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P70398 (USP9X_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Usp9x
Synonyms:Fafl, Fam
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2559 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 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 structure

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

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Ubiquitously expressed in adult tissues.

Developmental stage

At least expressed from 17 dpc to 21 postnatal days.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Chromosome partition
Mitosis
Ubl conjugation pathway
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

axon extension

Inferred from mutant phenotype PubMed 23861879. Source: MGI

cellular response to transforming growth factor beta stimulus

Inferred from mutant phenotype PubMed 23861879. Source: MGI

cerebellar cortex structural organization

Inferred from mutant phenotype PubMed 23861879. Source: MGI

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

hippocampus development

Inferred from mutant phenotype PubMed 23861879. Source: MGI

in utero embryonic development

Inferred from genetic interaction PubMed 23861879. Source: MGI

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection extension

Inferred from genetic interaction PubMed 23861879. Source: MGI

post-embryonic development

Inferred from mutant phenotype PubMed 23861879. Source: MGI

protein deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentapical part of cell

Inferred from direct assay PubMed 10704870. Source: MGI

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionco-SMAD binding

Inferred from sequence or structural similarity. Source: BHF-UCL

cysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 19135894PubMed 20339350. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PSDA5PKW43EBI-2214043,EBI-719999From a different organism.
SMAD4Q134854EBI-2214043,EBI-347263From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25592559Probable ubiquitin carboxyl-terminal hydrolase FAF-X
PRO_0000080691

Regions

Domain1557 – 1956400USP

Sites

Active site15661Nucleophile By similarity
Active site18791Proton acceptor By similarity

Amino acid modifications

Modified residue16001Phosphoserine Ref.5
Modified residue24431Phosphoserine By similarity
Modified residue25401Phosphotyrosine Ref.4
Modified residue25471Phosphoserine By similarity
Modified residue25511Phosphothreonine By similarity

Experimental info

Sequence conflict731A → P in AAB07731. Ref.1
Sequence conflict1821C → F in CAB01555. Ref.3
Sequence conflict1243 – 12442QK → HQ in AAB07731. Ref.1
Sequence conflict16261D → N in AAB07731. Ref.1
Sequence conflict16311S → I in AAB07731. Ref.1
Sequence conflict16351D → N in AAB07731. Ref.1
Sequence conflict16381E → K in AAB07731. Ref.1
Sequence conflict16451R → K in AAB07731. Ref.1
Sequence conflict16651R → K in AAB07731. Ref.1
Sequence conflict16711F → S in AAB07731. Ref.1
Sequence conflict1688 – 16892EF → KS in AAB07731. Ref.1
Sequence conflict19181N → T in AAB07731. Ref.1
Sequence conflict19301F → L in AAB07731. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P70398 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: CC380E9F44B410DD

FASTA2,559290,711
        10         20         30         40         50         60 
MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE QGQGDAPPQI 

        70         80         90        100        110        120 
EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA AIDLSKKGLD VKSEACQRFF 

       130        140        150        160        170        180 
RDGLTISFTK ILTDEAVSGW KFEIHRCIIN NTHRLVELCV AKLAQDWFPL LELLAMALNP 

       190        200        210        220        230        240 
HCKFHIYNGT RPCESVSSSV QLPEDELFAR SPDPRSPKGW LVDLLNKFGT LNGFQILHDR 

       250        260        270        280        290        300 
FINGSALNVQ IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DEELKKEAKN 

       310        320        330        340        350        360 
EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG KMNALNEVNK 

       370        380        390        400        410        420 
VISSVSYYTH RHGSSEDEEW LTAERMAEWI QQNNILSIVL RDSLHQPQYV EKLEKILRFV 

       430        440        450        460        470        480 
IKEKALTLQD LDNIWAAQAG KHEAIVKNVH DLLAKLAWDF SPEQLDHLFD CFKASWTNAS 

       490        500        510        520        530        540 
KKQREKLLEL IRRLAEDDKD GVMAHKVLNL LWNLAHSDDV PVDIMDLALS AHIKILDYSC 

       550        560        570        580        590        600 
SQDRDTQKIQ WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQS QRSPHVFYRH 

       610        620        630        640        650        660 
DLINQLQHNH ALVTLVAENL ATYMESMRMY GRDNEDYDPQ TVRLGSRYSH VQEVQERLNF 

       670        680        690        700        710        720 
LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW YSKLMGDEPD LDPDINKDFF 

       730        740        750        760        770        780 
ESNVLQLDPS LLTENGMKCF ERFFKAVNCR EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ 

       790        800        810        820        830        840 
SNDDIACRAI DLLKEIYTNL GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSI 

       850        860        870        880        890        900 
NCARQEAVRM VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFIV RFPNQGRQVD 

       910        920        930        940        950        960 
DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPGDDRKLI GQLNLKDKSL 

       970        980        990       1000       1010       1020 
ITAKLTQISS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP EVESCLPGVI MSLHPRYISF 

      1030       1040       1050       1060       1070       1080 
LWQVADLGSS LNMPPLRDGA RVLMKLMPPD STTIEKLRAI CLDHAKLGES SLSPSLDSLF 

      1090       1100       1110       1120       1130       1140 
FGPSASQVLY LTEVVYALLM PAGAPLTDDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD 

      1150       1160       1170       1180       1190       1200 
METRRGAYLN ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTSVNQV THDQAVVLQS 

      1210       1220       1230       1240       1250       1260 
ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIQKIIWTSG CGGLQLVFSP 

      1270       1280       1290       1300       1310       1320 
NEEVTKIYEK TNAGNEPDLE DEQVCCEALE VMTLCFALIP TALDALSKEK AWQTFIIDLL 

      1330       1340       1350       1360       1370       1380 
LHCHSKTVRQ VAQEQFFLMC TRCCMGHRPL LFFITLLFTV LGSTARERAK HSGDYFTLLR 

      1390       1400       1410       1420       1430       1440 
HLLNYAYNSN INVPNAEVLL NNEIDWLKRI RDDVKRTGET GVEETILEGH LGVTKELLAF 

      1450       1460       1470       1480       1490       1500 
QTPEKKFHIG CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPATINA 

      1510       1520       1530       1540       1550       1560 
GFELLVALAV GCVRNLKQIV DSLTEMYYIG TAITTCEALT EWEYLPPVGP RPPKGFVGLK 

      1570       1580       1590       1600       1610       1620 
NAGATCYMNS VIQQLYMIPS IRNGILAIEG TGSDVDDDMS GDEKQDNESN VDPRDDVFGY 

      1630       1640       1650       1660       1670       1680 
PQQFEDKPPL SKTEDRKEYN IGVLRHLQVI FGHLAASRLQ YYVPRGFWKQ FRLWGEPVNL 

      1690       1700       1710       1720       1730       1740 
REQHDALEFF NSLVDSLDEA LKALGHPAML SKVLGGSFAD QKICQGCPHR YECEESFTTL 

      1750       1760       1770       1780       1790       1800 
NVDIRNHQNL LDSLEQYVKG DLLEGANAYH CEKCNKKVDT VKRLLIKKLP PVLAIQLKRF 

      1810       1820       1830       1840       1850       1860 
DYDWERECAI KFNDYFEFPR ELDMEPYTVA GVAKLEGDNV NPESQLIQQN EQSESEKAGS 

      1870       1880       1890       1900       1910       1920 
TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGEKNRWYKF DDGDVTECKM DDDEEMKNQC 

      1930       1940       1950       1960       1970       1980 
FGGEYMGEVF DHMMKRMSYR RQKRWWNAYI LFYERMDTIG HDDEVIRYIS EIAITTRPHQ 

      1990       2000       2010       2020       2030       2040 
IVMPSAIERS VRKQNVQFMH NRMQYSLEYF QFMKKLLTCN GVYLNPPPGQ DHLSPEAEEI 

      2050       2060       2070       2080       2090       2100 
TMISIQLAAR FLFTTGFHTK KIVRGSASDW YDALCILLRH SKNVRFWFAH NVLFNVSNRF 

      2110       2120       2130       2140       2150       2160 
SEYLLECPSA EVRGAFAKLI VFIAHFSLQD GPCPSPFASP GPSSQAYDNL SLSDHLLRAV 

      2170       2180       2190       2200       2210       2220 
LNLLRREVSE HGRHLQQYFN LFVMYANLGV AEKTQLLKLS VPATFMLVSL DEGPGPPIKY 

      2230       2240       2250       2260       2270       2280 
QYAELGKLYS VVSQLIRCCN VSSRMQSSIN GNPSLPNPFG DPNLSQPIMP IQQNVVDILF 

      2290       2300       2310       2320       2330       2340 
VRTSYVKKII EDCSNSDETV KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL 

      2350       2360       2370       2380       2390       2400 
LQILLIEDSW QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSSCPV 

      2410       2420       2430       2440       2450       2460 
AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE TSNGYFLERS 

      2470       2480       2490       2500       2510       2520 
HSARMTLAKA CELCPEEEPD DQDAPDEHES PPPEDAPLYP HSPGSQYQQN NHVHGQPYTG 

      2530       2540       2550 
PAAHHMNNPQ RTGQRAQENY EGGEEVSPPQ TKGSVKCTY 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U67874 mRNA. Translation: AAB07731.1.
AL669967 Genomic DNA. No translation available.
Z78153 mRNA. Translation: CAB01555.1.
PIRT30850.
RefSeqNP_033507.2. NM_009481.2.
UniGeneMm.242646.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204467. 5 interactions.
IntActP70398. 7 interactions.
MINTMINT-4139688.

Protein family/group databases

MEROPSC19.017.

PTM databases

PhosphoSiteP70398.

Proteomic databases

MaxQBP70398.
PaxDbP70398.
PRIDEP70398.

Protocols and materials databases

DNASU22284.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID22284.
KEGGmmu:22284.

Organism-specific databases

CTD8239.
MGIMGI:894681. Usp9x.

Phylogenomic databases

eggNOGCOG5077.
HOGENOMHOG000231283.
HOVERGENHBG073749.
InParanoidP70398.
KOK11840.

Gene expression databases

CleanExMM_USP9X.
GenevestigatorP70398.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302415.
PROP70398.
SOURCESearch...

Entry information

Entry nameUSP9X_MOUSE
AccessionPrimary (citable) accession number: P70398
Secondary accession number(s): E9QLY0, Q62497
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot