UBP16_YEAST
ID UBP16_YEAST Reviewed; 499 AA.
AC Q02863; D6W3U3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 16;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 16;
DE AltName: Full=Ubiquitin thioesterase 16;
DE AltName: Full=Ubiquitin-specific-processing protease 16;
GN Name=UBP16; OrderedLocusNames=YPL072W; ORFNames=LPF12W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 450 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; U41849; AAB68265.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11359.1; -; Genomic_DNA.
DR PIR; S61114; S61114.
DR RefSeq; NP_015253.1; NM_001183886.1.
DR AlphaFoldDB; Q02863; -.
DR BioGRID; 36107; 62.
DR STRING; 4932.YPL072W; -.
DR MEROPS; C19.A18; -.
DR MaxQB; Q02863; -.
DR PaxDb; Q02863; -.
DR PRIDE; Q02863; -.
DR EnsemblFungi; YPL072W_mRNA; YPL072W; YPL072W.
DR GeneID; 856032; -.
DR KEGG; sce:YPL072W; -.
DR SGD; S000005993; UBP16.
DR VEuPathDB; FungiDB:YPL072W; -.
DR eggNOG; ENOG502QSIQ; Eukaryota.
DR HOGENOM; CLU_023181_0_0_1; -.
DR InParanoid; Q02863; -.
DR OMA; CHKGSHN; -.
DR BioCyc; YEAST:G3O-33980-MON; -.
DR PRO; PR:Q02863; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02863; protein.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA: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 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..499
FT /note="Ubiquitin carboxyl-terminal hydrolase 16"
FT /id="PRO_0000080601"
FT DOMAIN 53..497
FT /note="USP"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 407
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 499 AA; 56920 MW; 292021C9A268B4D1 CRC64;
MSWIKNVTES PTSLIKKVSC GLIIAASLYA IAPSLSALVF GDSKQSIGKY TTVGLINRGN
DCFITSSLQG LAGIPRFVEY LKRIRTVLLE LETKLSNNAK GDNPTVDNTT RHSRLENSSN
SLAPLHESLT SLILDLISVK DRKTSISPKI VINTLESIFK SKISSKQNDA HEFTLILLQT
LQEERSKLID YSKQICNLNI PKFPFEGETS KFLVCLKCKG LSEPSYKQTF IRELSVPQQT
SENLSNILAH DETEIIDDYS CLICQIRAIL NHEEYRNFKD CTPDEILMLD RLKNYATKAP
INENLPFEVE QYVKRYSKGN LQVSNIKGKV IKKDVVVQLP DILIVHLSRS TFNGITYSRN
PCNVKFGERI TLSEYTLAES GTITENRQVK YNLKSVVKHT GSHSSGHYMC YRRKTEIRFG
KEDESSFRRA PVVNNEVNKN REQNVAHNDY KKSRYKKVKN ALRYPYWQIS DTAIKESTAS
TVLNEQKYAY MLYYERVNK