UBP37_HUMAN
ID UBP37_HUMAN Reviewed; 979 AA.
AC Q86T82; A2RUQ8; B7ZM38; B7ZM41; E9PHL3; Q2KHT2; Q53S10; Q7Z3A5; Q9HCH8;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 37;
DE EC=3.4.19.12 {ECO:0000269|PubMed:27296872};
DE AltName: Full=Deubiquitinating enzyme 37;
DE AltName: Full=Ubiquitin thioesterase 37;
DE AltName: Full=Ubiquitin-specific-processing protease 37;
GN Name=USP37; Synonyms=KIAA1594;
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] (ISOFORM 1), AND VARIANT SER-979.
RC TISSUE=Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-979.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-979.
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-979 (ISOFORM 1), AND VARIANT
RP SER-979.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [6]
RP TISSUE SPECIFICITY, AND ENZYME ACTIVITY.
RX PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
RA Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S.,
RA Lopez-Otin C.;
RT "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
RT proteases.";
RL Biochem. Biophys. Res. Commun. 314:54-62(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650 AND SER-652, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, UBIQUITINATION, PHOSPHORYLATION AT SER-628 BY CDK2, DOMAIN KEN
RP BOX 3, DEVELOPMENTAL STAGE, INDUCTION, INTERACTION WITH FZR1, AND
RP MUTAGENESIS OF 32-LYS--ASN-34; 71-ARG-LEU-74; 96-ARG-LEU-99;
RP 160-ARG-LEU-163; 221-LYS--ASN-223; CYS-350; 782-LYS--ASN-784 AND SER-628.
RX PubMed=21596315; DOI=10.1016/j.molcel.2011.03.027;
RA Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G.,
RA Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.;
RT "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and
RT promote S phase entry.";
RL Mol. Cell 42:511-523(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-210 AND SER-770, AND
RP IDENTIFICATION BY 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 CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-350, INTERACTION WITH CDT1, AND
RP FUNCTION.
RX PubMed=27296872; DOI=10.1016/j.molonc.2016.05.008;
RA Hernandez-Perez S., Cabrera E., Amoedo H., Rodriguez-Acebes S.,
RA Koundrioukoff S., Debatisse M., Mendez J., Freire R.;
RT "USP37 deubiquitinates Cdt1 and contributes to regulate DNA replication.";
RL Mol. Oncol. 10:1196-1206(2016).
CC -!- FUNCTION: Deubiquitinase that antagonizes the anaphase-promoting
CC complex (APC/C) during G1/S transition by mediating deubiquitination of
CC cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry.
CC Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin
CC chains, a specific ubiquitin-linkage type mediated by the APC/C
CC complex. Also mediates deubiquitination of 'Lys-48'-linked
CC polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S
CC phase maximizes the deubiquitinase activity, leading to prevent
CC degradation of cyclin-A (CCNA1 and CCNA2) (PubMed:21596315). Plays an
CC important role in the regulation of DNA replication by stabilizing the
CC licensing factor CDT1 (PubMed:27296872). {ECO:0000269|PubMed:21596315,
CC ECO:0000269|PubMed:27296872}.
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:14715245,
CC ECO:0000269|PubMed:27296872};
CC -!- SUBUNIT: Interacts with FZR1/CDH1 (PubMed:21596315). Interacts with
CC CDT1 (PubMed:27296872). {ECO:0000269|PubMed:21596315,
CC ECO:0000269|PubMed:27296872}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86T82-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86T82-2; Sequence=VSP_041740, VSP_041741;
CC -!- TISSUE SPECIFICITY: Expressed in brain and prostate.
CC {ECO:0000269|PubMed:14715245}.
CC -!- DEVELOPMENTAL STAGE: Induced in G1 phase, accumulates at G1/S
CC transition, and degraded in late mitosis following ubiquitination and
CC degradation by the APC(CDH1) complex. {ECO:0000269|PubMed:21596315}.
CC -!- INDUCTION: Induced by E2F transcription factors in G1.
CC {ECO:0000269|PubMed:21596315}.
CC -!- DOMAIN: The KEN box 3 is required for interaction with FZR1/CDH1 and is
CC essential for APC(CDH1)-mediated ubiquitination.
CC {ECO:0000269|PubMed:21596315}.
CC -!- PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the APC(CDH1)
CC complex during late mitosis, leading to its degradation. Able to
CC mediate auto-deubiquitination. {ECO:0000269|PubMed:21596315}.
CC -!- PTM: Phosphorylated at Ser-628 by CDK2 during G1/S phase but not during
CC mitosis; phosphorylation at Ser-628 is required for deubiquitinase
CC activity. Also polyubiquitinated during early G1 phase, without leading
CC to degradation. {ECO:0000269|PubMed:21596315}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY14887.1; Type=Erroneous gene model prediction; 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; AL832645; CAD89955.1; -; mRNA.
DR EMBL; BX538024; CAD97970.1; -; mRNA.
DR EMBL; AC012510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073838; AAY14887.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471063; EAW70621.1; -; Genomic_DNA.
DR EMBL; BC112901; AAI12902.1; -; mRNA.
DR EMBL; BC133007; AAI33008.1; -; mRNA.
DR EMBL; BC133009; AAI33010.1; -; mRNA.
DR EMBL; BC144249; AAI44250.1; -; mRNA.
DR EMBL; BC144252; AAI44253.1; -; mRNA.
DR EMBL; AB046814; BAB13420.1; -; mRNA.
DR CCDS; CCDS2418.1; -. [Q86T82-1]
DR RefSeq; NP_065986.2; NM_020935.2. [Q86T82-1]
DR RefSeq; XP_005246777.1; XM_005246720.2. [Q86T82-1]
DR RefSeq; XP_005246778.1; XM_005246721.3. [Q86T82-1]
DR RefSeq; XP_005246779.1; XM_005246722.3. [Q86T82-1]
DR RefSeq; XP_011509840.1; XM_011511538.2. [Q86T82-1]
DR PDB; 3U12; X-ray; 2.08 A; A/B=4-125.
DR PDBsum; 3U12; -.
DR AlphaFoldDB; Q86T82; -.
DR SMR; Q86T82; -.
DR BioGRID; 121720; 104.
DR IntAct; Q86T82; 5.
DR MINT; Q86T82; -.
DR STRING; 9606.ENSP00000258399; -.
DR MEROPS; C19.053; -.
DR iPTMnet; Q86T82; -.
DR PhosphoSitePlus; Q86T82; -.
DR BioMuta; USP37; -.
DR DMDM; 300669620; -.
DR EPD; Q86T82; -.
DR jPOST; Q86T82; -.
DR MassIVE; Q86T82; -.
DR MaxQB; Q86T82; -.
DR PaxDb; Q86T82; -.
DR PeptideAtlas; Q86T82; -.
DR PRIDE; Q86T82; -.
DR ProteomicsDB; 69667; -. [Q86T82-1]
DR ProteomicsDB; 69668; -. [Q86T82-2]
DR Antibodypedia; 34273; 168 antibodies from 26 providers.
DR DNASU; 57695; -.
DR Ensembl; ENST00000258399.8; ENSP00000258399.3; ENSG00000135913.11. [Q86T82-1]
DR Ensembl; ENST00000415516.5; ENSP00000400902.1; ENSG00000135913.11. [Q86T82-2]
DR Ensembl; ENST00000418019.5; ENSP00000396585.1; ENSG00000135913.11. [Q86T82-1]
DR Ensembl; ENST00000454775.5; ENSP00000393662.1; ENSG00000135913.11. [Q86T82-1]
DR GeneID; 57695; -.
DR KEGG; hsa:57695; -.
DR MANE-Select; ENST00000258399.8; ENSP00000258399.3; NM_020935.3; NP_065986.3.
DR UCSC; uc002vie.3; human. [Q86T82-1]
DR CTD; 57695; -.
DR DisGeNET; 57695; -.
DR GeneCards; USP37; -.
DR HGNC; HGNC:20063; USP37.
DR HPA; ENSG00000135913; Low tissue specificity.
DR neXtProt; NX_Q86T82; -.
DR OpenTargets; ENSG00000135913; -.
DR PharmGKB; PA134928706; -.
DR VEuPathDB; HostDB:ENSG00000135913; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000158091; -.
DR HOGENOM; CLU_012557_0_0_1; -.
DR InParanoid; Q86T82; -.
DR OMA; NRVNISA; -.
DR OrthoDB; 129045at2759; -.
DR PhylomeDB; Q86T82; -.
DR TreeFam; TF323032; -.
DR PathwayCommons; Q86T82; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q86T82; -.
DR SIGNOR; Q86T82; -.
DR BioGRID-ORCS; 57695; 544 hits in 1097 CRISPR screens.
DR ChiTaRS; USP37; human.
DR GeneWiki; USP37; -.
DR GenomeRNAi; 57695; -.
DR Pharos; Q86T82; Tbio.
DR PRO; PR:Q86T82; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q86T82; protein.
DR Bgee; ENSG00000135913; Expressed in secondary oocyte and 194 other tissues.
DR ExpressionAtlas; Q86T82; baseline and differential.
DR Genevisible; Q86T82; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 2.30.29.180; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR032069; USP37-like_PH.
DR InterPro; IPR038093; USP37-like_PH_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 1.
DR Pfam; PF02809; UIM; 3.
DR SMART; SM00726; UIM; 4.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50330; UIM; 3.
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 3D-structure; Alternative splicing; Cell cycle; Cell division; Hydrolase;
KW Mitosis; Phosphoprotein; Protease; Reference proteome; Repeat;
KW Thiol protease; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..979
FT /note="Ubiquitin carboxyl-terminal hydrolase 37"
FT /id="PRO_0000080667"
FT DOMAIN 341..951
FT /note="USP"
FT DOMAIN 704..723
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 806..825
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 828..847
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 110..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..34
FT /note="KEN box 1"
FT MOTIF 71..79
FT /note="D-box 1"
FT MOTIF 96..105
FT /note="D-box 2"
FT MOTIF 160..168
FT /note="D-box 3"
FT MOTIF 221..223
FT /note="KEN box 2"
FT MOTIF 782..784
FT /note="KEN box 3"
FT COMPBIAS 119..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:27296872"
FT ACT_SITE 906
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 628
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000269|PubMed:21596315,
FT ECO:0000269|PubMed:27296872"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041740"
FT VAR_SEQ 612..634
FT /note="ISRPLKASQMVNSCITSPSTPSK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041741"
FT VARIANT 979
FT /note="L -> S (in dbSNP:rs6436058)"
FT /evidence="ECO:0000269|PubMed:10997877,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.3"
FT /id="VAR_059752"
FT MUTAGEN 32..34
FT /note="KEN->AAA: No effect."
FT /evidence="ECO:0000269|PubMed:21596315"
FT MUTAGEN 71..74
FT /note="RLML->ALMA: No effect."
FT /evidence="ECO:0000269|PubMed:21596315"
FT MUTAGEN 96..99
FT /note="RLFL->ALFA: No effect."
FT /evidence="ECO:0000269|PubMed:21596315"
FT MUTAGEN 160..163
FT /note="RKVL->AKVA: No effect."
FT /evidence="ECO:0000269|PubMed:21596315"
FT MUTAGEN 221..223
FT /note="KEN->AAA: No effect."
FT /evidence="ECO:0000269|PubMed:21596315"
FT MUTAGEN 350
FT /note="C->S: Abolishes deubiquitinase activity."
FT /evidence="ECO:0000269|PubMed:21596315"
FT MUTAGEN 628
FT /note="S->A: Abolishes phosphorylation by CDK2, leading to
FT lower deubiquitinase activity."
FT /evidence="ECO:0000269|PubMed:21596315"
FT MUTAGEN 782..784
FT /note="KEN->AAA: Impaired interaction with FZR1/CDH1 and
FT subsequent ubiquitination."
FT /evidence="ECO:0000269|PubMed:21596315"
FT CONFLICT 223..224
FT /note="ND -> DG (in Ref. 1; CAD89955)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="N -> K (in Ref. 1; CAD97970)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="V -> I (in Ref. 1; CAD89955)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="F -> I (in Ref. 4; AAI44250)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="S -> I (in Ref. 4; AAI44253)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="N -> Y (in Ref. 4; AAI44253)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="K -> E (in Ref. 1; CAD97970)"
FT /evidence="ECO:0000305"
FT CONFLICT 905
FT /note="G -> D (in Ref. 1; CAD97970)"
FT /evidence="ECO:0000305"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:3U12"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:3U12"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:3U12"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:3U12"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3U12"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3U12"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:3U12"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:3U12"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:3U12"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:3U12"
SQ SEQUENCE 979 AA; 110170 MW; 9F47F06A744EA449 CRC64;
MSPLKIHGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV
VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLPAA MKPSQGSGSF
GAILGSRTSQ KETSRQLSYS DNQASAKRGS LETKDDIPFR KVLGNPGRGS IKTVAGSGIA
RTIPSLTSTS TPLRSGLLEN RTEKRKRMIS TGSELNEDYP KENDSSSNNK AMTDPSRKYL
TSSREKQLSL KQSEENRTSG LLPLQSSSFY GSRAGSKEHS SGGTNLDRTN VSSQTPSAKR
SLGFLPQPVP LSVKKLRCNQ DYTGWNKPRV PLSSHQQQQL QGFSNLGNTC YMNAILQSLF
SLQSFANDLL KQGIPWKKIP LNALIRRFAH LLVKKDICNS ETKKDLLKKV KNAISATAER
FSGYMQNDAH EFLSQCLDQL KEDMEKLNKT WKTEPVSGEE NSPDISATRA YTCPVITNLE
FEVQHSIICK ACGEIIPKRE QFNDLSIDLP RRKKPLPPRS IQDSLDLFFR AEELEYSCEK
CGGKCALVRH KFNRLPRVLI LHLKRYSFNV ALSLNNKIGQ QVIIPRYLTL SSHCTENTKP
PFTLGWSAHM AISRPLKASQ MVNSCITSPS TPSKKFTFKS KSSLALCLDS DSEDELKRSV
ALSQRLCEML GNEQQQEDLE KDSKLCPIEP DKSELENSGF DRMSEEELLA AVLEISKRDA
SPSLSHEDDD KPTSSPDTGF AEDDIQEMPE NPDTMETEKP KTITELDPAS FTEITKDCDE
NKENKTPEGS QGEVDWLQQY DMEREREEQE LQQALAQSLQ EQEAWEQKED DDLKRATELS
LQEFNNSFVD ALGSDEDSGN EDVFDMEYTE AEAEELKRNA ETGNLPHSYR LISVVSHIGS
TSSSGHYISD VYDIKKQAWF TYNDLEVSKI QEAAVQSDRD RSGYIFFYMH KEIFDELLET
EKNSQSLSTE VGKTTRQAL
