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Q93008

- USP9X_HUMAN

UniProt

Q93008 - USP9X_HUMAN

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Protein

Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Gene

USP9X

Organism
Homo sapiens (Human)
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. Involved in axonal growth and neuronal cell migration.4 Publications

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 endopeptidase activity Source: ProtInc
  3. cysteine-type peptidase activity Source: ProtInc
  4. ubiquitin thiolesterase activity Source: Reactome

GO - Biological processi

  1. axon extension Source: UniProtKB
  2. BMP signaling pathway Source: UniProtKB
  3. cerebellar cortex structural organization Source: Ensembl
  4. chromosome segregation Source: UniProtKB-KW
  5. female gamete generation Source: ProtInc
  6. gene expression Source: Reactome
  7. hippocampus development Source: Ensembl
  8. in utero embryonic development Source: Ensembl
  9. mitotic nuclear division Source: UniProtKB-KW
  10. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
  11. neuron migration Source: UniProtKB
  12. post-embryonic development Source: Ensembl
  13. protein deubiquitination Source: UniProtKB
  14. transcription, DNA-templated Source: Reactome
  15. transcription initiation from RNA polymerase II promoter Source: Reactome
  16. transforming growth factor beta receptor signaling pathway Source: UniProtKB
  17. 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

Enzyme and pathway databases

ReactomeiREACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.

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 in mammals
Short name:
hFAM
Fat facets protein-related, X-linked
Ubiquitin thioesterase FAF-X
Ubiquitin-specific protease 9, X chromosome
Ubiquitin-specific-processing protease FAF-X
Gene namesi
Name:USP9X
Synonyms:DFFRX, FAM, USP9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:12632. USP9X.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. growth cone Source: UniProtKB
  5. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked 99 (MRX99) [MIM:300919]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2093 – 20931L → H in MRX99; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones. 1 Publication
VAR_071131
Natural varianti2157 – 21571L → I in MRX99; unknown pathological significance; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones. 1 Publication
VAR_071132

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi300919. phenotype.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA37257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25702570Probable ubiquitin carboxyl-terminal hydrolase FAF-XPRO_0000080689Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1600 – 16001Phosphoserine5 Publications
Modified residuei2443 – 24431Phosphoserine3 Publications
Modified residuei2556 – 25561Phosphotyrosine1 Publication
Modified residuei2563 – 25631Phosphoserine3 Publications
Modified residuei2567 – 25671Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ93008.
PaxDbiQ93008.
PRIDEiQ93008.

PTM databases

PhosphoSiteiQ93008.

Expressioni

Tissue specificityi

Widely expressed in embryonic and adult tissues.

Gene expression databases

BgeeiQ93008.
CleanExiHS_USP9X.
ExpressionAtlasiQ93008. baseline and differential.
GenevestigatoriQ93008.

Organism-specific databases

HPAiCAB011618.

Interactioni

Subunit structurei

Interacts with SMAD4, MARK4, NUAK1 and BIRC5/survivin. Interacts with DCX.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428588EBI-302524,EBI-466029
SMAD4Q134852EBI-302524,EBI-347263

Protein-protein interaction databases

BioGridi113867. 102 interactions.
DIPiDIP-27562N.
IntActiQ93008. 23 interactions.
MINTiMINT-5006529.
STRINGi9606.ENSP00000316357.

Structurei

3D structure databases

ProteinModelPortaliQ93008.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000119158.
HOGENOMiHOG000231283.
HOVERGENiHBG073749.
InParanoidiQ93008.
KOiK11840.
OMAiMAQEQFF.
OrthoDBiEOG722J7K.
PhylomeDBiQ93008.
TreeFamiTF323966.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q93008-3) [UniParc]FASTAAdd to Basket

Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE
60 70 80 90 100
QGQGDAPPQL EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA
110 120 130 140 150
AIDLSKKGLD VKSEACQRFF RDGLTISFTK ILTDEAVSGW KFEIHRCIIN
160 170 180 190 200
NTHRLVELCV AKLSQDWFPL 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 RHGNPEEEEW 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 GEAPQNLSQT QRSPHVFYRH
610 620 630 640 650
DLINQLQHNH ALVTLVAENL ATYMESMRLY ARDHEDYDPQ 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 SNDDIASRAI DLLKEIYTNL
810 820 830 840 850
GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSV NCARQEAVRM
860 870 880 890 900
VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFVV RFPNQGRQVD
910 920 930 940 950
DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPADDRKLI
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
PAGAPLADDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD METRRGAYLN
1160 1170 1180 1190 1200
ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTQINQV THDQAVVLQS
1210 1220 1230 1240 1250
ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIQKIIWASG
1260 1270 1280 1290 1300
CGSLQLVFSP NEEITKIYEK 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 GIEETILEGH LGVTKELLAF QTSEKKFHIG
1460 1470 1480 1490 1500
CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPPTINA
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 PQQFEDKPAL 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 NPESQLIQQS
1860 1870 1880 1890 1900
EQSESETAGS TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGERNRWYKF
1910 1920 1930 1940 1950
DDGDVTECKM DDDEEMKNQC FGGEYMGEVF DHMMKRMSYR RQKRWWNAYI
1960 1970 1980 1990 2000
LFYERMDTID QDDELIRYIS ELAITTRPHQ IIMPSAIERS VRKQNVQFMH
2010 2020 2030 2040 2050
NRMQYSMEYF QFMKKLLTCN GVYLNPPPGQ DHLLPEAEEI TMISIQLAAR
2060 2070 2080 2090 2100
FLFTTGFHTK KVVRGSASDW 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
GNPPLPNPFG DPNLSQPIMP IQQNVADILF VRTSYVKKII EDCSNSEETV
2310 2320 2330 2340 2350
KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL LQILLIEDSW
2360 2370 2380 2390 2400
QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSNCPV
2410 2420 2430 2440 2450
AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE
2460 2470 2480 2490 2500
TSNGYFLERS HSARMTLAKA CELCPEEVKK ATSVQQIEME ESKEPDDQDA
2510 2520 2530 2540 2550
PDEHESPPPE DAPLYPHSPG SQYQQNNHVH GQPYTGPAAH HMNNPQRTGQ
2560 2570
RAQENYEGSE EVSPPQTKDQ
Length:2,570
Mass (Da):292,280
Last modified:January 11, 2011 - v3
Checksum:i84CB979A405AA56F
GO
Isoform 2 (identifier: Q93008-1) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     2478-2493: Missing.

Show »
Length:2,554
Mass (Da):290,463
Checksum:i16B87B7FCC1428AF
GO

Sequence cautioni

The sequence CAD13527.2 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAD18900.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251Q → L in CAA66942. (PubMed:8922996)Curated
Sequence conflicti148 – 1547Missing in CAA66942. (PubMed:8922996)Curated
Sequence conflicti468 – 4681L → P in CAA66942. (PubMed:8922996)Curated
Sequence conflicti476 – 4761W → R in CAA66942. (PubMed:8922996)Curated
Sequence conflicti506 – 5061K → R in CAA66942. (PubMed:8922996)Curated
Sequence conflicti621 – 6211A → V in CAA66942. (PubMed:8922996)Curated
Sequence conflicti1400 – 14001L → F in CAA66942. (PubMed:8922996)Curated
Sequence conflicti1951 – 19511L → P in CAA66942. (PubMed:8922996)Curated
Sequence conflicti2330 – 23301T → P in CAA66942. (PubMed:8922996)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2093 – 20931L → H in MRX99; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones. 1 Publication
VAR_071131
Natural varianti2157 – 21571L → I in MRX99; unknown pathological significance; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones. 1 Publication
VAR_071132

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2478 – 249316Missing in isoform 2. 1 PublicationVSP_040478Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98296 mRNA. Translation: CAA66942.1.
AL391259, AL109797 Genomic DNA. Translation: CAD13527.2. Sequence problems.
AL109797, AL391259 Genomic DNA. Translation: CAD18900.2. Sequence problems.
AF070645 mRNA. Translation: AAC25395.1.
CCDSiCCDS43930.1. [Q93008-3]
CCDS55403.1. [Q93008-1]
RefSeqiNP_001034679.2. NM_001039590.2. [Q93008-3]
NP_001034680.2. NM_001039591.2. [Q93008-1]
UniGeneiHs.77578.

Genome annotation databases

EnsembliENST00000324545; ENSP00000316357; ENSG00000124486. [Q93008-3]
ENST00000378308; ENSP00000367558; ENSG00000124486. [Q93008-1]
GeneIDi8239.
KEGGihsa:8239.
UCSCiuc004dfb.3. human. [Q93008-3]
uc004dfc.3. human. [Q93008-1]

Polymorphism databases

DMDMi317373496.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98296 mRNA. Translation: CAA66942.1 .
AL391259 , AL109797 Genomic DNA. Translation: CAD13527.2 . Sequence problems.
AL109797 , AL391259 Genomic DNA. Translation: CAD18900.2 . Sequence problems.
AF070645 mRNA. Translation: AAC25395.1 .
CCDSi CCDS43930.1. [Q93008-3 ]
CCDS55403.1. [Q93008-1 ]
RefSeqi NP_001034679.2. NM_001039590.2. [Q93008-3 ]
NP_001034680.2. NM_001039591.2. [Q93008-1 ]
UniGenei Hs.77578.

3D structure databases

ProteinModelPortali Q93008.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113867. 102 interactions.
DIPi DIP-27562N.
IntActi Q93008. 23 interactions.
MINTi MINT-5006529.
STRINGi 9606.ENSP00000316357.

Chemistry

BindingDBi Q93008.
ChEMBLi CHEMBL2406899.

Protein family/group databases

MEROPSi C19.017.

PTM databases

PhosphoSitei Q93008.

Polymorphism databases

DMDMi 317373496.

Proteomic databases

MaxQBi Q93008.
PaxDbi Q93008.
PRIDEi Q93008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324545 ; ENSP00000316357 ; ENSG00000124486 . [Q93008-3 ]
ENST00000378308 ; ENSP00000367558 ; ENSG00000124486 . [Q93008-1 ]
GeneIDi 8239.
KEGGi hsa:8239.
UCSCi uc004dfb.3. human. [Q93008-3 ]
uc004dfc.3. human. [Q93008-1 ]

Organism-specific databases

CTDi 8239.
GeneCardsi GC0XP040944.
HGNCi HGNC:12632. USP9X.
HPAi CAB011618.
MIMi 300072. gene.
300919. phenotype.
neXtProti NX_Q93008.
Orphaneti 777. X-linked non-syndromic intellectual disability.
PharmGKBi PA37257.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5077.
GeneTreei ENSGT00760000119158.
HOGENOMi HOG000231283.
HOVERGENi HBG073749.
InParanoidi Q93008.
KOi K11840.
OMAi MAQEQFF.
OrthoDBi EOG722J7K.
PhylomeDBi Q93008.
TreeFami TF323966.

Enzyme and pathway databases

Reactomei REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.

Miscellaneous databases

ChiTaRSi USP9X. human.
GeneWikii USP9X.
GenomeRNAii 8239.
NextBioi 30989.
PROi Q93008.
SOURCEi Search...

Gene expression databases

Bgeei Q93008.
CleanExi HS_USP9X.
ExpressionAtlasi Q93008. baseline and differential.
Genevestigatori Q93008.

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. "The Drosophila developmental gene fat facets has a human homologue in Xp11.4 which escapes X-inactivation and has related sequences on Yq11.2."
    Jones M.H., Furlong R.A., Burkin H., Chalmers I.J., Brown G.M., Khwaja O., Affara N.A.
    Hum. Mol. Genet. 5:1695-1701(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Fetal brain, Retina and Testis.
  2. Erratum
    Jones M.H., Furlong R.A., Burkin H., Chalmers I.J., Brown G.M., Khwaja O., Affara N.A.
    Hum. Mol. Genet. 6:334-335(1996)
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Yu W., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2226-2570 (ISOFORM 1).
    Tissue: Brain.
  5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Chromosome alignment and segregation regulated by ubiquitination of survivin."
    Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.
    Science 310:1499-1504(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BIRC5.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains."
    Al-Hakim A.K., Zagorska A., Chapman L., Deak M., Peggie M., Alessi D.R.
    Biochem. J. 411:249-260(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MARK4 AND NUAK1.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600; SER-2443 AND SER-2563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination."
    Dupont S., Mamidi A., Cordenonsi M., Montagner M., Zacchigna L., Adorno M., Martello G., Stinchfield M.J., Soligo S., Morsut L., Inui M., Moro S., Modena N., Argenton F., Newfeld S.J., Piccolo S.
    Cell 136:123-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SMAD4, SUBCELLULAR LOCATION.
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2563 AND THR-2567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600 AND SER-2443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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: FUNCTION, INTERACTION WITH DCX, SUBCELLULAR LOCATION, VARIANTS MRX99 HIS-2093 AND ILE-2157, CHARACTERIZATION OF VARIANTS MRX99 HIS-2093 AND ILE-2157.

Entry informationi

Entry nameiUSP9X_HUMAN
AccessioniPrimary (citable) accession number: Q93008
Secondary accession number(s): O75550, Q8WWT3, Q8WX12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2011
Last modified: November 26, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Escapes X-inactivation.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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