UBP12_SCHPO
ID UBP12_SCHPO Reviewed; 979 AA.
AC O60079;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase 12;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 12;
DE AltName: Full=Ubiquitin thioesterase 12;
DE AltName: Full=Ubiquitin-specific-processing protease 12;
GN Name=ubp12; ORFNames=SPCC1494.05c;
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 SER-19; SER-37 AND SER-39, AND
RP 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}.
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; CU329672; CAA19303.1; -; Genomic_DNA.
DR PIR; T41006; T41006.
DR RefSeq; NP_588530.1; NM_001023518.2.
DR AlphaFoldDB; O60079; -.
DR SMR; O60079; -.
DR BioGRID; 275564; 6.
DR STRING; 4896.SPCC1494.05c.1; -.
DR MEROPS; C19.A64; -.
DR iPTMnet; O60079; -.
DR MaxQB; O60079; -.
DR PaxDb; O60079; -.
DR PRIDE; O60079; -.
DR EnsemblFungi; SPCC1494.05c.1; SPCC1494.05c.1:pep; SPCC1494.05c.
DR GeneID; 2538990; -.
DR KEGG; spo:SPCC1494.05c; -.
DR PomBase; SPCC1494.05c; ubp12.
DR VEuPathDB; FungiDB:SPCC1494.05c; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; O60079; -.
DR OMA; TGQLVIM; -.
DR PhylomeDB; O60079; -.
DR Reactome; R-SPO-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR PRO; PR:O60079; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA:PomBase.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2230.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51283; DUSP; 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..979
FT /note="Probable ubiquitin carboxyl-terminal hydrolase 12"
FT /id="PRO_0000080612"
FT DOMAIN 51..152
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 311..977
FT /note="USP"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 935
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 979 AA; 111967 MW; A705444BCDB437D2 CRC64;
MDSLSESSTS SYHGKRPRSL SEESQSSSNM DDISQKSISL GDASEISKNL PSIAEQKQLI
GELVNNQPEL ELGQVDNYIL SYSWYERLCS YLAEDGPFPG PVDQEDIADL ETGTLKPDLQ
EEIDFTIISR DVWDLLVRWY GLKGPEFPRE TVNLGSESHP HLVVEVYPPI FSLTLLSTNA
VDANESHKPK KISLSSKSTL EDLLEGVKYT LSLPSDQFRL WRVDTDQPLH RTIDPSSFIK
INSKEIIDFL EKSKTLVELG MDSSCSLVAE CMINETWPVD RALRLQFLIQ QRNNQSSNEE
QKQEKRVPGT CGLSNLGNTC YMNSALQCLT HTRELRDFFT SDEWKNQVNE SNPLGMGGQV
ASIFASLIKS LYSPEHSSFA PRQFKATIGK FNHSFLGYGQ QDSQEFLAFL LDGLHEDLNR
IYQKPYTSKP DLYEVDEEKI KNTAEECWRL HKLRNDSLIV DLFQGMYRST LVCPVCNTVS
ITFDPFMDLT LPLPVKQVWS HTVTFIPADT NLTPLAIEVV LESKAATIED LVKYVAEKSG
CSDYRKILVT ETYKGRFYRF LTQLSKSLLM EISEEDEIYL YELERPYEDG SDDILVPVYH
ISDDSTNSAN SYMSSRDFGH PFVLQLSDNE VTDASFISEK LKLKYQQFTT LKNLKNIDSL
ESLELGHEDE QVQKGPLDVD MDHSQTPLFE MRVFHDRFEK IPTGWNMSVS NLPLLTERDK
KDLESTVDPL DAHSIEEEDD SEFKDVAPGS YPEPSKSNEN TKLTAKENDR LLIQGDLLVC
EWPEKSYQFV FSVAPSSPQM GRSLWLESKT ILSDKKDDSE DSRTITLNDC LDEFEKTEQL
GEEDPWYCPT CKEFRQASKQ MEIWRCPEIL IFHLKRFSSE RRFRDKIDDL VEFPIDNLDM
SMRTGSYKLS EKENPKLIYE LYAVDNHYGG LGGGHYTAFA KNPDNGQFYC FDDSRVTPVC
PEETVTSAAY LLFYRRKTS
