UBP9_YEAST
ID UBP9_YEAST Reviewed; 754 AA.
AC P39967; D3DM05;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 9;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 9;
DE AltName: Full=Ubiquitin thioesterase 9;
DE AltName: Full=Ubiquitin-specific-processing protease 9;
GN Name=UBP9; OrderedLocusNames=YER098W;
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=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 [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).
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 98 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U18839; AAB64653.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07759.1; -; Genomic_DNA.
DR PIR; S50601; S50601.
DR RefSeq; NP_011024.1; NM_001178989.1.
DR AlphaFoldDB; P39967; -.
DR SMR; P39967; -.
DR BioGRID; 36844; 112.
DR DIP; DIP-6551N; -.
DR IntAct; P39967; 1.
DR MINT; P39967; -.
DR STRING; 4932.YER098W; -.
DR MEROPS; C19.A20; -.
DR iPTMnet; P39967; -.
DR MaxQB; P39967; -.
DR PaxDb; P39967; -.
DR PRIDE; P39967; -.
DR EnsemblFungi; YER098W_mRNA; YER098W; YER098W.
DR GeneID; 856835; -.
DR KEGG; sce:YER098W; -.
DR SGD; S000000900; UBP9.
DR VEuPathDB; FungiDB:YER098W; -.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00940000176606; -.
DR HOGENOM; CLU_008279_12_1_1; -.
DR InParanoid; P39967; -.
DR OMA; PMHGHYV; -.
DR BioCyc; YEAST:G3O-30264-MON; -.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR PRO; PR:P39967; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39967; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 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..754
FT /note="Ubiquitin carboxyl-terminal hydrolase 9"
FT /id="PRO_0000080594"
FT DOMAIN 134..667
FT /note="USP"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..754
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 143
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 618
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 754 AA; 86244 MW; D2C03D233D14D693 CRC64;
MIKRWLSVNR KKSHPEKNTQ GNDEINRKAT SLKKTKGSGD PSIAKSPSAK SSTSSIPSNL
ASHERRSKFS SQTDNLAGNK HYHEHYHNMA STSDEREYDS STTYEDRAFD TESSILFTTI
TDLMPYGDGS NKVFGYENFG NTCYCNSVLQ CLYNIPEFRC NVLRYPERVA AVNRIRKSDL
KGSKIRVFTN ESFETSTNSG NSNTGYQSND NEDAHNHHHL QQSDQDNSSS STQEKQNNFE
RKRNSFMGFG KDKSNYKDSA KKDDNNEMER PQPVHTVVMA SDTLTEKLHE GCKKIIVGRP
LLKQSDSLSK ASTTDCQANS HCQCDSQGSR ITSVDDDVLV NPESCNDAVN NSNNNKENTF
PTSEQRKKAA LIRGPVLNVD HLLYPTEEAT LYNGLKDIFE SITENLSLTG IVSPTEFVKI
LKKENVLFNT MMQQDAHEFL NFLLNDFSEY IQRNNPRMRF GPQKTDNSND NFITDLFKGT
LTNRIKCLTC DNITSRDEPF LDFPIEVQGD EETDIQKMLK SYHQREMLNG VNKFYCNKCY
GLQEAERMVG LKQLPHILSL HLKRFKYSEE QKSNIKLFNK ILYPLTLDVS STFNTSVYKK
YELSGVVIHM GSGPQHGHYV CICRNEKFGW LLYDDETVES IKEETVLQFT GHPGDQTTAY
VLFYKETQAD KTENQNENID TSSQDQMQTD NNIEQLIKCD DWLRDRKLRA AANIERKKTL
GNIPEVKTAE TKTPLNDKKR NKQKRKSRIL SFIK
