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P70398

- USP9X_MOUSE

UniProt

P70398 - USP9X_MOUSE

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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

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. 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
Complete GO annotation...

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. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB
Complete GO annotation...

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

        10         20         30         40         50
MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE
60 70 80 90 100
QGQGDAPPQI EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA
110 120 130 140 150
AIDLSKKGLD VKSEACQRFF RDGLTISFTK ILTDEAVSGW KFEIHRCIIN
160 170 180 190 200
NTHRLVELCV AKLAQDWFPL LELLAMALNP HCKFHIYNGT RPCESVSSSV
210 220 230 240 250
QLPEDELFAR SPDPRSPKGW LVDLLNKFGT LNGFQILHDR FINGSALNVQ
260 270 280 290 300
IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DEELKKEAKN
310 320 330 340 350
EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG
360 370 380 390 400
KMNALNEVNK VISSVSYYTH RHGSSEDEEW LTAERMAEWI QQNNILSIVL
410 420 430 440 450
RDSLHQPQYV EKLEKILRFV IKEKALTLQD LDNIWAAQAG KHEAIVKNVH
460 470 480 490 500
DLLAKLAWDF SPEQLDHLFD CFKASWTNAS KKQREKLLEL IRRLAEDDKD
510 520 530 540 550
GVMAHKVLNL LWNLAHSDDV PVDIMDLALS AHIKILDYSC SQDRDTQKIQ
560 570 580 590 600
WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQS QRSPHVFYRH
610 620 630 640 650
DLINQLQHNH ALVTLVAENL ATYMESMRMY GRDNEDYDPQ TVRLGSRYSH
660 670 680 690 700
VQEVQERLNF LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW
710 720 730 740 750
YSKLMGDEPD LDPDINKDFF ESNVLQLDPS LLTENGMKCF ERFFKAVNCR
760 770 780 790 800
EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ SNDDIACRAI DLLKEIYTNL
810 820 830 840 850
GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSI NCARQEAVRM
860 870 880 890 900
VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFIV RFPNQGRQVD
910 920 930 940 950
DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPGDDRKLI
960 970 980 990 1000
GQLNLKDKSL ITAKLTQISS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP
1010 1020 1030 1040 1050
EVESCLPGVI MSLHPRYISF LWQVADLGSS LNMPPLRDGA RVLMKLMPPD
1060 1070 1080 1090 1100
STTIEKLRAI CLDHAKLGES SLSPSLDSLF FGPSASQVLY LTEVVYALLM
1110 1120 1130 1140 1150
PAGAPLTDDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD METRRGAYLN
1160 1170 1180 1190 1200
ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTSVNQV THDQAVVLQS
1210 1220 1230 1240 1250
ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIQKIIWTSG
1260 1270 1280 1290 1300
CGGLQLVFSP NEEVTKIYEK TNAGNEPDLE DEQVCCEALE VMTLCFALIP
1310 1320 1330 1340 1350
TALDALSKEK AWQTFIIDLL LHCHSKTVRQ VAQEQFFLMC TRCCMGHRPL
1360 1370 1380 1390 1400
LFFITLLFTV LGSTARERAK HSGDYFTLLR HLLNYAYNSN INVPNAEVLL
1410 1420 1430 1440 1450
NNEIDWLKRI RDDVKRTGET GVEETILEGH LGVTKELLAF QTPEKKFHIG
1460 1470 1480 1490 1500
CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPATINA
1510 1520 1530 1540 1550
GFELLVALAV GCVRNLKQIV DSLTEMYYIG TAITTCEALT EWEYLPPVGP
1560 1570 1580 1590 1600
RPPKGFVGLK NAGATCYMNS VIQQLYMIPS IRNGILAIEG TGSDVDDDMS
1610 1620 1630 1640 1650
GDEKQDNESN VDPRDDVFGY PQQFEDKPPL SKTEDRKEYN IGVLRHLQVI
1660 1670 1680 1690 1700
FGHLAASRLQ YYVPRGFWKQ FRLWGEPVNL REQHDALEFF NSLVDSLDEA
1710 1720 1730 1740 1750
LKALGHPAML SKVLGGSFAD QKICQGCPHR YECEESFTTL NVDIRNHQNL
1760 1770 1780 1790 1800
LDSLEQYVKG DLLEGANAYH CEKCNKKVDT VKRLLIKKLP PVLAIQLKRF
1810 1820 1830 1840 1850
DYDWERECAI KFNDYFEFPR ELDMEPYTVA GVAKLEGDNV NPESQLIQQN
1860 1870 1880 1890 1900
EQSESEKAGS TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGEKNRWYKF
1910 1920 1930 1940 1950
DDGDVTECKM DDDEEMKNQC FGGEYMGEVF DHMMKRMSYR RQKRWWNAYI
1960 1970 1980 1990 2000
LFYERMDTIG HDDEVIRYIS EIAITTRPHQ IVMPSAIERS VRKQNVQFMH
2010 2020 2030 2040 2050
NRMQYSLEYF QFMKKLLTCN GVYLNPPPGQ DHLSPEAEEI TMISIQLAAR
2060 2070 2080 2090 2100
FLFTTGFHTK KIVRGSASDW YDALCILLRH SKNVRFWFAH NVLFNVSNRF
2110 2120 2130 2140 2150
SEYLLECPSA EVRGAFAKLI VFIAHFSLQD GPCPSPFASP GPSSQAYDNL
2160 2170 2180 2190 2200
SLSDHLLRAV LNLLRREVSE HGRHLQQYFN LFVMYANLGV AEKTQLLKLS
2210 2220 2230 2240 2250
VPATFMLVSL DEGPGPPIKY QYAELGKLYS VVSQLIRCCN VSSRMQSSIN
2260 2270 2280 2290 2300
GNPSLPNPFG DPNLSQPIMP IQQNVVDILF VRTSYVKKII EDCSNSDETV
2310 2320 2330 2340 2350
KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL LQILLIEDSW
2360 2370 2380 2390 2400
QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSSCPV
2410 2420 2430 2440 2450
AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE
2460 2470 2480 2490 2500
TSNGYFLERS HSARMTLAKA CELCPEEEPD DQDAPDEHES PPPEDAPLYP
2510 2520 2530 2540 2550
HSPGSQYQQN NHVHGQPYTG PAAHHMNNPQ RTGQRAQENY EGGEEVSPPQ

TKGSVKCTY
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

« Hide 'large scale' publications
  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 29, 2014
This is version 125 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