Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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P70398 (USP9X_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Usp9x
Synonyms:	Fafl, Fam

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2559 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Mitosis Ubl conjugation pathway
Cellular component	Cytoplasm
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW 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_component	apical part of cell Inferred from direct assay PubMed 10704870. Source: MGI cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	co-SMAD binding Inferred from sequence or structural similarity. Source: BHF-UCL cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin thiolesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMAD4	Q13485	4	EBI-2214043,EBI-347263	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2559

2559

Probable ubiquitin carboxyl-terminal hydrolase FAF-X

PRO_0000080691

Sites

Active site

1566

Nucleophile By similarity

Active site

1879

Proton acceptor By similarity

Amino acid modifications

Modified residue

1600

Phosphoserine Ref.5

Modified residue

1815

Phosphotyrosine Ref.4

Modified residue

2443

Phosphoserine By similarity

Modified residue

2540

Phosphotyrosine Ref.4

Modified residue

2547

Phosphoserine By similarity

Modified residue

2551

Phosphothreonine By similarity

Experimental info

Sequence conflict

A → P in AAB07731. Ref.1

Sequence conflict

182

C → F in CAB01555. Ref.3

Sequence conflict

1243 – 1244

QK → HQ in AAB07731. Ref.1

Sequence conflict

1626

D → N in AAB07731. Ref.1

Sequence conflict

1631

S → I in AAB07731. Ref.1

Sequence conflict

1635

D → N in AAB07731. Ref.1

Sequence conflict

1638

E → K in AAB07731. Ref.1

Sequence conflict

1645

R → K in AAB07731. Ref.1

Sequence conflict

1665

R → K in AAB07731. Ref.1

Sequence conflict

1671

F → S in AAB07731. Ref.1

Sequence conflict

1688 – 1689

EF → KS in AAB07731. Ref.1

Sequence conflict

1918

N → T in AAB07731. Ref.1

Sequence conflict

1930

F → L in AAB07731. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P70398 [UniParc].

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

2,559

290,711

        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' referencesShow '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. 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-1815 AND TYR-2540, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
IPI	IPI00108388.
PIR	T30850.
RefSeq	NP_033507.2. NM_009481.2.
UniGene	Mm.242646.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P70398. 2 interactions.
Protein family/group databases
MEROPS	C19.017.
PTM databases
PhosphoSite	P70398.
Proteomic databases
PaxDb	P70398.
PRIDE	P70398.
Protocols and materials databases
DNASU	22284.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	22284.
KEGG	mmu:22284.
Organism-specific databases
CTD	8239.
MGI	MGI:894681. Usp9x.
Phylogenomic databases
eggNOG	COG5077.
HOGENOM	HOG000231283.
HOVERGEN	HBG073749.
InParanoid	P70398.
KO	K11840.
OrthoDB	EOG46HG8S.
Gene expression databases
CleanEx	MM_USP9X.
Genevestigator	P70398.
GermOnline	ENSMUSG00000031010. Mus musculus.
Family and domain databases
InterPro	IPR018200. Pept_C19ubi-hydrolase_C_CS. IPR001394. Peptidase_C19. [Graphical view]
Pfam	PF00443. UCH. 1 hit. [Graphical view]
PROSITE	PS00972. UCH_2_1. 1 hit. PS00973. UCH_2_2. 1 hit. PS50235. UCH_2_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	302415.
SOURCE	Search...

Entry information

Entry name

USP9X_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents