE-23; HIS-33; ARG-42; LEU-50; LYS-58; LYS-61; TRP-77; ILE-78; VAL-84; ARG-96; ASN-97; MET-104; VAL-106; TRP-144; LYS-148 AND LYS-155 X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1-170 IN COMPLEX WITH PHOSPHATIDIC ACID AND MDM35 INTERACTION WITH MDM35 FUNCTION MUTAGENESIS OF ARG-25; LYS-61 AND LYS-155 SUBCELLULAR LOCATION Required for maintenance of normal mitochondrial morphology (PubMed:16754953, PubMed:26071601). Required for PCP1-dependent processing of MGM1 (PubMed:16754953). The UPS1:MDM35 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space (PubMed:26071602, PubMed:26071601, PubMed:26235513). Phosphatidic acid release requires dissociation of the UPS1:MDM35 complex (PubMed:26235513). Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane (PubMed:26071602). With UPS2, controls the level of cardiolipin in mitochondria (PubMed:19506038). Cardiolipin is a unique phospholipid with four fatty acid chains and is present mainly in the mitochondrial inner membrane where it stabilizes the electron transport chain supercomplex between complexes III and IV through direct interaction of their subunits. Interacts with MDM35 (PubMed:20622808, PubMed:20657548, PubMed:26071602, PubMed:26071601, PubMed:26235513). Found associated with a 170 kDa complex. O60200 MDM35 false 5 Mitochondrion inner membrane Peripheral membrane protein Intermembrane side Mitochondrion intermembrane space Lacks the two major intermembrane space-targeting signals, bipartite presequences and cysteine motifs, and import is mediated by another IMS protein, MDM35. Cells show slow growth, fragmented mitochondria and have a 50-fold reduced level of s-MGM1. These defects can be complemented by human PRELI or bypassed by growth on a nonfermentable carbon source. Present with 704 molecules/cell in log phase SD medium. Belongs to the slowmo family. 3D-structure Complete proteome Lipid transport Lipid-binding Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Transport F D R E R K H E R D L D R E K E K E K E L A W A W D I D V E R D N A M E V E W E K E K E K E MVLLHKSTHIFPTDFASVSRAFFNRYPNPYSPHVLSIDTISRNVDQEGNLRTTRLLKKSG KLPTWVKPFLRGITETWIIEVSVVNPANSTMKTYTRNLDHTGIMKVEEYTTYQFDSATSS TIADSRVKFSSGFNMGIKSKVEDWSRTKFDENVKKSRMGMAFVIQKLEEARNPQF P53110 D6VTZ2 YGP9_YEAST Uncharacterized protein YGL159W YGL159W G1840 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Present with 172 molecules/cell in log phase SD medium. Belongs to the ornithine cyclodeaminase/mu-crystallin family. Acetylation Complete proteome Reference proteome MNNSIITDDEVREFYLNCSSQTIIESLLSLHESLRLYSQNHEILLNRMFKKLDETNADSN ISHIFMPVVSKDFSGIKILVNNNNKNFQGVINVIEPETGKLIGCFEAKQITAIRTALASC IGLYKQLSCSHDKLFRFENGTCYLTCFGTGLQAFWHIYIAIKLIMSGIVGESLKLVEINI LYHNNMMSLDRLKSLKNLFGSNIKIELNQYQINDISSEGNGAVSNSDIIFGCLPTLEPNL FLRQLLNSKASVEQKHTYISLIGSYKPVMHECDKELIDKFKSDNESACILVDSREHTLLE SGELIDSNIAPHNLIEIGELDTLKNTVLNLNEKGCKRTITLCKIVGLAVMDVALAKEFLS LRTKNTENKE Q03829 D6VZY8 YM39_YEAST Uncharacterized mitochondrial carrier YMR166C YMR166C YM8520.15C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Mitochondrion inner membrane Multi-pass membrane protein Present with 2060 molecules/cell in log phase SD medium. Belongs to the mitochondrial carrier (TC 2.A.29) family. Complete proteome Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Repeat Transmembrane Transmembrane helix Transport MNSWNLSSSIPIIHTPHDHPPTSEGTPDQPNNNRKDDKLHKKRGDSDEDLSPIWHCVVSG GIGGKIGDSAMHSLDTVKTRQQGAPNVKKYRNMISAYRTIWLEEGVRRGLYGGYMAAMLG SFPSAAIFFGTYEYTKRTMIEDWQINDTITHLSAGFLGDFISSFVYVPSEVLKTRLQLQG RFNNPFFQSGYNYSNLRNAIKTVIKEEGFRSLFFGYKATLARDLPFSALQFAFYEKFRQL AFKIEQKDGRDGELSIPNEILTGACAGGLAGIITTPMDVVKTRVQTQQPPSQSNKSYSVT HPHVTNGRPAALSNSISLSLRTVYQSEGVLGFFSGVGPRFVWTSVQSSIMLLLYQMTLRG LSNAFPTD P47048 D6VWD4 YJE9_YEAST Uncharacterized protein YJL049W YJL049W J1162 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Present with 2530 molecules/cell in log phase SD medium. Complete proteome Reference proteome MKVDLPESRLPSLYRDFRPLKDLNPDGYEANISTWRDFFLQQYISNSNRIIFTIGTRTLQ ELTHEVYGVPKSIDIAIDVLVNEGNLIPMELFNLGGMYTDNSRKGFWKWVRSWKESTNMY KSRKDETNFYLREDKFIIKANLEKEYQRFHELLKRSVFMEASSITDLVFTRNEFVTTESL QSFFSTYDEETKNVFLHFIENYKHIIVSKDNVIKVIAAEVEDITSRFSKGITENDLRIAS VKVGIININKQITRLRKEINESNIKLRGPEFNELPKRIRIEYKQARLLSEKHLSRLLKFQ NNLAQVRTQIDTSATNAVLIQTLSESNEVIKSINGYIGSTEKVEDLLDEIKEGHDRTEEV NDLLAHYNKGQDEEAEEEIERELEQLELDEKNNNKEENKNQDLHEPKESSSEDLLKRLNN LKINTNEGPVQDNENHDNEIRKIMMEEQPR Q3E7Z8 D6VR34 YC204_YEAST Uncharacterized protein YCR024C-B YCR024C-B Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY Membrane Multi-pass membrane protein Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MCVCAIPFFEFFLPFIPHYAFLLFVSSVRFTVNERCYYLVCVLKLNCAFFFMVMIFELKR VCVSYLDRSRKIQIVSFFPFITIIFFHS P34161 D6VZE7 YOX1_YEAST Homeobox protein YOX1 YOX1 YML027W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296 FUNCTION DNA-BINDING DEVELOPMENTAL STAGE INTERACTION WITH MCM1 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Transcriptional repressor required to restrict transcription of ECB-dependent genes to the G1/M phase by repressing their transcription during the interval from late G1 to M phases. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. In vitro, is capable of binding to the DNA of the leucine tRNA gene. Interacts with MCM1. Nucleus Expressed from late G1 phase. Transcriptionally activated by SWI4-SWI6 heterodimer. Present with 861 molecules/cell in log phase SD medium. Cell cycle Complete proteome DNA-binding Homeobox Nucleus Reference proteome Repressor Transcription Transcription regulation PRPHHS QGLIIP MSQETKMLPSLSSLLSGTEISSSPVSPSFTNPRTSFHLDDRGTIKLPPLNTSINRPRSVE SALRHTVTSLHENSSAYGDDMLKHTQSDSALSSQLNSSQETVDESHENLLLTPLNSKKRD YSVSSKKNDILTPLSAAKSIIIPSASKEKRRAFAFITHSQETFPKKEPKIDNAPLARRKR RRTSSQELSILQAEFEKCPAPSKEKRIELAESCHMTEKAVQIWFQNKRQAVKRQRIATSK STTIIQTVSPPSPPLDVHATPLASRVKADILRDGSSCSRSSSSSPLENTPPRPHHSLNRR SSTPSIKRSQALTFHLNPQKKTLTPVKTSPNSRVNKLINSIDHSPSKAKRPVSNPSGSPK RKRKFGFKIVDQQPLKDLDPNAFRG P38735 D3DKT3 VMR1_YEAST ABC transporter ATP-binding protein/permease VMR1 Vacuolar multidrug resistance protein 1 VMR1 YHL035C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN FAMILY INDUCTION INDUCTION INDUCTION ABC transporter which may be involved in multidrug resistance. Vacuole membrane Multi-pass membrane protein Under the control of the iron homeostasis regulating AFT1 and AFT2 transcription factors. Up-regulated upon SUB2 overexpression. Belongs to the ABC transporter superfamily. ATP-binding Complete proteome Glycoprotein Membrane Nucleotide-binding Reference proteome Repeat Transmembrane Transmembrane helix Transport Vacuole MGTDPLIIRNNGSFWEVDDFTRLGRTQLLSYYLPLAIIASIGIFALCRSGLSRYVRSAEC DLVNEYLFGAQEERKEDNSIERLLRNSNTQANYVNVKKQGRILKLRHFDITTIDVKQIDA KNHGGLTFSRPSTSDHLRKSSEIVLMSLQIIGLSFLRVTKINIELTNRDVTTLLLFWLIL LSLSILRVYKRSTNLWAICFTAHTTIWISTWIPIRSVYIGNIDDVPSQIFYIFEFVITST LQPIKLTSPIKDNSSIIYVRDDHTSPSREHISSILSCITWSWITNFIWEAQKNTIKLKDI WGLSMEDYSIFILKGFTRRNKHINNLTLALFESFKTYLLIGMLWVLVNSIVNLLPTILMK RFLEIVDNPNRSSSCMNLAWLYIIGMFICRLTLAICNSQGQFVSDKICLRIRAILIGEIY AKGLRRRLFTSPKTSSDSDSISANLGTIINLISIDSFKVSELANYLYVTVQAVIMIIVVV GLLFNFLGVSAFAGISIILVMFPLNFLLANLLGKFQKQTLKCTDQRISKLNECLQNIRIV KYFAWERNIINEIKSIRQKELRSLLKKSLVWSVTSFLWFVTPTLVTGVTFAICTFVQHED LNAPLAFTTLSLFTLLKTPLDQLSNMLSFINQSKVSLKRISDFLRMDDTEKYNQLTISPD KNKIEFKNATLTWNENDSDMNAFKLCGLNIKFQIGKLNLILGSTGSGKSALLLGLLGELN LISGSIIVPSLEPKHDLIPDCEGLTNSFAYCSQSAWLLNDTVKNNIIFDNFYNEDRYNKV IDACGLKRDLEILPAGDLTEIGEKGITLSGGQKQRISLARAVYSSAKHVLLDDCLSAVDS HTAVWIYENCITGPLMKNRTCILVTHNVSLTLRNAHFAIVLENGKVKNQGTITELQSKGL FKEKYVQLSSRDSINEKNANRLKAPRKNDSQKIEPVTENINFDANFVNDGQLIEEEEKSN GAISPDVYKWYLKFFGGFKALTALFALYITAQILFISQSWWIRHWVNDTNVRINAPGFAM DTLPLKGMTDSSKNKHNAFYYLTVYFLIGIIQAMLGGFKTMMTFLSGMRASRKIFNNLLD LVLHAQIRFFDVTPVGRIMNRFSKDIEGVDQELIPYLEVTIFCLIQCASIIFLITVITPR FLTVAVIVFVLYFFVGKWYLTASRELKRLDSITKSPIFQHFSETLVGVCTIRAFGDERRF ILENMNKIDQNNRAFFYLSVTVKWFSFRVDMIGAFIVLASGSFILLNIANIDSGLAGISL TYAILFTDGALWLVRLYSTFEMNMNSVERLKEYSSIEQENYLGHDEGRILLLNEPSWPKD GEIEIENLSLRYAPNLPPVIRNVSFKVDPQSKIGIVGRTGAGKSTIITALFRLLEPITGC IKIDGQDISKIDLVTLRRSITIIPQDPILFAGTIKSNVDPYDEYDEKKIFKALSQVNLIS SHEFEEVLNSEERFNSTHNKFLNLHTEIAEGGLNLSQGERQLLFIARSLLREPKIILLDE ATSSIDYDSDHLIQGIIRSEFNKSTILTIAHRLRSVIDYDRIIVMDAGEVKEYDRPSELL KDERGIFYSMCRDSGGLELLKQIAKQSSKMMK Q08743 D6W2Z0 YO292_YEAST Vacuolar membrane protein YOR292C YOR292C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A GLYCOSYLATION [LARGE SCALE ANALYSIS] Vacuole membrane Multi-pass membrane protein N-glycosylated. Belongs to the peroxisomal membrane protein PXMP2/4 family. Complete proteome Glycoprotein Membrane Reference proteome Transmembrane Transmembrane helix Vacuole MPLQLFGRDQIVVHYDNGNMSNDDQNHQSVLGSWTRRAAAALRTLMNKRIQRITLTHWLL LVIWVTSLWKFTSHYRQLYANSAVFATLCTNILLFGISDILAQSIACFYSYHVDPIPQIL NDTFHHVQNNRDVENGGGYESDELSIFNDFTSEHSSYTDNDDYPELDRPLATFKTDTFDF FRWGCFMFWGFFISFFQAPWYKFLNFFYTEDPTVVQVFERVLSDQLLYSPISLYCFFMFS NYVMEGGDKDTLGKKIQRLYISTLGCNYLVWPMVQFINFLIMPRDFQAPFSSSVGVVWNC FLSMRNASK P32843 D6W0C9 YME2_YEAST Mitochondrial escape protein 2 Protein RNA12 YME2 PRP12 RNA12 YMR302C YM9952.04C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] MUTAGENESIS OF ASN-502 ATCC 28383 / FL100 / VTT C-80102 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION FUNCTION SUBCELLULAR LOCATION TOPOLOGY MUTAGENESIS OF ASN-502 FUNCTION FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 FUNCTION MUTAGENESIS OF ASN-502 Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA. Mitochondrion inner membrane Single-pass membrane protein Present with 5260 molecules/cell in log phase SD medium. Belongs to the YME2 family. Complete proteome Membrane Mitochondrion Mitochondrion inner membrane mRNA processing Reference proteome RNA-binding Transit peptide Transmembrane Transmembrane helix N Y MLLVRTTSLNVSRMPVPCLARGIGILKGKYRLANLMNAQPSVRHVSSEIQQKDQQAGESN TATDTGVIHKSDEETLIYFDNVYARTTSVWNPTLWYNLLLRNQSRDAVREKIRNLASPPN NPIYGLELKSTIPVKRDGGVFATFVVPPKYTKAQVNSLIQQNTARESSKNLLSYFTRASA FPVKGSPWIEDLRRLPSTTIVIKFQGPALTEEEIYSLFRRYGTIIDIFPPTAANNNVAKV RYRSFRGAISAKNCVSGIEIHNTVLHIQYENIRRGHLVSNFFTNHTRIAIPVLFALLSIF AVLVFDPIREFSIEQKITHKYSLSWDNKFWKQLKTLTSSTMTSIKYYWGGPDDNHQRKHL WEERIEKVNDLKMWLEENNNTFVVIRGPRGSGKHDLVMQHTLQNRANVLYLDCDKLIKSR TDPMFLKNAASQLGYFPIFPWIDSVTGVLDLTVQGLTGQKTGLSETKESRFRNMLTTSLM SIRRIALKNYKAFVSTGDGTVNVKEEDYLQQHPEAKPVIVIDRFEGKSEINGFVYKELSD WAAMLVQMNIAHVIFLTETVASNQRLSESLPNQVFKNLILSDASKENSRNYVLSQLEDYL YYNKKSKGENVKEPESEKETAENNDSDSEADTSVKKAEVILNEKELQEIDASLEPLGGRM LDLQAFVRRVKSGEEPSEAVDKMIEQASEQITQMFLSDKIDSNKSAQAWELIELLSANPV IPFHEIVNKPLFKAAPETGIMELENNGLITVSRDRGVLQEIRPAKPLYRAAFTYLINDPE LAKVLKTRYLLKVVGFETGRIKKWEEELKPLGKVPDQKLFKTRLDYLSGKINASNAVITK CEEEIKNLSK Q3E782 D6W075 YM247_YEAST Uncharacterized protein YMR247W-A YMR247W-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY Complete proteome Reference proteome Signal MAHKCASAKLLSGIMALLFNGKSLLRPICLHVHNHLVSNSDTNIVWP P40218 D6VZW9 YM24_YEAST Uncharacterized protein YMR147W YMR147W YM9375.17 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Complete proteome Reference proteome MAARNRRKNNKKKSLLVTSAAQEKNATYVLVAEELHKKTIDLNMGTETPLTENHENPIPA KEFKHQQKLEPIDEHDDGEDELSIKFKSMTKSSGPITEAEVQKLLLSYAFTSAAIQEDEN EKESRHYPIKPPSPSASSLSAYFQSFVEKCKQVFYNFSLQTVEKLNALQNSLYEVFWIIF IYLNYWFPNVGDYVRYVCRSFSRHNEIAQLLTRIFTYNINHLH Q3E7Z1 D6W136 YN146_YEAST Uncharacterized protein YNL146C-A YNL146C-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY Complete proteome Reference proteome MISVCFVFPHSLALDFKSRCKKNRTKLCSAYYVSQVLRICKEMPYRDLILFSTVRKGVYM RLYY Q3E7A8 D6W120 YN162_YEAST Uncharacterized protein YNL162W-A YNL162W-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c GENOME REANNOTATION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Cytoplasm Nucleus Present with 3140 molecules/cell in log phase SD medium. Complete proteome Cytoplasm Nucleus Reference proteome MSDKPDSQVFCPNCNERLQKCLVQQNYAIIICPSLVCGYPFNQREVLENLTYVDDNDVLK VAKKRLSSRSKP P32329 D6VYB8 Q12419 YPS1_YEAST Aspartic proteinase 3 3.4.23.41 Proprotein convertase Yapsin-1 Aspartic proteinase 3 subunit alpha Aspartic proteinase 3 subunit beta YPS1 YAP3 YLR120C L2961 L9233.9 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE ME768 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 90840 / EAY235 / FY23 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c CHARACTERIZATION GPI-ANCHOR SUBCELLULAR LOCATION GLYCOSYLATION PROTEIN SEQUENCE OF 68-82 AND 145-159 FUNCTION SUBCELLULAR LOCATION PROTEOLYTIC PROCESSING MUTAGENESIS OF ASP-101 GLYCOSYLATION BIOPHYSICOCHEMICAL PROPERTIES DISULFIDE BOND SUBCELLULAR LOCATION SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION INDUCTION FUNCTION FUNCTION PROTEOLYTIC PROCESSING 3D-STRUCTURE MODELING Cleaves proteins C-terminally to mono- and paired-basic residues. Involved in the shedding of a subset of GPI-anchored plasma membrane proteins from the cell surface, including itself, GAS1 and MSB2. May also play a role in the maturation of GPI-mannoproteins associated with the cell wall. Can process the alpha-mating factor precursor. Required for cell wall integrity. Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favorable in both non-prime and prime positions. Optimum pH is 4.0. Consists of an alpha and a beta subunit, which are maintained together by a disulfide bond. Cell membrane Lipid-anchor GPI-anchor GPI-anchored plasma membrane protein (GPI-PMP), peripherally distributed over the entire cell surface. Positively regulated by cell integrity signaling through MPK1 in response to cell wall perturbation. The zymogen is transported to the periplasm, where the propeptide is removed and the enzyme is further subjected to an internal, autocatalytic cleavage to generate an alpha/beta two-subunit endopeptidase. The proteolytic processing at the cell surface is regulated by the environmental pH. Extensively N-glycosylated. Present with 5000 molecules/cell in log phase SD medium. Belongs to the peptidase A1 family. 3D-structure Aspartyl protease Autocatalytic cleavage Cell membrane Cleavage on pair of basic residues Complete proteome Direct protein sequencing Disulfide bond Glycoprotein GPI-anchor Hydrolase Lipoprotein Membrane Protease Reference proteome Signal Zymogen D A E L S MKLKTVRSAVLSSLFASQVLGKIIPAANKRDDDSNSKFVKLPFHKLYGDSLENVGSDKKP EVRLLKRADGYEEIIITNQQSFYSVDLEVGTPPQNVTVLVDTGSSDLWIMGSDNPYCSSN SMGSSRRRVIDKRDDSSSGGSLINDINPFGWLTGTGSAIGPTATGLGGGSGTATQSVPAS EATMDCQQYGTFSTSGSSTFRSNNTYFSISYGDGTFASGTFGTDVLDLSDLNVTGLSFAV ANETNSTMGVLGIGLPELEVTYSGSTASHSGKAYKYDNFPIVLKNSGAIKSNTYSLYLND SDAMHGTILFGAVDHSKYTGTLYTIPIVNTLSASGFSSPIQFDVTINGIGISDSGSSNKT LTTTKIPALLDSGTTLTYLPQTVVSMIATELGAQYSSRIGYYVLDCPSDDSMEIVFDFGG FHINAPLSSFILSTGTTCLLGIIPTSDDTGTILGDSFLTNAYVVYDLENLEISMAQARYN TTSENIEIITSSVPSAVKAPGYTNTWSTSASIVTGGNIFTVNSSQTASFSGNLTTSTASA TSTSSKRNVGDHIVPSLPLTLISLLFAFI P53057 D6VV75 YPS5_YEAST Yapsin-5 Aspartic proteinase-like protein YPS5 YPS5 YGL259W NRA165 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c GENE NAME Belongs to the peptidase A1 family. Could be the product of a pseudogene. Contains only the N-ter part of the functional aspartic proteinases. Complete proteome Glycoprotein Reference proteome Signal MQLFSILSLLSSLMCSLTVLGSSASSYVKFPVQKFADIINIGTQDVSTVFKRNEVLNTTV INGIGVYVVKMEIGTPPQTVYLQLDTGSSDMIVNNADIAYCKSMSDGSDYASTDNYELTA TFTGPRSTTTSPELITLSALIGVNSMQETHLLLRITRLSSMTYTY P40583 D6VVX0 E9PAD7 YPS6_YEAST Aspartic proteinase yapsin-6 3.4.23.- YPS6 YIR039C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION FUNCTION GLYCOSYLATION [LARGE SCALE ANALYSIS] Cleaves proteins C-terminally to mono- and paired-basic residues (By similarity). Required for cell wall integrity. Cell membrane Lipid-anchor GPI-anchor N-glycosylated. Belongs to the peptidase A1 family. Aspartyl protease Cell membrane Cleavage on pair of basic residues Complete proteome Glycoprotein GPI-anchor Hydrolase Lipoprotein Membrane Protease Reference proteome Signal Zymogen MQLISILSLLSSLMCSLTVLGSSASSYVKFPVQKLADIINICTQDVSTVFKRNEVLNTTV INGIGVYVVKMEIGTPPQTLYLQLDTGSSDMIVNNADIAYCKSMSDGSDYASTDNYELTA TFNGLPSTTISSEAYNTLCSYWGTFDASNSSTFENNATFFNNTYGDGTYYAGTYGTDVVS FENITLNDFTFGVSNDTIGNPSGILGISLPIAEFTDGIEYALALNRTPFIYDNFPMELKN QGKINKIAYSLFLNGPDAHFGSILFGAVDKSKYTGQLYTLPMLQAFNTLGSNPGMIITAQ SVAILDSESGNKTVSDIQFPVMLDSGTTFSYLPTEIAEAIGKSFDGEYSSDDQGYIFDCS KVNDTLLSVDFGGFNISANISNFVTSAKDRCVLNVKQSESTYMLGDAFLVDAYVVYDLEN YEISIAQASFNNQEEDIEVISDTVPGATPAPGYFSTWVYKPGSPIGTGDFINVSWTSYSE FSQYKSLLATAAQSDDASSFSSSGGSSESTTKKQNAGYKYRSSFSFSLLSFISYFLL P14680 D6VW43 YAK1_YEAST Dual specificity protein kinase YAK1 2.7.12.1 YAK1 YJL141C J0652 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 96604 / S288c / FY1679 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION PHOSPHORYLATION AT TYR-530 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] YAL6B PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND TYR-530 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND THR-288 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-118; SER-127; SER-206; SER-240; SER-245; SER-247; THR-288 AND TYR-530 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Negative regulator of the cell cycle acting downstream of the cAMP-dependent protein kinase. Part of a glucose-sensing system involved in growth control in response to glucose availability. Phosphorylates POP2. ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Q08273 HRT1 false 3 Cytoplasm Nucleus Shuttles between both compartments in response to glucose. Phosphorylated; highly. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MNB/DYRK subfamily. ATP-binding Complete proteome Cytoplasm Kinase Nucleotide-binding Nucleus Phosphoprotein Reference proteome Serine/threonine-protein kinase Transferase Tyrosine-protein kinase MNSSNNNDSSSSNSNMNNSLSPTLVTHSDASMGSGRASPDNSHMGRGIWNPSYVNQGSQR SPQQQHQNHHQQQQQQQQQQQQNSQFCFVNPWNEEKVTNSQQNLVYPPQYDDLNSNESLD AYRRRKSSLVVPPARAPAPNPFQYDSYPAYTSSNTSLAGNSSGQYPSGYQQQQQQVYQQG AIHPSQFGSRFVPSLYDRQDFQRRQSLAATNYSSNFSSLNSNTNQGTNSIPVMSPYRRLS AYPPSTSPPLQPPFKQLRRDEVQGQKLSIPQMQLCNSKNDLQPVLNATPKFRRASLNSKT ISPLVSVTKSLITTYSLCSPEFTYQTSKNPKRVLTKPSEGKCNNGFDNINSDYILYVNDV LGVEQNRKYLVLDILGQGTFGQVVKCQNLLTKEILAVKVVKSRTEYLTQSITEAKILELL NQKIDPTNKHHFLRMYDSFVHKNHLCLVFELLSNNLYELLKQNKFHGLSIQLIRTFTTQI LDSLCVLKESKLIHCDLKPENILLCAPDKPELKIIDFGSSCEEARTVYTYIQSRFYRAPE IILGIPYSTSIDMWSLGCIVAELFLGIPIFPGASEYNQLTRIIDTLGYPPSWMIDMGKNS GKFMKKLAPEESSSSTQKHRMKTIEEFCREYNIVEKPSKQYFKWRKLPDIIRNYRYPKSI QNSQELIDQEMQNRECLIHFLGGVLNLNPLERWTPQQAMLHPFITKQEFTGEWFPPGSSL PGPSEKHDDAKGQQSEYGSANDSSNNAGHNYVYNPSSATGGADSVDIGAISKRKENTSGD ISNNFAVTHSVQEGPTSAFNKLHIVEE P35196 D6VQ03 RER2_YEAST Dehydrodolichyl diphosphate synthase complex subunit RER2 DEDOL-PP synthase 2.5.1.87 Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) RER2 YBR002C YBR0107 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] SUBCELLULAR LOCATION FUNCTION MUTAGENESIS OF GLY-164 AND SER-209 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION INDUCTION SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION CATALYTIC ACTIVITY FUNCTION SUBUNIT With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate Mg(2+) Protein modification; protein glycosylation. Forms an active dehydrodolichyl diphosphate synthase complex with NUS1. Endoplasmic reticulum membrane Peripheral membrane protein Mainly expressed in the early logarithmic phase. Present with 8970 molecules/cell in log phase SD medium. Belongs to the UPP synthase family. Complete proteome Endoplasmic reticulum Magnesium Membrane Reference proteome Transferase G D S N METDSGIPGHSFVLKWTKNIFSRTLRASNCVPRHVGFIMDGNRRFARKKEMDVKEGHEAG FVSMSRILELCYEAGVDTATVFAFSIENFKRSSREVESLMTLARERIRQITERGELACKY GVRIKIIGDLSLLDKSLLEDVRVAVETTKNNKRATLNICFPYTGREEILHAMKETIVQHK KGAAIDESTLESHLYTAGVPPLDLLIRTSGVSRLSDFLIWQASSKGVRIELLDCLWPEFG PIRMAWILLKFSFHKSFLNKEYRLEEGDYDEETNGDPIDLKEKKLN P32611 D3DLK0 RML2_YEAST 54S ribosomal protein RML2, mitochondrial L2 Mitochondrial large ribosomal subunit protein uL2m RML2 YEL050C SYGP-ORF37 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION SUBUNIT MUTAGENESIS OF 336-VAL--ASP-342 AND HIS-343 FUNCTION FUNCTION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) SUBUNIT SUBCELLULAR LOCATION Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. Component of the mitochondrial large ribosomal subunit (mt-LSU). Mature yeast 74S mitochondrial ribosomes consist of a small (37S) and a large (54S) subunit. The 37S small subunit contains a 15S ribosomal RNA (15S mt-rRNA) and 34 different proteins. The 54S large subunit contains a 21S rRNA (21S mt-rRNA) and 46 different proteins. uL2m has a Na/K ligand binding site. Mitochondrion Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. Present with 1600 molecules/cell in log phase SD medium. Belongs to the universal ribosomal protein uL2 family. 3D-structure Complete proteome Mitochondrion Reference proteome Ribonucleoprotein Ribosomal protein Transit peptide H Q MLVLGSLRSALSCSSTASLISKRNPCYPYGILCRTLSQSVKLWQENTSKDDSSLNITPRL LKIIPNDTDIVTLEKQDELIKRRRKLSKEVTQMKRLKPVSPGLRWYRSPIYPYLYKGRPV RALTVVRKKHGGRNNSGKITVRHQGGGHRNRTRLIDFNRWEGGAQTVQRIEYDPGRSSHI ALLKHNTTGELSYIIACDGLRPGDVVESFRRGIPQTLLNEMGGKVDPAILSVKTTQRGNC LPISMIPIGTIIHNVGITPVGPGKFCRSAGTYARVLAKLPEKKKAIVRLQSGEHRYVSLE AVATIGVVSNIDHQNRSLGKAGRSRWLGIRPTVRGVAMNKCDHPHGGGRGKSKSNKLSMS PWGQLAKGYKTRRGKNQNRMKVKDRPRGKDARL P02407 D6VZF0 RS17A_YEAST 40S ribosomal protein S17-A RP51A Small ribosomal subunit protein eS17-A RPS17A RP51A YML024W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] RY26 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NOMENCLATURE SUBUNIT SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] NOMENCLATURE X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME SUBUNIT SUBCELLULAR LOCATION Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). Cytoplasm Present with 30900 molecules/cell in log phase SD medium. There are 2 genes for eS17 in yeast. Belongs to the eukaryotic ribosomal protein eS17 family. 3D-structure Complete proteome Cytoplasm Reference proteome Ribonucleoprotein Ribosomal protein MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKR IQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLS VINVSAQRDRRYRKRV P38754 D3DKR3 RL14B_YEAST 60S ribosomal protein L14-B Large ribosomal subunit protein eL14-B RPL14B YHL001W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NOMENCLATURE SUBUNIT SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBUNIT SUBCELLULAR LOCATION NOMENCLATURE Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). Cytoplasm N-terminally acetylated by acetyltransferase NatA. Present with 35100 molecules/cell in log phase SD medium. There are 2 genes for eL14 in yeast. Belongs to the eukaryotic ribosomal protein eL14 family. 3D-structure Acetylation Complete proteome Cytoplasm Reference proteome Ribonucleoprotein Ribosomal protein MSTDSIVKASNWRLVEVGRVVLIKKGQSAGKLAAIVEIIDQKKVLIDGPKAGVPRQAINL GQVVLTPLTFALPRGARTATVSKKWAAAGVCEKWAASSWAKKIAQRERRAALTDFERFQV MVLRKQKRYTVKKALAKA P38426 D6W087 Q6B1W2 TPS3_YEAST Trehalose synthase complex regulatory subunit TPS3 Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 115 kDa subunit TPS3 YMR261C YM8156.03C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION INTERACTION WITH TPS1 AND TPS2 SUBUNIT SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-181 AND SER-960 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-150; THR-265; SER-267 AND SER-273 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Regulatory subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. May stabilize the trehalose synthase complex. The trehalose synthase complex is composed of the two catalytic subunits TPS1 and TPS2 and at least one of the two regulatory subunits TPS3 or TSL1. Q00764 TPS1 false 5 P31688 TPS2 false 5 Cytoplasm Repressed by glucose. Present with 13500 molecules/cell in log phase SD medium. In the N-terminal section; belongs to the glycosyltransferase 20 family. Complete proteome Cytoplasm Phosphoprotein Reference proteome P L N D S G D E MTIIVASLFLPYTPQFEADVTNSDTAKLVESSMIKVDCNNQELSNNKQERSSSVTSASSH YIGLPQEAQINGEPLQRANVGSPATGVNYHNEMEMLSSEQFLEELTANATHAANSGIPPA NNPVSSGSTAQRPSVEEFFSAPSARVCSPSQEASASSISASRSSAHHNDLSSSLMKNPNL SFDSHPPRVRSSSKSAVITPVSKSVPDVDPAVVDVAKVREEFQQQASLPSMKRVSGSTAG DSSIASSSSNLRYSQQFQDNFIEDTDSEDDIDSDLETDATKKYNVPKFGGYSNNAKLRAS LMRNSYELFKHLPWTIVDSDKGNGSLKNAVNIAVAEKTVKEPVSWVGTMGIPTDELPHEV CHKISKKLEQDFSSFPVVTDDITFKGAYKNYAKQILWPTLHYQIPDNPNSKAFEDHSWDY YQKVNQKFSDRIVSVYKPGDTIWIHDYHLMLVPQMVREKLPKAKIGFFLHVSFPSSEVFR CLANRERILEGIIGANFVGFQTKEYKRHFLQTCNRLLAADVSNDEVKYHCNIVSVMYAPI GIDYYHLTSQLRNGSVLEWRQLIKERWRNKKLIVCRDQFDRIRGLQKKMLAYERFLIENP EYIEKVVLIQICIGKSSDPEYERQIMVVVDRINSLSSNISISQPVVFLHQDLDFAQYLAL NCEADVFLVDALREGMNLTCHEFIVSSFEKNAPLLLSEFTGSSSVLKEGAILINPWDINH VAQSIKRSLEMSPEEKRRRWKKLFKSVIEHDSDNWITKCFEYINNAWESNQETSTVFNLA PEKFCADYKASKKHLFIFKISEPPTSRMLSLLSELSSNNIVYVLSSFTKNTFESLYNGVL NIGLIAENGAYVRVNGSWYNIVEELDWMKEVAKIFDEKVERLPGSYYKIADSMIRFHTEN ADDQDRVPTVIGEAITHINTLFDDRDIHAYVHKDIVFVQQTGLALAAAEFLMKFYNSGVS PTDNSRISLSRTSSSMSVGNNKKHFQNQVDFVCVSGSTSPIIEPLFKLVKQEVEKNNLKF GYTILYGSSRSTYAKEHINGVNELFTILHDLTAA Q3E775 D6VWX0 YJ151_YEAST Uncharacterized protein YJR151W-A YJR151W-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c GENOME REANNOTATION Complete proteome Reference proteome MLSLIFYLRFPSYIRG Q03083 D6W3X9 YP034_YEAST Uncharacterized protein YPL034W YPL034W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c Complete proteome Reference proteome MTTRKTVDSRLLEWQTTCKHPVINLTPEKVDKLYHLKLKSESKNISSNRLLPISLSSLQK KMEKLFIKDKSHSHKPSLPDPKVPTLRTYKDGGFFISGKGSMKLPDIESAIHKFLWKKYG KGLVYCYGCDPTGKKRHTEWFNVPVLELPSVLRLIDSYCLGGESR P0CX60 D6W2K0 Q99209 YP13A_YEAST Transposon Ty1-PR2 Gag polyprotein Gag-p49 Transposon Ty1 protein A TY1A TYA p58 Capsid protein CA Gag-p45 p54 Gag-p4 TY1A-PR2 YPRWTy1-3 GAG YPR158W-A P9584.3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NOMENCLATURE INDUCTION REVIEW Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity). Homotrimer. Cytoplasm P0CX60-1 Transposon Ty1-PR2 Gag polyprotein Produced by conventional translation. P0C2J0-1 Transposon Ty1-PR2 Gag-Pol polyprotein Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YPR158W-A ORF. The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity). Ty1-PR2 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4. The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities. Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae). Complete proteome Cytoplasm Phosphoprotein Reference proteome Ribosomal frameshifting RNA-binding Transposable element MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPAS SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRPITDDELTFLYNTFQIFAPSQFLPTWVKDI LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY RRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS TTEPIQLNNKHDLHLRPETY Q3E7A0 D6VXI1 YK106_YEAST Uncharacterized protein YKL106C-A YKL106C-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c GENOME REANNOTATION Complete proteome Reference proteome MPFPSILHLTIGRYASYDSNNHMRRRAKLMEAIFRIRTI O13544 A0A1S0T0A9 YL302_YEAST Uncharacterized protein YLR302C YLR302C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c Membrane Single-pass membrane protein Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MRWHCMDGGNRIVSMYLTTLYYTKEIVDEKTREQEKGKTSFLTDALLNLIYILFFSSSVF NWTRCHLFDTSVIMLHSFHEDGALTNLISHLPTTTVPQYRQLHVPFAILRSCDLKRKSKK Q12243 A0A1S0T0B9 YOR29_YEAST Uncharacterized protein YOR029W YOR029W O2663 OR26.19 YOL303.13 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c Complete proteome Reference proteome MMQTSTSSRVRRYPYQITLSLVLKGFYSPSAPSYDFCLVLLPTLFLIDLMPIKFSLHVTI GIGEATPVPIFFFSAPWYFRSGNPLPHCVRAYRCKVNFPFFRLGWSTWLHY O13512 D6VPF2 YA64B_YEAST Uncharacterized membrane protein YAL064W-B YAL064W-B Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A Membrane Multi-pass membrane protein Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MAGEAVSEHTPDSQEVTVTSVVCCLDSVVEIGHHVVYSVVTPLIVAVLIDTMAGEAVLEH TSDSQEEIVTTVVCSVVPLVCFVVSVVCFVISVVEIGHHVVYSVVAPLTVTVAVETIAEE MDSVHT Q06409 D6VZ58 YL422_YEAST DOCK-like protein YLR422W YLR422W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Cytoplasm Present with 238 molecules/cell in log phase SD medium. Belongs to the DOCK family. Complete proteome Cytoplasm Reference proteome MSQQDSQRWLPTDRLIYGVLVKSFLPLQRYPELVYENSNYANVYVGAEVYVFEESVDKKW CRAYQCLRPFPEEFISNMNSANDVLPDVKPKVVIFPRKYVHFEAEKAVSTMPFFKAPSAE DFKPLISKECESRSFCDSLYVSSTDDISTGKPRKTPRPPFPFFRYQKRSFKDEMGPILSL ISSHVYSMYSIGEFSIYRKMIKLYYDLDTIRFRLSMNLTTEAEKINLIRAATSLRTKIAK FLSSTYRKNKLIANSTPRNPDPYGFEGIFARDIDTGELLSYEIDKLRTLVSSSMLCGLTN NFPTVPVVESDDESSSNGLFGTVRSSILVNLKDLAWDPSISDPKYQDLSICVYLRTKDEV LTESFTMTKSSNMESALDEIPAMLFKNILETIVHKNKVYLVVVLKETIAITTETAPEISS YNISTEESSSHSPFSPFNSSTENKIDHVKKGLAAGVINISPVFKFYNGLSVANKAQRFNL YLYSSDSSDSQNFNSSKDADLGWGGLINKIIKDSSEGVSVNPRAVSLSVTVKEIIGKQEA EKVLSTSLVPIRSIPTYFYDTMFSQAERIYLNLGRVSLYGLPAADTNIENVTVQISCRNK AVKFCKNKLEERSGDWKFVSVRPNESIGESIRIEGVENMNEDETLRVLVYLNGFLMAKSN IHIKKKNEIIEYRKGTVFQIMSSKSVPLIHLELEASYFGRRYNINPAITNFLVLQTKNVE FDQQLKEHYSVTLKQLNNVSFKDLLKHFDTILAHYLLLLESVNEATDKKGPSSSLPNIVF SEFVKFLNLMLTHQENSRYWFNRLYKKVMSKELECPNVAPILIKHMTTIFDRSHSSWTRT GTAICRTILYIIVLAIGSSHSDEMPNFSHFFRSLHKFLMLADEPIMADQILLIESIPSML ETMTNHCKVEDLVRFAIGLFECCQEKEMNQKMYSRPLSVREEEYLNTKFNCLLKLINKKV LQNYLTNTESVDKLRLQFLSKTLEWLLTPYTPGDDKCFHVESLRLVNSVFITIIEDYKFD MLQRNLIRLLPYLCKSFVHLRRYCKKARLMRPRRVFTMLFPREIPCNYIPVDSIVNDEVV VEVLLELAIIICEITKIASSRFPSYQSFSEIINLCDKDTLFQSNFYSRQITNENVYTITK TVFLFFKQDWFPGMKWLGVSALLGRSSLILLSLCKDYIIENNSPSPSKESEKRVDMRLWA EYVKVILLVSNHKSASLTKLAITPRKAVYLISGDLKKISAYILNECWDALATGHYNITYA KKYGLGALSDCQFELFVHNQFLIREIFIFAFHRHIDATRICCKILWGLGLNFWRIFGSLQ PAVNACIPELFSAYQIGKLRLNDYELERFVSCLFFMMHVPDSDTFFPACMDFLRDLLGFL HIVNEIYKIPNQEEFDDDRTARHIEMFEYLLEANRPELFHKMIYDLFIHFIQKKDFVQAA LSLELLAGTYAWDSNDTLEAISFPPLPEQSSFERKEYLLKESARNFSRGQKPEKALAVYK DLIKAYDEINYDLNGLAFVHDQIAGIYTRLQSIDRLVPTYFKVSFMGFGFPKSLRNKSFV FEGLPFEHITSMHDRLLRSYHGSNIVHSQEEVDMLLMNPPMGKYIHVASVEPCLSISDNY NSSDKKSSINNKVRMYIENRDLRTFSNSRRLPGAKGVTDLWVEEYTYHTMNTFPTLMNRS EIVKVTKSKLSPLENAIRSLQVKIQELYGLENMCNKTLKDHGDVNDLFTELSTNITGTIS APVNGGISQYKAFLEPSTSKQFSTDDLGRLTLAFDELVAVLGRCLTLHAELLPSKDLKPS HDLLVRLFEENFAEEIERYSRTLSEANRSRNNMITARIISHKNPNKKASFSGRDHHTSGS NHSQFVLEHSDSFGPNSLLFGKYLTRTLSHSSTTSSLDKSGIVSGTSSTFLAGSQPNTNT DSQHKHDYSHSG P53134 D6VU33 YGL4_YEAST Putative oligopeptide transporter YGL114W YGL114W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Membrane Multi-pass membrane protein Belongs to the oligopeptide OPT transporter family. Complete proteome Membrane Peptide transport Protein transport Reference proteome Transmembrane Transmembrane helix Transport MPQSTPSQEVQRVPWDNKPALKQITLRATIAGIAIGSLVLTSNFQFGLQTGWVSMMSLPS ALLACAFFKNIWPLIFPNDRPFSDVENVYVQSMAVAVGTGPLAFGFVGVIPAIEKFLTND ESGGLREQGQSFTFRELLIWSTALAFFGIFFAVPLRKQVIVREKLPFPSGSATATLISVL NGTEILQEVSKSELLEMRQRRLNECPEVLQPNRDPEEADYLMNSSHSELGDYTATSQDGS SILSTGSENYRANIIILLKTFVVSSLYTMVSYFVPVIRSIPVFGKYLSNNYLWNFQPSPA YIGQGIIMGLPTVSYMLIGCFLGWGVLAPLARYKRWVPPDADVHDWEEGVQGWILWSSLS IMVADSVVAFIVVTVKSIVKFILIDDKAALLNNIIDDTFQSMLLEEERAINSSRRNTYVD GRQDTVRLVSRDNEIEVDSKHLVRYTTVISGCLVSSIICIVSIIYLFGIQVIPLYAIITA LILALFLSILGIRALGETDLNPVSGIGKISQLIFAFIIPRDRPGSVLMNVVSGGIAEASA QQAGDLMQDLKTGHLLGASPRAQFCAQLIGACWSIILSSFMYLCYNKVYSIPSEQFRIPT AVVWIDCARLVTGKGLPDKALECSMILGVIFAVLSLIRNTYRDYGYGWILYIPSGVAVGV GIFNSPSFTIARFIGGWASHFWLKNHRGDLNAKTKMIVFSSGLVLGEGIFSVINMLFICL NVPHY P47085 D6VWI3 YJX8_YEAST MEMO1 family protein YJR008W YJR008W J1431 YJR83.9 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Present with 339 molecules/cell in log phase SD medium. Belongs to the MEMO1 family. Complete proteome Reference proteome MSIRPATHAGSWYSNRAQELSQQLHTYLIKSTLKGPIHNARIIICPHAGYRYCGPTMAYS YASLDLNRNVKRIFILGPSHHIYFKNQILVSAFSELETPLGNLKVDTDLCKTLIQKEYPE NGKKLFKPMDHDTDMAEHSLEMQLPMLVETLKWREISLDTVKVFPMMVSHNSVDVDRCIG NILSEYIKDPNNLFIVSSDFCHWGRRFQYTGYVGSKEELNDAIQEETEVEMLTARSKLSH HQVPIWQSIEIMDRYAMKTLSDTPNGERYDAWKQYLEITGNTICGEKPISVILSALSKIR DAGPSGIKFQWPNYSQSSHVTSIDDSSVSYASGYVTIG P53139 D6VU38 YGK8_YEAST Uncharacterized protein YGL108C YGL108C G3070 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PALMITOYLATION MYRISTOYLATION AT GLY-2 PALMITOYLATION AT CYS-4 BY ERF2; PFA4 AND PFA5 Cell membrane Lipid-anchor Myristoylated. The N-myristoylated protein is further palmitoylated by ERF2, PFA4 and slightly by PFA5, but not by PFA3. Present with 2430 molecules/cell in log phase SD medium. To S.pombe new13. Cell membrane Complete proteome Lipoprotein Membrane Myristate Palmitate Reference proteome MGLCGSKTQPMPSQTTTVATKARTKPINRDTVKSKQELRHKEKKDKKKKTQLKSTTVPVV QRKEGSKLTDTSDPSKNKVSPKEAARLAAEKRFQETNEKYNKGELGKKLAQERAKSHKTR LMEEAEKKHAERERENMIYD P43582 D6VTM0 WWM1_YEAST WW domain-containing protein WWM1 WW domain-containing protein interacting with metacaspase WWM1 YFL010C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204511 / S288c / AB972 INTERACTION WITH MCA1 FUNCTION SUBCELLULAR LOCATION FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 DOMAIN PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND THR-78 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-50 AND LYS-60 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Involved in apoptosis. May play a role in nuclear function controlling cellular proliferation coupled to mitochondrial biogenesis. Causes impaired growth when overexpressed. Interacts with metacaspase MCA1. Cytoplasm Nucleus Mitochondrion Present with 6020 molecules/cell in log phase SD medium. Apoptosis Complete proteome Cytoplasm Isopeptide bond Mitochondrion Nucleus Phosphoprotein Reference proteome Ubl conjugation MAQSKSNPPQVPSGWKAVFDDEYQTWYYVDLSTNSSQWEPPRGTTWPRPKGPPPGVNNEK SSRQQADQAPPPYSSQSTPQVQAGAQAQQPRYYQPQQPQYPQYPQQQRYYPQQAPMPAAA PQQAYYGTAPSTSKGSGHGGAMMGGLLGVGAGLLGGAMLEHAFDDHNYDGPDTVVVENNY YGDDAGGSDGGFDDAGGFDGGFDDGFDGSDF P31111 D6VSR5 ZIP1_YEAST Synaptonemal complex protein ZIP1 ZIP1 YDR285W D9819.9 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] BR1824-3B NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Required for meiotic chromosome synapsis and cell cycle progression. May act as a molecular zipper to bring homologous chromosomes in close apposition. ZIP1 may encode the transverse filaments of the synaptonemal complex. Q06032 CST9 false 3 Nucleus Chromosome Synapsed meiotic chromosomes. Present with 391 molecules/cell in log phase SD medium. Chromosome Coiled coil Complete proteome Meiosis Nucleus Phosphoprotein Reference proteome T A MSNFFRDSSMGFKPRPNIFAKLRVRDVDSDSSANTVVENSSNCLDVGSSIEGDDTFKKPH KTSTEQELITSMSLSQRNHGYSDDMEIGSPKKTTSTDQYNRILKNDVAAIENDTDEDFEI TEVREVSEGVAKETKESHGDPNDSETTLKDSKMHEYTMTNGKAPLHTSINNSSTSSNDVL LEAFTNTQRICSNLKQELQKQQQDNAKLKVRLQSYASNSDKINEKVGKYKSCLETLQERI ATLTSHKNNQETKLKDLRQNHQLYQRRISGFKTSIENLNKTINDLGKNKKEADAELMKKG KEIEYLKRELDDCSGQLSEEKIKNSSLIQEMGKNREEMIKSIENFFSEDKAHHLLQFNKF EERVHDLFEKKLQKHFDVAKDTLNVGLRNTTVELSSNTETMLKQQYEDIKENLEQKMSSS KDEMAKTINELSVTQKGLIMGVQEELLTSSGNIQTALVSEMNNTRQELLDDASQTAKNYA SLENLVKAYKAEIVQSNEYEERIKHLESERSTLSSQKNQIISSLGTKEAQYEDLVKKLEA KNIEISQISGKEQSLTEKNENLSNELKKVQDQLEKLNNLNITTKSNYENKISSQNEIVKA LVSENDTLKQRIQQLVEIKENEQKDHTTKLEAFQKNNEQLQKLNVEVVQLKAHELELEEQ NRHLKNCLEKKETGVEESLSDVKTLKQQVIVLKSEKQDITAEKLELQDNLESLEEVTKNL QQKVQSQKRELEQKIKELEEIKNHKRNEPSKKGTQNFTKPSDSPKKNATTSNLFPNNSAA IHSPMKKCPKVDHISKSRINSSKETSKFNDEFDLSSSSNDDLELTNPSPIQIKPVRGKIK KGSNCMKPPISSRKKLLLVEDEDQSLKISKKRRRK Q03236 D6W011 YM49_YEAST Uncharacterized protein YMR187C YMR187C YM8010.17C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c Membrane Multi-pass membrane protein Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MTPPHFFLSLIKKRCICWICLEESTYDSTWLQHTCGCNLQIHKRCYIRWLYQMHVELFLP NTVDLPKDADLPIITCLKCLVDGHHDFMTTFSLTEIWETRPIWGQKSVPFQNDYVFNLMS LYTKRDNHPPYVLVKFGECPQCKKTNFIKRPTVTIQSSVLSLFYQWQKITRYVIPLGITS LFLLNPEKTSFDIGLWQLRCLFPENVLRNMLNISTTKALDVYAQTERGLLSIPLTSSIII YGFIHYLSNISNVSANAILFKWVYLSIVKTAGNKYYKGIGLPKIILYSNLATFCYNFTFK RLVDLIYRRLINKGGKYLYHGNFENSSNSVPAEEFFIRRNWYAILAEKILWPFVGKCTGG LLLNAFLWIQRKFKIEWTPNCSPSEFRMIFNIIGCGTAAIGWSSLKLYASYKRCQELEKI NEFIEQSCKGE Q08974 D6W3B4 YP257_YEAST Uncharacterized membrane protein YPL257W YPL257W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A May be required for cell cycle progression. Membrane Multi-pass membrane protein Cell cycle Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MTAHANERISDVSPSARGSSSESKYDKLCRVLFFIAITKSSFTPEHILYKHSIFTDKPIL ADIVTFMYAAFVSIGWFLIWGERAYRTQEMGQPPMYSNINYHLLSFKKRHPKKFTCALWL VFFLAYTVLTVLIWLVQLIFRKGNVFQMLLQLIILDIAIALVNVAIAFTFEIYLSQKAAI EIRDEGLNNLDTA Q06839 D6W496 YP097_YEAST PX domain-containing protein YPR097W YPR097W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION SEQUENCE REVISION TO 848 ATCC 204508 / S288c DOMAIN LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] ATCC 76625 / YPH499 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310 AND SER-451 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Mitochondrion membrane Peripheral membrane protein The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization. Present with 3080 molecules/cell in log phase SD medium. Complete proteome Membrane Mitochondrion Phosphoprotein Reference proteome S G MITQDTPALNPTEEHYLKRELLRCQLDYEIGKLNDQFALRKFGYPFSPNDPTAPQPISNN DSSPVLGGKGHFSVNYPMLSYVLQEFISTFPLLSTNLLVDEKFWQSKVQVFFEHFMSLGF SESYDREEASKRKKVSKKLSKVILLLFNSGVGSFQEQAYYNEDKFVLQSGQARKRSNIEK FAMPTRENLENLLTNESVFINGWDVNIISVFNKNSRKCTESVDNDKSSKSTPTSSPKSHA IKSFASTSKWMKNAFNNTINSTINSMPESSASLFSKLSLGVPSTKSKQSRKHHYFLIKIK KQDDDDQDNSNEENSNLDHHAGYFYVTRTYSDFKKLSHDLKSEFPGKKCPRLPHRNKKVT SMITKTEVLHNGQTKSAAREKIVNTFDTDLQSASESDNSSFLQTTNELSATETVLTEKET ETLRKNILNEIKEEDNIDEDEYEEEGEGEESDFDEYKDASDSKINTLVGEKMRTSLRQYL RTLCKDAEVSQSSSIRRFFLSGPNLDIKDINPKIADDIRNRALIDVSNLENQIRFQQMAL EKSLKLQDSMKDFKTSLLKDEKYLMSLLVEIKDNTKVEDLSPLLQDFVEWCKIYISSMIY QMFLGNDNSYELYTQIRRLHKLMPYTVMGQIMKFTNPIAIMRGMIELFMAQPFGGHSLLQ TMFSTILTDDLKTQKVAIKELERKIAEMDPGASVVTKCLKDFVFNNDTKDEHDTKLFTMD AVNAESESMNMPVPLIVLMKSAAANLIPDEVVAGLIESYSSWKLQKEDTDALNVTSEDQS GIYFTHVKDLWQLYIKEHDKQLMRQLWQDPELTQMLKAIVTMIYEPMVKIFKVARMDVAL KNFEKFMSDLIRLVDDVINGQLGVSTQFDVVEEIHNLVTKHQDAFFEFIHDVYLNDSEGI FEGFITWITTIVKFLQKSKFGGPSERIDFNKLICRDDIDIDVKLLKVQVNNVLNKKIGAR KIYKKLLDLKVKQGTKQNNKHAAGILQKNWSDINSLVMPSSSGSFGLGDGDLVDLDLDTG DYDFLHKENEVELEKQYKDLLNLVVDESEIDKLRSQVFAQELKNYLEAQIAKK Q06813 D6W480 YP078_YEAST Uncharacterized protein YPR078C YPR078C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION Induces the SOS system when expressed in E.coli, therefore, it may play a role in DNA metabolism and/or in genome stability. Complete proteome Reference proteome MQTISGVLPTVLSPSELRSDDERTFQFDEEAEITTHLTESEDLRRLINETAQLGVRVDHI HDKTDQEIARLEKVIKEVTESDTFFRSCSGWFKTNKNFSDSESSSNTQLKSLSQLHGRYD RDWRQRLNKWFRKNKSKLALPSDNNLEEVNDDKVYGYGEDLMERGKTPYFSDIDDFMNGL NIISPLTPDDFENDDTLVKIDETCQIHSASEPEKTSISPTFGKNIKKELVTDDTESIISG PPLQENKKTLLKYRYVRTSLDMLGSEKSSSKNNSGGMFRIFHKSANFGDKNQENVPRVWD TLRNNLGREIYLLQGRFKKWTTKHQNLKKGQPCKDEDAVTVPLPSSDPGKETQLETKLCF VPEPGDQPLVQA Q06523 D6W4E5 YP148_YEAST Uncharacterized protein YPR148C YPR148C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cytoplasm Cytoplasmic punctate structures. Complete proteome Cytoplasm Phosphoprotein Reference proteome MSGYFSGFSLNKITDSIATAAHKTQDTLNNALANANVNLNDPQTRLSIKSRTRFVQESLG TVSDISKLPPQYQFLEKKSDSLEKVCKRILLVSKTFEVEGYDYPPNLTESISDWWSLNKD GWFGSKKSESSTKKKGSNHDDAFLPRSFAQAISKAAVDCECEFQNLEHNEKAELKKKKES IKTAQTTEAQGADHNEEDEEDEEDEEDDEDLSNLIKVFDSWSTCYKNIDEGKAEMDSMMV KEFNKKLETLINQDFKKVHDLRKKVEESRLKFDTMRYEVKAKEAELEAKKAEATGEAHSK DVSAKDISANTTTSFDETPSTEDEKPKSEGAEEESKKEANEPTVDDVADRKEDLKSNKVN DEPPIEESEDNKLLEKLEDEFVSNTTAAVETMEEITDSSEILGLIKLFQNFQLVYFRQCV QEVEANLKVLNGLEI P36127 A0A1S0T091 YK12_YEAST Uncharacterized protein YKR032W YKR032W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c Complete proteome Reference proteome MAYSSLCLCLLFNPKGCSNLHPFVVDNEFPPYHLSLVLIKQQRMLDRNRSWAYLAALWRH PWTVISKCCLVYIYIQRQLEFGYSYCFFDFLLVILSETVVILYY I2HB52 YB56A_YEAST Uncharacterized protein YBR056W-A YBR056W-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION Complete proteome Reference proteome MRHQYYQPQPMYYQPQPQPIYIQQGPPPPRNDCCCCCNCGDCCSAIANVLCCLCLIDLCC SCAGGM P40105 D3DM99 YRF12_YEAST Y' element ATP-dependent helicase protein 1 copy 2 3.6.4.12 YRF1-2 YER190W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c FUNCTION INDUCTION Catalyzes DNA unwinding and is involved in telomerase-independent telomere maintenance. ATP + H2O = ADP + H(+) + phosphate Induced in absence of telomerase TLC1. Belongs to the helicase family. Yeast subtelomeric Y' repeat subfamily. ATP-binding Complete proteome Helicase Hydrolase Nucleotide-binding Reference proteome Repeat MVYTLFQVHTLKFNRKDYDTLSLFYLNRGYYNELSFRVLERCHEKASARPNDSSTMRTFT DFVSGAPIVRSLQKSTIRKYGYNLAPYMFLLLHVDELSIFSAYQASLPGEKKVDTERLKR DLCPRKPTEIKYFSQICNDMMNKKDRLGDILHIILRACALNFGAGPRGGAGDEEDRSITN EEPIIPSVDEHGLKVCKLRSPNTPRRLRKTLDAVKALLVSSCACTARDLDIFDDNNGVAM WKWIKILYHEVAQETALKDSYRITLVPSSDGVSVCGKLFNREYVRGFYFACKAQFDNLWE ELNDCFYMPTVVDIASLILRNREVLFREPKRGIDEYLENDSFLQMIPVKYREIVLPKLRR DTNKMTAALKNKVTVAIDELTVPLMWMIHFAVGYPYRYPELQLLAFAGPQRNVYVDDTTR RIQLYTDYNKNGSSEPRLKTLDGLTSDYVFYFVTVLRQMQICALGNSYDAFNHDPWMDVV GFEDPDQVTNRDISRIVLYSYMFLNTAKGCLVEYATFRQYMRELPKNAPQKLNFREMRQG LIALGRHCVGSRFETDLYESATSELMANHSVQTGRNIYGVDSFSLTSVSGTTATLLQERA SERWIQWLGLESDYHCSFSSTRNAEDVVAGEAASSDHHQKISRVTRKRPREPKSTNDILV AGQKLFGSSFEFRDLHQLRLCHEIYMADTPSVAVQAPPGYGKTELFHLPLIALASKGDVK YVSFLFVPYTVLLANCMIRLSRCGCLNVAPVRNFIEEGCDGVTDLYVGIYDDLASTNFTD RIAAWENIVECTFRTNNVKLGYLIVDEFHNFETEVYRQSQFGGITNLDFDAFEKAIFLSG TAPEAVADAALQRIGLTGLAKKSMDINELKRSEDLSRGLSSYPTRMFNLIKEKSEVPLGH VHKIWKKVESQPEEALKLLLALFEIEPESKAIVVASTTNEVEELACSWRKYFRVVWIHGK LGAAEKVSRTKEFVTDGSMRVLIGTKLVTEGIDIKQLMMVIMLDNRLNIIELIQGVGRLR DGGLCYLLSRKNSWAARNRKGELPPIKEGCITEQVREFYGLESKKGKKGQHVGCCGSRTD LSADTVELIERMDRLAEKQATASMSIVALPSSFQESNSSDRCRKYCSSDEDSDTCIHGSA NASTNATTNSSTNATTTASTNVRTSATTTASINVRTSATTTESTNSSTNATTTASTNVRT SATTTASINVRTSATTTESTNSNTSATTTESTDSNTSATTTESTDSNTSATTTASTNSST NATTTASTNSSTNATTTESTNASAKEDANKDGNAEDNRFHPVTDINKESYKRKGSQMVLL ERKKLKAQFPNTSENMNVLQFLGFRSDEIKHLFLYGIDVYFCPEGVFTQYGLCKGCQKMF ELCVCWAGQKVSYRRMAWEALAVERMLRNDEEYKEYLEDIEPYHGDPVGYLKYFSVKRGE IYSQIQRNYAWYLAITRRRETISVLDSTRGKQGSQVFRMSGRQIKELYYKVWSNLRESKT EVLQYFLNWDEKKCREEWEAKDDTVFVEALEKVGVFQRLRSMTSAGLQGPQYVKLQFSRH HRQLRSRYELSLGMHLRDQLALGVTPSKVPHWTAFLSMLIGLFCNKTFRQKLEYLLEQIS EVWLLPHWLDLANVEVLAADNTRVPLYMLMVAVHKELDSDDVPDGRFDILLCRDSSREVG E P38298 D6VQH8 YPC1_YEAST Alkaline ceramidase YPC1 3.5.1.- YPC1 YBR183W YBR1305 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] CHARACTERIZATION NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c TOPOLOGY [LARGE SCALE ANALYSIS] ATCC 208353 / W303-1A Hydrolyzes phytoceramide and also dihydroceramide into phytosphingosine or dihydrosphingosine. Prefers phytoceramide. Has also reverse hydrolysis activity, catalyzing synthesis of phytoceramide and dihydroceramide from palmitic acid and phytosphingosine or dihydrosphingosine. Is not responsible for the breakdown of unsaturated ceramide. Endoplasmic reticulum membrane Multi-pass membrane protein Golgi apparatus membrane Multi-pass membrane protein Belongs to the alkaline ceramidase family. Complete proteome Endoplasmic reticulum Golgi apparatus Hydrolase Membrane Reference proteome Transmembrane Transmembrane helix MGIFRWNYPESSVPGVWGETTSTIDWCEENYVVSPYIAEWSNTLTNSVFILSAIYTTYSA YKNKLEKRFLLIGFGYGLVGVGSWLFHMTLKYRFQLLDELPMIYAMCIPTWSLVCEAKEA LLNGDNHKKVPLFEQIFIGVIIGLAVTTASILYVIYKNVDIHQILFGVQIVVVAATAGSL TYRYVHDPLAKRNLKASMALGAILFLSGYISWLLDIHYCSFWVHVRRSILALPLGVLLEP HGWWHILTGMGIYFYIVSLEHLRVITLNVSCNYQFIWRWKVFPELIWKGRKPSTRYSLEL FGPYVEDQSIEVKKEK P43587 D6VTN3 YPI1_YEAST Type 1 phosphatases regulator YPI1 YPI1 YFR003C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c FUNCTION MUTAGENESIS OF TRP-53 INTERACTION WITH GLC7 AND PPZ1 IDENTIFICATION BY MASS SPECTROMETRY INTERACTION WITH GLC7 AND SDS22 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] YAL6B FUNCTION SUBCELLULAR LOCATION INTERACTION WITH GLC7 AND SDS22 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] FUNCTION SUBCELLULAR LOCATION INTERACTION WITH GLC7 MUTAGENESIS OF VAL-51 AND TRP-53 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control. Regulates the nuclear localization of type 1 phosphatase GLC7 and SDS22, and is involved in the regulation of mRNA 3'-end processing. May also regulate the activity of type 1 phosphatase PPZ1. Interacts with GLC7, PPZ1 and SDS22. P32598 GLC7 false 11 P36047 SDS22 false 10 Nucleus Present with 1080 molecules/cell in log phase SD medium. Belongs to the YPI1 family. Was originally (PubMed:14506263) thought to be an inhibitor of type 1 phosphatases using in vitro experiments, but further in vivo experiments (PubMed:18172024) showed that it was rather an activator of these phosphatases. Acetylation Complete proteome Nucleus Phosphoprotein Reference proteome V A W A MSGNQMAMGSEQQQTVGSRTVSVEEVPAVLQLRATQDPPRSQEAMPTRHNVRWEENVIDN ENMNKKKTKICCIFHPQNEDEEECNHHSDDDGSSSSGSSSSESENEKDLDFNERRQRRLE RRHRKLEKKRSYSPNAYEIQPDYSEYRRKQQEKKD P53303 D6VUZ4 Q02807 Q02808 ZPR1_YEAST Zinc finger protein ZPR1 ZPR1 YGR211W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-459 S288c / GRF88 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Binds to the elongation factor 1-alpha. Cytoplasm Nucleus Translocates to the nucleus after nutrient stimulation. Present with 39900 molecules/cell in log phase SD medium. Belongs to the ZPR1 family. Complete proteome Cytoplasm Metal-binding Nucleus Phosphoprotein Reference proteome Repeat Zinc Zinc-finger MSEQKEDLFKPVGEAAAEVEDESIAEQNKANDGVKLTGAQDAMGHPVQEIESLCMNCGKN GTTRLLLTSIPYFREIIIMSFDCPHCGFKNCEIQPASQIQEKGSRYVLKVECREDFNRQV IKSETATCKFVELDIEIPAKRGQLTTVEGLLSEMIDDLSQDQEMRKSIDEALYKKIDDFI QKVKSYINCEPNTIPITFILDDPAGNSWIEYKPGEPQHKWSHTQYVRTDEQNVQVGIITR DQLEQRRQEQLKQLANRERNPSESVKVGSANPQFLSDATDIENFNNEVQTFRASCPSCTQ ECETHMKPVNIPHFKEVIIMSTVCDHCGYKSNEVKTGGAIPDKGRRITLYCDDAADLSRD ILKSETCSMVIPELHLDIQEGTLGGRFTTLEGLLRQVYEELESRIFTQTSDSMDEATKAR WVEFFAKLKEAIAGKVKFTVIMEDPLAGSYIQNVYAPDPDPNMTIEDYERTKEQNEDLGL SDIKVE P53832 D6W0R1 WSC2_YEAST Cell wall integrity and stress response component 2 WSC2 YNL283C N0583 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-458 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] ADR376 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] GLYCOSYLATION [LARGE SCALE ANALYSIS] PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-402; SER-455 AND SER-458 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] Cell membrane Single-pass membrane protein N-glycosylated. Cell membrane Cell wall biogenesis/degradation Complete proteome Glycoprotein Membrane Phosphoprotein Reference proteome Signal Transmembrane Transmembrane helix MHLDLIHKSFILVWLIYIRAALADQFTYKACYSASDIRKLGLTYKGVYEYQSVSYCQNEC PGQAVVALFNGTGCYCGGSVAQLQSLTQVDSSKCDVSCAGWPYQNCGGSSAMNVYINNAA STADSTSSTATSTSTTSSSSTSVSSKTSTKLDTKTSTSSSATHSSSSSSTTSTTTSSSET TTSSSSSSSSSSTSTTSTTSTTSSTTSTSSSPSTTSSSTSASSSSETSSTQATSSSTTST SSSTSTATVTSTPSSTSIGTSTHYTTRVVTQSVVSQANQQASTIFTTRTSVYATVSSTSS STSSLLNGKSSSSKSKGLSGGAIAGVVVGVVCGTVALLALALFFFVWKKRRQSSQHVDLE ETKQYQPYSLGDADANPVIPPSASSTNWHIPSRNNTALSKNTASTFATYDLPTRAPGGRD SIITGDAHNISKRSHFPSVVYEEPPSIYNGNQRFSATSLPDMMEERQLHIVNPDNVSSNI GSNVSDGDDDYDDAKDSNNSSLR Q07381 D6VRT6 Q03128 TSR1_YEAST Ribosome biogenesis protein TSR1 20S rRNA accumulation protein 1 TSR1 YDL060W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 570-788 FUNCTION SUBCELLULAR LOCATION FUNCTION INTERACTION WITH RIO2 SUBCELLULAR LOCATION LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION SUBCELLULAR LOCATION FUNCTION Required for 40S ribosomal subunit synthesis. Required for normal export of the pre-40S particles from the nucleus to the cytoplasm. Its subcellular location and association with pre-40S subunitshifts from mixed cytoplasm/nucleus to all nuclear in RPS19 disruptions, suggesting it acts after the ribosomal protein. Interacts with RIO2. Cytoplasm Nucleus Nucleolus Present with 1390 molecules/cell in log phase SD medium. Belongs to the TRAFAC class translation factor GTPase superfamily. Bms1-like GTPase family. TSR1 subfamily. 3D-structure Complete proteome Cytoplasm Nucleus Reference proteome Ribosome biogenesis MAGHSHRSSLKNGHKSYKSKHASKGALKRLYKGKVEKEPVGTGKPDKQVSKLQRKNKAKQ LRAQRILDSIENRKLFEGKNGAAKIITIVPLVNDLDPLDILYKLLKCADDEGIMVQEVDS KRIFNVHIKKFKSNLKIIIPDMTNFLNILDCAKVADFVVFGLSGVQEVDEEFGEQIIRAL ELQGIASYIGVISNLSAVHEKEKFQLDVKQSLESYFKHFFPSEERVYNLEKNSDALNVLR TLCQRLPRSINWRDNRGYVVADFVDFVETSPDSGDLVIEGTVRGIGFNANRLVHIPDFGD FQLNKIEKISESSQKRKIIKEKATDSLSLELDLQTVFESNMNRDTLDEYAPEGTEDWSDY DEDFEYDGLTTARYDDHGFLPGREQTSKKAAVPKGTSDYQAKWYLDDVIDANEEEEAEQT NGKDETMMEIDDEMMVEQDNEEVAGDEEYDIEDNEGFEELSPEEEERQLREFRDMEKEDR EFPDEIELEPSESAIERLKRYRGLKNLYNCDWQVDEKDPSSPAEWKRLLRIGNYKNTKNR IIKETKNEAQAIAGDRIRMFIRFPKFLLEKIQDPKQLLFAVYGLLLHEHKNAVVNFSLQR WEQYDKPVPSQEPIVVQYGVRRYTIQPLFSQGSNSPNNVHKYERFLHPDTVSVATCIAPV DFTQSPAIFFKPSPTDAKNIELIGHGTFLNADHSRILAKRAILTGHPFRFHKTVVTVRYM FFRPEDVEWFKSIPLFTKSGRSGFIKESLGTHGYFKATFDGKLSAQDVVAMSLYKRMWPM PSLPWNGM Q04670 D6VZM5 YM14B_YEAST Transposon Ty1-MR2 Gag-Pol polyprotein Gag-Pol-p199 TY1A-TY1B Transposon Ty1 TYA-TYB polyprotein p190 Capsid protein CA Gag-p45 p54 Ty1 protease PR 3.4.23.- Pol-p20 p23 Integrase IN Pol-p71 p84 p90 Reverse transcriptase/ribonuclease H RT RT-RH 2.7.7.49 2.7.7.7 3.1.26.4 Pol-p63 p60 TY1B-MR2 YMRCTy1-4 POL YMR050C YM9796.03C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c NOMENCLATURE REVIEW REVIEW DOMAINS Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity). The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP. Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity). Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity). a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) Endonucleolytic cleavage to 5'-phosphomonoester. The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity). Cytoplasm Nucleus Q04670-1 Transposon Ty1-MR2 Gag-Pol polyprotein Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YMR051C ORF. P0CX69-1 Transposon Ty1-MR2 Gag polyprotein Produced by conventional translation. The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift between the codons for Leu-435 and Gly-436. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity). The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities. Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity). Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity). Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae). Aspartyl protease ATP-binding Complete proteome Cytoplasm DNA integration DNA recombination DNA-binding DNA-directed DNA polymerase Endonuclease Hydrolase Magnesium Metal-binding Multifunctional enzyme Nuclease Nucleotide-binding Nucleotidyltransferase Nucleus Phosphoprotein Protease Reference proteome Ribosomal frameshifting RNA-binding RNA-directed DNA polymerase Transferase Transposable element Transposition Viral release from host cell Virion maturation Zinc Zinc-finger MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPAS SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY RRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS TTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC FTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHR MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN SYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN YDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVS PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES PTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIQAYHKEVNQ LLKMKTWDTDRYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDPGMQS NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS LYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANK KIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL NPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINT LAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYK SQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITK GLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKP LPIKTFKLLTNKWIH P06104 D6VU83 UBC2_YEAST Ubiquitin-conjugating enzyme E2 2 2.3.2.23 E2 ubiquitin-conjugating enzyme 2 Radiation sensitivity protein 6 Ubiquitin carrier protein UBC2 Ubiquitin-protein ligase UBC2 RAD6 UBC2 YGL058W Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c PROTEIN SEQUENCE OF 77-91 FUNCTION FUNCTION INDUCTION FUNCTION MUTAGENESIS OF CYS-88 FUNCTION INTERACTION WITH UBR1 FUNCTION FUNCTION SUBCELLULAR LOCATION INTERACTION WITH UBR1 MUTAGENESIS OF 1-MET--LEU-9 FUNCTION INTERACTION WITH RAD18 AND UBR1 FUNCTION INTERACTION WITH RAD18 FUNCTION INTERACTION WITH UBR1 AND UBR2 FUNCTION SUBCELLULAR LOCATION FUNCTION MUTAGENESIS OF CYS-88 AND 1-MET--LEU-9 FUNCTION SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] FUNCTION FUNCTION FUNCTION PHOSPHORYLATION AT SER-120 FUNCTION INTERACTION WITH RTF1; PAF1 AND THE RNA POLYMERASE II HYPERPHOSPHORYLATED FORM FUNCTION PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS] X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In association with the E3 enzyme RAD18, it catalyzes the monoubiquitination of POL30 'Lys-164', involved in postreplication repair of UV-damaged DNA. The RAD6/UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. In association with the E3 enzyme UBR1, is involved in N-end rule-dependent protein degradation. Also involved in sporulation. S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine. Protein modification; protein ubiquitination. Forms a heterodimer complexes with the E3 enzymes BRE1, RAD18 and UBR1. Interacts also with UBR2, RTF1, PAF1 and the RNA polymerase II hyperphosphorylated form. The interaction with RNA polymerase II is BRE1- and PAF1-dependent. Q07457 BRE1 false 4 P10862 RAD18 false 4 P19812 UBR1 false 4 Q07963 UBR2 false 6 Cytoplasm Nucleus Up-regulated by UV radiations and during meiosis. The acidic-tail domain of UBC2 mediates interaction with UBR1 and UBR2, and thus is important for polyubiquitination of histones. This domain is also important for sporulation. The N-terminus is blocked. Present with 2770 molecules/cell in log phase SD medium. Belongs to the ubiquitin-conjugating enzyme family. 3D-structure ATP-binding Chromatin regulator Complete proteome Cytoplasm Direct protein sequencing DNA damage DNA repair Nucleotide-binding Nucleus Phosphoprotein Reference proteome Sporulation Transcription Transcription regulation Transferase Ubl conjugation pathway C A V MSTPARRRLMRDFKRMKEDAPPGVSASPLPDNVMVWNAMIIGPADTPYEDGTFRLLLEFD EEYPNKPPHVKFLSEMFHPNVYANGEICLDILQNRWTPTYDVASILTSIQSLFNDPNPAS PANVEAATLFKDHKSQYVKRVKETVEKSWEDDMDDMDDDDDDDDDDDDDEAD P15732 D6VS45 UBC5_YEAST Ubiquitin-conjugating enzyme E2-16 kDa 2.3.2.23 E2 ubiquitin-conjugating enzyme 5 Ubiquitin carrier protein Ubiquitin-protein ligase UBC5 YDR059C D4234 YD9609.13C Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 40-64 AND 119-125 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine. Protein modification; protein ubiquitination. By heat shock and cadmium. The N-terminus is blocked. Present with 981 molecules/cell in log phase SD medium. Belongs to the ubiquitin-conjugating enzyme family. ATP-binding Complete proteome Direct protein sequencing Isopeptide bond Nucleotide-binding Phosphoprotein Reference proteome Stress response Transferase Ubl conjugation Ubl conjugation pathway MSSSKRIAKELSDLGRDPPASCSAGPVGDDLYHWQASIMGPSDSPYAGGVFFLSIHFPTD YPFKPPKVNFTTKIYHPNINSSGNICLDILKDQWSPALTLSKVLLSICSLLTDANPDDPL VPEIAQIYKTDKAKYEATAKEWTKKYAV P46951 D6VUY0 YPP1_YEAST Cargo-transport protein YPP1 Alpha-synuclein protective protein 1 YPP1 YGR198W G7594 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [GENOMIC DNA] ATCC 204508 / S288c NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS] LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS] IDENTIFICATION BY MASS SPECTROMETRY INTERACTION WITH RIBOSOMES FUNCTION SUBCELLULAR LOCATION Involved in endocytosis. Interacts with ribosomes. P37297 STT4 false 2 Cytoplasmic granule Cell membrane Peripheral membrane protein Cytoplasmic side Present with 1640 molecules/cell in log phase SD medium. Belongs to the YPP1 family. 3D-structure Cell membrane Complete proteome Endocytosis Membrane Reference proteome MPNSNVRIPPTVPSKIIDVVDQALRARLLGGSTFNSGFDSLDSVLNLQFRLHYHVIGSNG PAKPVCDVLLKESQNLEKNMSMMEELNDYPEITKLVEKILFNCLGILFFHRGQFQESQRC LLHSLKIHNNTASQKTALMEQYDRYLIVENLYYRGLVSQDINIMQNVFYKELLAHVDTIP PESNGLLFEYISLIVAKLRFNQIQDLAENFKTTVENPFILFLYMIKKFQSPLKKHIDNDD LYLKFGQNVLLKAKFPTASETNDEALEHFNVFLQYYFKFTHIKKIKVNPSWYNFIISSME KTFQSIEVSKTAMFLFQNLSDNSNDEIKKKTFKRESILNFVNFVKYNDKYYQLHDNSHRD IISFIDAYSFILQNSSKTDSIENVFDYDNTVSTFATSLNSFYKEYNLPLMSQSESLDWLE NSTRCVYPGNISKVLTNAWSTLYEIRKYQLDFLVSNNLTSYLCNAMMLSTKEKDNADVEE QEEGEEEKALRELQFKYSYTLAQQRHIETAIKTLESLILSKNPNYYKAWHLLALCRSVQE DKEMSYKIVCSVLEAMNESLQNNTLLLNDRWQFIHLKLTQLALIEEIFGTLEALETLPEV FELYATLFPDSQPELNSMGPKYSQTKEYLLQMVWIFAANMYMRTKDNDEDAKAAIKEASN VESKFKNLNCNIANGYLSIIKDEPGVALKEFETVLYYDENNLDALVGFAELIFPEELGVE ETNLERYYTLSLDKKPGKRAKLTFVNDTDRSAAYARLKFLLECAILESIEAYYSPEVWWY LSLIYEKYQDDEYKNSLLKCIKYQELNPIRSLRYCNY Q3E7B9 D6W275 YO08A_YEAST Uncharacterized protein YOR008C-A YOR008C-A Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Baker's yeast Eukaryota Fungi Dikarya Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] ATCC 204508 / S288c GENOME REANNOTATION ATCC 204508 / S288c