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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, Fafl, Fam
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.

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 – 15661Nucleophile By similarity
Active sitei1879 – 18791Proton acceptor By similarity

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
Complete GO annotation...

GO - Biological processi

  1. BMP signaling pathway Source: UniProtKB
  2. axon extension Source: MGI
  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 projection extension Source: MGI
  10. post-embryonic development Source: MGI
  11. protein deubiquitination Source: UniProtKB
  12. transforming growth factor beta receptor signaling pathway Source: UniProtKB
  13. 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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25592559Probable ubiquitin carboxyl-terminal hydrolase FAF-X
PRO_0000080691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1600 – 16001Phosphoserine1 Publication
Modified residuei2443 – 24431Phosphoserine By similarity
Modified residuei2540 – 25401Phosphotyrosine1 Publication
Modified residuei2547 – 25471Phosphoserine By similarity
Modified residuei2551 – 25511Phosphothreonine By 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 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 – 1956400USP
Add
BLAST

Sequence similaritiesi

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

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731A → P in AAB07731. 1 Publication
Sequence conflicti182 – 1821C → F in CAB01555. 1 Publication
Sequence conflicti1243 – 12442QK → HQ in AAB07731. 1 Publication
Sequence conflicti1626 – 16261D → N in AAB07731. 1 Publication
Sequence conflicti1631 – 16311S → I in AAB07731. 1 Publication
Sequence conflicti1635 – 16351D → N in AAB07731. 1 Publication
Sequence conflicti1638 – 16381E → K in AAB07731. 1 Publication
Sequence conflicti1645 – 16451R → K in AAB07731. 1 Publication
Sequence conflicti1665 – 16651R → K in AAB07731. 1 Publication
Sequence conflicti1671 – 16711F → S in AAB07731. 1 Publication
Sequence conflicti1688 – 16892EF → KS in AAB07731. 1 Publication
Sequence conflicti1918 – 19181N → T in AAB07731. 1 Publication
Sequence conflicti1930 – 19301F → L in AAB07731. 1 Publication

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...

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.

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: September 3, 2014
This is version 123 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

Similar proteinsi