UBP16_SCHPO
ID UBP16_SCHPO Reviewed; 457 AA.
AC O74442;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable 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; ORFNames=SPCC1682.12c;
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-61; THR-64 AND SER-65, 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}.
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DR EMBL; CU329672; CAA20678.1; -; Genomic_DNA.
DR PIR; T41069; T41069.
DR RefSeq; NP_587805.1; NM_001022798.2.
DR AlphaFoldDB; O74442; -.
DR SMR; O74442; -.
DR BioGRID; 275521; 28.
DR STRING; 4896.SPCC1682.12c.1; -.
DR MEROPS; C19.A66; -.
DR iPTMnet; O74442; -.
DR MaxQB; O74442; -.
DR PaxDb; O74442; -.
DR PRIDE; O74442; -.
DR EnsemblFungi; SPCC1682.12c.1; SPCC1682.12c.1:pep; SPCC1682.12c.
DR GeneID; 2538947; -.
DR KEGG; spo:SPCC1682.12c; -.
DR PomBase; SPCC1682.12c; ubp16.
DR VEuPathDB; FungiDB:SPCC1682.12c; -.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_008279_10_0_1; -.
DR InParanoid; O74442; -.
DR OMA; HEFARCL; -.
DR PhylomeDB; O74442; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-9648002; RAS processing.
DR PRO; PR:O74442; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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:0101005; F:deubiquitinase activity; IDA:PomBase.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; HDA: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: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; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..457
FT /note="Probable ubiquitin carboxyl-terminal hydrolase 16"
FT /id="PRO_0000248399"
FT DOMAIN 125..429
FT /note="USP"
FT REGION 34..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 457 AA; 51582 MW; 56AADB2AA996EFF3 CRC64;
MSLATLQGQS LDFAVKHSLD DLLKNPVRFR PAVVSSPSVP EGTYTVLNNP KQSTVSRKSF
SAPTSPTRNK RSGSSSQEYK KSSGTRGDGA NDFVDEDPAF IPPARILFPE EKLSMEWDNI
MPNAPGLVNL GNTCFMNSVL QLMTQTPPLV QYLLSGQHSL SCRMNACVLC RMEQHVARAY
PNKGTKRASA FKPSGIQSML KVISSHFRPY RQEDAHEFMR YLVDAWQKSC LQNHKNLDHP
SRETSVVHRI FGGYLRQQIL CSVCKKPSNT YQALLDLSVD AKGSSLADSL KHFVHAEKLT
KQNKYRCENC KQLVDASKQM TIYRAPNILT IHFKRFTFNG FQSSKISKQI SYPESFNLGP
YMSDPNCSCW YELIGVLVHA GGSTRSGHYY SFCKSSNGVW LKFDDDFVSN SSIDRVLNQQ
AYILQYKRKS TSSSKHKLNT ENTVTKTSNK KRRKISF
