UBP2_SCHPO
ID UBP2_SCHPO Reviewed; 1141 AA.
AC Q9P3U0;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 2;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 2;
DE AltName: Full=Ubiquitin thioesterase 2;
DE AltName: Full=Ubiquitin-specific-processing protease 2;
GN Name=ubp2; ORFNames=SPAC328.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-112; SER-113; THR-115;
RP THR-721 AND SER-722, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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; CU329670; CAB96001.1; -; Genomic_DNA.
DR RefSeq; NP_594208.1; NM_001019631.2.
DR AlphaFoldDB; Q9P3U0; -.
DR BioGRID; 278537; 152.
DR STRING; 4896.SPAC328.06.1; -.
DR MEROPS; C19.A56; -.
DR iPTMnet; Q9P3U0; -.
DR MaxQB; Q9P3U0; -.
DR PaxDb; Q9P3U0; -.
DR PRIDE; Q9P3U0; -.
DR EnsemblFungi; SPAC328.06.1; SPAC328.06.1:pep; SPAC328.06.
DR GeneID; 2542059; -.
DR KEGG; spo:SPAC328.06; -.
DR PomBase; SPAC328.06; ubp2.
DR VEuPathDB; FungiDB:SPAC328.06; -.
DR eggNOG; KOG1863; Eukaryota.
DR HOGENOM; CLU_003155_0_0_1; -.
DR InParanoid; Q9P3U0; -.
DR OMA; CDIKVDV; -.
DR PhylomeDB; Q9P3U0; -.
DR PRO; PR:Q9P3U0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
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:0061578; F:Lys63-specific deubiquitinase activity; IDA:PomBase.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA:PomBase.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:PomBase.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:PomBase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR025305; UCH_repeat_domain.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF13446; RPT; 4.
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; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1141
FT /note="Probable ubiquitin carboxyl-terminal hydrolase 2"
FT /id="PRO_0000080603"
FT DOMAIN 614..1124
FT /note="USP"
FT REGION 748..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 623
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 1076
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 721
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1141 AA; 130297 MW; 1499E32DB6CB26CB CRC64;
MATVKNLRIG KSPNRLIQDL DVFDSPSAGW NDPWSPHSSR YHWQLHSNLG ESAVFDENDF
WCVCQKTRKH LHVKVRRDRG KPLIEEPEEN YGIKDRIPVY YEEEELPEPH VTSPTKSEFA
TTSTCMKWSS KTTKSEIEVE WRDSYLDANC IKEIIDSRRP SFASLLTKKS SSHQGSSHSS
QPSLFTTFTS LELFLRNVLV HNDQRAISAA PEGTFERHVG KGRQIQSLMK SLLFEYHHEN
VNYVPTIADA PLTDEQKLNL YLARNELIVL ANHFRDTKED PAIVANPFPV RLARPALINA
FGVPNYDSVV PMYTTVFRDN SASLPDDPAF IALGITNDYP DSFVRYFYEE QKKNDEANVR
VYADALAHIY NLRKSSFLRD LIAADRKNGI VSSDVIQAAY SSLGLEAEVG PDYRYSQEKI
FEAFHSALLR KPEFARAIRN DLETIGYARK SSEILNYVLS TEQAFYTVNE AYQWLGIKSN
TEDAMVASVA LVKFEDDSDK AIEAVKWIAE ERNSSILYDF LASQGRPSNK KPKEVPMDED
LAYNTLGVQD RALSDDVLIN VYGFAVEDHP EQSDTLRAAL KCIGEVRNSR LITHYLEHGN
LDIPPEVSSL DTPIGLENTG NLCYLNSLIQ YYFIIKPLRN AILDIDENKD LNMIENKEAV
KKVGGRIVTR IEFLRALQFT YELRKLFIEL ITSKSSSVHP SSVLTYLALI PLTLDQVKSG
TSSVMDLSSS RELSNLNERS ITIDPRAEEQ AQGLEQEQGQ DEAKSPAEQS SSVNLIDFPM
ANTNGESQTQ PHYFEVSEEE INSSMDLGRQ QDVLECIDHV LFQLEASLGR ISNSEDRLGS
DNDLIRRLFS GKLKQTLNDA SQGVRSNYEI FSHLIVDLFE EKQTLYDALD GVFETVNIDM
GSETAQRSLC ITELPIILQL QIQRVQFDRT TGQPFKSNAF VEFGKELSMD RYVEDTDGKM
APLLQRYWDL KREIINLQKR QQLLLTTNSN LMSSVDTLSI LSKWAAQQQD SRLPINPKLP
DILQEEINNV VAEVDMLKKQ EASLKEERTH LFDNYISHSY DLLAVFVHRG QASFGHYWTY
IHDFENNVYR KYNDEYVTVV DESEIFADTT GNNANPYMLT YIRKEYRHII ECVHREHNLL
L
