UBP11_YEAST
ID UBP11_YEAST Reviewed; 717 AA.
AC P36026; D6VXF9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 11;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 11;
DE AltName: Full=Ubiquitin thioesterase 11;
DE AltName: Full=Ubiquitin-specific-processing protease 11;
GN Name=UBP11; OrderedLocusNames=YKR098C;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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).
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 -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; Z28323; CAA82178.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09249.1; -; Genomic_DNA.
DR PIR; S38177; S38177.
DR RefSeq; NP_013024.1; NM_001179888.1.
DR AlphaFoldDB; P36026; -.
DR SMR; P36026; -.
DR BioGRID; 34229; 75.
DR IntAct; P36026; 1.
DR MINT; P36026; -.
DR STRING; 4932.YKR098C; -.
DR MEROPS; C19.102; -.
DR iPTMnet; P36026; -.
DR MaxQB; P36026; -.
DR PaxDb; P36026; -.
DR PRIDE; P36026; -.
DR EnsemblFungi; YKR098C_mRNA; YKR098C; YKR098C.
DR GeneID; 853973; -.
DR KEGG; sce:YKR098C; -.
DR SGD; S000001806; UBP11.
DR VEuPathDB; FungiDB:YKR098C; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000168459; -.
DR HOGENOM; CLU_004122_1_0_1; -.
DR InParanoid; P36026; -.
DR OMA; GICRTIK; -.
DR BioCyc; YEAST:G3O-32060-MON; -.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR PRO; PR:P36026; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36026; protein.
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; IDA:SGD.
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 3: Inferred from homology;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..717
FT /note="Ubiquitin carboxyl-terminal hydrolase 11"
FT /id="PRO_0000080596"
FT DOMAIN 298..707
FT /note="USP"
FT REGION 231..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..565
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 649
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 717 AA; 82703 MW; 9BAA1EEEB5DD9A65 CRC64;
MLLNPDQILN LVRKVYEVDI KQFYSQLRLK NLRGLLDHAA HLFNVYLRDL EINQEMEALT
AFIIGCYYLY LIIPQSLQFQ TRNNLYSSYA KLKNDYQDEH VMGYVLKVVR DESTVIVDRY
LAESNGICRT IKRKRAYSLP LRPLPVHMAS LSIHNKFDGS LHEIPNELTK PTNDNSKEDI
VRESNQIASS NKLEAGSEVA YYTSKEALSK PSYLKLSTGK DALFKTLSSP ATAPPVHSLE
VSSQIRDSSQ DSSSSLSKVE KPKEEEGKIE AIESSAPKAY NLPVIEDSND LLSELSITGL
QNPCNTCYIN SIIQCLFGTT LFRDLFLTKK YRLFLNTNKY PKEVQLSRSI YVLFKKMYLN
GGRAIIPNRF LKMCKKLRPD LNIPDDQQDT QEFLLIVLAR IHEELSNENV VKYYPDLVSY
DANALQVNPS KYEKWYERNV ITDGLSPIDH IYRGQLENIL KCQRCGNSSY SYSTFYVLSL
AIPKLSLYSF TSKSRKIKLE DCINLFTGDE ELSGDNAWDC PNCRITDSKS KKEEITSQKK
KSTIFGFHSR SRSKSPHHHH HHHHSSDDST KNAKKRNSKK LTTIKSLDFI VLPPILVIHL
SRFYYDLTKK NSTVITYPLI LNIILKNGKV IRYKLYGTVN HSGNLINGHY TSVVNKEKSH
EIGLNRQVWV TFDDDYIQQH RKDRNNFEAG KTEMSSDEVY VLFYERMDEE NYEEEFC
