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Protein Page:
ataxin-3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ataxin-3 Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates. Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins. Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. In response to misfolded substrate ubiquitination, mediates deubiquitination of monoubiquitinated STUB1/CHIP. Interacts with key regulators of transcription and represses transcription: acts as a histone- binding protein that regulates transcription. Defects in ATXN3 are the cause of spinocerebellar ataxia type 3 (SCA3); also known as Machado-Joseph disease (MJD). Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA3 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. The molecular defect in SCA3 is the a CAG repeat expansion in ATXN3 coding region. Longer expansions result in earlier onset and more severe clinical manifestations of the disease. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin-specific protease; EC 3.4.22.-; Protease; Transcription regulation; DNA repair, damage; EC 3.4.19.12
Cellular Component: nucleoplasm; nuclear matrix; cytoplasm
Molecular Function: ubiquitin thiolesterase activity; identical protein binding; omega peptidase activity; protein binding; ubiquitin protein ligase binding; ubiquitin-specific protease activity; ATPase binding
Biological Process: cell death; synaptic transmission; proteasomal ubiquitin-dependent protein catabolic process; nervous system development; transcription, DNA-dependent; regulation of transcription, DNA-dependent; nucleotide-excision repair; misfolded or incompletely synthesized protein catabolic process; intermediate filament cytoskeleton organization and biogenesis; microtubule cytoskeleton organization and biogenesis; actin cytoskeleton organization and biogenesis
Reference #:  P54252 (UniProtKB)
Alt. Names/Synonyms: AT3; ataxin 3; Ataxin-3; ATX3; ATXN3; JOS; josephin; Machado-Joseph disease (spinocerebellar ataxia 3, olivopontocerebellar ataxia 3, autosomal dominant, ataxin 3); Machado-Joseph disease protein 1; MJD; MJD1; olivopontocerebellar ataxia 3; SCA3; Spinocerebellar ataxia type 3 protein
Gene Symbols: ATXN3
Molecular weight: 41,781 Da
Basal Isoelectric point: 4.81  Predict pI for various phosphorylation states
Select Structure to View Below

ataxin-3

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: S256‑p

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

► Hide Isoforms
 
1 1 S29 LLQGEYFSPVELSSI
0 13 Y58-p GGVTSEDyRTFLQQP
0 93 K117-ub RSFICNYkEHWFTVR
1 0 K166-sm GYSIFVVkGDLPDCE
0 18 K190-ub VQQMHRPkLIGEELA
0 104 K200-ub GEELAQLkEQRVHkT
0 51 K206-ub LkEQRVHkTDLERVL
0 6 S219-p VLEANDGsGMLDEDE
1 0 S236 LQRALALSRQEIDME
2 0 S256-p LRRAIQLsMQGsSRN
1 1 S260-p IQLsMQGsSRNIsQD
1 0 S261 QLsMQGsSRNIsQDM
0 2 N263 sMQGsSRNIsQDMtQ
0 12 S265-p QGsSRNIsQDMtQTS
0 6 M268 SRNIsQDMtQTSGTN
0 2 T269-p RNIsQDMtQTSGTNL
0 3 T271 IsQDMtQTSGTNLTS
0 2 S272 sQDMtQTSGTNLTSE
0 6 G273 QDMtQTSGTNLTSEE
0 16 K291-ub RREAYFEkQQQKQQQ
0 3 S328 TSSGALGSDLGKACS
1 0 S335 SDLGKACSPFIMFAT
1 0 Y346 MFATFTLYLTYELHV
0 1 - gap
0 1 - gap
  ataxin-3 iso2  
S29 LLQGEYFSPVELSSI
Y58 GGVTSEDYRTFLQQP
K117-ub RSFICNYkEHWFTVR
K166 GYSIFVVKGDLPDCE
K190 VQQMHRPKLIGEELA
K200-ub GEELAQLkEQRVHKT
K206 LkEQRVHKTDLERVL
S219 VLEANDGSGMLDEDE
S236-p LQRALALsRQEIDME
S256-p LRRAIQLsMQGssRN
S260-p IQLsMQGssRNISQD
S261-p QLsMQGssRNISQDM
N263 sMQGssRNISQDMTQ
S265 QGssRNISQDMTQTS
M268 sRNISQDMTQTSGTN
T269 RNISQDMTQTSGTNL
T271 ISQDMTQTSGTNLTS
S272 SQDMTQTSGTNLTSE
G273 QDMTQTSGTNLTSEE
K291 RREAYFEKQQQKQQQ
S328 TSSGALGSDLGDAMs
S335-p SDLGDAMsEEDMLQA
S347-p LQAAVTMsLETVRND
R352 TMsLETVRNDLKTEG
K360-ac NDLKTEGkK______
  mouse

 
S29-p LLQGEYFsPVELSSI
Y58 GGVTSEDYRTFLQQP
K117-ub RSFICNYkEHWFTVR
K166 GYSIFVVKGDLPDCE
K190 VQQMHRPKLIGEELA
K200-ub GEELAHLkEQSALkA
K206-ub LkEQSALkADLERVL
S219-p VLEAADGsGIFDEDE
S236 LQRALAISRQEIDME
S256 LRRAIQLSMQGSSRs
S260 IQLSMQGSSRsMCEN
S261 QLSMQGSSRsMCENs
S263-p SMQGSSRsMCENsPQ
C265 QGSSRsMCENsPQts
S268-p SRsMCENsPQtssPD
P269 RsMCENsPQtssPDL
T271-p MCENsPQtssPDLSS
S272-p CENsPQtssPDLSSE
S273-p ENsPQtssPDLSSEE
K291-ub RREAYFEkQQQQQQE
S321-p TSSGGRRsDQGGDAV
S329 DQGGDAVSEEDMLRA
S341 LRAAVTMSLETAkDN
K346-ub TMSLETAkDNLKAER
K354 DNLKAERKK______
  rat

 
S29 LLQGEYFSPVELSSI
Y58 GGVTSEDYRTFLQQP
K117 RSFICNYKEHWFTVR
K166 GYSIFVVKGDLPDCE
K190 VQQMHRPKLIGEELA
K200 GEELAHLKEQSALKA
K206 LKEQSALKADLERVL
P219 VLEAADGPGMFDDDE
S236 LQRALAMSRQEIDME
S256 LRRAIQLSMQGSSRG
S260 IQLSMQGSSRGMCED
S261 QLSMQGSSRGMCEDS
G263 SMQGSSRGMCEDSPQ
C265 QGSSRGMCEDSPQTS
S268 SRGMCEDSPQTSSTD
P269 RGMCEDSPQTSSTDL
T271 MCEDSPQTSSTDLSS
S272 CEDSPQTSSTDLSSE
S273 EDSPQTSSTDLSSEE
K291 RREAYFEKQQHQQQE
S321 TSSGGLRSNQAGNAM
S329 NQAGNAMSEEDVLRA
S341 LRATVTVSLETAKDS
K346 TVSLETAKDSLKAER
K354 DSLKAERKK______
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