Ataxin 1

Ataxin 1

PDB rendering based on 1oa8.
Identifiers
Symbols ATXN1; ATX1; D6S504E; SCA1
External IDs OMIM: 601556 MGI: 104783 HomoloGene: 281 GeneCards: ATXN1 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 6310 20238
Ensembl ENSG00000124788 ENSMUSG00000046876
UniProt P54253 Q8C866
RefSeq (mRNA) NM_000332.3 NM_009124
RefSeq (protein) NP_000323.2 NP_033150
Location (UCSC) Chr 6:
16.3 – 16.76 Mb		 Chr 13:
45.65 – 46.06 Mb
PubMed search [1] [2]

Ataxin-1 is a protein that in humans is encoded by the ATXN1 gene.[1][2]

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.[2]

[3] [4] [5] [6] [7] [8]

Interactions

Ataxin 1 has been shown to interact with Glyceraldehyde 3-phosphate dehydrogenase,[9] Coilin,[10][11] USP7[12] and UBE2E1.[11]

References

  1. ^ Volz A, Fonatsch C, Ziegler A (Jun 1992). "Regional mapping of the gene for autosomal dominant spinocerebellar ataxia (SCA1) by localizing the closely linked D6S89 locus to 6p24.2----p23.05". Cytogenet Cell Genet 60 (1): 37–9. doi:10.1159/000133291. PMID 1582256. 
  2. ^ a b "Entrez Gene: ATXN1 ataxin 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6310. 
  3. ^ 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 (2006). "CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation". J. Biol. Chem. 281 (36): 26714–24. doi:10.1074/jbc.M601603200. PMID 16831871. 
  4. ^ de Chiara C, Menon RP, Dal Piaz F, Calder L, Pastore A (2005). "Polyglutamine is not all: the functional role of the AXH domain in the ataxin-1 protein". J. Mol. Biol. 354 (4): 883–93. doi:10.1016/j.jmb.2005.09.083. PMID 16277991. 
  5. ^ Tsuda H, Jafar-Nejad H, Patel AJ, Sun Y, Chen HK, Rose MF, Venken KJ, Botas J, Orr HT, Bellen HJ, Zoghbi HY (2005). "The AXH domain of Ataxin-1 mediates neurodegeneration through its interaction with Gfi-1/Senseless proteins". Cell 122 (4): 633–44. doi:10.1016/j.cell.2005.06.012. PMID 16122429. 
  6. ^ Mizutani A, Wang L, Rajan H, Vig PJ, Alaynick WA, Thaler JP, Tsai CC (2005). "Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1". EMBO J. 24 (18): 3339–51. doi:10.1038/sj.emboj.7600785. PMC 1224676. PMID 16121196. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1224676. 
  7. ^ Park Y, Hong S, Kim SJ, Kang S (2005). "Proteasome function is inhibited by polyglutamine-expanded ataxin-1, the SCA1 gene product". Mol. Cells 19 (1): 23–30. PMID 15750336. 
  8. ^ Irwin S, Vandelft M, Pinchev D, Howell JL, Graczyk J, Orr HT, Truant R (2005). "RNA association and nucleocytoplasmic shuttling by ataxin-1". J. Cell. Sci. 118 (Pt 1): 233–42. doi:10.1242/jcs.01611. PMID 15615787. 
  9. ^ Koshy, B; Matilla T, Burright E N, Merry D E, Fischbeck K H, Orr H T, Zoghbi H Y (Sep. 1996). "Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase". Hum. Mol. Genet. (ENGLAND) 5 (9): 1311–8. doi:10.1093/hmg/5.9.1311. ISSN 0964-6906. PMID 8872471. 
  10. ^ Hong, Sunghoi; Ka Sojeong, Kim Sungjo, Park Yongjae, Kang Seongman (May. 2003). "p80 coilin, a coiled body-specific protein, interacts with ataxin-1, the SCA1 gene product". Biochim. Biophys. Acta (Netherlands) 1638 (1): 35–42. ISSN 0006-3002. PMID 12757932. 
  11. ^ a b Hong, Sunghoi; Lee Soyeon, Cho Ssang-Goo, Kang Seongman (Jun. 2008). "UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1". Biochem. Biophys. Res. Commun. (United States) 371 (2): 256–60. doi:10.1016/j.bbrc.2008.04.066. PMID 18439907. 
  12. ^ Hong, Sunghoi; Kim Sung-Jo, Ka Sojeong, Choi Inho, Kang Seongman (Jun. 2002). "USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product". Mol. Cell. Neurosci. (United States) 20 (2): 298–306. doi:10.1006/mcne.2002.1103. ISSN 1044-7431. PMID 12093161. 

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.