[1]	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).
[2]	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).
[3]	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).
[4]	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).
[5]	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).
[6]	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).
[7]	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).
[8]	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).
[9]	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).
[10]	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).
[11]	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).

Comments

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 and USP7.
INTERACTION:
Self; NbExp=2; IntAct=EBI-930964, EBI-930964;
Q9NWB1:A2BP1; NbExp=1; IntAct=EBI-930964, EBI-945906;
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;
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-946034;
Q9NRR5:UBQLN4; NbExp=3; IntAct=EBI-930964, EBI-711226;
Q6P1N6: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.

Name 1

Isoform ID P54253-1

This is the isoform sequence displayed in this entry.
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";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X79204; CAA55793.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL009031; CAA15622.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC117125; AAI17126.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S82497; AAD14401.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S46268; S46268.

UniGene

Hs.434961

3D structure databases

PDB

1OA8; X-ray; 1.70 A; A/B/C/D=562-693.

[ExPASy / RCSB / EBI]

PDBsum

1OA8; -.

ModBase

P54253.

Protein-protein interaction databases

IntAct

P54253; -.

PTM databases

PhosphoSite

P54253; -.

Organism-specific databases

HIX0032878; -.

HGNC:10548; ATXN1.

HPA008335; -.

164400; phenotype. [NCBI / EBI]
601556; gene. [NCBI / EBI]

Orphanet

99; Cerebellar ataxia, autosomal dominant.
102; Multiple system atrophy.

PharmGKB

PA34958; -.

GeneCards

P54253.

Gene expression databases

ArrayExpress

P54253; -.

CleanEx

HS_ATXN1; -.

GermOnline

ENSG00000124788; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0042405;	Cellular component: nuclear inclusion body (inferred from direct assay from UniProtKB).
GO:0016363;	Cellular component: nuclear matrix (inferred from direct assay from UniProtKB).
GO:0005654;	Cellular component: nucleoplasm (inferred from direct assay from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0034046;	Molecular function: poly(rG) binding (inferred from direct assay from UniProtKB).
GO:0008266;	Molecular function: poly(U) binding (inferred from direct assay from UniProtKB).
GO:0008022;	Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0043621;	Molecular function: protein self-association (inferred from direct assay from UniProtKB).
GO:0016564;	Molecular function: transcription repressor activity (inferred from direct assay from UniProtKB).
GO:0016481;	Biological process: negative regulation of transcription (inferred from direct assay from UniProtKB).
GO:0051168;	Biological process: nuclear export (inferred from direct assay from UniProtKB).
GO:0006396;	Biological process: RNA processing (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR013723; Ataxin-1_HBP1.
IPR003652; Ataxin_AXH.
Graphical view of domain structure.

Pfam

PF08517; AXH; 1.
Pfam graphical view of domain structure.

SMART

SM00536; AXH; 1.
SMART graphical view of domain structure.

PROSITE

PS51148; AXH; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P54253.

Genome annotation databases

Ensembl

ENSG00000124788; Homo sapiens. [Contig view]

KEGG

hsa:6310; -.

Phylogenomic databases

HOGENOM

P54253; -.

HOVERGEN

P54253; -.

Other

P54253; -.

ATXN1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Cytoplasm; Neurodegeneration; Nucleus; Polymorphism; RNA-binding; Spinocerebellar ataxia; Triplet repeat expansion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 815`	`815`	`Ataxin-1.`	`PRO_0000064751`
`DOMAIN`	`562 693`	`132`	`AXH.`
`REGION`	`494 604`	`111`	`Self-association.`
`REGION`	`538 815`	`278`	`Interaction with USP7.`
`REGION`	`540 766`	`227`	`RNA-binding.`
`MOTIF`	`794 797`	`4`	`Nuclear localization signal (By similarity).`
`COMPBIAS`	`197 225`	`29`	`Poly-Gln.`
`VARIANT`	`209 209`	`1`	`H -> Q (in dbSNP:rs11969612 [NCBI]).`	`VAR_046616`
`VARIANT`	`753 753`	`1`	`P -> S (in dbSNP:rs16885 [NCBI]).`	`VAR_046617`
`CONFLICT`	`211 211`		`H -> HQ (in Ref. 1; CAA55793).`
`HELIX`	`572 574`	`3`
`STRAND`	`579 581`	`3`
`STRAND`	`587 589`	`3`
`HELIX`	`590 592`	`3`
`HELIX`	`595 604`	`10`
`STRAND`	`606 620`	`15`
`STRAND`	`626 633`	`8`
`TURN`	`634 637`	`4`
`STRAND`	`638 645`	`8`
`STRAND`	`650 652`	`3`
`TURN`	`653 655`	`3`
`STRAND`	`656 660`	`5`
`HELIX`	`662 669`	`8`
`STRAND`	`681 687`	`7`

Sequence information

Length: 815 AA [This is the length of the unprocessed precursor]

Molecular weight: 86923 Da [This is the MW of the unprocessed precursor]

CRC64: 657876F8FD19ECB2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKSNQERSNE CLPPKKREIP ATSRSSEEKA PTLPSDNHRV EGTAWLPGNP GGRGHGGGRH 

        70         80         90        100        110        120 
GPAGTSVELG LQQGIGLHKA LSTGLDYSPP SAPRSVPVAT TLPAAYATPQ PGTPVSPVQY 

       130        140        150        160        170        180 
AHLPHTFQFI GSSQYSGTYA SFIPSQLIPP TANPVTSAVA SAAGATTPSQ RSQLEAYSTL 

       190        200        210        220        230        240 
LANMGSLSQT PGHKAEQQQQ QQQQQQQQHQ HQQQQQQQQQ QQQQQHLSRA PGLITPGSPP 

       250        260        270        280        290        300 
PAQQNQYVHI SSSPQNTGRT ASPPAIPVHL HPHQTMIPHT LTLGPPSQVV MQYADSGSHF 

       310        320        330        340        350        360 
VPREATKKAE SSRLQQAIQA KEVLNGEMEK SRRYGAPSSA DLGLGKAGGK SVPHPYESRH 

       370        380        390        400        410        420 
VVVHPSPSDY SSRDPSGVRA SVMVLPNSNT PAADLEVQQA THREASPSTL NDKSGLHLGK 

       430        440        450        460        470        480 
PGHRSYALSP HTVIQTTHSA SEPLPVGLPA TAFYAGTQPP VIGYLSGQQQ AITYAGSLPQ 

       490        500        510        520        530        540 
HLVIPGTQPL LIPVGSTDME ASGAAPAIVT SSPQFAAVPH TFVTTALPKS ENFNPEALVT 

       550        560        570        580        590        600 
QAAYPAMVQA QIHLPVVQSV ASPAAAPPTL PPYFMKGSII QLANGELKKV EDLKTEDFIQ 

       610        620        630        640        650        660 
SAEISNDLKI DSSTVERIED SHSPGVAVIQ FAVGEHRAQV SVEVLVEYPF FVFGQGWSSC 

       670        680        690        700        710        720 
CPERTSQLFD LPCSKLSVGD VCISLTLKNL KNGSVKKGQP VDPASVLLKH SKADGLAGSR 

       730        740        750        760        770        780 
HRYAEQENGI NQGSAQMLSE NGELKFPEKM GLPAAPFLTK IEPSKPAATR KRRWSAPESR 

       790        800        810 
KLEKSEDEPP LTLPKPSLIP QEVKICIEGR SNVGK

P54253 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools