ULP2_SCHPO
ID ULP2_SCHPO Reviewed; 638 AA.
AC O13769;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ubiquitin-like-specific protease 2;
DE EC=3.4.22.-;
GN Name=ulp2; ORFNames=SPAC17A5.07c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP GENE NAME.
RA Watts F.;
RL Submitted (MAR-2001) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526, AND IDENTIFICATION BY
RP 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11507.2; -; Genomic_DNA.
DR PIR; T37822; T37822.
DR RefSeq; NP_593475.2; NM_001018908.2.
DR AlphaFoldDB; O13769; -.
DR SMR; O13769; -.
DR BioGRID; 278737; 109.
DR STRING; 4896.SPAC17A5.07c.1; -.
DR MEROPS; C48.A09; -.
DR iPTMnet; O13769; -.
DR MaxQB; O13769; -.
DR PaxDb; O13769; -.
DR PRIDE; O13769; -.
DR EnsemblFungi; SPAC17A5.07c.1; SPAC17A5.07c.1:pep; SPAC17A5.07c.
DR GeneID; 2542268; -.
DR KEGG; spo:SPAC17A5.07c; -.
DR PomBase; SPAC17A5.07c; ulp2.
DR VEuPathDB; FungiDB:SPAC17A5.07c; -.
DR eggNOG; KOG0779; Eukaryota.
DR HOGENOM; CLU_417467_0_0_1; -.
DR InParanoid; O13769; -.
DR OMA; FHAKVPQ; -.
DR PRO; PR:O13769; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016929; F:deSUMOylase activity; IDA:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:2000765; P:regulation of cytoplasmic translation; EXP:PomBase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..638
FT /note="Ubiquitin-like-specific protease 2"
FT /id="PRO_0000101734"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 440
FT /evidence="ECO:0000250"
FT ACT_SITE 494
FT /evidence="ECO:0000250"
FT ACT_SITE 544
FT /evidence="ECO:0000250"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 638 AA; 71917 MW; 0F83228A45C50020 CRC64;
MRDSKDALDD KSGSFTSLLP PFGKQRGTSP NDAIPIKSPL ERLANSVTSP EKPTVRTAIQ
KDSPRRKQID DDQTPPKHLK RSFQNVTVVS PRKKKTIDVV ELPFTKGGYG GFYDPRPGCL
KFTTHEINVS YTDTSIPVIH IPVQLLKRCC WLQGWRDNLV ESPVHAIHLT LKNRDMKRIT
IGDSASLLFL YNPLHVESAR AGLDLLDQSD FSLTSPSSAK EFKQLLTLKQ STIIPRTPQK
TVRSIVKQTS SPHSSKMPKH SLPSSPTPFN SNSGDSLLSR IKNSNQSSSE RPTANNGAQE
QNQSSSSAGN TSNDFSTLCS QGSDKTLLSD ASCTTILVYP FSGTNSIAIT NTDLTRLNEG
EFLNDTIVDF YLRYLYCKLQ TQNPSLANDT HIFNTFFYNR LTSKDKDGKR LGHRGVRKWT
QKVDLFHKKY IIVPINETFH WYLAIICNID RLMPVDTKLE EQDEIVMSSV EQPSASKTRQ
AELTSNSPAI LIFDSLANLH KGALNYLREY LLEEAFERKN VHLKSTDIRG FHAKVPQQSN
FSDCGIYALH FVELFLETPE QVIANTLDKS LRRTDAKNFD QQWNLQKINT MRCDLKGLIR
RLSTEWSSNN ERQSLSSGSN DEEDKENDDD LAILPITN
