UBP47_HUMAN
ID UBP47_HUMAN Reviewed; 1375 AA.
AC Q96K76; B3KXF5; E9PM46; Q658U0; Q86Y73; Q8TEP6; Q9BWI0; Q9NWN1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 47;
DE AltName: Full=Ubiquitin thioesterase 47;
DE AltName: Full=Ubiquitin-specific-processing protease 47;
GN Name=USP47;
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] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-163.
RC TISSUE=Embryo, Hepatoma, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 940-1375 (ISOFORMS 1/2), AND VARIANT
RP VAL-163.
RC TISSUE=Eye, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-1375 (ISOFORMS 1/2).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 630-1375 (ISOFORMS 1/2).
RC TISSUE=Stomach;
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 [6]
RP TISSUE SPECIFICITY.
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-832, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 AND SER-910, VARIANT
RP [LARGE SCALE ANALYSIS] VAL-163, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, VARIANT [LARGE SCALE
RP ANALYSIS] VAL-163, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP FUNCTION, AND INTERACTION WITH BTRC AND FBXW11.
RX PubMed=19966869; DOI=10.1038/onc.2009.430;
RA Peschiaroli A., Skaar J.R., Pagano M., Melino G.;
RT "The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor
RT regulating cell survival.";
RL Oncogene 29:1384-1393(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 AND SER-910, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP POLB.
RX PubMed=21362556; DOI=10.1016/j.molcel.2011.02.016;
RA Parsons J.L., Dianova I.I., Khoronenkova S.V., Edelmann M.J., Kessler B.M.,
RA Dianov G.L.;
RT "USP47 is a deubiquitylating enzyme that regulates base excision repair by
RT controlling steady-state levels of DNA Polymerase beta.";
RL Mol. Cell 41:609-615(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832; SER-910 AND SER-933, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1013; THR-1015 AND SER-1017,
RP AND 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).
CC -!- FUNCTION: Ubiquitin-specific protease that specifically deubiquitinates
CC monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby
CC playing a role in base-excision repair (BER). Acts as a regulator of
CC cell growth and genome integrity. May also indirectly regulate CDC25A
CC expression at a transcriptional level. {ECO:0000269|PubMed:19966869,
CC ECO:0000269|PubMed:21362556}.
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:21362556};
CC -!- SUBUNIT: Interacts with BTRC and FBXW11. Interacts with POLB.
CC {ECO:0000269|PubMed:19966869, ECO:0000269|PubMed:21362556}.
CC -!- INTERACTION:
CC Q96K76; O00189: AP4M1; NbExp=3; IntAct=EBI-2514143, EBI-3914106;
CC Q96K76-3; O00189: AP4M1; NbExp=3; IntAct=EBI-12313025, EBI-3914106;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21362556}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96K76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96K76-2; Sequence=VSP_014415;
CC Name=3;
CC IsoId=Q96K76-3; Sequence=VSP_014414;
CC Name=4;
CC IsoId=Q96K76-4; Sequence=VSP_055650;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart and testis.
CC {ECO:0000269|PubMed:14715245}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to catalytically inactive
CC (PubMed:14715245). However, it was later shown that it is active
CC (PubMed:21362556). {ECO:0000305|PubMed:14715245,
CC ECO:0000305|PubMed:21362556}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91348.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BC071559; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK000734; BAA91348.1; ALT_INIT; mRNA.
DR EMBL; AK027362; BAB55063.1; -; mRNA.
DR EMBL; AK092290; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK127264; BAG54467.1; -; mRNA.
DR EMBL; AC104383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000226; AAH00226.2; -; mRNA.
DR EMBL; BC047044; AAH47044.2; -; mRNA.
DR EMBL; BC071559; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK074076; BAB84902.1; -; mRNA.
DR EMBL; AL832991; CAH56337.1; -; mRNA.
DR CCDS; CCDS41619.1; -. [Q96K76-2]
DR CCDS; CCDS60725.1; -. [Q96K76-4]
DR CCDS; CCDS81554.1; -. [Q96K76-1]
DR RefSeq; NP_001269588.1; NM_001282659.1. [Q96K76-4]
DR RefSeq; NP_001317137.1; NM_001330208.1. [Q96K76-1]
DR RefSeq; NP_060414.3; NM_017944.3. [Q96K76-2]
DR AlphaFoldDB; Q96K76; -.
DR SMR; Q96K76; -.
DR BioGRID; 120360; 141.
DR DIP; DIP-53629N; -.
DR IntAct; Q96K76; 76.
DR MINT; Q96K76; -.
DR STRING; 9606.ENSP00000433146; -.
DR BindingDB; Q96K76; -.
DR ChEMBL; CHEMBL2157851; -.
DR MEROPS; C19.055; -.
DR CarbonylDB; Q96K76; -.
DR GlyGen; Q96K76; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q96K76; -.
DR MetOSite; Q96K76; -.
DR PhosphoSitePlus; Q96K76; -.
DR BioMuta; USP47; -.
DR DMDM; 313104266; -.
DR EPD; Q96K76; -.
DR jPOST; Q96K76; -.
DR MassIVE; Q96K76; -.
DR MaxQB; Q96K76; -.
DR PaxDb; Q96K76; -.
DR PeptideAtlas; Q96K76; -.
DR PRIDE; Q96K76; -.
DR ProteomicsDB; 21996; -.
DR ProteomicsDB; 77047; -. [Q96K76-1]
DR ProteomicsDB; 77048; -. [Q96K76-2]
DR ProteomicsDB; 77049; -. [Q96K76-3]
DR Antibodypedia; 24483; 159 antibodies from 26 providers.
DR DNASU; 55031; -.
DR Ensembl; ENST00000339865.9; ENSP00000339957.5; ENSG00000170242.19. [Q96K76-2]
DR Ensembl; ENST00000399455.2; ENSP00000382382.2; ENSG00000170242.19. [Q96K76-1]
DR Ensembl; ENST00000527733.7; ENSP00000433146.2; ENSG00000170242.19. [Q96K76-4]
DR GeneID; 55031; -.
DR KEGG; hsa:55031; -.
DR MANE-Select; ENST00000527733.7; ENSP00000433146.2; NM_001282659.2; NP_001269588.1. [Q96K76-4]
DR UCSC; uc001mjr.4; human. [Q96K76-1]
DR CTD; 55031; -.
DR DisGeNET; 55031; -.
DR GeneCards; USP47; -.
DR HGNC; HGNC:20076; USP47.
DR HPA; ENSG00000170242; Low tissue specificity.
DR MIM; 614460; gene.
DR neXtProt; NX_Q96K76; -.
DR OpenTargets; ENSG00000170242; -.
DR PharmGKB; PA134880952; -.
DR VEuPathDB; HostDB:ENSG00000170242; -.
DR eggNOG; KOG4598; Eukaryota.
DR GeneTree; ENSGT00940000157223; -.
DR HOGENOM; CLU_002928_0_0_1; -.
DR InParanoid; Q96K76; -.
DR OMA; FLCEWIV; -.
DR OrthoDB; 77113at2759; -.
DR PhylomeDB; Q96K76; -.
DR TreeFam; TF314142; -.
DR PathwayCommons; Q96K76; -.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q96K76; -.
DR BioGRID-ORCS; 55031; 16 hits in 1123 CRISPR screens.
DR ChiTaRS; USP47; human.
DR GeneWiki; USP47; -.
DR GenomeRNAi; 55031; -.
DR Pharos; Q96K76; Tchem.
DR PRO; PR:Q96K76; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96K76; protein.
DR Bgee; ENSG00000170242; Expressed in tendon of biceps brachii and 210 other tissues.
DR Genevisible; Q96K76; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0101005; F:deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0071987; F:WD40-repeat domain binding; IPI:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
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; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR045578; USP47_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF19718; USP47_C; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 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 Acetylation; Alternative splicing; Cytoplasm; DNA damage; DNA repair;
KW Hydrolase; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1375
FT /note="Ubiquitin carboxyl-terminal hydrolase 47"
FT /id="PRO_0000080676"
FT DOMAIN 188..564
FT /note="USP"
FT REGION 425..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 503
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1015
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..1218
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014414"
FT VAR_SEQ 14..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014415"
FT VAR_SEQ 14..33
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055650"
FT VARIANT 163
FT /note="G -> V (in dbSNP:rs11022079)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT /id="VAR_022787"
FT CONFLICT 340
FT /note="F -> L (in Ref. 1; BAG54467)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="V -> A (in Ref. 1; BAB55063/BAG54467 and 3;
FT BC071559)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="N -> D (in Ref. 1; BAB55063)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="D -> G (in Ref. 1; BAB55063)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="R -> G (in Ref. 4; BAB84902)"
FT /evidence="ECO:0000305"
FT CONFLICT 911
FT /note="P -> S (in Ref. 1; BAG54467)"
FT /evidence="ECO:0000305"
FT CONFLICT 1157
FT /note="E -> G (in Ref. 1; BAA91348)"
FT /evidence="ECO:0000305"
FT CONFLICT 1313
FT /note="A -> G (in Ref. 1; BAA91348)"
FT /evidence="ECO:0000305"
FT CONFLICT 1368
FT /note="P -> Q (in Ref. 3; BC071559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1375 AA; 157311 MW; 1EDEAA9B5AFC97FE CRC64;
MVPGEENQLV PKEDVFWRCR QNIFDEMKKK FLQIENAAEE PRVLCIIQDT TNSKTVNERI
TLNLPASTPV RKLFEDVANK VGYINGTFDL VWGNGINTAD MAPLDHTSDK SLLDANFEPG
KKNFLHLTDK DGEQPQILLE DSSAGEDSVH DRFIGPLPRE GSGGSTSDYV SQSYSYSSIL
NKSETGYVGL VNQAMTCYLN SLLQTLFMTP EFRNALYKWE FEESEEDPVT SIPYQLQRLF
VLLQTSKKRA IETTDVTRSF GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL
YQGKLKDYVR CLECGYEGWR IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN
QYFCERCKKK CDARKGLRFL HFPYLLTLQL KRFDFDYTTM HRIKLNDRMT FPEELDMSTF
IDVEDEKSPQ TESCTDSGAE NEGSCHSDQM SNDFSNDDGV DEGICLETNS GTEKISKSGL
EKNSLIYELF SVMVHSGSAA GGHYYACIKS FSDEQWYSFN DQHVSRITQE DIKKTHGGSS
GSRGYYSSAF ASSTNAYMLI YRLKDPARNA KFLEVDEYPE HIKNLVQKER ELEEQEKRQR
EIERNTCKIK LFCLHPTKQV MMENKLEVHK DKTLKEAVEM AYKMMDLEEV IPLDCCRLVK
YDEFHDYLER SYEGEEDTPM GLLLGGVKST YMFDLLLETR KPDQVFQSYK PGEVMVKVHV
VDLKAESVAA PITVRAYLNQ TVTEFKQLIS KAIHLPAETM RIVLERCYND LRLLSVSSKT
LKAEGFFRSN KVFVESSETL DYQMAFADSH LWKLLDRHAN TIRLFVLLPE QSPVSYSKRT
AYQKAGGDSG NVDDDCERVK GPVGSLKSVE AILEESTEKL KSLSLQQQQD GDNGDSSKST
ETSDFENIES PLNERDSSAS VDNRELEQHI QTSDPENFQS EERSDSDVNN DRSTSSVDSD
ILSSSHSSDT LCNADNAQIP LANGLDSHSI TSSRRTKANE GKKETWDTAE EDSGTDSEYD
ESGKSRGEMQ YMYFKAEPYA ADEGSGEGHK WLMVHVDKRI TLAAFKQHLE PFVGVLSSHF
KVFRVYASNQ EFESVRLNET LSSFSDDNKI TIRLGRALKK GEYRVKVYQL LVNEQEPCKF
LLDAVFAKGM TVRQSKEELI PQLREQCGLE LSIDRFRLRK KTWKNPGTVF LDYHIYEEDI
NISSNWEVFL EVLDGVEKMK SMSQLAVLSR RWKPSEMKLD PFQEVVLESS SVDELREKLS
EISGIPLDDI EFAKGRGTFP CDISVLDIHQ DLDWNPKVST LNVWPLYICD DGAVIFYRDK
TEELMELTDE QRNELMKKES SRLQKTGHRV TYSPRKEKAL KIYLDGAPNK DLTQD
