Ataxin 1

Ataxin 1, also known as ATXN1, is a human gene.cite web | title = Entrez Gene: ATXN1 ataxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6310| accessdate = ]

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summary_text = The autosomal dominant cerebellar ataxias (ADCA) are a heterogeneous group of neurodegenerative disorders characterized by progressive degeneration of the cerebellum, brain stem and spinal cord. ADCAs include spinocerebellar ataxia type 1 (previously also known as olivopontocerebellar atrophy type 1). Clinically, ADCA has been divided into three groups: ADCA types I-III. ADCAI is genetically heterogeneous, with five genetic loci, designated spinocerebellar ataxia (SCA) 1, 2, 3, 4 and 6, being assigned to five different chromosomes. ADCAII, which always presents with retinal degeneration (SCA7), and ADCAIII often referred to as the `pure' cerebellar syndrome (SCA5), are most likely homogeneous disorders. Several SCA genes have been cloned and shown to contain CAG repeats in their coding regions. ADCA is caused by the expansion of the CAG repeats, producing an elongated polyglutamine tract in the corresponding protein. The expanded repeats are variable in size and unstable, usually increasing in size when transmitted to successive generations. The function of the ataxins is not known. This locus has been mapped to chromosome 6, and it has been determined that the diseased allele contains 41-81 CAG repeats, compared to 6-39 in the normal allele. Several transcript variants in the 5' UTR have been described; however, their full-length nature is not known.cite web | title = Entrez Gene: ATXN1 ataxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6310| accessdate = ]

cite journal | author = Al-Ramahi I, Lam YC, Chen HK, de Gouyon B, Zhang M, Pérez AM, Branco J, de Haro M, Patterson C, Zoghbi HY, Botas J | title = CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation | journal = J. Biol. Chem. | volume = 281 | issue = 36 | pages = 26714–24 | year = 2006 | pmid = 16831871 | doi = 10.1074/jbc.M601603200 | issn = ] cite journal | author = de Chiara C, Menon RP, Dal Piaz F, Calder L, Pastore A | title = Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein | journal = J. Mol. Biol. | volume = 354 | issue = 4 | pages = 883–93 | year = 2005 | pmid = 16277991 | doi = 10.1016/j.jmb.2005.09.083 | issn = ] cite journal | author = Tsuda H, Jafar-Nejad H, Patel AJ, Sun Y, Chen HK, Rose MF, Venken KJ, Botas J, Orr HT, Bellen HJ, Zoghbi HY | title = The AXH domain of Ataxin-1 mediates neurodegeneration through its interaction with Gfi-1/Senseless proteins | journal = Cell | volume = 122 | issue = 4 | pages = 633–44 | year = 2005 | pmid = 16122429 | doi = 10.1016/j.cell.2005.06.012 | issn = ] cite journal | author = Mizutani A, Wang L, Rajan H, Vig PJ, Alaynick WA, Thaler JP, Tsai CC | title = Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1 | journal = EMBO J. | volume = 24 | issue = 18 | pages = 3339–51 | year = 2005 | pmid = 16121196 | doi = 10.1038/sj.emboj.7600785 | issn = ] cite journal | author = Park Y, Hong S, Kim SJ, Kang S | title = Proteasome function is inhibited by polyglutamine-expanded ataxin-1, the SCA1 gene product | journal = Mol. Cells | volume = 19 | issue = 1 | pages = 23–30 | year = 2005 | pmid = 15750336 | doi = | issn = ] cite journal | author = Irwin S, Vandelft M, Pinchev D, Howell JL, Graczyk J, Orr HT, Truant R | title = RNA association and nucleocytoplasmic shuttling by ataxin-1 | journal = J. Cell. Sci. | volume = 118 | issue = Pt 1 | pages = 233–42 | year = 2005 | pmid = 15615787 | doi = 10.1242/jcs.01611 | issn = ]

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