LOCUS       NP_001269588            1355 aa            linear   PRI 29-APR-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 47 isoform a [Homo sapiens].
ACCESSION   NP_001269588 XP_005253055
VERSION     NP_001269588.1
DBSOURCE    REFSEQ: accession NM_001282659.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1355)
  AUTHORS   Lei,H., Xu,H., Yang,L., Wang,Y., Zhang,Y. and Wu,Y.
  TITLE     USP47 stabilizes YBX1 to promote the progression of acute myeloid
            leukemia
  JOURNAL   Oncogene 43 (7), 539-542 (2024)
   PUBMED   38104157
  REMARK    GeneRIF: USP47 stabilizes YBX1 to promote the progression of acute
            myeloid leukemia.
REFERENCE   2  (residues 1 to 1355)
  AUTHORS   Wang,A., Huang,H., Shi,J.H., Yu,X., Ding,R., Zhang,Y., Han,Q.,
            Ni,Z.Y., Li,X., Zhao,R. and Zou,Q.
  TITLE     USP47 inhibits m6A-dependent c-Myc translation to maintain
            regulatory T cell metabolic and functional homeostasis
  JOURNAL   J Clin Invest 133 (23), e169365 (2023)
   PUBMED   37788092
  REMARK    GeneRIF: USP47 inhibits m6A-dependent c-Myc translation to maintain
            regulatory T cell metabolic and functional homeostasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1355)
  AUTHORS   Shin,S.C., Park,J., Kim,K.H., Yoon,J.M., Cho,J., Ha,B.H., Oh,Y.,
            Choo,H., Song,E.J. and Kim,E.E.
  TITLE     Structural and functional characterization of USP47 reveals a hot
            spot for inhibitor design
  JOURNAL   Commun Biol 6 (1), 970 (2023)
   PUBMED   37740002
  REMARK    GeneRIF: Structural and functional characterization of USP47
            reveals a hot spot for inhibitor design.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1355)
  AUTHORS   Chen,H.Y., Tang,R.C., Liang,J.W., Zhao,W., Yu,S.S., Yao,R.R.,
            Xu,R., Zhang,A., Geng,S., Sun,X.Y., Ge,Q. and Zhang,J.
  TITLE     Deubiquitinase USP47 attenuates virus-induced type I interferon
            signaling
  JOURNAL   Int Immunopharmacol 118, 110040 (2023)
   PUBMED   37001379
  REMARK    GeneRIF: Deubiquitinase USP47 attenuates virus-induced type I
            interferon signaling.
REFERENCE   5  (residues 1 to 1355)
  AUTHORS   Kassel,S., Hanson,A.J., Benchabane,H., Saito-Diaz,K., Cabel,C.R.,
            Goldsmith,L., Taha,M., Kanuganti,A., Ng,V.H., Xu,G., Ye,F.,
            Picker,J., Port,F., Boutros,M., Weiss,V.L., Robbins,D.J.,
            Thorne,C.A., Ahmed,Y. and Lee,E.
  TITLE     USP47 deubiquitylates Groucho/TLE to promote Wnt-beta-catenin
            signaling
  JOURNAL   Sci Signal 16 (771), eabn8372 (2023)
   PUBMED   36749823
  REMARK    GeneRIF: USP47 deubiquitylates Groucho/TLE to promote
            Wnt-beta-catenin signaling.
REFERENCE   6  (residues 1 to 1355)
  AUTHORS   Yang,S.W., Oh,K.H., Park,E., Chang,H.M., Park,J.M., Seong,M.W.,
            Ka,S.H., Song,W.K., Park,D.E., Baas,P.W., Jeon,Y.J. and Chung,C.H.
  TITLE     USP47 and C terminus of Hsp70-interacting protein (CHIP)
            antagonistically regulate katanin-p60-mediated axonal growth
  JOURNAL   J Neurosci 33 (31), 12728-12738 (2013)
   PUBMED   23904609
  REMARK    GeneRIF: The results of this study indicated that USP47 plays a
            crucial role in the control of axonal growth during neuronal
            development by antagonizing CHIP-mediated katanin-p60 degradation.
REFERENCE   7  (residues 1 to 1355)
  AUTHORS   Parsons,J.L., Dianova,I.I., Khoronenkova,S.V., Edelmann,M.J.,
            Kessler,B.M. and Dianov,G.L.
  TITLE     USP47 is a deubiquitylating enzyme that regulates base excision
            repair by controlling steady-state levels of DNA polymerase beta
  JOURNAL   Mol Cell 41 (5), 609-615 (2011)
   PUBMED   21362556
  REMARK    GeneRIF: USP47 has a role in regulating DNA repair and maintaining
            genome integrity
REFERENCE   8  (residues 1 to 1355)
  AUTHORS   Peschiaroli,A., Skaar,J.R., Pagano,M. and Melino,G.
  TITLE     The ubiquitin-specific protease USP47 is a novel beta-TRCP
            interactor regulating cell survival
  JOURNAL   Oncogene 29 (9), 1384-1393 (2010)
   PUBMED   19966869
  REMARK    GeneRIF: USP47, a novel beta-Trcp interactor, regulates cell growth
            and survival, potentially providing a novel target for anticancer
            therapies.
REFERENCE   9  (residues 1 to 1355)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   10 (residues 1 to 1355)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104383.4 and AC124276.5.
            
            On Sep 17, 2013 this sequence version replaced XP_005253055.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.34955.1, BC071559.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000527733.7/ ENSP00000433146.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.3"
     Protein         1..1355
                     /product="ubiquitin carboxyl-terminal hydrolase 47 isoform
                     a"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 47; ubiquitin
                     thioesterase 47; deubiquitinating enzyme 47;
                     ubiquitin-specific-processing protease 47; ubiquitin
                     thiolesterase 47; Trf (TATA binding protein-related
                     factor)-proximal homolog"
                     /calculated_mol_wt=154567
     Site            102
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96K76.3)"
     Region          166..546
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(172,177,483,501)
                     /site_type="active"
                     /db_xref="CDD:239124"
     Region          405..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K76.3)"
     Site            812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96K76.3)"
     Region          <814..>1005
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          820..839
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K76.3)"
     Region          860..948
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K76.3)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96K76.3)"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96K76.3)"
     Region          963..1004
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K76.3)"
     Site            993
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96K76.3)"
     Site            995
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96K76.3)"
     Site            997
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96K76.3)"
     Region          1104..1343
                     /region_name="USP47_C"
                     /note="Ubiquitin carboxyl-terminal hydrolase 47
                     C-terminal; pfam19718"
                     /db_xref="CDD:466158"
     CDS             1..1355
                     /gene="USP47"
                     /gene_synonym="TRFP"
                     /coded_by="NM_001282659.2:215..4282"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS60725.1"
                     /db_xref="GeneID:55031"
                     /db_xref="HGNC:HGNC:20076"
                     /db_xref="MIM:614460"
ORIGIN      
        1 mvpgeenqlv pkeienaaee prvlciiqdt tnsktvneri tlnlpastpv rklfedvank
       61 vgyingtfdl vwgngintad mapldhtsdk slldanfepg kknflhltdk dgeqpqille
      121 dssagedsvh drfigplpre gsggstsdyv sqsysyssil nksetgyvgl vnqamtcyln
      181 sllqtlfmtp efrnalykwe feeseedpvt sipyqlqrlf vllqtskkra iettdvtrsf
      241 gwdsseawqq hdvqelcrvm fdaleqkwkq teqadlinel yqgklkdyvr clecgyegwr
      301 idtyldiplv irpygssqaf asveealhaf iqpeildgpn qyfcerckkk cdarkglrfl
      361 hfpylltlql krfdfdyttm hriklndrmt fpeeldmstf idvedekspq tesctdsgae
      421 negschsdqm sndfsnddgv degicletns gtekisksgl eknsliyelf svmvhsgsaa
      481 gghyyaciks fsdeqwysfn dqhvsritqe dikkthggss gsrgyyssaf asstnaymli
      541 yrlkdparna kflevdeype hiknlvqker eleeqekrqr eierntckik lfclhptkqv
      601 mmenklevhk dktlkeavem aykmmdleev ipldccrlvk ydefhdyler syegeedtpm
      661 glllggvkst ymfdllletr kpdqvfqsyk pgevmvkvhv vdlkaesvaa pitvraylnq
      721 tvtefkqlis kaihlpaetm rivlercynd lrllsvsskt lkaegffrsn kvfvessetl
      781 dyqmafadsh lwklldrhan tirlfvllpe qspvsyskrt ayqkaggdsg nvdddcervk
      841 gpvgslksve aileestekl kslslqqqqd gdngdsskst etsdfenies plnerdssas
      901 vdnreleqhi qtsdpenfqs eersdsdvnn drstssvdsd ilssshssdt lcnadnaqip
      961 langldshsi tssrrtkane gkketwdtae edsgtdseyd esgksrgemq ymyfkaepya
     1021 adegsgeghk wlmvhvdkri tlaafkqhle pfvgvlsshf kvfrvyasnq efesvrlnet
     1081 lssfsddnki tirlgralkk geyrvkvyql lvneqepckf lldavfakgm tvrqskeeli
     1141 pqlreqcgle lsidrfrlrk ktwknpgtvf ldyhiyeedi nissnwevfl evldgvekmk
     1201 smsqlavlsr rwkpsemkld pfqevvless svdelrekls eisgiplddi efakgrgtfp
     1261 cdisvldihq dldwnpkvst lnvwplyicd dgavifyrdk teelmeltde qrnelmkkes
     1321 srlqktghrv tysprkekal kiyldgapnk dltqd
//
