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   24-JAN-2024, entry version 184.
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; 179.
DR   DIP; DIP-53629N; -.
DR   IntAct; Q96K76; 79.
DR   MINT; Q96K76; -.
DR   STRING; 9606.ENSP00000382382; -.
DR   BindingDB; Q96K76; -.
DR   ChEMBL; CHEMBL2157851; -.
DR   MEROPS; C19.055; -.
DR   CarbonylDB; Q96K76; -.
DR   GlyCosmos; Q96K76; 2 sites, 1 glycan.
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; 9606-ENSP00000433146; -.
DR   PeptideAtlas; Q96K76; -.
DR   ProteomicsDB; 21996; -.
DR   ProteomicsDB; 77047; -. [Q96K76-1]
DR   ProteomicsDB; 77048; -. [Q96K76-2]
DR   ProteomicsDB; 77049; -. [Q96K76-3]
DR   Pumba; Q96K76; -.
DR   Antibodypedia; 24483; 173 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   AGR; HGNC:20076; -.
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; 51419at2759; -.
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 1201 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 212 other cell types or tissues.
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; IDA:FlyBase.
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: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:0034644; P:cellular response to UV; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IMP: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:0045892; P:negative regulation of DNA-templated transcription; 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: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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:UniProtKB.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF702; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 47; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF19718; USP47_C; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q96K76; HS.
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
//