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Protein Page:
USP9X (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
USP9X 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. Interacts with SMAD4, MARK4, NUAK1 and BIRC5/survivin. Widely expressed in embryonic and adult tissues. Belongs to the peptidase C19 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.2.15; Protease; EC 3.4.19.12; Ubiquitin-specific protease; Ubiquitin conjugating system
Cellular Component: apical part of cell; cytoplasm; cytosol
Molecular Function: ubiquitin thiolesterase activity; protein binding; cysteine-type endopeptidase activity; cysteine-type peptidase activity
Biological Process: ubiquitin-dependent protein catabolic process; BMP signaling pathway; transcription initiation from RNA polymerase II promoter; mitosis; protein deubiquitination; transcription, DNA-dependent; cell division; transforming growth factor beta receptor signaling pathway; female gamete generation; gene expression; negative regulation of transcription from RNA polymerase II promoter; chromosome segregation
Reference #:  Q93008 (UniProtKB)
Alt. Names/Synonyms: Deubiquitinating enzyme FAF-X; DFFRX; Drosophila fat facets related, X-linked; FAF; FAM; Fat facets in mammals; fat facets protein related, X-linked; Fat facets protein-related, X-linked; hFAM; Probable ubiquitin carboxyl-terminal hydrolase FAF-X; ubiquitin specific peptidase 9, X-linked; ubiquitin specific protease 9, X chromosome (fat facets-like Drosophila); Ubiquitin thioesterase FAF-X; ubiquitin thiolesterase FAF-X; ubiquitin-specific processing protease FAF-X; Ubiquitin-specific protease 9, X chromosome; Ubiquitin-specific-processing protease FAF-X; USP9; USP9X
Gene Symbols: USP9X
Molecular weight: 292,280 Da
Basal Isoelectric point: 5.52  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

USP9X
Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
0 1 S199-p PCESVSSsVQLPEDE
0 1 K218-u SPDPRSPkGWLVDLL
0 1 K303-a KEAKNEAkNDALSMI
0 1 K303 KEAKNEAKNDALSMI
0 1 K315-a SMIIKSLkNLASRVP
0 2 K315-u SMIIKSLkNLASRVP
0 1 K329-u PGQEETVkNLEIFRL
0 4 Y367-p KVISSVSyyTHRHGN
0 16 Y368-p VISSVSyyTHRHGNP
0 1 N374 yyTHRHGNPEEEEWL
0 1 P375 yTHRHGNPEEEEWLT
0 1 K412 HQPQYVEKLEKILRF
0 11 S588-p GEAPQNLsQtQRsPH
0 20 T590-p APQNLsQtQRsPHVF
0 3 S593-p NLsQtQRsPHVFYRH
0 1 K745 KCFERFFKAVNCREG
0 1 K837 LCVLDGDKDSVNCAr
0 1 R844-m1 KDSVNCArQEAVRMV
0 1 Y868-p INECDSDyHEERTIL
0 1 S887-p AFRGKHLsFVVRFPN
0 1 T930-p IKANVAHtKIELFVG
0 1 T984-p DSSSDSStGSPGNHG
0 2 K1045-u DGARVLMkLMPPDST
0 9 K1066-u AICLDHAkLGESSLS
0 1 S1226 VRLAQQISDEASRYM
0 2 K1370-u STARERAkHSGDYFT
0 1 K1435 EGHLGVTKELLAFQT
0 1 K1453 KFHIGCEKGGANLIK
0 2 T1591-p GILAIEGtGsDVDDD
0 3 S1593-p LAIEGtGsDVDDDMs
0 18 S1600-p sDVDDDMsGDEKQDN
0 4 S1609-p DEKQDNEsNVDPRDD
0 1 Y1620-p PRDDVFGyPQQFEDk
0 43 K1627-u yPQQFEDkPALSkTE
0 6 K1632-u EDkPALSkTEDRkEY
0 2 K1637-u LSkTEDRkEYNIGVL
0 2 K1669-u YVPRGFWkQFRLWGE
0 2 K1712-u GHPAMLSkVLGGSFA
0 2 K1798-u PVLAIQLkRFDYDWE
0 2 K1811-u WERECAIkFNDYFEF
0 2 Y1815 CAIkFNDYFEFPREL
0 1 K1862-u SETAGSTkYRLVGVL
0 1 K1899 GERNRWYKFDDGDVT
0 1 Y2185 YFNLFVMYANLGVAE
0 1 T2194 NLGVAEKTQLLKLSV
0 4 K2219-u EGPGPPIkYQYAELG
0 1 K2288 VRTSYVKKIIEDCSN
0 1 K2301-u SNSEETVkLLRFCCW
0 2 K2360-u HRIHNALkGIPDDRD
0 1 Y2431 DELERRPYTGNPQYt
0 1 T2432 ELERRPYTGNPQYty
0 1 Y2437 PYTGNPQYtyNNWsP
0 2 T2438-p YTGNPQYtyNNWsPP
0 5 Y2439-p TGNPQYtyNNWsPPV
0 14 S2443-p QYtyNNWsPPVQsNE
0 2 S2448-p NWsPPVQsNETSNGY
0 2 Y2455 sNETSNGYFLERSHS
0 166 Y2556-p GQRAQENyEGSEEVs
0 10 S2563-p yEGSEEVsPPQtKDQ
0 1 T2567-p EEVsPPQtKDQ____
  mouse

 
S199 PCESVSSSVQLPEDE
K218 SPDPRSPKGWLVDLL
K303 KEAKNEAKNDALSMI
K303-u KEAKNEAkNDALSMI
K315 SMIIKSLKNLASRVP
K315-u SMIIKSLkNLASRVP
K329 PGQEETVKNLEIFRL
Y367-p KVISSVSyYTHRHGs
Y368 VISSVSyYTHRHGss
S374-p yYTHRHGssEDEEWL
S375-p YTHRHGssEDEEWLT
K412-u HQPQYVEkLEKILRF
S588-p GEAPQNLsQsQRsPH
S590-p APQNLsQsQRsPHVF
S593-p NLsQsQRsPHVFYRH
K745-u KCFERFFkAVNCREG
K837-u LCVLDGDkDSINCAR
R844 kDSINCARQEAVRMV
Y868 INECDSDYHEERTIL
S887-p AFRGKHLsFIVRFPN
T930 IKANVAHTKIELFVG
T984 DSSSDSSTGSPGNHG
K1045-u DGARVLMkLMPPDST
K1066-u AICLDHAkLGESSLS
S1226-p VRLAQQIsDEASRYM
K1370-u STARERAkHSGDYFT
K1435-u EGHLGVTkELLAFQT
K1453-u KFHIGCEkGGANLIK
T1591-p GILAIEGtGsDVDDD
S1593-p LAIEGtGsDVDDDMs
S1600-p sDVDDDMsGDEKQDN
S1609-p DEKQDNEsNVDPRDD
Y1620 PRDDVFGYPQQFEDk
K1627-u YPQQFEDkPPLSkTE
K1632-u EDkPPLSkTEDRkEY
K1637-u LSkTEDRkEYNIGVL
K1669-u YVPRGFWkQFRLWGE
K1712-u GHPAMLSkVLGGSFA
K1798-u PVLAIQLkRFDYDWE
K1811-u WERECAIkFNDyFEF
Y1815-p CAIkFNDyFEFPREL
K1862 SEKAGSTKYRLVGVL
K1899-u GEKNRWYkFDDGDVT
Y2185-p YFNLFVMyANLGVAE
T2194-p NLGVAEKtQLLKLSV
K2219-u EGPGPPIkYQYAELG
K2288-u VRTSYVKkIIEDCSN
K2301 SNSDETVKLLRFCCW
K2360-u HRIHNALkGIPDDRD
Y2431-p DELERRPytGNPQyt
T2432-p ELERRPytGNPQyty
Y2437-p PytGNPQytyNNWsP
T2438-p ytGNPQytyNNWsPP
Y2439-p tGNPQytyNNWsPPV
S2443-p QytyNNWsPPVQsNE
S2448-p NWsPPVQsNETSNGy
Y2455-p sNETSNGyFLERSHS
Y2540 GQRAQENYEGGEEVs
S2547-p YEGGEEVsPPQTKGS
T2551 EEVsPPQTKGSVKCT
  rat

 
S199 PCESVSSSVQLPEDE
K218 SPDPRSPKGWLVDLL
K303 KEAKNEAKNDALSMI
K303 KEAKNEAKNDALSMI
K315 SMIIKSLKSLASRVP
K315 SMIIKSLKSLASRVP
K329 PGQEETVKNLEIFRL
Y367 KVISSVSYYTHRHGS
Y368 VISSVSYYTHRHGSS
S374 YYTHRHGSSEEEEWL
S375 YTHRHGSSEEEEWLT
K412 HQPQYVEKLEKILRF
S588 GEAPQNLSQTQRSPH
T590 APQNLSQTQRSPHVF
S593 NLSQTQRSPHVFYRH
K745 KCFERFFKAVNCREG
K837 LCVLDGDKDSINCAR
R844 KDSINCARQEAVRMV
Y868 INECDSDYHEERTIL
S887 AFRGKHLSFIVRFPN
T930 IKANVAHTKIELFVG
T984 DSSSDSSTGSPGNHG
K1045 DGARVLMKLMPPDST
K1066 AICLDHAKLGESSLS
S1226 VRLAQQISDEASRYM
K1370 STARERAKHSGDYFT
K1435 EGHLGVTKELLAFQT
K1453 KFHIGCEKGGANLIK
T1591 GILAIEGTGSDVDDD
S1593 LAIEGTGSDVDDDMS
S1600 SDVDDDMSGDEKQDN
S1609 DEKQDNESNVDPRDD
Y1620 PRDDVFGYPQQFEDk
K1627-u YPQQFEDkPPLSKTE
K1632 EDkPPLSKTEDRKEY
K1637 LSKTEDRKEYNIGVL
K1669 YVPRGFWKQFRLWGE
K1712 GHPAMLSKVLGGSFA
K1798 PVLAIQLKRFDYDWE
K1811 WERECAIKFNDYFEF
Y1815 CAIKFNDYFEFPREL
K1862 SEKAGSTKYRLVGVL
K1899 GEKNRWYKFDDGDVT
Y2185 YFNLFVMYANLGVAE
T2194 NLGVAEKTQLLKLSV
K2219 EGPGPPIKYQYAELG
K2288 VRTSYVKKIIEDCSN
K2301 SNSDETVKLLRFCCW
K2360 HRIHNALKGIPDDRD
Y2431 DELERRPYTGNPQYT
T2432 ELERRPYTGNPQYTY
Y2437 PYTGNPQYTYNNWsP
T2438 YTGNPQYTYNNWsPP
Y2439 TGNPQYTYNNWsPPV
S2443-p QYTYNNWsPPVQSNE
S2448 NWsPPVQSNETSNGY
Y2455 SNETSNGYFLERSHS
Y2533 GQRAQENYEGSEEVS
S2540 YEGSEEVSPPQTKDQ
T2544 EEVSPPQTKDQ____
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