UBP15_YEAST
ID UBP15_YEAST Reviewed; 1230 AA.
AC P50101; D6W0D1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 15;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 15;
DE AltName: Full=Ubiquitin thioesterase 15;
DE AltName: Full=Ubiquitin-specific-processing protease 15;
GN Name=UBP15; OrderedLocusNames=YMR304W; ORFNames=YM9952.06;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- MISCELLANEOUS: Present with 2810 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; Z49212; CAA89137.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10205.1; -; Genomic_DNA.
DR PIR; S53974; S53974.
DR RefSeq; NP_014033.1; NM_001182814.1.
DR AlphaFoldDB; P50101; -.
DR SMR; P50101; -.
DR BioGRID; 35484; 250.
DR DIP; DIP-6313N; -.
DR IntAct; P50101; 26.
DR MINT; P50101; -.
DR STRING; 4932.YMR304W; -.
DR MEROPS; C19.099; -.
DR iPTMnet; P50101; -.
DR MaxQB; P50101; -.
DR PaxDb; P50101; -.
DR PRIDE; P50101; -.
DR EnsemblFungi; YMR304W_mRNA; YMR304W; YMR304W.
DR GeneID; 855350; -.
DR KEGG; sce:YMR304W; -.
DR SGD; S000004920; UBP15.
DR VEuPathDB; FungiDB:YMR304W; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003532_2_1_1; -.
DR InParanoid; P50101; -.
DR OMA; KMKGTCL; -.
DR BioCyc; YEAST:G3O-32969-MON; -.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SCE-8948747; Regulation of PTEN localization.
DR PRO; PR:P50101; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P50101; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:SGD.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0010995; P:free ubiquitin chain depolymerization; IDA:SGD.
DR GO; GO:0016579; P:protein deubiquitination; IDA:SGD.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 2.60.210.10; -; 1.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR024729; USP7_ICP0-binding_dom.
DR InterPro; IPR029346; USP_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF14533; USP7_C2; 1.
DR Pfam; PF12436; USP7_ICP0_bdg; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1230
FT /note="Ubiquitin carboxyl-terminal hydrolase 15"
FT /id="PRO_0000080600"
FT DOMAIN 39..179
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 205..536
FT /note="USP"
FT ACT_SITE 214
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 1230 AA; 143564 MW; BEB8F6E3DD71A0CC CRC64;
MSSEDELGSI GTVFPGSPID KSIGSILPQF DEEVETLLED SFTWNIPDWN ELTNPKYNSP
RFRIGDFEWD ILLFPQGNHN KGVAVYLEPH PEEKLDETTG EMVPVDPDWY CCAQFAIGIS
RPGNGDTINL INKSHHRFNA LDTDWGFANL IDLNNLKHPS KGRPLSFLNE GTLNITAYVR
ILKDPTGVLW HNFLNYDSKK VTGYVGFRNQ GATCYLNSLL QSYFFTKYFR KLVYEIPTEH
ESPNNSVPLA LQRAFYQLQV SDIPLDTLEL TRSFGWDTAE SFTQHDVQEL NRILMDRLEN
NMKGTPVEGK LNEIFVGKMK SYIKCINVDY ESARVEDFWD LQLNVKNFKN LQESFDNYIE
MELMNGENQY AAQDYGLQDA QKGVIFESFP PVLHLQLKRF EYDFNYDQMV KVNDKYEFPE
TIDLSPFVDK DVLKKTLDSE NKDKNPYVYN LHGVLVHSGD ISTGHYYTLI KPGVEDQWYR
FDDERVWRVT KKQVFQENFG CDRLPDEKVR TMTRGEYQNY IIQRHTSAYM LVYIRQEQEE
DLLRPVLESD VPKHVITRVR EEIKERETKE KEIREAHLYV TLRLHSIKEF IHYEGFDYFA
HDGFRLFAEE LNDSGLQQIN LKVLRTTKLS DIFASIKETM NIPQERDVKY WKMDYRRNST
LRLTQPINFE SVNITLQEAL KKEKKRTMQT QYGEEGVAST EEDDKALLET VSFLDLFIEE
PYLELQFLNK LKEASLISKA QLDDELISTI RTNLPELTKG GIEPVFATDN KSNLLFVKSY
DPHTQKLLGF GHFAVNQLQQ LSDISAIIED SISSNEKLTF YEEVQPGTIN EIYMKETIYD
ADIDTGDIVS FEVPGAVLPD TFPVYATIKD FYSYLRYRVK LKFSKFDGSS EEYGVSNEIP
ESFEFWISAY APYDDLARMV SKYAHVKPEY LKIIALYSNG RFVLKSTSLL NDYLLKDFNC
DQIPPFAFEV LSVPLKELER LRPIKLYWLK NSYIHYQCFE FEVANDYTES QFLEKVQHKI
GFTDEEKENI LLWTNTNFQF QGLLSDQNTF KDVSKHSLLF GRILPEESKL FKELNRLENV
QTSSLEDFMD DENATDRPMD DEQDLGMAIE HSEDMKGRIV VVQQYFKDLE NRHGISFLFN
LIPDETFPKT KDRLHAKFGL GQKEFSKIKL SIGYSTEEGT VFRSLQGFSD EELDKVILYD
IMSNLDYIYM DHPDRLRSHS SYDRPMIIKN
