Full text data of USP9X
USP9X
(DFFRX, FAM, USP9)
[Confidence: high (present in two of the MS resources)]
Probable ubiquitin carboxyl-terminal hydrolase FAF-X; 3.4.19.12 (Deubiquitinating enzyme FAF-X; Fat facets in mammals; hFAM; Fat facets protein-related, X-linked; Ubiquitin thioesterase FAF-X; Ubiquitin-specific protease 9, X chromosome; Ubiquitin-specific-processing protease FAF-X)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Probable ubiquitin carboxyl-terminal hydrolase FAF-X; 3.4.19.12 (Deubiquitinating enzyme FAF-X; Fat facets in mammals; hFAM; Fat facets protein-related, X-linked; Ubiquitin thioesterase FAF-X; Ubiquitin-specific protease 9, X chromosome; Ubiquitin-specific-processing protease FAF-X)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00003964
IPI00003964 Splice Isoform 1 Of Probable ubiquitin carboxyl-terminal hydrolase FAF-X May function as a ubiquitin-protein or polyubiquitin hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins, Ubiquitin C-terminal thiolester + H2O = ubiquitin + a thiol soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic Isoform 1 or 2 found at its expected molecular weight found at molecular weight
IPI00003964 Splice Isoform 1 Of Probable ubiquitin carboxyl-terminal hydrolase FAF-X May function as a ubiquitin-protein or polyubiquitin hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins, Ubiquitin C-terminal thiolester + H2O = ubiquitin + a thiol soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic Isoform 1 or 2 found at its expected molecular weight found at molecular weight
UniProt
Q93008
ID USP9X_HUMAN Reviewed; 2570 AA.
AC Q93008; O75550; Q8WWT3; Q8WX12;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 3.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase FAF-X;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme FAF-X;
DE AltName: Full=Fat facets in mammals;
DE Short=hFAM;
DE AltName: Full=Fat facets protein-related, X-linked;
DE AltName: Full=Ubiquitin thioesterase FAF-X;
DE AltName: Full=Ubiquitin-specific protease 9, X chromosome;
DE AltName: Full=Ubiquitin-specific-processing protease FAF-X;
GN Name=USP9X; Synonyms=DFFRX, FAM, USP9;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain, Retina, and Testis;
RX PubMed=8922996; DOI=10.1093/hmg/5.11.1695;
RA Jones M.H., Furlong R.A., Burkin H., Chalmers I.J., Brown G.M.,
RA Khwaja O., Affara N.A.;
RT "The Drosophila developmental gene fat facets has a human homologue in
RT Xp11.4 which escapes X-inactivation and has related sequences on
RT Yq11.2.";
RL Hum. Mol. Genet. 5:1695-1701(1996).
RN [2]
RP ERRATUM.
RA Jones M.H., Furlong R.A., Burkin H., Chalmers I.J., Brown G.M.,
RA Khwaja O., Affara N.A.;
RL Hum. Mol. Genet. 6:334-335(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2226-2570 (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2556, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH BIRC5.
RX PubMed=16322459; DOI=10.1126/science.1120160;
RA Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.;
RT "Chromosome alignment and segregation regulated by ubiquitination of
RT survivin.";
RL Science 310:1499-1504(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2443, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [10]
RP FUNCTION, AND INTERACTION WITH MARK4 AND NUAK1.
RX PubMed=18254724; DOI=10.1042/BJ20080067;
RA Al-Hakim A.K., Zagorska A., Chapman L., Deak M., Peggie M.,
RA Alessi D.R.;
RT "Control of AMPK-related kinases by USP9X and atypical
RT Lys(29)/Lys(33)-linked polyubiquitin chains.";
RL Biochem. J. 411:249-260(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600; SER-2443 AND
RP SER-2563, 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP FUNCTION, INTERACTION WITH SMAD4, AND SUBCELLULAR LOCATION.
RX PubMed=19135894; DOI=10.1016/j.cell.2008.10.051;
RA Dupont S., Mamidi A., Cordenonsi M., Montagner M., Zacchigna L.,
RA Adorno M., Martello G., Stinchfield M.J., Soligo S., Morsut L.,
RA Inui M., Moro S., Modena N., Argenton F., Newfeld S.J., Piccolo S.;
RT "FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling,
RT controls Smad4 monoubiquitination.";
RL Cell 136:123-135(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASS
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563 AND THR-2567, 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600 AND SER-2443, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Deubiquitinase involved both in the processing of
CC ubiquitin precursors and of ubiquitinated proteins. May therefore
CC play an important role regulatory role at the level of protein
CC turnover by preventing degradation of proteins through the removal
CC of conjugated ubiquitin. Essential component of TGF-beta/BMP
CC signaling cascade. Regulates chromosome alignment and segregation
CC in mitosis by regulating the localization of BIRC5/survivin to
CC mitotic centromeres. Specifically hydrolyzes both 'Lys-29'- and
CC 'Lys-33'-linked polyubiquitins chains. Specifically
CC deubiquitinates monoubiquitinated SMAD4, opposing the activity of
CC E3 ubiquitin-protein ligase TRIM33.
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 SMAD4, MARK4, NUAK1 and BIRC5/survivin.
CC -!- INTERACTION:
CC Q13485:SMAD4; NbExp=2; IntAct=EBI-302524, EBI-347263;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q93008-3; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q93008-1; Sequence=VSP_040478;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryonic and adult
CC tissues.
CC -!- MISCELLANEOUS: Escapes X-inactivation.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD13527.2; Type=Erroneous gene model prediction;
CC Sequence=CAD18900.2; Type=Erroneous gene model prediction;
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DR EMBL; X98296; CAA66942.1; -; mRNA.
DR EMBL; AL391259; CAD13527.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109797; CAD13527.2; JOINED; Genomic_DNA.
DR EMBL; AL109797; CAD18900.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL391259; CAD18900.2; JOINED; Genomic_DNA.
DR EMBL; AF070645; AAC25395.1; -; mRNA.
DR RefSeq; NP_001034679.2; NM_001039590.2.
DR RefSeq; NP_001034680.2; NM_001039591.2.
DR UniGene; Hs.77578; -.
DR ProteinModelPortal; Q93008; -.
DR DIP; DIP-27562N; -.
DR IntAct; Q93008; 19.
DR MINT; MINT-5006529; -.
DR STRING; 9606.ENSP00000316357; -.
DR MEROPS; C19.017; -.
DR PhosphoSite; Q93008; -.
DR DMDM; 81175100; -.
DR PaxDb; Q93008; -.
DR PRIDE; Q93008; -.
DR Ensembl; ENST00000324545; ENSP00000316357; ENSG00000124486.
DR Ensembl; ENST00000378308; ENSP00000367558; ENSG00000124486.
DR GeneID; 8239; -.
DR KEGG; hsa:8239; -.
DR UCSC; uc004dfb.3; human.
DR CTD; 8239; -.
DR GeneCards; GC0XP040944; -.
DR HGNC; HGNC:12632; USP9X.
DR HPA; CAB011618; -.
DR MIM; 300072; gene.
DR neXtProt; NX_Q93008; -.
DR PharmGKB; PA37257; -.
DR eggNOG; COG5077; -.
DR HOGENOM; HOG000231283; -.
DR HOVERGEN; HBG073749; -.
DR KO; K11840; -.
DR OMA; MAQEQFF; -.
DR OrthoDB; EOG722J7K; -.
DR PhylomeDB; Q93008; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; USP9X; human.
DR GeneWiki; USP9X; -.
DR GenomeRNAi; 8239; -.
DR NextBio; 30989; -.
DR PRO; PR:Q93008; -.
DR ArrayExpress; Q93008; -.
DR Bgee; Q93008; -.
DR CleanEx; HS_USP9X; -.
DR Genevestigator; Q93008; -.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; TAS:Reactome.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF48371; SSF48371; 5.
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 Alternative splicing; Cell cycle; Cell division; Chromosome partition;
KW Complete proteome; Cytoplasm; Hydrolase; Mitosis; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1 2570 Probable ubiquitin carboxyl-terminal
FT hydrolase FAF-X.
FT /FTId=PRO_0000080689.
FT ACT_SITE 1566 1566 Nucleophile (By similarity).
FT ACT_SITE 1879 1879 Proton acceptor (By similarity).
FT MOD_RES 1600 1600 Phosphoserine.
FT MOD_RES 2443 2443 Phosphoserine.
FT MOD_RES 2556 2556 Phosphotyrosine.
FT MOD_RES 2563 2563 Phosphoserine.
FT MOD_RES 2567 2567 Phosphothreonine.
FT VAR_SEQ 2478 2493 Missing (in isoform 2).
FT /FTId=VSP_040478.
FT CONFLICT 25 25 Q -> L (in Ref. 1; CAA66942).
FT CONFLICT 148 154 Missing (in Ref. 1; CAA66942).
FT CONFLICT 468 468 L -> P (in Ref. 1; CAA66942).
FT CONFLICT 476 476 W -> R (in Ref. 1; CAA66942).
FT CONFLICT 506 506 K -> R (in Ref. 1; CAA66942).
FT CONFLICT 621 621 A -> V (in Ref. 1; CAA66942).
FT CONFLICT 1400 1400 L -> F (in Ref. 1; CAA66942).
FT CONFLICT 1951 1951 L -> P (in Ref. 1; CAA66942).
FT CONFLICT 2330 2330 T -> P (in Ref. 1; CAA66942).
SQ SEQUENCE 2570 AA; 292280 MW; 84CB979A405AA56F CRC64;
MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE QGQGDAPPQL
EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA AIDLSKKGLD VKSEACQRFF
RDGLTISFTK ILTDEAVSGW KFEIHRCIIN NTHRLVELCV AKLSQDWFPL LELLAMALNP
HCKFHIYNGT RPCESVSSSV QLPEDELFAR SPDPRSPKGW LVDLLNKFGT LNGFQILHDR
FINGSALNVQ IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DEELKKEAKN
EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG KMNALNEVNK
VISSVSYYTH RHGNPEEEEW LTAERMAEWI QQNNILSIVL RDSLHQPQYV EKLEKILRFV
IKEKALTLQD LDNIWAAQAG KHEAIVKNVH DLLAKLAWDF SPEQLDHLFD CFKASWTNAS
KKQREKLLEL IRRLAEDDKD GVMAHKVLNL LWNLAHSDDV PVDIMDLALS AHIKILDYSC
SQDRDTQKIQ WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQT QRSPHVFYRH
DLINQLQHNH ALVTLVAENL ATYMESMRLY ARDHEDYDPQ TVRLGSRYSH VQEVQERLNF
LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW YSKLMGDEPD LDPDINKDFF
ESNVLQLDPS LLTENGMKCF ERFFKAVNCR EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ
SNDDIASRAI DLLKEIYTNL GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSV
NCARQEAVRM VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFVV RFPNQGRQVD
DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPADDRKLI GQLNLKDKSL
ITAKLTQISS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP EVESCLPGVI MSLHPRYISF
LWQVADLGSS LNMPPLRDGA RVLMKLMPPD STTIEKLRAI CLDHAKLGES SLSPSLDSLF
FGPSASQVLY LTEVVYALLM PAGAPLADDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD
METRRGAYLN ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTQINQV THDQAVVLQS
ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIQKIIWASG CGSLQLVFSP
NEEITKIYEK TNAGNEPDLE DEQVCCEALE VMTLCFALIP TALDALSKEK AWQTFIIDLL
LHCHSKTVRQ VAQEQFFLMC TRCCMGHRPL LFFITLLFTV LGSTARERAK HSGDYFTLLR
HLLNYAYNSN INVPNAEVLL NNEIDWLKRI RDDVKRTGET GIEETILEGH LGVTKELLAF
QTSEKKFHIG CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPPTINA
GFELLVALAV GCVRNLKQIV DSLTEMYYIG TAITTCEALT EWEYLPPVGP RPPKGFVGLK
NAGATCYMNS VIQQLYMIPS IRNGILAIEG TGSDVDDDMS GDEKQDNESN VDPRDDVFGY
PQQFEDKPAL SKTEDRKEYN IGVLRHLQVI FGHLAASRLQ YYVPRGFWKQ FRLWGEPVNL
REQHDALEFF NSLVDSLDEA LKALGHPAML SKVLGGSFAD QKICQGCPHR YECEESFTTL
NVDIRNHQNL LDSLEQYVKG DLLEGANAYH CEKCNKKVDT VKRLLIKKLP PVLAIQLKRF
DYDWERECAI KFNDYFEFPR ELDMEPYTVA GVAKLEGDNV NPESQLIQQS EQSESETAGS
TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGERNRWYKF DDGDVTECKM DDDEEMKNQC
FGGEYMGEVF DHMMKRMSYR RQKRWWNAYI LFYERMDTID QDDELIRYIS ELAITTRPHQ
IIMPSAIERS VRKQNVQFMH NRMQYSMEYF QFMKKLLTCN GVYLNPPPGQ DHLLPEAEEI
TMISIQLAAR FLFTTGFHTK KVVRGSASDW YDALCILLRH SKNVRFWFAH NVLFNVSNRF
SEYLLECPSA EVRGAFAKLI VFIAHFSLQD GPCPSPFASP GPSSQAYDNL SLSDHLLRAV
LNLLRREVSE HGRHLQQYFN LFVMYANLGV AEKTQLLKLS VPATFMLVSL DEGPGPPIKY
QYAELGKLYS VVSQLIRCCN VSSRMQSSIN GNPPLPNPFG DPNLSQPIMP IQQNVADILF
VRTSYVKKII EDCSNSEETV KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL
LQILLIEDSW QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSNCPV
AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE TSNGYFLERS
HSARMTLAKA CELCPEEVKK ATSVQQIEME ESKEPDDQDA PDEHESPPPE DAPLYPHSPG
SQYQQNNHVH GQPYTGPAAH HMNNPQRTGQ RAQENYEGSE EVSPPQTKDQ
//
ID USP9X_HUMAN Reviewed; 2570 AA.
AC Q93008; O75550; Q8WWT3; Q8WX12;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 3.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase FAF-X;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme FAF-X;
DE AltName: Full=Fat facets in mammals;
DE Short=hFAM;
DE AltName: Full=Fat facets protein-related, X-linked;
DE AltName: Full=Ubiquitin thioesterase FAF-X;
DE AltName: Full=Ubiquitin-specific protease 9, X chromosome;
DE AltName: Full=Ubiquitin-specific-processing protease FAF-X;
GN Name=USP9X; Synonyms=DFFRX, FAM, USP9;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain, Retina, and Testis;
RX PubMed=8922996; DOI=10.1093/hmg/5.11.1695;
RA Jones M.H., Furlong R.A., Burkin H., Chalmers I.J., Brown G.M.,
RA Khwaja O., Affara N.A.;
RT "The Drosophila developmental gene fat facets has a human homologue in
RT Xp11.4 which escapes X-inactivation and has related sequences on
RT Yq11.2.";
RL Hum. Mol. Genet. 5:1695-1701(1996).
RN [2]
RP ERRATUM.
RA Jones M.H., Furlong R.A., Burkin H., Chalmers I.J., Brown G.M.,
RA Khwaja O., Affara N.A.;
RL Hum. Mol. Genet. 6:334-335(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2226-2570 (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2556, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH BIRC5.
RX PubMed=16322459; DOI=10.1126/science.1120160;
RA Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.;
RT "Chromosome alignment and segregation regulated by ubiquitination of
RT survivin.";
RL Science 310:1499-1504(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2443, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [10]
RP FUNCTION, AND INTERACTION WITH MARK4 AND NUAK1.
RX PubMed=18254724; DOI=10.1042/BJ20080067;
RA Al-Hakim A.K., Zagorska A., Chapman L., Deak M., Peggie M.,
RA Alessi D.R.;
RT "Control of AMPK-related kinases by USP9X and atypical
RT Lys(29)/Lys(33)-linked polyubiquitin chains.";
RL Biochem. J. 411:249-260(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600; SER-2443 AND
RP SER-2563, 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP FUNCTION, INTERACTION WITH SMAD4, AND SUBCELLULAR LOCATION.
RX PubMed=19135894; DOI=10.1016/j.cell.2008.10.051;
RA Dupont S., Mamidi A., Cordenonsi M., Montagner M., Zacchigna L.,
RA Adorno M., Martello G., Stinchfield M.J., Soligo S., Morsut L.,
RA Inui M., Moro S., Modena N., Argenton F., Newfeld S.J., Piccolo S.;
RT "FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling,
RT controls Smad4 monoubiquitination.";
RL Cell 136:123-135(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASS
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563 AND THR-2567, 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600 AND SER-2443, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Deubiquitinase involved both in the processing of
CC ubiquitin precursors and of ubiquitinated proteins. May therefore
CC play an important role regulatory role at the level of protein
CC turnover by preventing degradation of proteins through the removal
CC of conjugated ubiquitin. Essential component of TGF-beta/BMP
CC signaling cascade. Regulates chromosome alignment and segregation
CC in mitosis by regulating the localization of BIRC5/survivin to
CC mitotic centromeres. Specifically hydrolyzes both 'Lys-29'- and
CC 'Lys-33'-linked polyubiquitins chains. Specifically
CC deubiquitinates monoubiquitinated SMAD4, opposing the activity of
CC E3 ubiquitin-protein ligase TRIM33.
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 SMAD4, MARK4, NUAK1 and BIRC5/survivin.
CC -!- INTERACTION:
CC Q13485:SMAD4; NbExp=2; IntAct=EBI-302524, EBI-347263;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q93008-3; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q93008-1; Sequence=VSP_040478;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryonic and adult
CC tissues.
CC -!- MISCELLANEOUS: Escapes X-inactivation.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD13527.2; Type=Erroneous gene model prediction;
CC Sequence=CAD18900.2; Type=Erroneous gene model prediction;
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DR EMBL; X98296; CAA66942.1; -; mRNA.
DR EMBL; AL391259; CAD13527.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109797; CAD13527.2; JOINED; Genomic_DNA.
DR EMBL; AL109797; CAD18900.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL391259; CAD18900.2; JOINED; Genomic_DNA.
DR EMBL; AF070645; AAC25395.1; -; mRNA.
DR RefSeq; NP_001034679.2; NM_001039590.2.
DR RefSeq; NP_001034680.2; NM_001039591.2.
DR UniGene; Hs.77578; -.
DR ProteinModelPortal; Q93008; -.
DR DIP; DIP-27562N; -.
DR IntAct; Q93008; 19.
DR MINT; MINT-5006529; -.
DR STRING; 9606.ENSP00000316357; -.
DR MEROPS; C19.017; -.
DR PhosphoSite; Q93008; -.
DR DMDM; 81175100; -.
DR PaxDb; Q93008; -.
DR PRIDE; Q93008; -.
DR Ensembl; ENST00000324545; ENSP00000316357; ENSG00000124486.
DR Ensembl; ENST00000378308; ENSP00000367558; ENSG00000124486.
DR GeneID; 8239; -.
DR KEGG; hsa:8239; -.
DR UCSC; uc004dfb.3; human.
DR CTD; 8239; -.
DR GeneCards; GC0XP040944; -.
DR HGNC; HGNC:12632; USP9X.
DR HPA; CAB011618; -.
DR MIM; 300072; gene.
DR neXtProt; NX_Q93008; -.
DR PharmGKB; PA37257; -.
DR eggNOG; COG5077; -.
DR HOGENOM; HOG000231283; -.
DR HOVERGEN; HBG073749; -.
DR KO; K11840; -.
DR OMA; MAQEQFF; -.
DR OrthoDB; EOG722J7K; -.
DR PhylomeDB; Q93008; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; USP9X; human.
DR GeneWiki; USP9X; -.
DR GenomeRNAi; 8239; -.
DR NextBio; 30989; -.
DR PRO; PR:Q93008; -.
DR ArrayExpress; Q93008; -.
DR Bgee; Q93008; -.
DR CleanEx; HS_USP9X; -.
DR Genevestigator; Q93008; -.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0004221; F:ubiquitin thiolesterase activity; TAS:Reactome.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR InterPro; IPR001394; Peptidase_C19/C67.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF48371; SSF48371; 5.
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 Alternative splicing; Cell cycle; Cell division; Chromosome partition;
KW Complete proteome; Cytoplasm; Hydrolase; Mitosis; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1 2570 Probable ubiquitin carboxyl-terminal
FT hydrolase FAF-X.
FT /FTId=PRO_0000080689.
FT ACT_SITE 1566 1566 Nucleophile (By similarity).
FT ACT_SITE 1879 1879 Proton acceptor (By similarity).
FT MOD_RES 1600 1600 Phosphoserine.
FT MOD_RES 2443 2443 Phosphoserine.
FT MOD_RES 2556 2556 Phosphotyrosine.
FT MOD_RES 2563 2563 Phosphoserine.
FT MOD_RES 2567 2567 Phosphothreonine.
FT VAR_SEQ 2478 2493 Missing (in isoform 2).
FT /FTId=VSP_040478.
FT CONFLICT 25 25 Q -> L (in Ref. 1; CAA66942).
FT CONFLICT 148 154 Missing (in Ref. 1; CAA66942).
FT CONFLICT 468 468 L -> P (in Ref. 1; CAA66942).
FT CONFLICT 476 476 W -> R (in Ref. 1; CAA66942).
FT CONFLICT 506 506 K -> R (in Ref. 1; CAA66942).
FT CONFLICT 621 621 A -> V (in Ref. 1; CAA66942).
FT CONFLICT 1400 1400 L -> F (in Ref. 1; CAA66942).
FT CONFLICT 1951 1951 L -> P (in Ref. 1; CAA66942).
FT CONFLICT 2330 2330 T -> P (in Ref. 1; CAA66942).
SQ SEQUENCE 2570 AA; 292280 MW; 84CB979A405AA56F CRC64;
MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE QGQGDAPPQL
EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA AIDLSKKGLD VKSEACQRFF
RDGLTISFTK ILTDEAVSGW KFEIHRCIIN NTHRLVELCV AKLSQDWFPL LELLAMALNP
HCKFHIYNGT RPCESVSSSV QLPEDELFAR SPDPRSPKGW LVDLLNKFGT LNGFQILHDR
FINGSALNVQ IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DEELKKEAKN
EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG KMNALNEVNK
VISSVSYYTH RHGNPEEEEW LTAERMAEWI QQNNILSIVL RDSLHQPQYV EKLEKILRFV
IKEKALTLQD LDNIWAAQAG KHEAIVKNVH DLLAKLAWDF SPEQLDHLFD CFKASWTNAS
KKQREKLLEL IRRLAEDDKD GVMAHKVLNL LWNLAHSDDV PVDIMDLALS AHIKILDYSC
SQDRDTQKIQ WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQT QRSPHVFYRH
DLINQLQHNH ALVTLVAENL ATYMESMRLY ARDHEDYDPQ TVRLGSRYSH VQEVQERLNF
LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW YSKLMGDEPD LDPDINKDFF
ESNVLQLDPS LLTENGMKCF ERFFKAVNCR EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ
SNDDIASRAI DLLKEIYTNL GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSV
NCARQEAVRM VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFVV RFPNQGRQVD
DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPADDRKLI GQLNLKDKSL
ITAKLTQISS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP EVESCLPGVI MSLHPRYISF
LWQVADLGSS LNMPPLRDGA RVLMKLMPPD STTIEKLRAI CLDHAKLGES SLSPSLDSLF
FGPSASQVLY LTEVVYALLM PAGAPLADDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD
METRRGAYLN ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTQINQV THDQAVVLQS
ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIQKIIWASG CGSLQLVFSP
NEEITKIYEK TNAGNEPDLE DEQVCCEALE VMTLCFALIP TALDALSKEK AWQTFIIDLL
LHCHSKTVRQ VAQEQFFLMC TRCCMGHRPL LFFITLLFTV LGSTARERAK HSGDYFTLLR
HLLNYAYNSN INVPNAEVLL NNEIDWLKRI RDDVKRTGET GIEETILEGH LGVTKELLAF
QTSEKKFHIG CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPPTINA
GFELLVALAV GCVRNLKQIV DSLTEMYYIG TAITTCEALT EWEYLPPVGP RPPKGFVGLK
NAGATCYMNS VIQQLYMIPS IRNGILAIEG TGSDVDDDMS GDEKQDNESN VDPRDDVFGY
PQQFEDKPAL SKTEDRKEYN IGVLRHLQVI FGHLAASRLQ YYVPRGFWKQ FRLWGEPVNL
REQHDALEFF NSLVDSLDEA LKALGHPAML SKVLGGSFAD QKICQGCPHR YECEESFTTL
NVDIRNHQNL LDSLEQYVKG DLLEGANAYH CEKCNKKVDT VKRLLIKKLP PVLAIQLKRF
DYDWERECAI KFNDYFEFPR ELDMEPYTVA GVAKLEGDNV NPESQLIQQS EQSESETAGS
TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGERNRWYKF DDGDVTECKM DDDEEMKNQC
FGGEYMGEVF DHMMKRMSYR RQKRWWNAYI LFYERMDTID QDDELIRYIS ELAITTRPHQ
IIMPSAIERS VRKQNVQFMH NRMQYSMEYF QFMKKLLTCN GVYLNPPPGQ DHLLPEAEEI
TMISIQLAAR FLFTTGFHTK KVVRGSASDW YDALCILLRH SKNVRFWFAH NVLFNVSNRF
SEYLLECPSA EVRGAFAKLI VFIAHFSLQD GPCPSPFASP GPSSQAYDNL SLSDHLLRAV
LNLLRREVSE HGRHLQQYFN LFVMYANLGV AEKTQLLKLS VPATFMLVSL DEGPGPPIKY
QYAELGKLYS VVSQLIRCCN VSSRMQSSIN GNPPLPNPFG DPNLSQPIMP IQQNVADILF
VRTSYVKKII EDCSNSEETV KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL
LQILLIEDSW QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSNCPV
AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE TSNGYFLERS
HSARMTLAKA CELCPEEVKK ATSVQQIEME ESKEPDDQDA PDEHESPPPE DAPLYPHSPG
SQYQQNNHVH GQPYTGPAAH HMNNPQRTGQ RAQENYEGSE EVSPPQTKDQ
//
MIM
300072
*RECORD*
*FIELD* NO
300072
*FIELD* TI
*300072 UBIQUITIN-SPECIFIC PROTEASE 9, X CHROMOSOME; USP9X
;;DROSOPHILA FAT FACETS-RELATED, X-LINKED; DFFRX;;
read moreFAM
*FIELD* TX
CLONING
Jones et al. (1996) reported that an expressed sequence tag (EST 221)
derived from human adult testis shares homology with the Drosophila fat
facets (faf) gene. They detected related sequences on both the human X
and Y chromosomes. They used EST 221 to derive clones covering the
complete open reading frame of the X-specific locus, which they termed
DFFRX. Y-specific cDNA clones were derived, and they termed that locus
DFFRY (400005). Over the 2 regions corresponding to nucleotides 6 to
1901 and nucleotides 5815 to 7907 of the DFFRX sequence, the X- and
Y-specific sequences share 91% and 88% identity, respectively. Both
putative gene products contain conserved cysteine and histidine domains
that have been described in ubiquitin C-terminal hydrolases (e.g.,
191342). Northern blot analysis of 16 different adult human tissues with
the EST 221 revealed expression in all tissues. They also detected both
DFFRX and DFFRY expression in developing human tissues.
GENE FUNCTION
Jones et al. (1996) determined the X inactivation status of DFFRX
through use of quantitative RT-PCR with X-specific primers and found
that the level of DFFRX expression rises as the copy number of the X
chromosome increases, indicating that DFFRX escapes inactivation. In
Drosophila the faf gene has been shown to be important in eye function
and in oocyte development. The high degree of conservation between the
Drosophila faf gene and the DFFRX sequence led Jones et al. (1996) to
conclude that DFFRX has an important function in humans.
Proper chromosome segregation requires the attachment of sister
kinetochores to microtubules from opposite spindle poles to form
bioriented chromosomes on the metaphase spindle. The chromosome
passenger complex containing survivin (603352) and the kinase aurora B
(604970) regulates this process from the centromeres. Vong et al. (2005)
reported that a deubiquitinating enzyme, FAM, also known as USP9X,
regulates chromosome alignment and segregation by controlling both the
dynamic association of survivin with centromeres and the proper
targeting of survivin and aurora B to centromeres. Survivin is
ubiquitinated in mitosis through both lys48 and lys63 ubiquitin
linkages. Lys63 deubiquitination mediated by FAM is required for the
dissociation of survivin from centromeres, whereas lys63 ubiquitination
mediated by the ubiquitin-binding protein UFD1 (601754) is required for
the association of survivin with centromeres. Thus, ubiquitination
regulates dynamic protein-protein interactions and chromosome
segregation independently of protein degradation.
Schwickart et al. (2010) showed that the deubiquitinase USP9X binds to
and stabilizes MCL1 (159552) and removes the lys48-linked polyubiquitin
chains that normally mark MCL1 for proteasomal degradation. Increased
USP9X expression correlated with increased MCL1 protein in human
follicular lymphomas and diffuse large B-cell lymphomas. Moreover,
patients with multiple myeloma overexpressing USP9X have a poor
prognosis. Knockdown of USP9X increased MCL1 polyubiquitination, which
enhances MCL1 turnover and cell killing by the BH3 mimetic ABT-737.
Schwickart et al. (2010) concluded that their results identified USP9X
as a prognostic and therapeutic target and showed that deubiquitinases
may stabilize labile oncoproteins in human malignancies.
MAPPING
Jones et al. (1996) mapped DFFRX to Xp11.4 by somatic cell hybrid
analysis and a YAC library screen. They noted that the map location
coincides with the region of the X chromosome defined by partial
deletions as being critical for the major stigmata associated with
Turner syndrome (163950). They raised the possibility that DFFRX plays a
role in the defects of oocyte proliferation and subsequent gonadal
degeneration found in Turner syndrome.
ANIMAL MODEL
Perez-Mancera et al. (2012) used 'Sleeping Beauty' transposon-mediated
insertional mutagenesis in a mouse model of pancreatic ductal
preneoplasia to identify genes that cooperate with oncogenic Kras(G12D)
(190070.0003) to accelerate tumorigenesis and promote progression. This
screen revealed novel candidate genes for pancreatic ductal
adenocarcinoma (PDA) and confirmed the importance of many genes and
pathways previously implicated in human PDA. The most commonly mutated
gene was the X-linked deubiquitinase Usp9x, which was inactivated in
over 50% of the tumors. Although previous work had attributed a
presurvival role to USP9X in human neoplasia, Perez-Mancera et al.
(2012) found instead that loss of Usp9x enhances transformation and
protects pancreatic cancer cells from anoikis. Clinically, low USP9X
protein and mRNA expression in PDA correlates with poor survival after
surgery, and USP9X levels are inversely associated with metastatic
burden in advanced disease. Furthermore, chromatin modulation with
trichostatin A or 5-aza-2-prime-deoxycytidine elevates USP9X expression
in human PDA cell lines, indicating a clinical approach for certain
patients. The conditional deletion of Usp9x cooperated with Kras(G12D)
to accelerate pancreatic tumorigenesis in mice, validating their genetic
interaction. Perez-Mancera et al. (2012) proposed that USP9X is a major
tumor suppressor gene with prognostic and therapeutic relevance in PDA.
*FIELD* RF
1. Jones, M. H.; Furlong, R. A.; Burkin, H.; Chalmers, I. J.; Brown,
G. M.; Khwaja, O.; Affara, N. A.: The Drosophila developmental gene
fat facets has a human homologue in Xp11.4 which escapes X-inactivation
and has related sequences on Yq11.2. Hum. Molec. Genet. 5: 1695-1701,
1996. Note: Erratum: Hum. Molec. Genet. 6: 334-335, 1997.
2. Perez-Mancera, P. A.; Rust, A. G.; van der Weyden, L.; Kristiansen,
G.; Li, A.; Sarver, A. L.; Silverstein, K. A. T.; Grutzmann, R.; Aust,
D.; Rummele, P.; Knosel, T.; Herd, C.; and 25 others: The deubiquitinase
USP9X suppresses pancreatic ductal adenocarcinoma. Nature 486: 266-270,
2012. Note: Erratum: Nature 494, 390 only, 2013.
3. Schwickart, M.; Huang, X.; Lill, J. R.; Liu, J.; Ferrando, R.;
French, D. M.; Maecker, H.; O'Rourke, K.; Bazan, F.; Eastham-Anderson,
J.; Yue, P.; Dornan, D.; Huang, D. C. S.; Dixit, V. M.: Deubiquitinase
USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 463:
103-107, 2010.
4. Vong, Q. P.; Cao, K.; Li, H. Y.; Iglesias, P. A.; Zheng, Y.: Chromosome
alignment and segregation regulated by ubiquitination of survivin. Science 310:
1499-1504, 2005.
*FIELD* CN
Ada Hamosh - updated: 03/21/2013
Ada Hamosh - updated: 6/27/2012
Ada Hamosh - updated: 2/2/2010
Ada Hamosh - updated: 1/11/2006
*FIELD* CD
Moyra Smith: 1/24/1997
*FIELD* ED
terry: 03/21/2013
terry: 8/9/2012
alopez: 7/10/2012
terry: 6/27/2012
alopez: 2/22/2010
terry: 2/2/2010
alopez: 1/12/2006
terry: 1/11/2006
alopez: 2/5/1999
mark: 7/8/1997
mark: 1/25/1997
terry: 1/24/1997
mark: 1/24/1997
*RECORD*
*FIELD* NO
300072
*FIELD* TI
*300072 UBIQUITIN-SPECIFIC PROTEASE 9, X CHROMOSOME; USP9X
;;DROSOPHILA FAT FACETS-RELATED, X-LINKED; DFFRX;;
read moreFAM
*FIELD* TX
CLONING
Jones et al. (1996) reported that an expressed sequence tag (EST 221)
derived from human adult testis shares homology with the Drosophila fat
facets (faf) gene. They detected related sequences on both the human X
and Y chromosomes. They used EST 221 to derive clones covering the
complete open reading frame of the X-specific locus, which they termed
DFFRX. Y-specific cDNA clones were derived, and they termed that locus
DFFRY (400005). Over the 2 regions corresponding to nucleotides 6 to
1901 and nucleotides 5815 to 7907 of the DFFRX sequence, the X- and
Y-specific sequences share 91% and 88% identity, respectively. Both
putative gene products contain conserved cysteine and histidine domains
that have been described in ubiquitin C-terminal hydrolases (e.g.,
191342). Northern blot analysis of 16 different adult human tissues with
the EST 221 revealed expression in all tissues. They also detected both
DFFRX and DFFRY expression in developing human tissues.
GENE FUNCTION
Jones et al. (1996) determined the X inactivation status of DFFRX
through use of quantitative RT-PCR with X-specific primers and found
that the level of DFFRX expression rises as the copy number of the X
chromosome increases, indicating that DFFRX escapes inactivation. In
Drosophila the faf gene has been shown to be important in eye function
and in oocyte development. The high degree of conservation between the
Drosophila faf gene and the DFFRX sequence led Jones et al. (1996) to
conclude that DFFRX has an important function in humans.
Proper chromosome segregation requires the attachment of sister
kinetochores to microtubules from opposite spindle poles to form
bioriented chromosomes on the metaphase spindle. The chromosome
passenger complex containing survivin (603352) and the kinase aurora B
(604970) regulates this process from the centromeres. Vong et al. (2005)
reported that a deubiquitinating enzyme, FAM, also known as USP9X,
regulates chromosome alignment and segregation by controlling both the
dynamic association of survivin with centromeres and the proper
targeting of survivin and aurora B to centromeres. Survivin is
ubiquitinated in mitosis through both lys48 and lys63 ubiquitin
linkages. Lys63 deubiquitination mediated by FAM is required for the
dissociation of survivin from centromeres, whereas lys63 ubiquitination
mediated by the ubiquitin-binding protein UFD1 (601754) is required for
the association of survivin with centromeres. Thus, ubiquitination
regulates dynamic protein-protein interactions and chromosome
segregation independently of protein degradation.
Schwickart et al. (2010) showed that the deubiquitinase USP9X binds to
and stabilizes MCL1 (159552) and removes the lys48-linked polyubiquitin
chains that normally mark MCL1 for proteasomal degradation. Increased
USP9X expression correlated with increased MCL1 protein in human
follicular lymphomas and diffuse large B-cell lymphomas. Moreover,
patients with multiple myeloma overexpressing USP9X have a poor
prognosis. Knockdown of USP9X increased MCL1 polyubiquitination, which
enhances MCL1 turnover and cell killing by the BH3 mimetic ABT-737.
Schwickart et al. (2010) concluded that their results identified USP9X
as a prognostic and therapeutic target and showed that deubiquitinases
may stabilize labile oncoproteins in human malignancies.
MAPPING
Jones et al. (1996) mapped DFFRX to Xp11.4 by somatic cell hybrid
analysis and a YAC library screen. They noted that the map location
coincides with the region of the X chromosome defined by partial
deletions as being critical for the major stigmata associated with
Turner syndrome (163950). They raised the possibility that DFFRX plays a
role in the defects of oocyte proliferation and subsequent gonadal
degeneration found in Turner syndrome.
ANIMAL MODEL
Perez-Mancera et al. (2012) used 'Sleeping Beauty' transposon-mediated
insertional mutagenesis in a mouse model of pancreatic ductal
preneoplasia to identify genes that cooperate with oncogenic Kras(G12D)
(190070.0003) to accelerate tumorigenesis and promote progression. This
screen revealed novel candidate genes for pancreatic ductal
adenocarcinoma (PDA) and confirmed the importance of many genes and
pathways previously implicated in human PDA. The most commonly mutated
gene was the X-linked deubiquitinase Usp9x, which was inactivated in
over 50% of the tumors. Although previous work had attributed a
presurvival role to USP9X in human neoplasia, Perez-Mancera et al.
(2012) found instead that loss of Usp9x enhances transformation and
protects pancreatic cancer cells from anoikis. Clinically, low USP9X
protein and mRNA expression in PDA correlates with poor survival after
surgery, and USP9X levels are inversely associated with metastatic
burden in advanced disease. Furthermore, chromatin modulation with
trichostatin A or 5-aza-2-prime-deoxycytidine elevates USP9X expression
in human PDA cell lines, indicating a clinical approach for certain
patients. The conditional deletion of Usp9x cooperated with Kras(G12D)
to accelerate pancreatic tumorigenesis in mice, validating their genetic
interaction. Perez-Mancera et al. (2012) proposed that USP9X is a major
tumor suppressor gene with prognostic and therapeutic relevance in PDA.
*FIELD* RF
1. Jones, M. H.; Furlong, R. A.; Burkin, H.; Chalmers, I. J.; Brown,
G. M.; Khwaja, O.; Affara, N. A.: The Drosophila developmental gene
fat facets has a human homologue in Xp11.4 which escapes X-inactivation
and has related sequences on Yq11.2. Hum. Molec. Genet. 5: 1695-1701,
1996. Note: Erratum: Hum. Molec. Genet. 6: 334-335, 1997.
2. Perez-Mancera, P. A.; Rust, A. G.; van der Weyden, L.; Kristiansen,
G.; Li, A.; Sarver, A. L.; Silverstein, K. A. T.; Grutzmann, R.; Aust,
D.; Rummele, P.; Knosel, T.; Herd, C.; and 25 others: The deubiquitinase
USP9X suppresses pancreatic ductal adenocarcinoma. Nature 486: 266-270,
2012. Note: Erratum: Nature 494, 390 only, 2013.
3. Schwickart, M.; Huang, X.; Lill, J. R.; Liu, J.; Ferrando, R.;
French, D. M.; Maecker, H.; O'Rourke, K.; Bazan, F.; Eastham-Anderson,
J.; Yue, P.; Dornan, D.; Huang, D. C. S.; Dixit, V. M.: Deubiquitinase
USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 463:
103-107, 2010.
4. Vong, Q. P.; Cao, K.; Li, H. Y.; Iglesias, P. A.; Zheng, Y.: Chromosome
alignment and segregation regulated by ubiquitination of survivin. Science 310:
1499-1504, 2005.
*FIELD* CN
Ada Hamosh - updated: 03/21/2013
Ada Hamosh - updated: 6/27/2012
Ada Hamosh - updated: 2/2/2010
Ada Hamosh - updated: 1/11/2006
*FIELD* CD
Moyra Smith: 1/24/1997
*FIELD* ED
terry: 03/21/2013
terry: 8/9/2012
alopez: 7/10/2012
terry: 6/27/2012
alopez: 2/22/2010
terry: 2/2/2010
alopez: 1/12/2006
terry: 1/11/2006
alopez: 2/5/1999
mark: 7/8/1997
mark: 1/25/1997
terry: 1/24/1997
mark: 1/24/1997