[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN SCA1.
TISSUE=Brain, and Cerebellum;
DOI=10.1038/ng0894-513; PubMed=7951322 [NCBI, ExPASy, EBI, Israel, Japan]
Banfi S.,
Servadio A.,
Chung M.-Y.,
Kwiatkowski T.J. Jr.,
McCall A.E.,
Duvick L.A.,
Shen Y.,
Roth E.J.,
Orr H.T.,
Zoghbi H.Y.;
"Identification and characterization of the gene causing type 1 spinocerebellar ataxia.";
Nat. Genet. 7:513-519(1994).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J.,
Palmer S.A.,
Sims S.K.,
Edwards C.A.,
Ashurst J.L.,
Wilming L.,
Jones M.C.,
Horton R.,
Hunt S.E.,
Scott C.E.,
Gilbert J.G.R.,
Clamp M.E.,
Bethel G.,
Milne S.,
Ainscough R.,
Almeida J.P.,
Ambrose K.D.,
Andrews T.D.,
Ashwell R.I.S., ![]()
Babbage A.K.,
Bagguley C.L.,
Bailey J.,
Banerjee R.,
Barker D.J.,
Barlow K.F.,
Bates K.,
Beare D.M.,
Beasley H.,
Beasley O.,
Bird C.P.,
Blakey S.E.,
Bray-Allen S.,
Brook J.,
Brown A.J.,
Brown J.Y.,
Burford D.C.,
Burrill W.,
Burton J.,
Carder C.,
Carter N.P.,
Chapman J.C.,
Clark S.Y.,
Clark G.,
Clee C.M.,
Clegg S.,
Cobley V.,
Collier R.E.,
Collins J.E.,
Colman L.K.,
Corby N.R.,
Coville G.J.,
Culley K.M.,
Dhami P.,
Davies J.,
Dunn M.,
Earthrowl M.E.,
Ellington A.E.,
Evans K.A.,
Faulkner L.,
Francis M.D.,
Frankish A.,
Frankland J.,
French L.,
Garner P.,
Garnett J.,
Ghori M.J.,
Gilby L.M.,
Gillson C.J.,
Glithero R.J.,
Grafham D.V.,
Grant M.,
Gribble S.,
Griffiths C.,
Griffiths M.N.D.,
Hall R.,
Halls K.S.,
Hammond S.,
Harley J.L.,
Hart E.A.,
Heath P.D.,
Heathcott R.,
Holmes S.J.,
Howden P.J.,
Howe K.L.,
Howell G.R.,
Huckle E.,
Humphray S.J.,
Humphries M.D.,
Hunt A.R.,
Johnson C.M.,
Joy A.A.,
Kay M.,
Keenan S.J.,
Kimberley A.M.,
King A.,
Laird G.K.,
Langford C.,
Lawlor S.,
Leongamornlert D.A.,
Leversha M.,
Lloyd C.R.,
Lloyd D.M.,
Loveland J.E.,
Lovell J.,
Martin S.,
Mashreghi-Mohammadi M.,
Maslen G.L.,
Matthews L.,
McCann O.T.,
McLaren S.J.,
McLay K.,
McMurray A.,
Moore M.J.F.,
Mullikin J.C.,
Niblett D.,
Nickerson T.,
Novik K.L.,
Oliver K.,
Overton-Larty E.K.,
Parker A.,
Patel R.,
Pearce A.V.,
Peck A.I.,
Phillimore B.J.C.T.,
Phillips S.,
Plumb R.W.,
Porter K.M.,
Ramsey Y.,
Ranby S.A.,
Rice C.M.,
Ross M.T.,
Searle S.M.,
Sehra H.K.,
Sheridan E.,
Skuce C.D.,
Smith S.,
Smith M.,
Spraggon L.,
Squares S.L.,
Steward C.A.,
Sycamore N.,
Tamlyn-Hall G.,
Tester J.,
Theaker A.J.,
Thomas D.W.,
Thorpe A.,
Tracey A.,
Tromans A.,
Tubby B.,
Wall M.,
Wallis J.M.,
West A.P.,
White S.S.,
Whitehead S.L.,
Whittaker H.,
Wild A.,
Willey D.J.,
Wilmer T.E.,
Wood J.M.,
Wray P.W.,
Wyatt J.C.,
Young L.,
Younger R.M.,
Bentley D.R.,
Coulson A.,
Durbin R.M.,
Hubbard T.,
Sulston J.E.,
Dunham I.,
Rogers J.,
Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-230, AND INVOLVEMENT IN SCA1.
DOI=10.1093/hmg/4.12.2411; PubMed=8634720 [NCBI, ExPASy, EBI, Israel, Japan]
Quan F.,
Janas J.,
Popovich B.W.;
"A novel CAG repeat configuration in the SCA1 gene: implications for the molecular diagnostics of spinocerebellar ataxia type 1.";
Hum. Mol. Genet. 4:2411-2413(1995).
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[5]
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SELF-ASSOCIATION SITE.
DOI=10.1093/hmg/6.4.513; PubMed=9097953 [NCBI, ExPASy, EBI, Israel, Japan]
Burright E.N.,
Davidson J.D.,
Duvick L.A.,
Koshy B.,
Zoghbi H.Y.,
Orr H.T.;
"Identification of a self-association region within the SCA1 gene product, ataxin-1.";
Hum. Mol. Genet. 6:513-518(1997).
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[6]
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INTERACTION WITH ANP32A.
DOI=10.1038/40159; PubMed=9353121 [NCBI, ExPASy, EBI, Israel, Japan]
Matilla A.,
Koshy B.T.,
Cummings C.J.,
Isobe T.,
Orr H.T.,
Zoghbi H.Y.;
"The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1.";
Nature 389:974-978(1997).
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[7]
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RNA-BINDING DOMAIN.
DOI=10.1093/hmg/10.1.25; PubMed=11136710 [NCBI, ExPASy, EBI, Israel, Japan]
Yue S.,
Serra H.G.,
Zoghbi H.Y.,
Orr H.T.;
"The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract.";
Hum. Mol. Genet. 10:25-30(2001).
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[8]
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INTERACTION WITH UBIN.
PubMed=11001934 [NCBI, ExPASy, EBI, Israel, Japan]
Davidson J.D.,
Riley B.,
Burright E.N.,
Duvick L.A.,
Zoghbi H.Y.,
Orr H.T.;
"Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein.";
Hum. Mol. Genet. 9:2305-2312(2000).
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[9]
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INTERACTION WITH PQBP1.
DOI=10.1016/S0896-6273(02)00697-9; PubMed=12062018 [NCBI, ExPASy, EBI, Israel, Japan]
Okazawa H.,
Rich T.,
Chang A.,
Lin X.,
Waragai M.,
Kajikawa M.,
Enokido Y.,
Komuro A.,
Kato S.,
Shibata M.,
Hatanaka H.,
Mouradian M.M.,
Sudol M.,
Kanazawa I.;
"Interaction between mutant ataxin-1 and PQBP-1 affects transcription and cell death.";
Neuron 34:701-713(2002).
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[10]
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SUBCELLULAR LOCATION, AND INTERACTION WITH USP7.
DOI=10.1006/mcne.2002.1103; PubMed=12093161 [NCBI, ExPASy, EBI, Israel, Japan]
Hong S.,
Kim S.J.,
Ka S.,
Choi I.,
Kang S.;
"USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product.";
Mol. Cell. Neurosci. 20:298-306(2002).
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[11]
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INTERACTION WITH ATXN1L.
DOI=10.1038/sj.emboj.7600785; PubMed=16121196 [NCBI, ExPASy, EBI, Israel, Japan]
Mizutani A.,
Wang L.,
Rajan H.,
Vig P.J.S.,
Alaynick W.A.,
Thaler J.P.,
Tsai C.-C.;
"Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1.";
EMBO J. 24:3339-3351(2005).
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[12]
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INTERACTION WITH ZNF804A.
DOI=10.1016/j.cell.2006.03.032; PubMed=16713569 [NCBI, ExPASy, EBI, Israel, Japan]
Lim J.,
Hao T.,
Shaw C.,
Patel A.J.,
Szabo G.,
Rual J.-F.,
Fisk C.J.,
Li N.,
Smolyar A.,
Hill D.E.,
Barabasi A.-L.,
Vidal M.,
Zoghbi H.Y.;
"A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.";
Cell 125:801-814(2006).
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[13]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238 AND SER-253, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N.,
Zhou C.,
Villen J.,
Beausoleil S.A.,
Bakalarski C.E.,
Elledge S.J.,
Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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- FUNCTION: Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function.
- SUBUNIT: Interacts with CIC (By similarity). Interacts with ANP32A, PQBP1, UBIN, ATXN1L, USP7 and ZNF804A.
- INTERACTION:
Self; NbExp=2; IntAct=EBI-930964, EBI-930964;
Q99700:ATXN2; NbExp=1; IntAct=EBI-930964, EBI-697691;
P48634:BAT2; NbExp=1; IntAct=EBI-930964, EBI-347545;
Q6P1W5:C1orf94; NbExp=1; IntAct=EBI-930964, EBI-946029;
O75909:CCNK; NbExp=1; IntAct=EBI-930964, EBI-739806;
P23528:CFL1; NbExp=1; IntAct=EBI-930964, EBI-352733;
P38432:COIL; NbExp=5; IntAct=EBI-930975, EBI-945751;
Q8N684:CPSF7; NbExp=1; IntAct=EBI-930964, EBI-746909;
P46108:CRK; NbExp=1; IntAct=EBI-930964, EBI-886;
Q15038:DAZAP2; NbExp=1; IntAct=EBI-930964, EBI-724310;
Q8TE02:DERP6; NbExp=1; IntAct=EBI-930964, EBI-946189;
Q9NWB1:FOX1; NbExp=1; IntAct=EBI-930964, EBI-945906;
P15822:HIVEP1; NbExp=1; IntAct=EBI-930964, EBI-722264;
Q92993:HTATIP; NbExp=1; IntAct=EBI-930964, EBI-399080;
P53990:KIAA0174; NbExp=1; IntAct=EBI-930964, EBI-945994;
Q53G59:KLHL12; NbExp=1; IntAct=EBI-930964, EBI-740929;
O43809:NUDT21; NbExp=1; IntAct=EBI-930964, EBI-355720;
Q9HAU0:PLEKHA5; NbExp=1; IntAct=EBI-930964, EBI-945934;
O43251:RBM9; NbExp=1; IntAct=EBI-930964, EBI-746056;
Q93062:RBPMS; NbExp=1; IntAct=EBI-930964, EBI-740322;
Q8N196:SIX5; NbExp=1; IntAct=EBI-930964, EBI-946167;
Q92609:TBC1D5; NbExp=1; IntAct=EBI-930964, EBI-742381;
Q12933:TRAF2; NbExp=1; IntAct=EBI-930964, EBI-355744;
Q13049:TRIM32; NbExp=1; IntAct=EBI-930964, EBI-742790;
P26368:U2AF2; NbExp=1; IntAct=EBI-930964, EBI-742339;
Q9NRR5:UBQLN4; NbExp=3; IntAct=EBI-930964, EBI-711226;
Q70EL1:USP54; NbExp=1; IntAct=EBI-930964, EBI-946185;
Q9H869:YY1AP1; NbExp=1; IntAct=EBI-930964, EBI-946122;
Q9UKY1:ZHX1; NbExp=1; IntAct=EBI-930964, EBI-347767;
- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus. Note=Colocalizes with USP7 in the nucleus.
- ALTERNATIVE PRODUCTS:
1 named isoform [FASTA] produced by alternative splicing. At least 2 isoforms are produced.
- TISSUE SPECIFICITY: Widely expressed throughout the body.
- DOMAIN: The AXH domain is required for interaction with CIC (By similarity).
- POLYMORPHISM: The poly-Gln region of ATXN1 is highly polymorphic (4 to 39 repeats) in the normal population and is expanded to about 40-83 repeats in spinocerebellar ataxia 1 (SCA1) patients.
- DISEASE: Defects in ATXN1 are the cause of spinocerebellar ataxia type 1 (SCA1) [MIM:164400]; also known as olivopontocerebellar atrophy I (OPCA I or OPCA1). 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 cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA1 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. SCA1 is caused by expansion of a CAG repeat in the coding region of ATXN1. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.
- MISCELLANEOUS: The self-association seems to be necessary to form nuclear aggregates.
- SIMILARITY: Belongs to the ATXN1 family.
- SIMILARITY: Contains 1 AXH domain.
- WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ATXN1";.
- WEB RESOURCE: Name=Wikipedia; Note=Ataxin-1 entry; URL="http://en.wikipedia.org/wiki/Ataxin_1";.
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