UBP5_YEAST
ID UBP5_YEAST Reviewed; 805 AA.
AC P39944; D3DM51;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 5;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 5;
DE AltName: Full=Ubiquitin thioesterase 5;
DE AltName: Full=Ubiquitin-specific-processing protease 5;
GN Name=UBP5; OrderedLocusNames=YER144C;
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 [GENOMIC DNA].
RX PubMed=7871889; DOI=10.1002/yea.320101114;
RA Xiao W., Fontanie T., Tang M.;
RT "UBP5 encodes a putative yeast ubiquitin-specific protease that is related
RT to the human Tre-2 oncogene product.";
RL Yeast 10:1497-1502(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
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 [4]
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).
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 300 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; U10082; AAC48928.1; -; Genomic_DNA.
DR EMBL; U18917; AAB64671.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07805.1; -; Genomic_DNA.
DR PIR; S50277; S50277.
DR RefSeq; NP_011071.3; NM_001179034.3.
DR AlphaFoldDB; P39944; -.
DR SMR; P39944; -.
DR BioGRID; 36893; 82.
DR DIP; DIP-1716N; -.
DR IntAct; P39944; 7.
DR MINT; P39944; -.
DR STRING; 4932.YER144C; -.
DR MEROPS; C19.006; -.
DR iPTMnet; P39944; -.
DR MaxQB; P39944; -.
DR PaxDb; P39944; -.
DR PRIDE; P39944; -.
DR EnsemblFungi; YER144C_mRNA; YER144C; YER144C.
DR GeneID; 856887; -.
DR KEGG; sce:YER144C; -.
DR SGD; S000000946; UBP5.
DR VEuPathDB; FungiDB:YER144C; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000173629; -.
DR HOGENOM; CLU_005922_1_0_1; -.
DR InParanoid; P39944; -.
DR OMA; LEWERFL; -.
DR BioCyc; YEAST:G3O-30305-MON; -.
DR Reactome; R-SCE-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR PRO; PR:P39944; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39944; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; TAS:SGD.
DR GO; GO:0016579; P:protein deubiquitination; TAS:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50206; RHODANESE_3; 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..805
FT /note="Ubiquitin carboxyl-terminal hydrolase 5"
FT /id="PRO_0000080590"
FT DOMAIN 159..283
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 446..804
FT /note="USP"
FT REGION 359..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 455
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 761
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 805 AA; 92261 MW; 884054A66370DFF7 CRC64;
MGSEQALSEV VESAKERFGR LRHLVQKFLD DDDVPQECLP LLQECAEIWS SYVDACQDIT
MQAPKEDANR LSKGFLRLNE TAFLYYMIVY TLLEDTLPRL KEFSSNKDQN VRNLYGERIQ
LLHNDPNIER IRNVIENYPK FIQLQTIEPG KLSSMLHFHG DALLLIDVRP RSEFVRAHIK
CKNIICIDPA SFKDSFTDQQ IESVSLITSP HSDITFFSNR DKFKFIILYT DTQLHNNFQQ
RQTRILAKIL SQNSVIKPLS GTKILILENG FSNWVKLGGA YQSSVSETAH LTSSSSTPAF
GSPQVPTGLF NQKSLSPNKD KSMPMVSMNT QPLLTTVQRP QLPLYYSDLP IIPQPSPNRN
SPTVQKFSPH PPTTLSKLNT PSTIQNKANT VERISPDIRA AQAHAYLPPA SNVFSPRIPP
LPQQNLSSSR QTILNNSQVL DLDLIVGLEN IGNCCYMNCI LQCLVGTHDL VRMFLDNTYL
NFINFDSSRG SKGLLAKNFA ILVNNMHRHG AFTPPNVRTI PVQTIQFKKI CGHINPMYSD
SMQQDCQEFC QFLLDGLHED LNQNGSKKHL KQLSDEEERM REKMSIRKAS ALEWERFLLT
DFSAIIDLFQ GQYASRLQCQ VCEHTSTTYQ TFSVLSVPVP RVKTCNILDC FREFTKCERL
GVDEQWSCPK CLKKQPSTKQ LKITRLPKKL IINLKRFDNQ MNKNNVFVQY PYSLDLTPYW
ARDFNHEAIV NEDIPTRGQV PPFRYRLYGV ACHSGSLYGG HYTSYVYKGP KKGWYFFDDS
LYRPITFSTE FITPSAYVLF YERIF
