Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P70398

- USP9X_MOUSE

UniProt

P70398 - USP9X_MOUSE

Protein

Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Gene

Usp9x

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 By similarity. Involved in axonal growth and neuronal cell migration.By similarity1 Publication

    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 peptidase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. ubiquitinyl hydrolase activity Source: InterPro

    GO - Biological processi

    1. axon extension Source: UniProtKB
    2. BMP signaling pathway Source: UniProtKB
    3. cellular response to transforming growth factor beta stimulus Source: MGI
    4. cerebellar cortex structural organization Source: MGI
    5. chromosome segregation Source: UniProtKB-KW
    6. hippocampus development Source: MGI
    7. in utero embryonic development Source: MGI
    8. mitotic nuclear division Source: UniProtKB-KW
    9. neuron migration Source: UniProtKB
    10. neuron projection extension Source: MGI
    11. post-embryonic development Source: MGI
    12. protein deubiquitination Source: UniProtKB
    13. transforming growth factor beta receptor signaling pathway Source: UniProtKB
    14. 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

    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 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
    Gene namesi
    Name:Usp9x
    Synonyms:Fafl, Fam
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:894681. Usp9x.

    Subcellular locationi

    Cytoplasm By similarity. Cell projectiongrowth cone 1 Publication

    GO - Cellular componenti

    1. apical part of cell Source: MGI
    2. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25592559Probable ubiquitin carboxyl-terminal hydrolase FAF-XPRO_0000080691Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1600 – 16001Phosphoserine1 Publication
    Modified residuei2443 – 24431PhosphoserineBy similarity
    Modified residuei2540 – 25401Phosphotyrosine1 Publication
    Modified residuei2547 – 25471PhosphoserineBy similarity
    Modified residuei2551 – 25511PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP70398.
    PaxDbiP70398.
    PRIDEiP70398.

    PTM databases

    PhosphoSiteiP70398.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in adult tissues.

    Developmental stagei

    At least expressed from 17 dpc to 21 postnatal days.

    Gene expression databases

    CleanExiMM_USP9X.
    GenevestigatoriP70398.

    Interactioni

    Subunit structurei

    Interacts with SMAD4, MARK4, NUAK1 and BIRC5/survivin. Interacts with DCX.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PSDA5PKW43EBI-2214043,EBI-719999From a different organism.
    SMAD4Q134854EBI-2214043,EBI-347263From a different organism.

    Protein-protein interaction databases

    BioGridi204467. 5 interactions.
    IntActiP70398. 7 interactions.
    MINTiMINT-4139688.

    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.
    InParanoidiP70398.
    KOiK11840.

    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]

    Sequencei

    Sequence statusi: Complete.

    P70398-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE     50
    QGQGDAPPQI EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA 100
    AIDLSKKGLD VKSEACQRFF RDGLTISFTK ILTDEAVSGW KFEIHRCIIN 150
    NTHRLVELCV AKLAQDWFPL LELLAMALNP HCKFHIYNGT RPCESVSSSV 200
    QLPEDELFAR SPDPRSPKGW LVDLLNKFGT LNGFQILHDR FINGSALNVQ 250
    IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DEELKKEAKN 300
    EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG 350
    KMNALNEVNK VISSVSYYTH RHGSSEDEEW LTAERMAEWI QQNNILSIVL 400
    RDSLHQPQYV EKLEKILRFV IKEKALTLQD LDNIWAAQAG KHEAIVKNVH 450
    DLLAKLAWDF SPEQLDHLFD CFKASWTNAS KKQREKLLEL IRRLAEDDKD 500
    GVMAHKVLNL LWNLAHSDDV PVDIMDLALS AHIKILDYSC SQDRDTQKIQ 550
    WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQS QRSPHVFYRH 600
    DLINQLQHNH ALVTLVAENL ATYMESMRMY GRDNEDYDPQ TVRLGSRYSH 650
    VQEVQERLNF LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW 700
    YSKLMGDEPD LDPDINKDFF ESNVLQLDPS LLTENGMKCF ERFFKAVNCR 750
    EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ SNDDIACRAI DLLKEIYTNL 800
    GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSI NCARQEAVRM 850
    VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFIV RFPNQGRQVD 900
    DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPGDDRKLI 950
    GQLNLKDKSL ITAKLTQISS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP 1000
    EVESCLPGVI MSLHPRYISF LWQVADLGSS LNMPPLRDGA RVLMKLMPPD 1050
    STTIEKLRAI CLDHAKLGES SLSPSLDSLF FGPSASQVLY LTEVVYALLM 1100
    PAGAPLTDDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD METRRGAYLN 1150
    ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTSVNQV THDQAVVLQS 1200
    ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIQKIIWTSG 1250
    CGGLQLVFSP NEEVTKIYEK TNAGNEPDLE DEQVCCEALE VMTLCFALIP 1300
    TALDALSKEK AWQTFIIDLL LHCHSKTVRQ VAQEQFFLMC TRCCMGHRPL 1350
    LFFITLLFTV LGSTARERAK HSGDYFTLLR HLLNYAYNSN INVPNAEVLL 1400
    NNEIDWLKRI RDDVKRTGET GVEETILEGH LGVTKELLAF QTPEKKFHIG 1450
    CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPATINA 1500
    GFELLVALAV GCVRNLKQIV DSLTEMYYIG TAITTCEALT EWEYLPPVGP 1550
    RPPKGFVGLK NAGATCYMNS VIQQLYMIPS IRNGILAIEG TGSDVDDDMS 1600
    GDEKQDNESN VDPRDDVFGY PQQFEDKPPL 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 NPESQLIQQN 1850
    EQSESEKAGS TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGEKNRWYKF 1900
    DDGDVTECKM DDDEEMKNQC FGGEYMGEVF DHMMKRMSYR RQKRWWNAYI 1950
    LFYERMDTIG HDDEVIRYIS EIAITTRPHQ IVMPSAIERS VRKQNVQFMH 2000
    NRMQYSLEYF QFMKKLLTCN GVYLNPPPGQ DHLSPEAEEI TMISIQLAAR 2050
    FLFTTGFHTK KIVRGSASDW YDALCILLRH SKNVRFWFAH NVLFNVSNRF 2100
    SEYLLECPSA EVRGAFAKLI VFIAHFSLQD GPCPSPFASP GPSSQAYDNL 2150
    SLSDHLLRAV LNLLRREVSE HGRHLQQYFN LFVMYANLGV AEKTQLLKLS 2200
    VPATFMLVSL DEGPGPPIKY QYAELGKLYS VVSQLIRCCN VSSRMQSSIN 2250
    GNPSLPNPFG DPNLSQPIMP IQQNVVDILF VRTSYVKKII EDCSNSDETV 2300
    KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL LQILLIEDSW 2350
    QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSSCPV 2400
    AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE 2450
    TSNGYFLERS HSARMTLAKA CELCPEEEPD DQDAPDEHES PPPEDAPLYP 2500
    HSPGSQYQQN NHVHGQPYTG PAAHHMNNPQ RTGQRAQENY EGGEEVSPPQ 2550
    TKGSVKCTY 2559
    Length:2,559
    Mass (Da):290,711
    Last modified:July 27, 2011 - v2
    Checksum:iCC380E9F44B410DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731A → P in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti182 – 1821C → F in CAB01555. (PubMed:9119401)Curated
    Sequence conflicti1243 – 12442QK → HQ in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1626 – 16261D → N in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1631 – 16311S → I in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1635 – 16351D → N in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1638 – 16381E → K in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1645 – 16451R → K in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1665 – 16651R → K in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1671 – 16711F → S in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1688 – 16892EF → KS in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1918 – 19181N → T in AAB07731. (PubMed:9178254)Curated
    Sequence conflicti1930 – 19301F → L in AAB07731. (PubMed:9178254)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67874 mRNA. Translation: AAB07731.1.
    AL669967 Genomic DNA. No translation available.
    Z78153 mRNA. Translation: CAB01555.1.
    PIRiT30850.
    RefSeqiNP_033507.2. NM_009481.2.
    UniGeneiMm.242646.

    Genome annotation databases

    GeneIDi22284.
    KEGGimmu:22284.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67874 mRNA. Translation: AAB07731.1 .
    AL669967 Genomic DNA. No translation available.
    Z78153 mRNA. Translation: CAB01555.1 .
    PIRi T30850.
    RefSeqi NP_033507.2. NM_009481.2.
    UniGenei Mm.242646.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204467. 5 interactions.
    IntActi P70398. 7 interactions.
    MINTi MINT-4139688.

    Protein family/group databases

    MEROPSi C19.017.

    PTM databases

    PhosphoSitei P70398.

    Proteomic databases

    MaxQBi P70398.
    PaxDbi P70398.
    PRIDEi P70398.

    Protocols and materials databases

    DNASUi 22284.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 22284.
    KEGGi mmu:22284.

    Organism-specific databases

    CTDi 8239.
    MGIi MGI:894681. Usp9x.

    Phylogenomic databases

    eggNOGi COG5077.
    HOGENOMi HOG000231283.
    HOVERGENi HBG073749.
    InParanoidi P70398.
    KOi K11840.

    Miscellaneous databases

    NextBioi 302415.
    PROi P70398.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_USP9X.
    Genevestigatori P70398.

    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. "Cloning and expression analysis of a novel mouse gene with sequence similarity to the Drosophila fat facets gene."
      Wood S.A., Pascoe W.S., Ru K., Yamada T., Hirchenhain J., Kemler R., Mattick J.S.
      Mech. Dev. 63:29-38(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Cloning of the genes encoding two murine and human cochlear unconventional type I myosins."
      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.
      Genomics 40:332-341(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 152-240.
      Tissue: Cochlea.
    4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "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: SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiUSP9X_MOUSE
    AccessioniPrimary (citable) accession number: P70398
    Secondary accession number(s): E9QLY0, Q62497
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3