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Probable ubiquitin carboxyl-terminal hydrolase FAF-X (EC 3.4.19.12) (Deubiquitinating enzyme FAF-X) (Fat facets homolog) (Fat facets protein-related, X-linked) (Ubiquitin carboxyl-terminal hydrolase FAM) (Ubiquitin thioesterase FAF-X) (Ubiquitin-specific protease 9, X chromosome) (Ubiquitin-specific-processing protease FAF-X)

 USP9X_MOUSE             Reviewed;        2559 AA.
P70398; E9QLY0; Q62497;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 151.
RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase FAF-X;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme FAF-X;
AltName: Full=Fat facets homolog;
AltName: Full=Fat facets protein-related, X-linked;
AltName: Full=Ubiquitin carboxyl-terminal hydrolase FAM;
AltName: Full=Ubiquitin thioesterase FAF-X;
AltName: Full=Ubiquitin-specific protease 9, X chromosome;
AltName: Full=Ubiquitin-specific-processing protease FAF-X;
Name=Usp9x; Synonyms=Fafl, Fam;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9178254; DOI=10.1016/S0925-4773(97)00672-2;
Wood S.A., Pascoe W.S., Ru K., Yamada T., Hirchenhain J., Kemler R.,
Mattick J.S.;
"Cloning and expression analysis of a novel mouse gene with sequence
similarity to the Drosophila fat facets gene.";
Mech. Dev. 63:29-38(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 152-240.
TISSUE=Cochlea;
PubMed=9119401; DOI=10.1006/geno.1996.4526;
Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G.,
Weil D., Pujol R., Petit C.;
"Cloning of the genes encoding two murine and human cochlear
unconventional type I myosins.";
Genomics 40:332-341(1997).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2540, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-375; SER-1600
AND SER-2443, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24607389; DOI=10.1016/j.ajhg.2014.02.004;
Homan C.C., Kumar R., Nguyen L.S., Haan E., Raymond F.L., Abidi F.,
Raynaud M., Schwartz C.E., Wood S.A., Gecz J., Jolly L.A.;
"Mutations in USP9X are associated with X-linked intellectual
disability and disrupt neuronal cell migration and growth.";
Am. J. Hum. Genet. 94:470-478(2014).
-!- FUNCTION: Deubiquitinase involved both in the processing of
ubiquitin precursors and of ubiquitinated proteins. May therefore
play an important regulatory role at the level of protein turnover
by preventing degradation of proteins through the removal of
conjugated ubiquitin. Essential component of TGF-beta/BMP
signaling cascade. Regulates chromosome alignment and segregation
in mitosis by regulating the localization of BIRC5/survivin to
mitotic centromeres. Specifically hydrolyzes both 'Lys-29'- and
'Lys-33'-linked polyubiquitins chains. Specifically
deubiquitinates monoubiquitinated SMAD4, opposing the activity of
E3 ubiquitin-protein ligase TRIM33 (By similarity). Involved in
axonal growth and neuronal cell migration. {ECO:0000250,
ECO:0000269|PubMed:24607389}.
-!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
thioester, amide, peptide and isopeptide bonds formed by the C-
terminal Gly of ubiquitin (a 76-residue protein attached to
proteins as an intracellular targeting signal).
-!- SUBUNIT: Interacts with SMAD4, MARK4, NUAK1 and BIRC5/survivin.
Interacts with DCX. {ECO:0000250}.
-!- INTERACTION:
A5PKW4:PSD (xeno); NbExp=3; IntAct=EBI-2214043, EBI-719999;
Q13485:SMAD4 (xeno); NbExp=4; IntAct=EBI-2214043, EBI-347263;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q93008}.
Cell projection, growth cone {ECO:0000269|PubMed:24607389}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues.
-!- DEVELOPMENTAL STAGE: At least expressed from 17 dpc to 21
postnatal days.
-!- DISRUPTION PHENOTYPE: Brain-specific USP9X deletion results in
early postnatal death, whereas forebrain-specific deletion is
compatible with survival to adulthood. In the absence of USP9X the
cortical architecture is disorganized, and neurons display reduced
neurite growth. {ECO:0000269|PubMed:24607389}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U67874; AAB07731.1; -; mRNA.
EMBL; AL669967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z78153; CAB01555.1; -; mRNA.
PIR; T30850; T30850.
RefSeq; NP_033507.2; NM_009481.2.
UniGene; Mm.242646; -.
SMR; P70398; -.
BioGrid; 204467; 11.
CORUM; P70398; -.
IntAct; P70398; 7.
MINT; MINT-4139688; -.
STRING; 10090.ENSMUSP00000086716; -.
MEROPS; C19.017; -.
iPTMnet; P70398; -.
PhosphoSitePlus; P70398; -.
SwissPalm; P70398; -.
EPD; P70398; -.
MaxQB; P70398; -.
PaxDb; P70398; -.
PeptideAtlas; P70398; -.
PRIDE; P70398; -.
DNASU; 22284; -.
GeneID; 22284; -.
KEGG; mmu:22284; -.
CTD; 8239; -.
MGI; MGI:894681; Usp9x.
eggNOG; KOG1866; Eukaryota.
eggNOG; COG5077; LUCA.
HOGENOM; HOG000231283; -.
HOVERGEN; HBG073749; -.
InParanoid; P70398; -.
KO; K11840; -.
PRO; PR:P70398; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_USP9X; -.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0070410; F:co-SMAD binding; ISS:BHF-UCL.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0048675; P:axon extension; IMP:UniProtKB.
GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:MGI.
GO; GO:0021698; P:cerebellar cortex structural organization; IMP:MGI.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0021766; P:hippocampus development; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
GO; GO:1990138; P:neuron projection extension; IGI:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
GO; GO:0050856; P:regulation of T cell receptor signaling pathway; ISO:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
SUPFAM; SSF48371; SSF48371; 5.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Cell projection; Chromosome partition;
Complete proteome; Cytoplasm; Hydrolase; Mitosis; Phosphoprotein;
Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
CHAIN 1 2559 Probable ubiquitin carboxyl-terminal
hydrolase FAF-X.
/FTId=PRO_0000080691.
DOMAIN 1557 1956 USP.
ACT_SITE 1566 1566 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
ACT_SITE 1879 1879 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 374 374 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000250|UniProtKB:Q93008}.
MOD_RES 1600 1600 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 2443 2443 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2540 2540 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 2547 2547 Phosphoserine.
{ECO:0000250|UniProtKB:Q93008}.
MOD_RES 2551 2551 Phosphothreonine.
{ECO:0000250|UniProtKB:Q93008}.
CONFLICT 73 73 A -> P (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 182 182 C -> F (in Ref. 3; CAB01555).
{ECO:0000305}.
CONFLICT 1243 1244 QK -> HQ (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1626 1626 D -> N (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1631 1631 S -> I (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1635 1635 D -> N (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1638 1638 E -> K (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1645 1645 R -> K (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1665 1665 R -> K (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1671 1671 F -> S (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1688 1689 EF -> KS (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1918 1918 N -> T (in Ref. 1; AAB07731).
{ECO:0000305}.
CONFLICT 1930 1930 F -> L (in Ref. 1; AAB07731).
{ECO:0000305}.
SEQUENCE 2559 AA; 290711 MW; CC380E9F44B410DD CRC64;
MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE QGQGDAPPQI
EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA AIDLSKKGLD VKSEACQRFF
RDGLTISFTK ILTDEAVSGW KFEIHRCIIN NTHRLVELCV AKLAQDWFPL LELLAMALNP
HCKFHIYNGT RPCESVSSSV QLPEDELFAR SPDPRSPKGW LVDLLNKFGT LNGFQILHDR
FINGSALNVQ IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DEELKKEAKN
EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG KMNALNEVNK
VISSVSYYTH RHGSSEDEEW LTAERMAEWI QQNNILSIVL RDSLHQPQYV EKLEKILRFV
IKEKALTLQD LDNIWAAQAG KHEAIVKNVH DLLAKLAWDF SPEQLDHLFD CFKASWTNAS
KKQREKLLEL IRRLAEDDKD GVMAHKVLNL LWNLAHSDDV PVDIMDLALS AHIKILDYSC
SQDRDTQKIQ WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQS QRSPHVFYRH
DLINQLQHNH ALVTLVAENL ATYMESMRMY GRDNEDYDPQ TVRLGSRYSH VQEVQERLNF
LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW YSKLMGDEPD LDPDINKDFF
ESNVLQLDPS LLTENGMKCF ERFFKAVNCR EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ
SNDDIACRAI DLLKEIYTNL GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSI
NCARQEAVRM VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFIV RFPNQGRQVD
DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPGDDRKLI GQLNLKDKSL
ITAKLTQISS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP EVESCLPGVI MSLHPRYISF
LWQVADLGSS LNMPPLRDGA RVLMKLMPPD STTIEKLRAI CLDHAKLGES SLSPSLDSLF
FGPSASQVLY LTEVVYALLM PAGAPLTDDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD
METRRGAYLN ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTSVNQV THDQAVVLQS
ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIQKIIWTSG CGGLQLVFSP
NEEVTKIYEK TNAGNEPDLE DEQVCCEALE VMTLCFALIP TALDALSKEK AWQTFIIDLL
LHCHSKTVRQ VAQEQFFLMC TRCCMGHRPL LFFITLLFTV LGSTARERAK HSGDYFTLLR
HLLNYAYNSN INVPNAEVLL NNEIDWLKRI RDDVKRTGET GVEETILEGH LGVTKELLAF
QTPEKKFHIG CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPATINA
GFELLVALAV GCVRNLKQIV DSLTEMYYIG TAITTCEALT EWEYLPPVGP RPPKGFVGLK
NAGATCYMNS VIQQLYMIPS IRNGILAIEG TGSDVDDDMS GDEKQDNESN VDPRDDVFGY
PQQFEDKPPL SKTEDRKEYN IGVLRHLQVI FGHLAASRLQ YYVPRGFWKQ FRLWGEPVNL
REQHDALEFF NSLVDSLDEA LKALGHPAML SKVLGGSFAD QKICQGCPHR YECEESFTTL
NVDIRNHQNL LDSLEQYVKG DLLEGANAYH CEKCNKKVDT VKRLLIKKLP PVLAIQLKRF
DYDWERECAI KFNDYFEFPR ELDMEPYTVA GVAKLEGDNV NPESQLIQQN EQSESEKAGS
TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGEKNRWYKF DDGDVTECKM DDDEEMKNQC
FGGEYMGEVF DHMMKRMSYR RQKRWWNAYI LFYERMDTIG HDDEVIRYIS EIAITTRPHQ
IVMPSAIERS VRKQNVQFMH NRMQYSLEYF QFMKKLLTCN GVYLNPPPGQ DHLSPEAEEI
TMISIQLAAR FLFTTGFHTK KIVRGSASDW YDALCILLRH SKNVRFWFAH NVLFNVSNRF
SEYLLECPSA EVRGAFAKLI VFIAHFSLQD GPCPSPFASP GPSSQAYDNL SLSDHLLRAV
LNLLRREVSE HGRHLQQYFN LFVMYANLGV AEKTQLLKLS VPATFMLVSL DEGPGPPIKY
QYAELGKLYS VVSQLIRCCN VSSRMQSSIN GNPSLPNPFG DPNLSQPIMP IQQNVVDILF
VRTSYVKKII EDCSNSDETV KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL
LQILLIEDSW QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSSCPV
AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE TSNGYFLERS
HSARMTLAKA CELCPEEEPD DQDAPDEHES PPPEDAPLYP HSPGSQYQQN NHVHGQPYTG
PAAHHMNNPQ RTGQRAQENY EGGEEVSPPQ TKGSVKCTY


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