ID   JOS1_HUMAN              Reviewed;         202 AA.
AC   Q15040; A8K712;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 170.
DE   RecName: Full=Josephin-1;
DE            EC=3.4.19.12;
DE   AltName: Full=Josephin domain-containing protein 1;
GN   Name=JOSD1; Synonyms=JSPH1, KIAA0063;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA   Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA   Kawarabayasi Y., Ishikawa K., Tabata S.;
RT   "Prediction of the coding sequences of unidentified human genes. II. The
RT   coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 1:223-229(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   CATALYTIC ACTIVITY.
RX   PubMed=17696782; DOI=10.1515/bc.2007.107;
RA   Tzvetkov N., Breuer P.;
RT   "Josephin domain-containing proteins from a variety of species are active
RT   de-ubiquitination enzymes.";
RL   Biol. Chem. 388:973-978(2007).
RN   [8]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=21118805; DOI=10.1074/jbc.m110.177360;
RA   Weeks S.D., Grasty K.C., Hernandez-Cuebas L., Loll P.J.;
RT   "Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints
RT   on ataxin-3 deubiquitinating activity.";
RL   J. Biol. Chem. 286:4555-4565(2011).
RN   [9]
RP   FUNCTION, INTERACTION WITH ACTB, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   CYS-36.
RX   PubMed=23625928; DOI=10.1074/jbc.m113.463406;
RA   Seki T., Gong L., Williams A.J., Sakai N., Todi S.V., Paulson H.L.;
RT   "JosD1, a membrane-targeted deubiquitinating enzyme, is activated by
RT   ubiquitination and regulates membrane dynamics, cell motility, and
RT   endocytosis.";
RL   J. Biol. Chem. 288:17145-17155(2013).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   3D-STRUCTURE MODELING.
RX   PubMed=12486728; DOI=10.1002/prot.10280;
RA   Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T.;
RT   "Structural modeling of ataxin-3 reveals distant homology to adaptins.";
RL   Proteins 50:355-370(2003).
CC   -!- FUNCTION: Deubiquitinates monoubiquitinated probes (in vitro). When
CC       ubiquitinated, cleaves 'Lys-63'-linked and 'Lys-48'-linked poly-
CC       ubiquitin chains (in vitro), hence may act as a deubiquitinating
CC       enzyme. May increase macropinocytosis and suppress clathrin- and
CC       caveolae-mediated endocytosis. May enhance membrane dynamics and cell
CC       motility independently of its catalytic activity.
CC       {ECO:0000269|PubMed:21118805, ECO:0000269|PubMed:23625928}.
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; Evidence={ECO:0000269|PubMed:17696782,
CC         ECO:0000269|PubMed:21118805};
CC   -!- SUBUNIT: Interacts with beta-actin/ACTB. {ECO:0000269|PubMed:23625928}.
CC   -!- INTERACTION:
CC       Q15040; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-2510602, EBI-10173507;
CC       Q15040; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-2510602, EBI-3866279;
CC       Q15040; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2510602, EBI-3867333;
CC       Q15040; P98095: FBLN2; NbExp=3; IntAct=EBI-2510602, EBI-947973;
CC       Q15040; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2510602, EBI-3044087;
CC       Q15040; Q15323: KRT31; NbExp=3; IntAct=EBI-2510602, EBI-948001;
CC       Q15040; O76011: KRT34; NbExp=3; IntAct=EBI-2510602, EBI-1047093;
CC       Q15040; Q6A162: KRT40; NbExp=6; IntAct=EBI-2510602, EBI-10171697;
CC       Q15040; O43790: KRT86; NbExp=3; IntAct=EBI-2510602, EBI-9996498;
CC       Q15040; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-2510602, EBI-11959885;
CC       Q15040; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-2510602, EBI-11749135;
CC       Q15040; P60372: KRTAP10-4; NbExp=3; IntAct=EBI-2510602, EBI-10178153;
CC       Q15040; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-2510602, EBI-10171774;
CC       Q15040; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-2510602, EBI-11953334;
CC       Q15040; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-2510602, EBI-14065470;
CC       Q15040; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-2510602, EBI-3958099;
CC       Q15040; Q9BYQ4: KRTAP9-2; NbExp=6; IntAct=EBI-2510602, EBI-1044640;
CC       Q15040; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-2510602, EBI-1043191;
CC       Q15040; Q99750: MDFI; NbExp=3; IntAct=EBI-2510602, EBI-724076;
CC       Q15040; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-2510602, EBI-10172526;
CC       Q15040; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2510602, EBI-11522433;
CC       Q15040; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-2510602, EBI-945833;
CC       Q15040; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2510602, EBI-22310682;
CC       Q15040; P22735: TGM1; NbExp=3; IntAct=EBI-2510602, EBI-2562368;
CC       Q15040; Q13077: TRAF1; NbExp=3; IntAct=EBI-2510602, EBI-359224;
CC       Q15040; P36406: TRIM23; NbExp=3; IntAct=EBI-2510602, EBI-740098;
CC       Q15040; P14373: TRIM27; NbExp=4; IntAct=EBI-2510602, EBI-719493;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23625928}.
CC       Cytoplasm {ECO:0000269|PubMed:23625928}. Note=Ubiquitination increases
CC       localization the plasma membrane. In the cytosol, the unubiquitinated
CC       form may be associated with the cytoskeleton via ACTB-binding.
CC   -!- PTM: Monoubiquitinated (By similarity). Ubiquitination activates
CC       deubiquitination activity in vitro. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA06682.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; D31884; BAA06682.2; ALT_INIT; mRNA.
DR   EMBL; CR456473; CAG30359.1; -; mRNA.
DR   EMBL; AK291827; BAF84516.1; -; mRNA.
DR   EMBL; AL021707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471095; EAW60259.1; -; Genomic_DNA.
DR   EMBL; BC015026; AAH15026.1; -; mRNA.
DR   CCDS; CCDS13976.1; -.
DR   RefSeq; NP_055691.1; NM_014876.5.
DR   RefSeq; XP_005261933.1; XM_005261876.2.
DR   RefSeq; XP_005261934.1; XM_005261877.2.
DR   RefSeq; XP_005261935.1; XM_005261878.2.
DR   RefSeq; XP_005261936.1; XM_005261879.2.
DR   AlphaFoldDB; Q15040; -.
DR   SMR; Q15040; -.
DR   BioGRID; 115257; 55.
DR   IntAct; Q15040; 30.
DR   MINT; Q15040; -.
DR   STRING; 9606.ENSP00000216039; -.
DR   BindingDB; Q15040; -.
DR   ChEMBL; CHEMBL4630825; -.
DR   MEROPS; C86.004; -.
DR   iPTMnet; Q15040; -.
DR   PhosphoSitePlus; Q15040; -.
DR   BioMuta; JOSD1; -.
DR   DMDM; 3123051; -.
DR   EPD; Q15040; -.
DR   jPOST; Q15040; -.
DR   MassIVE; Q15040; -.
DR   MaxQB; Q15040; -.
DR   PaxDb; 9606-ENSP00000216039; -.
DR   PeptideAtlas; Q15040; -.
DR   ProteomicsDB; 60388; -.
DR   Pumba; Q15040; -.
DR   Antibodypedia; 202; 122 antibodies from 16 providers.
DR   DNASU; 9929; -.
DR   Ensembl; ENST00000216039.9; ENSP00000216039.5; ENSG00000100221.11.
DR   Ensembl; ENST00000683374.1; ENSP00000506752.1; ENSG00000100221.11.
DR   GeneID; 9929; -.
DR   KEGG; hsa:9929; -.
DR   MANE-Select; ENST00000683374.1; ENSP00000506752.1; NM_001360236.2; NP_001347165.1.
DR   UCSC; uc003awf.4; human.
DR   AGR; HGNC:28953; -.
DR   CTD; 9929; -.
DR   DisGeNET; 9929; -.
DR   GeneCards; JOSD1; -.
DR   HGNC; HGNC:28953; JOSD1.
DR   HPA; ENSG00000100221; Low tissue specificity.
DR   MIM; 615323; gene.
DR   neXtProt; NX_Q15040; -.
DR   OpenTargets; ENSG00000100221; -.
DR   PharmGKB; PA142671644; -.
DR   VEuPathDB; HostDB:ENSG00000100221; -.
DR   eggNOG; KOG2934; Eukaryota.
DR   GeneTree; ENSGT00390000009228; -.
DR   HOGENOM; CLU_103892_0_0_1; -.
DR   InParanoid; Q15040; -.
DR   OMA; MSCMPWK; -.
DR   OrthoDB; 239839at2759; -.
DR   PhylomeDB; Q15040; -.
DR   TreeFam; TF313660; -.
DR   PathwayCommons; Q15040; -.
DR   Reactome; R-HSA-5689877; Josephin domain DUBs.
DR   SignaLink; Q15040; -.
DR   BioGRID-ORCS; 9929; 20 hits in 1197 CRISPR screens.
DR   ChiTaRS; JOSD1; human.
DR   GenomeRNAi; 9929; -.
DR   Pharos; Q15040; Tbio.
DR   PRO; PR:Q15040; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q15040; Protein.
DR   Bgee; ENSG00000100221; Expressed in mucosa of sigmoid colon and 212 other cell types or tissues.
DR   ExpressionAtlas; Q15040; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.40; -; 1.
DR   InterPro; IPR040053; JOSD1/2.
DR   InterPro; IPR006155; Josephin.
DR   PANTHER; PTHR13291; JOSEPHIN 1, 2; 1.
DR   PANTHER; PTHR13291:SF1; JOSEPHIN-1; 1.
DR   Pfam; PF02099; Josephin; 1.
DR   SMART; SM01246; Josephin; 1.
DR   PROSITE; PS50957; JOSEPHIN; 1.
DR   Genevisible; Q15040; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Hydrolase; Membrane; Phosphoprotein; Protease;
KW   Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..202
FT                   /note="Josephin-1"
FT                   /id="PRO_0000053839"
FT   DOMAIN          23..202
FT                   /note="Josephin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   ACT_SITE        36
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00331"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         48
FT                   /note="S -> R (in dbSNP:rs6001200)"
FT                   /id="VAR_050031"
FT   MUTAGEN         36
FT                   /note="C->A: Loss of deubiquitination activity, no change
FT                   in subcellular location."
FT                   /evidence="ECO:0000269|PubMed:23625928"
SQ   SEQUENCE   202 AA;  23198 MW;  837268C393C0A5A9 CRC64;
     MSCVPWKGDK AKSESLELPQ AAPPQIYHEK QRRELCALHA LNNVFQDSNA FTRDTLQEIF
     QRLSPNTMVT PHKKSMLGNG NYDVNVIMAA LQTKGYEAVW WDKRRDVGVI ALTNVMGFIM
     NLPSSLCWGP LKLPLKRQHW ICVREVGGAY YNLDSKLKMP EWIGGESELR KFLKHHLRGK
     NCELLLVVPE EVEAHQSWRT DV
//