Full text data of USP47
USP47
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin carboxyl-terminal hydrolase 47; 3.4.19.12 (Deubiquitinating enzyme 47; Ubiquitin thioesterase 47; Ubiquitin-specific-processing protease 47)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin carboxyl-terminal hydrolase 47; 3.4.19.12 (Deubiquitinating enzyme 47; Ubiquitin thioesterase 47; Ubiquitin-specific-processing protease 47)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96K76
ID UBP47_HUMAN Reviewed; 1375 AA.
AC Q96K76; B3KXF5; Q658U0; Q86Y73; Q8TEP6; Q9BWI0; Q9NWN1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-NOV-2010, sequence version 3.
DT 22-JAN-2014, entry version 105.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 940-1375 (ISOFORMS 1/2).
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
RT project: 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
RT 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Cal S., 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 MASS
RP SPECTROMETRY.
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
RT phosphorylation 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 MASS SPECTROMETRY.
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
RP SCALE ANALYSIS] VAL-163, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RP WITH 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.,
RA Kessler B.M., Dianov G.L.;
RT "USP47 is a deubiquitylating enzyme that regulates base excision
RT repair by controlling steady-state levels of DNA Polymerase beta.";
RL Mol. Cell 41:609-615(2011).
CC -!- FUNCTION: Ubiquitin-specific protease that specifically
CC deubiquitinates monoubiquitinated DNA polymerase beta (POLB),
CC stabilizing POLB thereby playing a role in base-excision repair
CC (BER). Acts as a regulator of cell growth and genome integrity.
CC May also indirectly regulates CDC25A expression at a
CC transcriptional level.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Interacts with BTRC and FBXW11. Interacts with POLB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart and
CC testis.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- CAUTION: Was initially thought to catalytically inactive
CC (PubMed:14715245). However, it was later shown that it is active
CC (PubMed:21362556).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91348.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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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; AK074076; BAB84902.1; -; mRNA.
DR EMBL; AL832991; CAH56337.1; -; mRNA.
DR RefSeq; NP_001269588.1; NM_001282659.1.
DR RefSeq; NP_060414.3; NM_017944.3.
DR RefSeq; XP_005253054.1; XM_005252997.1.
DR UniGene; Hs.577256; -.
DR ProteinModelPortal; Q96K76; -.
DR SMR; Q96K76; 182-596.
DR DIP; DIP-53629N; -.
DR IntAct; Q96K76; 3.
DR STRING; 9606.ENSP00000339957; -.
DR ChEMBL; CHEMBL2157851; -.
DR MEROPS; C19.055; -.
DR PhosphoSite; Q96K76; -.
DR DMDM; 68566222; -.
DR PaxDb; Q96K76; -.
DR PRIDE; Q96K76; -.
DR Ensembl; ENST00000339865; ENSP00000339957; ENSG00000170242.
DR Ensembl; ENST00000399455; ENSP00000382382; ENSG00000170242.
DR Ensembl; ENST00000539466; ENSP00000440405; ENSG00000170242.
DR GeneID; 55031; -.
DR KEGG; hsa:55031; -.
DR UCSC; uc001mjq.1; human.
DR CTD; 55031; -.
DR GeneCards; GC11P011819; -.
DR HGNC; HGNC:20076; USP47.
DR HPA; HPA029286; -.
DR HPA; HPA029289; -.
DR MIM; 614460; gene.
DR neXtProt; NX_Q96K76; -.
DR PharmGKB; PA134880952; -.
DR eggNOG; COG5077; -.
DR HOVERGEN; HBG058854; -.
DR InParanoid; Q96K76; -.
DR KO; K11857; -.
DR OMA; LCEISGI; -.
DR OrthoDB; EOG7M3HZD; -.
DR ChiTaRS; USP47; human.
DR GeneWiki; USP47; -.
DR GenomeRNAi; 55031; -.
DR NextBio; 58447; -.
DR PRO; PR:Q96K76; -.
DR ArrayExpress; Q96K76; -.
DR Bgee; Q96K76; -.
DR CleanEx; HS_USP47; -.
DR Genevestigator; Q96K76; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IMP:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
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:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0042493; P:response to drug; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR Pfam; PF00443; UCH; 1.
DR PROSITE; PS00972; UCH_2_1; 1.
DR PROSITE; PS00973; UCH_2_2; 1.
DR PROSITE; PS50235; UCH_2_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW DNA damage; DNA repair; Hydrolase; Phosphoprotein; Polymorphism;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1 1375 Ubiquitin carboxyl-terminal hydrolase 47.
FT /FTId=PRO_0000080676.
FT ACT_SITE 197 197 Nucleophile (By similarity).
FT ACT_SITE 503 503 Proton acceptor (By similarity).
FT MOD_RES 122 122 N6-acetyllysine.
FT MOD_RES 832 832 Phosphoserine.
FT MOD_RES 910 910 Phosphoserine.
FT MOD_RES 1015 1015 Phosphothreonine (By similarity).
FT VAR_SEQ 1 1218 Missing (in isoform 3).
FT /FTId=VSP_014414.
FT VAR_SEQ 14 101 Missing (in isoform 2).
FT /FTId=VSP_014415.
FT VARIANT 163 163 G -> V (in dbSNP:rs11022079).
FT /FTId=VAR_022787.
FT CONFLICT 340 340 F -> L (in Ref. 1; BAG54467).
FT CONFLICT 494 494 V -> A (in Ref. 1; BAB55063/BAG54467).
FT CONFLICT 520 520 N -> D (in Ref. 1; BAB55063).
FT CONFLICT 576 576 D -> G (in Ref. 1; BAB55063).
FT CONFLICT 604 604 R -> G (in Ref. 4; BAB84902).
FT CONFLICT 911 911 P -> S (in Ref. 1; BAG54467).
FT CONFLICT 1157 1157 E -> G (in Ref. 1; BAA91348).
FT CONFLICT 1313 1313 A -> G (in Ref. 1; BAA91348).
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
//
ID UBP47_HUMAN Reviewed; 1375 AA.
AC Q96K76; B3KXF5; Q658U0; Q86Y73; Q8TEP6; Q9BWI0; Q9NWN1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 30-NOV-2010, sequence version 3.
DT 22-JAN-2014, entry version 105.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA 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] (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 940-1375 (ISOFORMS 1/2).
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
RT project: 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
RT 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Cal S., 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 MASS
RP SPECTROMETRY.
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
RT phosphorylation 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 MASS SPECTROMETRY.
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
RP SCALE ANALYSIS] VAL-163, AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RP WITH 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.,
RA Kessler B.M., Dianov G.L.;
RT "USP47 is a deubiquitylating enzyme that regulates base excision
RT repair by controlling steady-state levels of DNA Polymerase beta.";
RL Mol. Cell 41:609-615(2011).
CC -!- FUNCTION: Ubiquitin-specific protease that specifically
CC deubiquitinates monoubiquitinated DNA polymerase beta (POLB),
CC stabilizing POLB thereby playing a role in base-excision repair
CC (BER). Acts as a regulator of cell growth and genome integrity.
CC May also indirectly regulates CDC25A expression at a
CC transcriptional level.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Interacts with BTRC and FBXW11. Interacts with POLB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart and
CC testis.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- CAUTION: Was initially thought to catalytically inactive
CC (PubMed:14715245). However, it was later shown that it is active
CC (PubMed:21362556).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91348.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
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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; AK074076; BAB84902.1; -; mRNA.
DR EMBL; AL832991; CAH56337.1; -; mRNA.
DR RefSeq; NP_001269588.1; NM_001282659.1.
DR RefSeq; NP_060414.3; NM_017944.3.
DR RefSeq; XP_005253054.1; XM_005252997.1.
DR UniGene; Hs.577256; -.
DR ProteinModelPortal; Q96K76; -.
DR SMR; Q96K76; 182-596.
DR DIP; DIP-53629N; -.
DR IntAct; Q96K76; 3.
DR STRING; 9606.ENSP00000339957; -.
DR ChEMBL; CHEMBL2157851; -.
DR MEROPS; C19.055; -.
DR PhosphoSite; Q96K76; -.
DR DMDM; 68566222; -.
DR PaxDb; Q96K76; -.
DR PRIDE; Q96K76; -.
DR Ensembl; ENST00000339865; ENSP00000339957; ENSG00000170242.
DR Ensembl; ENST00000399455; ENSP00000382382; ENSG00000170242.
DR Ensembl; ENST00000539466; ENSP00000440405; ENSG00000170242.
DR GeneID; 55031; -.
DR KEGG; hsa:55031; -.
DR UCSC; uc001mjq.1; human.
DR CTD; 55031; -.
DR GeneCards; GC11P011819; -.
DR HGNC; HGNC:20076; USP47.
DR HPA; HPA029286; -.
DR HPA; HPA029289; -.
DR MIM; 614460; gene.
DR neXtProt; NX_Q96K76; -.
DR PharmGKB; PA134880952; -.
DR eggNOG; COG5077; -.
DR HOVERGEN; HBG058854; -.
DR InParanoid; Q96K76; -.
DR KO; K11857; -.
DR OMA; LCEISGI; -.
DR OrthoDB; EOG7M3HZD; -.
DR ChiTaRS; USP47; human.
DR GeneWiki; USP47; -.
DR GenomeRNAi; 55031; -.
DR NextBio; 58447; -.
DR PRO; PR:Q96K76; -.
DR ArrayExpress; Q96K76; -.
DR Bgee; Q96K76; -.
DR CleanEx; HS_USP47; -.
DR Genevestigator; Q96K76; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IMP:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
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:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0042493; P:response to drug; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR Pfam; PF00443; UCH; 1.
DR PROSITE; PS00972; UCH_2_1; 1.
DR PROSITE; PS00973; UCH_2_2; 1.
DR PROSITE; PS50235; UCH_2_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW DNA damage; DNA repair; Hydrolase; Phosphoprotein; Polymorphism;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1 1375 Ubiquitin carboxyl-terminal hydrolase 47.
FT /FTId=PRO_0000080676.
FT ACT_SITE 197 197 Nucleophile (By similarity).
FT ACT_SITE 503 503 Proton acceptor (By similarity).
FT MOD_RES 122 122 N6-acetyllysine.
FT MOD_RES 832 832 Phosphoserine.
FT MOD_RES 910 910 Phosphoserine.
FT MOD_RES 1015 1015 Phosphothreonine (By similarity).
FT VAR_SEQ 1 1218 Missing (in isoform 3).
FT /FTId=VSP_014414.
FT VAR_SEQ 14 101 Missing (in isoform 2).
FT /FTId=VSP_014415.
FT VARIANT 163 163 G -> V (in dbSNP:rs11022079).
FT /FTId=VAR_022787.
FT CONFLICT 340 340 F -> L (in Ref. 1; BAG54467).
FT CONFLICT 494 494 V -> A (in Ref. 1; BAB55063/BAG54467).
FT CONFLICT 520 520 N -> D (in Ref. 1; BAB55063).
FT CONFLICT 576 576 D -> G (in Ref. 1; BAB55063).
FT CONFLICT 604 604 R -> G (in Ref. 4; BAB84902).
FT CONFLICT 911 911 P -> S (in Ref. 1; BAG54467).
FT CONFLICT 1157 1157 E -> G (in Ref. 1; BAA91348).
FT CONFLICT 1313 1313 A -> G (in Ref. 1; BAA91348).
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
//
MIM
614460
*RECORD*
*FIELD* NO
614460
*FIELD* TI
*614460 UBIQUITIN-SPECIFIC PROTEASE 47; USP47
*FIELD* TX
DESCRIPTION
USP47 belongs to a family of ubiquitin-specific cysteine proteases.
read moreThese enzymes catalyze the removal of ubiquitin from proteins that are
ubiquitinated and thus targeted for degradation via the proteasome
(Quesada et al., 2004).
CLONING
By searching databases for sequences similar to USP family members,
followed by PCR of human cDNA libraries, Quesada et al. (2004) cloned
USP47. The deduced protein has a catalytic domain containing a cys box,
a QQD box, and a his box, all of which are characteristic of USP
enzymes. Northern blot analysis detected high expression of a 5.5-kb
transcript in skeletal muscle, with lower expression in testis and
heart, and little to no expression in other tissues examined.
SKP1 (601434)/CUL1 (603134)/F-box protein (see 609102) (SCF) complexes
function as E3 ubiquitin ligases. By mass spectrometric analysis of
peptides that immunoprecipitated with an SCF complex containing
beta-TRCP2 (FBXW11; 603482) as its F-box protein subunit, Peschiaroli et
al. (2010) identified USP47. The deduced full-length protein contains
1,287 amino acids.
GENE FUNCTION
Peschiaroli et al. (2010) found that the F-box proteins beta-TRCP1
(BTRC; 603482) and beta-TRCP2, but not other F-box proteins, bound
USP47. Mutation analysis revealed that an N-terminal domain of USP47
interacted with the WD40 repeat domain of beta-TRCP. Knockdown of either
USP47 or beta-TRCP in several human cell lines reduced cell survival and
sensitized cells to pharmacologic induction of apoptosis. However,
beta-TRCP did not appear to use USP47 as a substrate or induce its
degradation. Conversely, knockdown of USP47 had no effect on beta-TRCP
activity.
MAPPING
Hartz (2012) mapped the USP47 gene to chromosome 11p15.3 based on an
alignment of the USP47 sequence (GenBank GENBANK AK000734) with the
genomic sequence (GRCh37).
ANIMAL MODEL
Peschiaroli et al. (2010) found that mice homozygous for a hypomorphic
Usp47 allele were viable and fertile. However, fibroblasts derived from
homozygous mutant embryos were more sensitive than wildtype to
ultraviolet radiation-induced apoptosis.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/30/2012.
2. Peschiaroli, A.; Skaar, J. R.; Pagano, M.; Melino, G.: The ubiquitin-specific
protease USP47 is a novel beta-TRCP interactor regulating cell survival. Oncogene 29:
1384-1393, 2010.
3. Quesada, V.; Diaz-Perales, A.; Gutierrez-Fernandez, A.; Garabaya,
C.; Cal, S.; Lopez-Otin, C.: Cloning and enzymatic analysis of 22
novel human ubiquitin-specific proteases. Biochem. Biophys. Res.
Commun. 314: 54-62, 2004.
*FIELD* CD
Patricia A. Hartz: 1/31/2012
*FIELD* ED
mgross: 01/31/2012
*RECORD*
*FIELD* NO
614460
*FIELD* TI
*614460 UBIQUITIN-SPECIFIC PROTEASE 47; USP47
*FIELD* TX
DESCRIPTION
USP47 belongs to a family of ubiquitin-specific cysteine proteases.
read moreThese enzymes catalyze the removal of ubiquitin from proteins that are
ubiquitinated and thus targeted for degradation via the proteasome
(Quesada et al., 2004).
CLONING
By searching databases for sequences similar to USP family members,
followed by PCR of human cDNA libraries, Quesada et al. (2004) cloned
USP47. The deduced protein has a catalytic domain containing a cys box,
a QQD box, and a his box, all of which are characteristic of USP
enzymes. Northern blot analysis detected high expression of a 5.5-kb
transcript in skeletal muscle, with lower expression in testis and
heart, and little to no expression in other tissues examined.
SKP1 (601434)/CUL1 (603134)/F-box protein (see 609102) (SCF) complexes
function as E3 ubiquitin ligases. By mass spectrometric analysis of
peptides that immunoprecipitated with an SCF complex containing
beta-TRCP2 (FBXW11; 603482) as its F-box protein subunit, Peschiaroli et
al. (2010) identified USP47. The deduced full-length protein contains
1,287 amino acids.
GENE FUNCTION
Peschiaroli et al. (2010) found that the F-box proteins beta-TRCP1
(BTRC; 603482) and beta-TRCP2, but not other F-box proteins, bound
USP47. Mutation analysis revealed that an N-terminal domain of USP47
interacted with the WD40 repeat domain of beta-TRCP. Knockdown of either
USP47 or beta-TRCP in several human cell lines reduced cell survival and
sensitized cells to pharmacologic induction of apoptosis. However,
beta-TRCP did not appear to use USP47 as a substrate or induce its
degradation. Conversely, knockdown of USP47 had no effect on beta-TRCP
activity.
MAPPING
Hartz (2012) mapped the USP47 gene to chromosome 11p15.3 based on an
alignment of the USP47 sequence (GenBank GENBANK AK000734) with the
genomic sequence (GRCh37).
ANIMAL MODEL
Peschiaroli et al. (2010) found that mice homozygous for a hypomorphic
Usp47 allele were viable and fertile. However, fibroblasts derived from
homozygous mutant embryos were more sensitive than wildtype to
ultraviolet radiation-induced apoptosis.
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 1/30/2012.
2. Peschiaroli, A.; Skaar, J. R.; Pagano, M.; Melino, G.: The ubiquitin-specific
protease USP47 is a novel beta-TRCP interactor regulating cell survival. Oncogene 29:
1384-1393, 2010.
3. Quesada, V.; Diaz-Perales, A.; Gutierrez-Fernandez, A.; Garabaya,
C.; Cal, S.; Lopez-Otin, C.: Cloning and enzymatic analysis of 22
novel human ubiquitin-specific proteases. Biochem. Biophys. Res.
Commun. 314: 54-62, 2004.
*FIELD* CD
Patricia A. Hartz: 1/31/2012
*FIELD* ED
mgross: 01/31/2012