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Q93008

- USP9X_HUMAN

UniProt

Q93008 - USP9X_HUMAN

Protein

Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Gene

USP9X

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. May therefore play an important role 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. Involved in axonal growth and neuronal cell migration.4 Publications

    Catalytic activityi

    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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1566 – 15661NucleophilePROSITE-ProRule annotation
    Active sitei1879 – 18791Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. co-SMAD binding Source: BHF-UCL
    2. cysteine-type endopeptidase activity Source: ProtInc
    3. cysteine-type peptidase activity Source: ProtInc
    4. protein binding Source: UniProtKB
    5. ubiquitin thiolesterase activity Source: Reactome

    GO - Biological processi

    1. axon extension Source: UniProtKB
    2. BMP signaling pathway Source: UniProtKB
    3. chromosome segregation Source: UniProtKB-KW
    4. female gamete generation Source: ProtInc
    5. gene expression Source: Reactome
    6. mitotic nuclear division Source: UniProtKB-KW
    7. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
    8. neuron migration Source: UniProtKB
    9. protein deubiquitination Source: UniProtKB
    10. transcription, DNA-templated Source: Reactome
    11. transcription initiation from RNA polymerase II promoter Source: Reactome
    12. transforming growth factor beta receptor signaling pathway Source: UniProtKB
    13. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, Mitosis, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.

    Protein family/group databases

    MEROPSiC19.017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable ubiquitin carboxyl-terminal hydrolase FAF-X (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme FAF-X
    Fat facets in mammals
    Short name:
    hFAM
    Fat facets protein-related, X-linked
    Ubiquitin thioesterase FAF-X
    Ubiquitin-specific protease 9, X chromosome
    Ubiquitin-specific-processing protease FAF-X
    Gene namesi
    Name:USP9X
    Synonyms:DFFRX, FAM, USP9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12632. USP9X.

    Subcellular locationi

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. growth cone Source: UniProtKB
    5. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2093 – 20931L → H in MRX99; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones. 1 Publication
    VAR_071131
    Natural varianti2157 – 21571L → I in MRX99; unknown pathological significance; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones. 1 Publication
    VAR_071132

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi300919. phenotype.
    PharmGKBiPA37257.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25702570Probable ubiquitin carboxyl-terminal hydrolase FAF-XPRO_0000080689Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1600 – 16001Phosphoserine5 Publications
    Modified residuei2443 – 24431Phosphoserine3 Publications
    Modified residuei2556 – 25561Phosphotyrosine1 Publication
    Modified residuei2563 – 25631Phosphoserine3 Publications
    Modified residuei2567 – 25671Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ93008.
    PaxDbiQ93008.
    PRIDEiQ93008.

    PTM databases

    PhosphoSiteiQ93008.

    Expressioni

    Tissue specificityi

    Widely expressed in embryonic and adult tissues.

    Gene expression databases

    ArrayExpressiQ93008.
    BgeeiQ93008.
    CleanExiHS_USP9X.
    GenevestigatoriQ93008.

    Organism-specific databases

    HPAiCAB011618.

    Interactioni

    Subunit structurei

    Interacts with SMAD4, MARK4, NUAK1 and BIRC5/survivin. Interacts with DCX.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428588EBI-302524,EBI-466029
    SMAD4Q134852EBI-302524,EBI-347263

    Protein-protein interaction databases

    BioGridi113867. 99 interactions.
    DIPiDIP-27562N.
    IntActiQ93008. 23 interactions.
    MINTiMINT-5006529.
    STRINGi9606.ENSP00000316357.

    Structurei

    3D structure databases

    ProteinModelPortaliQ93008.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1557 – 1956400USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5077.
    HOGENOMiHOG000231283.
    HOVERGENiHBG073749.
    KOiK11840.
    OMAiMAQEQFF.
    OrthoDBiEOG722J7K.
    PhylomeDBiQ93008.
    TreeFamiTF323966.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 5 hits.
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q93008-3) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE     50
    QGQGDAPPQL EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA 100
    AIDLSKKGLD VKSEACQRFF RDGLTISFTK ILTDEAVSGW KFEIHRCIIN 150
    NTHRLVELCV AKLSQDWFPL LELLAMALNP HCKFHIYNGT RPCESVSSSV 200
    QLPEDELFAR SPDPRSPKGW LVDLLNKFGT LNGFQILHDR FINGSALNVQ 250
    IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DEELKKEAKN 300
    EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG 350
    KMNALNEVNK VISSVSYYTH RHGNPEEEEW LTAERMAEWI QQNNILSIVL 400
    RDSLHQPQYV EKLEKILRFV IKEKALTLQD LDNIWAAQAG KHEAIVKNVH 450
    DLLAKLAWDF SPEQLDHLFD CFKASWTNAS KKQREKLLEL IRRLAEDDKD 500
    GVMAHKVLNL LWNLAHSDDV PVDIMDLALS AHIKILDYSC SQDRDTQKIQ 550
    WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQT QRSPHVFYRH 600
    DLINQLQHNH ALVTLVAENL ATYMESMRLY ARDHEDYDPQ TVRLGSRYSH 650
    VQEVQERLNF LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW 700
    YSKLMGDEPD LDPDINKDFF ESNVLQLDPS LLTENGMKCF ERFFKAVNCR 750
    EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ SNDDIASRAI DLLKEIYTNL 800
    GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSV NCARQEAVRM 850
    VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFVV RFPNQGRQVD 900
    DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPADDRKLI 950
    GQLNLKDKSL ITAKLTQISS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP 1000
    EVESCLPGVI MSLHPRYISF LWQVADLGSS LNMPPLRDGA RVLMKLMPPD 1050
    STTIEKLRAI CLDHAKLGES SLSPSLDSLF FGPSASQVLY LTEVVYALLM 1100
    PAGAPLADDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD METRRGAYLN 1150
    ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTQINQV THDQAVVLQS 1200
    ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIQKIIWASG 1250
    CGSLQLVFSP NEEITKIYEK TNAGNEPDLE DEQVCCEALE VMTLCFALIP 1300
    TALDALSKEK AWQTFIIDLL LHCHSKTVRQ VAQEQFFLMC TRCCMGHRPL 1350
    LFFITLLFTV LGSTARERAK HSGDYFTLLR HLLNYAYNSN INVPNAEVLL 1400
    NNEIDWLKRI RDDVKRTGET GIEETILEGH LGVTKELLAF QTSEKKFHIG 1450
    CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPPTINA 1500
    GFELLVALAV GCVRNLKQIV DSLTEMYYIG TAITTCEALT EWEYLPPVGP 1550
    RPPKGFVGLK NAGATCYMNS VIQQLYMIPS IRNGILAIEG TGSDVDDDMS 1600
    GDEKQDNESN VDPRDDVFGY PQQFEDKPAL SKTEDRKEYN IGVLRHLQVI 1650
    FGHLAASRLQ YYVPRGFWKQ FRLWGEPVNL REQHDALEFF NSLVDSLDEA 1700
    LKALGHPAML SKVLGGSFAD QKICQGCPHR YECEESFTTL NVDIRNHQNL 1750
    LDSLEQYVKG DLLEGANAYH CEKCNKKVDT VKRLLIKKLP PVLAIQLKRF 1800
    DYDWERECAI KFNDYFEFPR ELDMEPYTVA GVAKLEGDNV NPESQLIQQS 1850
    EQSESETAGS TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGERNRWYKF 1900
    DDGDVTECKM DDDEEMKNQC FGGEYMGEVF DHMMKRMSYR RQKRWWNAYI 1950
    LFYERMDTID QDDELIRYIS ELAITTRPHQ IIMPSAIERS VRKQNVQFMH 2000
    NRMQYSMEYF QFMKKLLTCN GVYLNPPPGQ DHLLPEAEEI TMISIQLAAR 2050
    FLFTTGFHTK KVVRGSASDW YDALCILLRH SKNVRFWFAH NVLFNVSNRF 2100
    SEYLLECPSA EVRGAFAKLI VFIAHFSLQD GPCPSPFASP GPSSQAYDNL 2150
    SLSDHLLRAV LNLLRREVSE HGRHLQQYFN LFVMYANLGV AEKTQLLKLS 2200
    VPATFMLVSL DEGPGPPIKY QYAELGKLYS VVSQLIRCCN VSSRMQSSIN 2250
    GNPPLPNPFG DPNLSQPIMP IQQNVADILF VRTSYVKKII EDCSNSEETV 2300
    KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL LQILLIEDSW 2350
    QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSNCPV 2400
    AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE 2450
    TSNGYFLERS HSARMTLAKA CELCPEEVKK ATSVQQIEME ESKEPDDQDA 2500
    PDEHESPPPE DAPLYPHSPG SQYQQNNHVH GQPYTGPAAH HMNNPQRTGQ 2550
    RAQENYEGSE EVSPPQTKDQ 2570
    Length:2,570
    Mass (Da):292,280
    Last modified:January 11, 2011 - v3
    Checksum:i84CB979A405AA56F
    GO
    Isoform 2 (identifier: Q93008-1) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         2478-2493: Missing.

    Show »
    Length:2,554
    Mass (Da):290,463
    Checksum:i16B87B7FCC1428AF
    GO

    Sequence cautioni

    The sequence CAD13527.2 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAD18900.2 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251Q → L in CAA66942. (PubMed:8922996)Curated
    Sequence conflicti148 – 1547Missing in CAA66942. (PubMed:8922996)Curated
    Sequence conflicti468 – 4681L → P in CAA66942. (PubMed:8922996)Curated
    Sequence conflicti476 – 4761W → R in CAA66942. (PubMed:8922996)Curated
    Sequence conflicti506 – 5061K → R in CAA66942. (PubMed:8922996)Curated
    Sequence conflicti621 – 6211A → V in CAA66942. (PubMed:8922996)Curated
    Sequence conflicti1400 – 14001L → F in CAA66942. (PubMed:8922996)Curated
    Sequence conflicti1951 – 19511L → P in CAA66942. (PubMed:8922996)Curated
    Sequence conflicti2330 – 23301T → P in CAA66942. (PubMed:8922996)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2093 – 20931L → H in MRX99; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones. 1 Publication
    VAR_071131
    Natural varianti2157 – 21571L → I in MRX99; unknown pathological significance; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones. 1 Publication
    VAR_071132

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2478 – 249316Missing in isoform 2. 1 PublicationVSP_040478Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98296 mRNA. Translation: CAA66942.1.
    AL391259, AL109797 Genomic DNA. Translation: CAD13527.2. Sequence problems.
    AL109797, AL391259 Genomic DNA. Translation: CAD18900.2. Sequence problems.
    AF070645 mRNA. Translation: AAC25395.1.
    CCDSiCCDS43930.1. [Q93008-3]
    CCDS55403.1. [Q93008-1]
    RefSeqiNP_001034679.2. NM_001039590.2. [Q93008-3]
    NP_001034680.2. NM_001039591.2. [Q93008-1]
    UniGeneiHs.77578.

    Genome annotation databases

    EnsembliENST00000324545; ENSP00000316357; ENSG00000124486. [Q93008-3]
    ENST00000378308; ENSP00000367558; ENSG00000124486. [Q93008-1]
    GeneIDi8239.
    KEGGihsa:8239.
    UCSCiuc004dfb.3. human. [Q93008-3]
    uc004dfc.3. human. [Q93008-1]

    Polymorphism databases

    DMDMi317373496.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98296 mRNA. Translation: CAA66942.1 .
    AL391259 , AL109797 Genomic DNA. Translation: CAD13527.2 . Sequence problems.
    AL109797 , AL391259 Genomic DNA. Translation: CAD18900.2 . Sequence problems.
    AF070645 mRNA. Translation: AAC25395.1 .
    CCDSi CCDS43930.1. [Q93008-3 ]
    CCDS55403.1. [Q93008-1 ]
    RefSeqi NP_001034679.2. NM_001039590.2. [Q93008-3 ]
    NP_001034680.2. NM_001039591.2. [Q93008-1 ]
    UniGenei Hs.77578.

    3D structure databases

    ProteinModelPortali Q93008.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113867. 99 interactions.
    DIPi DIP-27562N.
    IntActi Q93008. 23 interactions.
    MINTi MINT-5006529.
    STRINGi 9606.ENSP00000316357.

    Chemistry

    ChEMBLi CHEMBL2406899.

    Protein family/group databases

    MEROPSi C19.017.

    PTM databases

    PhosphoSitei Q93008.

    Polymorphism databases

    DMDMi 317373496.

    Proteomic databases

    MaxQBi Q93008.
    PaxDbi Q93008.
    PRIDEi Q93008.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324545 ; ENSP00000316357 ; ENSG00000124486 . [Q93008-3 ]
    ENST00000378308 ; ENSP00000367558 ; ENSG00000124486 . [Q93008-1 ]
    GeneIDi 8239.
    KEGGi hsa:8239.
    UCSCi uc004dfb.3. human. [Q93008-3 ]
    uc004dfc.3. human. [Q93008-1 ]

    Organism-specific databases

    CTDi 8239.
    GeneCardsi GC0XP040944.
    HGNCi HGNC:12632. USP9X.
    HPAi CAB011618.
    MIMi 300072. gene.
    300919. phenotype.
    neXtProti NX_Q93008.
    PharmGKBi PA37257.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5077.
    HOGENOMi HOG000231283.
    HOVERGENi HBG073749.
    KOi K11840.
    OMAi MAQEQFF.
    OrthoDBi EOG722J7K.
    PhylomeDBi Q93008.
    TreeFami TF323966.

    Enzyme and pathway databases

    Reactomei REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.

    Miscellaneous databases

    ChiTaRSi USP9X. human.
    GeneWikii USP9X.
    GenomeRNAii 8239.
    NextBioi 30989.
    PROi Q93008.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q93008.
    Bgeei Q93008.
    CleanExi HS_USP9X.
    Genevestigatori Q93008.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 5 hits.
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Drosophila developmental gene fat facets has a human homologue in Xp11.4 which escapes X-inactivation and has related sequences on Yq11.2."
      Jones M.H., Furlong R.A., Burkin H., Chalmers I.J., Brown G.M., Khwaja O., Affara N.A.
      Hum. Mol. Genet. 5:1695-1701(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fetal brain, Retina and Testis.
    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. "The DNA sequence of the human X chromosome."
      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.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Yu W., Gibbs R.A.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2226-2570 (ISOFORM 1).
      Tissue: Brain.
    5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      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.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Chromosome alignment and segregation regulated by ubiquitination of survivin."
      Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.
      Science 310:1499-1504(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BIRC5.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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."
      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.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains."
      Al-Hakim A.K., Zagorska A., Chapman L., Deak M., Peggie M., Alessi D.R.
      Biochem. J. 411:249-260(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MARK4 AND NUAK1.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600; SER-2443 AND SER-2563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination."
      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.
      Cell 136:123-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMAD4, SUBCELLULAR LOCATION.
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563 AND THR-2567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600 AND SER-2443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Mutations in USP9X are associated with X-linked intellectual disability and disrupt neuronal cell migration and growth."
      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.
      Am. J. Hum. Genet. 94:470-478(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DCX, SUBCELLULAR LOCATION, VARIANTS MRX99 HIS-2093 AND ILE-2157, CHARACTERIZATION OF VARIANTS MRX99 HIS-2093 AND ILE-2157.

    Entry informationi

    Entry nameiUSP9X_HUMAN
    AccessioniPrimary (citable) accession number: Q93008
    Secondary accession number(s): O75550, Q8WWT3, Q8WX12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Escapes X-inactivation.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3