ID UBP47_MOUSE Reviewed; 1376 AA. AC Q8BY87; Q32NY0; Q5EBP2; Q6KAR9; Q80V06; Q8BHU1; Q8BI15; Q8BI16; Q8BUW4; AC Q91X25; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 24-JAN-2024, entry version 165. 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 Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-379 (ISOFORM 1), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-591 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 637-1376 (ISOFORMS 1/2). RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1376. RC TISSUE=Brain; RX PubMed=15449545; DOI=10.1093/dnares/11.2.127; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified RT by screening of terminal sequences of cDNA clones randomly sampled from RT size-fractionated libraries."; RL DNA Res. 11:127-135(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C3H/He, and Czech II; RC TISSUE=Brain, Liver, Mammary gland, and Mesenchymal stem cell; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1016, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; SER-934; SER-1014 AND RP THR-1016, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP FUNCTION. 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). 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) (By similarity). Acts as a CC regulator of cell growth and genome integrity. May also indirectly CC regulate CDC25A expression at a transcriptional level. {ECO:0000250, CC ECO:0000269|PubMed:19966869}. 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; CC -!- SUBUNIT: Interacts with BTRC and FBXW11. Interacts with POLB (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8BY87-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8BY87-2; Sequence=VSP_014416; CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP47 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC27179.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC27195.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC38411.1; Type=Frameshift; 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; AK030909; BAC27179.1; ALT_INIT; mRNA. DR EMBL; AK030963; BAC27195.1; ALT_INIT; mRNA. DR EMBL; AK041541; BAC30979.1; -; mRNA. DR EMBL; AK082114; BAC38411.1; ALT_FRAME; mRNA. DR EMBL; AK087981; BAC40073.1; -; mRNA. DR EMBL; AK131138; BAD21388.1; -; mRNA. DR EMBL; BC012722; AAH12722.1; -; mRNA. DR EMBL; BC024117; AAH24117.1; -; mRNA. DR EMBL; BC089364; AAH89364.1; -; mRNA. DR EMBL; BC108425; AAI08426.1; -; mRNA. DR CCDS; CCDS40089.1; -. [Q8BY87-2] DR CCDS; CCDS85384.1; -. [Q8BY87-1] DR RefSeq; NP_598519.2; NM_133758.3. [Q8BY87-2] DR RefSeq; NP_796223.2; NM_177249.3. [Q8BY87-1] DR AlphaFoldDB; Q8BY87; -. DR SMR; Q8BY87; -. DR BioGRID; 217138; 6. DR IntAct; Q8BY87; 1. DR MINT; Q8BY87; -. DR STRING; 10090.ENSMUSP00000147619; -. DR MEROPS; C19.055; -. DR iPTMnet; Q8BY87; -. DR PhosphoSitePlus; Q8BY87; -. DR EPD; Q8BY87; -. DR jPOST; Q8BY87; -. DR MaxQB; Q8BY87; -. DR PaxDb; 10090-ENSMUSP00000102264; -. DR PeptideAtlas; Q8BY87; -. DR ProteomicsDB; 298364; -. [Q8BY87-1] DR ProteomicsDB; 298365; -. [Q8BY87-2] DR Pumba; Q8BY87; -. DR Antibodypedia; 24483; 173 antibodies from 26 providers. DR DNASU; 74996; -. DR Ensembl; ENSMUST00000106653.4; ENSMUSP00000102264.3; ENSMUSG00000059263.10. [Q8BY87-2] DR Ensembl; ENSMUST00000210309.2; ENSMUSP00000147619.2; ENSMUSG00000059263.10. [Q8BY87-1] DR GeneID; 74996; -. DR KEGG; mmu:74996; -. DR UCSC; uc009jgg.2; mouse. [Q8BY87-2] DR UCSC; uc009jgh.2; mouse. [Q8BY87-1] DR AGR; MGI:1922246; -. DR CTD; 55031; -. DR MGI; MGI:1922246; Usp47. DR VEuPathDB; HostDB:ENSMUSG00000059263; -. DR eggNOG; KOG4598; Eukaryota. DR GeneTree; ENSGT00940000157223; -. DR HOGENOM; CLU_002928_0_0_1; -. DR InParanoid; Q8BY87; -. DR OMA; FLCEWIV; -. DR OrthoDB; 51419at2759; -. DR PhylomeDB; Q8BY87; -. DR TreeFam; TF314142; -. DR Reactome; R-MMU-5689880; Ub-specific processing proteases. DR BioGRID-ORCS; 74996; 2 hits in 112 CRISPR screens. DR ChiTaRS; Usp47; mouse. DR PRO; PR:Q8BY87; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q8BY87; Protein. DR Bgee; ENSMUSG00000059263; Expressed in ciliary body and 243 other cell types or tissues. DR ExpressionAtlas; Q8BY87; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0101005; F:deubiquitinase activity; ISO:MGI. DR GO; GO:0071987; F:WD40-repeat domain binding; ISO:MGI. DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB. DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI. DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS: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; Q8BY87; MM. 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..1376 FT /note="Ubiquitin carboxyl-terminal hydrolase 47" FT /id="PRO_0000080677" FT DOMAIN 188..564 FT /note="USP" FT REGION 426..452 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 835..863 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 880..971 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 985..1025 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..927 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 928..950 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 951..971 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 994..1011 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:0000250|UniProtKB:Q96K76" FT MOD_RES 832 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96K76" FT MOD_RES 911 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15345747, FT ECO:0007744|PubMed:21183079" FT MOD_RES 934 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1014 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1016 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1018 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96K76" FT VAR_SEQ 14..33 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_014416" FT CONFLICT 341 FT /note="A -> G (in Ref. 1; BAC38411)" FT /evidence="ECO:0000305" FT CONFLICT 376..379 FT /note="GLRF -> VRDL (in Ref. 1; BAC38411)" FT /evidence="ECO:0000305" FT CONFLICT 562 FT /note="R -> G (in Ref. 3; AAI08426)" FT /evidence="ECO:0000305" FT CONFLICT 1174 FT /note="I -> T (in Ref. 3; AAI08426)" FT /evidence="ECO:0000305" FT CONFLICT 1178 FT /note="R -> H (in Ref. 1; BAC27195)" FT /evidence="ECO:0000305" FT CONFLICT 1200..1203 FT /note="DINI -> IYNF (in Ref. 1; BAC40073)" FT /evidence="ECO:0000305" FT CONFLICT 1257 FT /note="R -> Q (in Ref. 1; BAC27195)" FT /evidence="ECO:0000305" FT CONFLICT 1299..1301 FT /note="VST -> TRP (in Ref. 3; AAH12722)" FT /evidence="ECO:0000305" SQ SEQUENCE 1376 AA; 157455 MW; 09729C3B691C3709 CRC64; MVPGEENQLV PKEDVFWRCR QNIFDEMKKK FLQIENAAEE PRVLCIIQDT TNSKTVSERI TLNLPASTPV RKLFEDVANK VGYINGTFDL TRENGVTTAD MAPLDHTSDK SLLDANFEPG KKNFLHLTDK DGEPPQMLLE DSNNVDDSVH DRFIGPLPRE GSVASTNDYV SQNYSYSSIL NKSETGYVGL VNQAMTCYLN SLLQTLFMTP EFRNALYKWE FEDSEEDPVT SIPYQLQRLF VLLQTSKKRA IETTDVTRSF GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL YQGKLKDYVR CLECGYEGWR IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN QYFCERCKKK CDARKGLRFL HFPYLLTLQL KRFDFDYTTM HRIKLNDRMS FPEELDMSTF IDIEDEKSPQ TESCTDSGAE NEGSCHSDQM SNDFSTDDAV DEGICLESSS GSEKISKPGL EKNSLMYELF SVMVHSGSAA GGHYYACIKS FSDDQWYSFN DQHVSRITQE DIKKTHGGSS GSRGYYSSAF ASSTNAYMLI YRLKDPTRNA KFLEVDEYPE HIKNLVQKER ELEEQEKRQR EIERNTCKIK LFCLHPVKQV MMENKLEVHK DKTLKEAVEM AYKMMDLEDV IPLDCCRLVK YDEFHDYLER SYEGEEDTPM GLLLGGVKST YMFDLLLETR KPDQIFQSYK PGEVMVKVHV VDLKAETVAA PVTVRAYLNQ TVTEFKQLIS KATHLPADSM RIVLERCYND LRLLSMPSKT LKAEGFFRSN KVFVESSETV DHQAAFTDSH LWKLLDRHAN TIRLFVLLPE QSPGSYSKRT AYQKAGGDSG NVDDDCERVK GPAGNLKSVD AILEESTEKL KSLSLQQQQQ DGDNGDSSKS TETSDFENIE SPLNERGSST SVDNRELEQH IQTSDPENFQ SEERSDSDVN NDRSTSSVDS DILSSSHSSD TLCNADSAQI PLANGLDSHS ITSSRRTKAN EGKKETWDTA EEDSGTDSEY DESGKSRGDM QYMYFKADPY TADEGSGEGH KWLMVHVDKR ITLAAFKQHL EPFVGVLSSH FKVFRVYTSN QEFETVRLNE TLSSFSDDNK ITIRLGRALK KGEYRVKVCQ LLVNEQEPCK FLLDAVFAKG MTVRQSKEEL IPQLREQCGL DLSIDRFRLR KKTWKNPGTV FLDYHIYEED INISSNWEVF LEVLDGVEKM KSMSQLAILT RRWRPAEMKL DPFQELVLES NSVDELREKL SEISGIPLED IEFAKGRGTF PCDISVLDIH QDLDWNPKVS TLNVWPLYIC DDGAVIFYRD RTEEVMELTD EQRNELMKKE SSRLQKTGHR VTYSPRKEKA LKIYLDGAPN KDVAQD //