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Probable ubiquitin carboxyl-terminal hydrolase FAF-X (EC 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)

 USP9X_HUMAN             Reviewed;        2570 AA.
Q93008; O75550; Q8WWT3; Q8WX12;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
20-JUN-2018, entry version 187.
RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase FAF-X;
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme FAF-X;
AltName: Full=Fat facets in mammals;
Short=hFAM;
AltName: Full=Fat facets protein-related, X-linked;
AltName: Full=Ubiquitin thioesterase FAF-X;
AltName: Full=Ubiquitin-specific protease 9, X chromosome;
AltName: Full=Ubiquitin-specific-processing protease FAF-X;
Name=USP9X {ECO:0000312|HGNC:HGNC:12632}; Synonyms=DFFRX, FAM, USP9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Fetal brain, Retina, and Testis;
PubMed=8922996; DOI=10.1093/hmg/5.11.1695;
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. Mol. Genet. 5:1695-1701(1996).
[2]
ERRATUM.
Jones M.H., Furlong R.A., Burkin H., Chalmers I.J., Brown G.M.,
Khwaja O., Affara N.A.;
Hum. Mol. Genet. 6:334-335(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2226-2570 (ISOFORM 1).
TISSUE=Brain;
Yu W., Gibbs R.A.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2556, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[6]
FUNCTION, AND INTERACTION WITH BIRC5.
PubMed=16322459; DOI=10.1126/science.1120160;
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2443, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[10]
FUNCTION, AND INTERACTION WITH MARK4 AND NUAK1.
PubMed=18254724; DOI=10.1042/BJ20080067;
Al-Hakim A.K., Zagorska A., Chapman L., Deak M., Peggie M.,
Alessi D.R.;
"Control of AMPK-related kinases by USP9X and atypical
Lys(29)/Lys(33)-linked polyubiquitin chains.";
Biochem. J. 411:249-260(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600; SER-2443 AND
SER-2563, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
FUNCTION, INTERACTION WITH SMAD4, AND SUBCELLULAR LOCATION.
PubMed=19135894; DOI=10.1016/j.cell.2008.10.051;
Dupont S., Mamidi A., Cordenonsi M., Montagner M., Zacchigna L.,
Adorno M., Martello G., Stinchfield M.J., Soligo S., Morsut L.,
Inui M., Moro S., Modena N., Argenton F., Newfeld S.J., Piccolo S.;
"FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling,
controls Smad4 monoubiquitination.";
Cell 136:123-135(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563 AND THR-2567, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600 AND SER-2443, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; THR-590; SER-1600;
SER-2443 AND SER-2563, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
FUNCTION, INTERACTION WITH DCX, SUBCELLULAR LOCATION, VARIANTS MRX99
HIS-2093 AND ILE-2157, AND CHARACTERIZATION OF VARIANTS MRX99 HIS-2093
AND ILE-2157.
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).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
INTERACTION WITH OTUD4; ALKBH3 AND USP7, AND FUNCTION.
PubMed=25944111; DOI=10.15252/embj.201490497;
Zhao Y., Majid M.C., Soll J.M., Brickner J.R., Dango S.,
Mosammaparast N.;
"Noncanonical regulation of alkylation damage resistance by the OTUD4
deubiquitinase.";
EMBO J. 34:1687-1703(2015).
-!- 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. Specifically hydrolyzes 'Lys-48'-, 'Lys-
29'- and 'Lys-33'-linked polyubiquitins chains. Essential
component of TGF-beta/BMP signaling cascade. Specifically
deubiquitinates monoubiquitinated SMAD4, opposing the activity of
E3 ubiquitin-protein ligase TRIM33. Deubiquitinates alkylation
repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize
ALKBH3, thereby promoting the repair of alkylated DNA lesions
(PubMed:25944111). Regulates chromosome alignment and segregation
in mitosis by regulating the localization of BIRC5/survivin to
mitotic centromeres. Involved in axonal growth and neuronal cell
migration (PubMed:16322459, PubMed:18254724, PubMed:19135894,
PubMed:24607389). {ECO:0000269|PubMed:16322459,
ECO:0000269|PubMed:18254724, ECO:0000269|PubMed:19135894,
ECO:0000269|PubMed:24607389, ECO:0000269|PubMed:25944111}.
-!- 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. Interacts with OTUD4 and USP7; the interaction
is direct (PubMed:25944111). {ECO:0000269|PubMed:16322459,
ECO:0000269|PubMed:18254724, ECO:0000269|PubMed:19135894,
ECO:0000269|PubMed:24607389, ECO:0000269|PubMed:25944111}.
-!- INTERACTION:
P42858:HTT; NbExp=8; IntAct=EBI-302524, EBI-466029;
P08393:ICP0 (xeno); NbExp=3; IntAct=EBI-302524, EBI-6148881;
Q07820:MCL1; NbExp=10; IntAct=EBI-302524, EBI-1003422;
Q13485:SMAD4; NbExp=2; IntAct=EBI-302524, EBI-347263;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19135894}.
Cell projection, growth cone {ECO:0000269|PubMed:24607389}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=Q93008-3; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=Q93008-1; Sequence=VSP_040478;
-!- TISSUE SPECIFICITY: Widely expressed in embryonic and adult
tissues.
-!- DISEASE: Mental retardation, X-linked 99 (MRX99) [MIM:300919]: A
disorder characterized by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
Intellectual deficiency is the only primary symptom of non-
syndromic X-linked mental retardation, while syndromic mental
retardation presents with associated physical, neurological and/or
psychiatric manifestations. {ECO:0000269|PubMed:24607389}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Escapes X-inactivation.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD13527.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAD18900.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X98296; CAA66942.1; -; mRNA.
EMBL; AL391259; CAD13527.2; ALT_SEQ; Genomic_DNA.
EMBL; AL109797; CAD13527.2; JOINED; Genomic_DNA.
EMBL; AL109797; CAD18900.2; ALT_SEQ; Genomic_DNA.
EMBL; AL391259; CAD18900.2; JOINED; Genomic_DNA.
EMBL; AF070645; AAC25395.1; -; mRNA.
CCDS; CCDS43930.1; -. [Q93008-3]
CCDS; CCDS55403.1; -. [Q93008-1]
RefSeq; NP_001034679.2; NM_001039590.2. [Q93008-3]
RefSeq; NP_001034680.2; NM_001039591.2. [Q93008-1]
UniGene; Hs.77578; -.
PDB; 5VBD; X-ray; 1.50 A; A=880-970.
PDBsum; 5VBD; -.
ProteinModelPortal; Q93008; -.
SMR; Q93008; -.
BioGrid; 113867; 158.
CORUM; Q93008; -.
DIP; DIP-27562N; -.
IntAct; Q93008; 42.
MINT; Q93008; -.
STRING; 9606.ENSP00000316357; -.
BindingDB; Q93008; -.
ChEMBL; CHEMBL2406899; -.
MEROPS; C19.017; -.
iPTMnet; Q93008; -.
PhosphoSitePlus; Q93008; -.
BioMuta; USP9X; -.
DMDM; 317373496; -.
EPD; Q93008; -.
MaxQB; Q93008; -.
PaxDb; Q93008; -.
PeptideAtlas; Q93008; -.
PRIDE; Q93008; -.
ProteomicsDB; 75667; -.
ProteomicsDB; 75668; -. [Q93008-1]
Ensembl; ENST00000324545; ENSP00000316357; ENSG00000124486. [Q93008-3]
Ensembl; ENST00000378308; ENSP00000367558; ENSG00000124486. [Q93008-1]
GeneID; 8239; -.
KEGG; hsa:8239; -.
UCSC; uc004dfb.3; human. [Q93008-3]
CTD; 8239; -.
DisGeNET; 8239; -.
EuPathDB; HostDB:ENSG00000124486.12; -.
GeneCards; USP9X; -.
HGNC; HGNC:12632; USP9X.
HPA; CAB011618; -.
HPA; CAB070164; -.
HPA; HPA047417; -.
MalaCards; USP9X; -.
MIM; 300072; gene.
MIM; 300919; phenotype.
neXtProt; NX_Q93008; -.
OpenTargets; ENSG00000124486; -.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA37257; -.
eggNOG; KOG1866; Eukaryota.
eggNOG; COG5077; LUCA.
GeneTree; ENSGT00760000119158; -.
HOGENOM; HOG000231283; -.
HOVERGEN; HBG073749; -.
InParanoid; Q93008; -.
KO; K11840; -.
OMA; HSALQFY; -.
OrthoDB; EOG091G0069; -.
PhylomeDB; Q93008; -.
TreeFam; TF323966; -.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-9033241; Peroxisomal protein import.
Reactome; R-HSA-977225; Amyloid fiber formation.
SIGNOR; Q93008; -.
ChiTaRS; USP9X; human.
GeneWiki; USP9X; -.
GenomeRNAi; 8239; -.
PRO; PR:Q93008; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000124486; -.
CleanEx; HS_USP9X; -.
Genevisible; Q93008; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0070410; F:co-SMAD binding; IPI:BHF-UCL.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:Reactome.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; EXP:Reactome.
GO; GO:0048675; P:axon extension; IMP:UniProtKB.
GO; GO:0030509; P:BMP signaling pathway; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
GO; GO:1901537; P:positive regulation of DNA demethylation; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
SUPFAM; SSF48371; SSF48371; 5.
SUPFAM; SSF54001; SSF54001; 2.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Cell projection; Chromosome partition; Complete proteome; Cytoplasm;
Disease mutation; Hydrolase; Mental retardation; Mitosis;
Phosphoprotein; Protease; Reference proteome; Thiol protease;
Ubl conjugation pathway.
CHAIN 1 2570 Probable ubiquitin carboxyl-terminal
hydrolase FAF-X.
/FTId=PRO_0000080689.
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 588 588 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 590 590 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1600 1600 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2443 2443 Phosphoserine.
{ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2556 2556 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 2563 2563 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2567 2567 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 2478 2493 Missing (in isoform 2).
{ECO:0000303|PubMed:8922996}.
/FTId=VSP_040478.
VARIANT 2093 2093 L -> H (in MRX99; does not affect
interaction with DCX; reduced subcellular
localization in the axonal growth cones;
dbSNP:rs587777317).
{ECO:0000269|PubMed:24607389}.
/FTId=VAR_071131.
VARIANT 2157 2157 L -> I (in MRX99; unknown pathological
significance; does not affect interaction
with DCX; reduced subcellular
localization in the axonal growth cones;
dbSNP:rs587777319).
{ECO:0000269|PubMed:24607389}.
/FTId=VAR_071132.
CONFLICT 25 25 Q -> L (in Ref. 1; CAA66942).
{ECO:0000305}.
CONFLICT 148 154 Missing (in Ref. 1; CAA66942).
{ECO:0000305}.
CONFLICT 468 468 L -> P (in Ref. 1; CAA66942).
{ECO:0000305}.
CONFLICT 476 476 W -> R (in Ref. 1; CAA66942).
{ECO:0000305}.
CONFLICT 506 506 K -> R (in Ref. 1; CAA66942).
{ECO:0000305}.
CONFLICT 621 621 A -> V (in Ref. 1; CAA66942).
{ECO:0000305}.
CONFLICT 1400 1400 L -> F (in Ref. 1; CAA66942).
{ECO:0000305}.
CONFLICT 1951 1951 L -> P (in Ref. 1; CAA66942).
{ECO:0000305}.
CONFLICT 2330 2330 T -> P (in Ref. 1; CAA66942).
{ECO:0000305}.
STRAND 889 891 {ECO:0000244|PDB:5VBD}.
HELIX 912 928 {ECO:0000244|PDB:5VBD}.
STRAND 930 936 {ECO:0000244|PDB:5VBD}.
HELIX 943 945 {ECO:0000244|PDB:5VBD}.
HELIX 950 952 {ECO:0000244|PDB:5VBD}.
STRAND 960 967 {ECO:0000244|PDB:5VBD}.
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


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