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P54253 (ATX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ataxin-1
Alternative name(s):
Spinocerebellar ataxia type 1 protein
Gene names
Name:ATXN1
Synonyms:ATX1, SCA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length815 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism. The expansion of the polyglutamine tract may alter this function. Ref.16

Subunit structure

Homooligomer. Interacts with CIC By similarity. Interacts with ANP32A, PQBP1, UBQLN4, ATXN1L, USP7 and ZNF804A. Directly interacts with RBPJ; this interaction is disrupted in the presence of Notch intracellular domain. Competes with ATXN1L for RBPJ-binding. Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.16 Ref.17

Subcellular location

Cytoplasm By similarity. Nucleus. Note: Colocalizes with USP7 in the nucleus. Ref.10

Tissue specificity

Widely expressed throughout the body.

Domain

The AXH domain is required for interaction with CIC By similarity. Ref.7

Post-translational modification

Phosphorylation at Ser-775 increases the pathogenicity of proteins with an expanded polyglutamine tract.

Sumoylation is dependent on nuclear localization and phosphorylation at Ser-775. It is reduced in the presence of an expanded polyglutamine tract. Ref.13

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.

Involvement in disease

Spinocerebellar ataxia 1 (SCA1) [MIM:164400]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.4

Miscellaneous

Self-association seems to be necessary for formation of nuclear aggregates which are associated with pathogenesis.

Sequence similarities

Belongs to the ATXN1 family.

Contains 1 AXH domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
Triplet repeat expansion
   DiseaseNeurodegeneration
Spinocerebellar ataxia
   LigandDNA-binding
RNA-binding
   Molecular functionRepressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Non-traceable author statement PubMed 15615787. Source: UniProtKB

adult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of phosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15016912. Source: UniProtKB

nuclear export

Inferred from direct assay PubMed 15615787. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 7647801. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear inclusion body

Inferred from direct assay PubMed 15615787. Source: UniProtKB

nuclear matrix

Inferred from direct assay PubMed 17557114. Source: UniProtKB

nucleoplasm

Inferred from direct assay PubMed 12757932. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 7647801. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction Ref.8Ref.14. Source: IntAct

poly(G) binding

Inferred from direct assay Ref.7. Source: UniProtKB

poly(U) RNA binding

Inferred from direct assay Ref.7. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 12757932PubMed 15016912. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.10PubMed 15016912PubMed 17557114. Source: UniProtKB

protein self-association

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: At least 2 isoforms are produced.
Isoform 1 (identifier: P54253-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 815815Ataxin-1
PRO_0000064751

Regions

Domain562 – 693132AXH
Region494 – 604111Self-association
Region538 – 815278Interaction with USP7
Region540 – 766227RNA-binding
Motif794 – 7974Nuclear localization signal By similarity
Compositional bias197 – 22529Poly-Gln

Amino acid modifications

Modified residue2381Phosphoserine Ref.15
Modified residue7751Phosphoserine Ref.11
Cross-link16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13
Cross-link194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13
Cross-link609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13
Cross-link696Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13
Cross-link745Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Natural variant2091H → Q.
Corresponds to variant rs11969612 [ dbSNP | Ensembl ].
VAR_046616
Natural variant7531P → S.
Corresponds to variant rs16885 [ dbSNP | Ensembl ].
VAR_046617

Experimental info

Mutagenesis161K → R: Sumoylation reduced to 40% of wild-type. Ref.13
Mutagenesis1941K → R: Sumoylation reduced to 46% of wild-type. Ref.13
Mutagenesis4201K → R: No effect on sumoylation. Ref.13
Mutagenesis5291K → R: Sumoylation reduced to 57% of wild-type. Ref.13
Mutagenesis5891K → R: Sumoylation reduced to 53% of wild-type. Ref.13
Mutagenesis5941K → R: Sumoylation reduced to 68% of wild-type. Ref.13
Mutagenesis6091K → R: Sumoylation reduced to 43% of wild-type. Ref.13
Mutagenesis6911K → R: No effect on sumoylation. Ref.13
Mutagenesis6961K → R: Sumoylation reduced to 42% of wild-type. Ref.13
Mutagenesis7451K → R: Sumoylation reduced to 44% of wild-type. Ref.13
Mutagenesis7751S → A: Reduces phosphorylation but does not affect nuclear localization. Ref.11
Mutagenesis7841K → R: Sumoylation reduced to 62% of wild-type. Ref.13
Sequence conflict2111H → HQ in CAA55793. Ref.1

Secondary structure

............................ 815
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 23, 2008. Version 2.
Checksum: 657876F8FD19ECB2

FASTA81586,923
        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 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of the gene causing type 1 spinocerebellar ataxia."
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.
Nat. Genet. 7:513-519(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN SCA1.
Tissue: Brain and Cerebellum.
[2]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"A novel CAG repeat configuration in the SCA1 gene: implications for the molecular diagnostics of spinocerebellar ataxia type 1."
Quan F., Janas J., Popovich B.W.
Hum. Mol. Genet. 4:2411-2413(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-230, INVOLVEMENT IN SCA1.
[5]"Identification of a self-association region within the SCA1 gene product, ataxin-1."
Burright E.N., Davidson J.D., Duvick L.A., Koshy B., Zoghbi H.Y., Orr H.T.
Hum. Mol. Genet. 6:513-518(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-ASSOCIATION SITE.
[6]"The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1."
Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y.
Nature 389:974-978(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANP32A.
[7]"The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract."
Yue S., Serra H.G., Zoghbi H.Y., Orr H.T.
Hum. Mol. Genet. 10:25-30(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING DOMAIN.
[8]"Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein."
Davidson J.D., Riley B., Burright E.N., Duvick L.A., Zoghbi H.Y., Orr H.T.
Hum. Mol. Genet. 9:2305-2312(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBQLN4.
[9]"Interaction between mutant ataxin-1 and PQBP-1 affects transcription and cell death."
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.
Neuron 34:701-713(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PQBP1.
[10]"USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product."
Hong S., Kim S.J., Ka S., Choi I., Kang S.
Mol. Cell. Neurosci. 20:298-306(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH USP7.
[11]"Serine 776 of ataxin-1 is critical for polyglutamine-induced disease in SCA1 transgenic mice."
Emamian E.S., Kaytor M.D., Duvick L.A., Zu T., Tousey S.K., Zoghbi H.Y., Clark H.B., Orr H.T.
Neuron 38:375-387(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-775, MUTAGENESIS OF SER-775.
[12]"Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1."
Mizutani A., Wang L., Rajan H., Vig P.J.S., Alaynick W.A., Thaler J.P., Tsai C.-C.
EMBO J. 24:3339-3351(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATXN1L.
[13]"SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal."
Riley B.E., Zoghbi H.Y., Orr H.T.
J. Biol. Chem. 280:21942-21948(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-16; LYS-194; LYS-609; LYS-696 AND LYS-745, MUTAGENESIS OF LYS-16; LYS-194; LYS-420; LYS-529; LYS-589; LYS-594; LYS-609; LYS-691; LYS-696; LYS-745 AND LYS-784.
[14]"A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration."
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.
Cell 125:801-814(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF804A.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Ataxin-1 and Brother of ataxin-1 are components of the Notch signalling pathway."
Tong X., Gui H., Jin F., Heck B.W., Lin P., Ma J., Fondell J.D., Tsai C.C.
EMBO Rep. 12:428-435(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RBPJ.
[17]"The structure of the AXH domain of spinocerebellar ataxin-1."
Chen Y.W., Allen M.D., Veprintsev D.B., Lowe J., Bycroft M.
J. Biol. Chem. 279:3758-3765(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 563-693, SUBUNIT.
+Additional computationally mapped references.

Web resources

Wikipedia

Ataxin-1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79204 mRNA. Translation: CAA55793.1.
AL009031 Genomic DNA. Translation: CAA15622.1.
BC117125 mRNA. Translation: AAI17126.1.
S82497 Genomic DNA. Translation: AAD14401.1.
CCDSCCDS34342.1. [P54253-1]
PIRS46268.
RefSeqNP_000323.2. NM_000332.3. [P54253-1]
NP_001121636.1. NM_001128164.1. [P54253-1]
UniGeneHs.434961.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OA8X-ray1.70A/B/C/D562-693[»]
2M41NMR-B566-688[»]
4APTX-ray2.50A/B/C/D566-688[»]
4AQPX-ray2.45A/B/C/D566-688[»]
4J2JX-ray2.50A/B/C562-688[»]
4J2LX-ray3.15A/B562-688[»]
ProteinModelPortalP54253.
SMRP54253. Positions 573-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112217. 249 interactions.
DIPDIP-35353N.
IntActP54253. 242 interactions.
MINTMINT-266093.
STRING9606.ENSP00000244769.

PTM databases

PhosphoSiteP54253.

Polymorphism databases

DMDM206729854.

Proteomic databases

MaxQBP54253.
PaxDbP54253.
PRIDEP54253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244769; ENSP00000244769; ENSG00000124788. [P54253-1]
ENST00000436367; ENSP00000416360; ENSG00000124788. [P54253-1]
GeneID6310.
KEGGhsa:6310.
UCSCuc003nbt.3. human. [P54253-1]

Organism-specific databases

CTD6310.
GeneCardsGC06M016299.
GeneReviewsATXN1.
H-InvDBHIX0032878.
HGNCHGNC:10548. ATXN1.
HPAHPA008335.
MIM164400. phenotype.
601556. gene.
neXtProtNX_P54253.
Orphanet98755. Spinocerebellar ataxia type 1.
PharmGKBPA34958.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306883.
HOGENOMHOG000034225.
HOVERGENHBG004319.
OMAHRSYALS.
OrthoDBEOG7SBNQX.
PhylomeDBP54253.
TreeFamTF350643.

Gene expression databases

BgeeP54253.
CleanExHS_ATXN1.
GenevestigatorP54253.

Family and domain databases

InterProIPR013723. Ataxin-1_HBP1.
IPR003652. Ataxin_AXH_dom.
IPR020997. Capicua_tscrpt_rep_mod.
[Graphical view]
PfamPF12547. ATXN-1_C. 1 hit.
PF08517. AXH. 1 hit.
[Graphical view]
SMARTSM00536. AXH. 1 hit.
[Graphical view]
SUPFAMSSF102031. SSF102031. 1 hit.
PROSITEPS51148. AXH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATXN1. human.
EvolutionaryTraceP54253.
GeneWikiAtaxin_1.
GenomeRNAi6310.
NextBio24497.
PROP54253.
SOURCESearch...

Entry information

Entry nameATX1_HUMAN
AccessionPrimary (citable) accession number: P54253
Secondary accession number(s): Q17S02, Q9UJG2, Q9Y4J1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM