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P54253

- ATX1_HUMAN

UniProt

P54253 - ATX1_HUMAN

Protein

Ataxin-1

Gene

ATXN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. poly(G) binding Source: UniProtKB
    4. poly(U) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein C-terminus binding Source: UniProtKB
    7. protein self-association Source: UniProtKB

    GO - Biological processi

    1. adult locomotory behavior Source: Ensembl
    2. cell death Source: UniProtKB-KW
    3. negative regulation of insulin-like growth factor receptor signaling pathway Source: Ensembl
    4. negative regulation of phosphorylation Source: Ensembl
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. nuclear export Source: UniProtKB
    7. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    8. regulation of excitatory postsynaptic membrane potential Source: Ensembl
    9. RNA processing Source: UniProtKB
    10. transcription, DNA-templated Source: UniProtKB-KW
    11. visual learning Source: Ensembl

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ataxin-1
    Alternative name(s):
    Spinocerebellar ataxia type 1 protein
    Gene namesi
    Name:ATXN1
    Synonyms:ATX1, SCA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10548. ATXN1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus 1 Publication
    Note: Colocalizes with USP7 in the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. intracellular membrane-bounded organelle Source: HPA
    3. nuclear inclusion body Source: UniProtKB
    4. nuclear matrix Source: UniProtKB
    5. nucleoplasm Source: UniProtKB
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161K → R: Sumoylation reduced to 40% of wild-type. 1 Publication
    Mutagenesisi194 – 1941K → R: Sumoylation reduced to 46% of wild-type. 1 Publication
    Mutagenesisi420 – 4201K → R: No effect on sumoylation. 1 Publication
    Mutagenesisi529 – 5291K → R: Sumoylation reduced to 57% of wild-type. 1 Publication
    Mutagenesisi589 – 5891K → R: Sumoylation reduced to 53% of wild-type. 1 Publication
    Mutagenesisi594 – 5941K → R: Sumoylation reduced to 68% of wild-type. 1 Publication
    Mutagenesisi609 – 6091K → R: Sumoylation reduced to 43% of wild-type. 1 Publication
    Mutagenesisi691 – 6911K → R: No effect on sumoylation. 1 Publication
    Mutagenesisi696 – 6961K → R: Sumoylation reduced to 42% of wild-type. 1 Publication
    Mutagenesisi745 – 7451K → R: Sumoylation reduced to 44% of wild-type. 1 Publication
    Mutagenesisi775 – 7751S → A: Reduces phosphorylation but does not affect nuclear localization. 1 Publication
    Mutagenesisi784 – 7841K → R: Sumoylation reduced to 62% of wild-type. 1 Publication

    Keywords - Diseasei

    Neurodegeneration, Spinocerebellar ataxia

    Organism-specific databases

    MIMi164400. phenotype.
    Orphaneti98755. Spinocerebellar ataxia type 1.
    PharmGKBiPA34958.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 815815Ataxin-1PRO_0000064751Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki194 – 194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei238 – 2381Phosphoserine1 Publication
    Cross-linki609 – 609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki696 – 696Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki745 – 745Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei775 – 7751Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-775 increases the pathogenicity of proteins with an expanded polyglutamine tract.2 Publications
    Sumoylation is dependent on nuclear localization and phosphorylation at Ser-775. It is reduced in the presence of an expanded polyglutamine tract.3 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP54253.
    PaxDbiP54253.
    PRIDEiP54253.

    PTM databases

    PhosphoSiteiP54253.

    Expressioni

    Tissue specificityi

    Widely expressed throughout the body.

    Gene expression databases

    BgeeiP54253.
    CleanExiHS_ATXN1.
    GenevestigatoriP54253.

    Organism-specific databases

    HPAiHPA008335.

    Interactioni

    Subunit structurei

    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.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-930964,EBI-930964
    ARID5AQ039893EBI-930964,EBI-948603
    ATXN2Q997004EBI-930964,EBI-697691
    C1orf94Q6P1W53EBI-930964,EBI-946029
    CCNKO759092EBI-930964,EBI-739806
    CFL1P235285EBI-930964,EBI-352733
    CICQ96RK05EBI-930964,EBI-945857
    COILP384326EBI-930975,EBI-945751
    CPSF7Q8N6842EBI-930964,EBI-746909
    CRKP461083EBI-930964,EBI-886
    DAZAP2Q150382EBI-930964,EBI-724310
    ELP5Q8TE022EBI-930964,EBI-946189
    GPATCH8Q9UKJ34EBI-930964,EBI-948259
    HIVEP1P158226EBI-930964,EBI-722264
    HSFX2Q9UBD03EBI-930964,EBI-947253
    IST1P539902EBI-930964,EBI-945994
    KAT5Q929933EBI-930964,EBI-399080
    KLHL12Q53G592EBI-930964,EBI-740929
    METTL17Q9H7H05EBI-930964,EBI-749353
    NUDT21O438092EBI-930964,EBI-355720
    PLEKHA5Q9HAU02EBI-930964,EBI-945934
    PRRC2AP486344EBI-930964,EBI-347545
    RBFOX1Q9NWB12EBI-930964,EBI-945906
    RBFOX2O432517EBI-930964,EBI-746056
    RBPJQ063307EBI-930964,EBI-632552
    RBPMSQ930623EBI-930964,EBI-740322
    RCN1Q152933EBI-930964,EBI-948278
    SIX5Q8N1964EBI-930964,EBI-946167
    SYBUQ9NX953EBI-930964,EBI-948293
    TBC1D5Q926092EBI-930964,EBI-742381
    TRAF2Q129332EBI-930964,EBI-355744
    TRIM32Q130492EBI-930964,EBI-742790
    U2AF2P263684EBI-930964,EBI-742339
    UBQLN4Q9NRR56EBI-930964,EBI-711226
    USP54Q70EL13EBI-930964,EBI-946185
    VSTM2LQ96N033EBI-930964,EBI-948213
    YY1AP1Q9H8694EBI-930964,EBI-946122
    ZC3H10Q96K804EBI-930964,EBI-742550
    ZHX1Q9UKY15EBI-930964,EBI-347767
    ZNF488Q96MN93EBI-930964,EBI-948288

    Protein-protein interaction databases

    BioGridi112217. 249 interactions.
    DIPiDIP-35353N.
    IntActiP54253. 242 interactions.
    MINTiMINT-266093.
    STRINGi9606.ENSP00000244769.

    Structurei

    Secondary structure

    1
    815
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi568 – 5703
    Helixi572 – 5743
    Beta strandi579 – 5813
    Beta strandi587 – 5893
    Helixi590 – 5923
    Helixi595 – 60410
    Beta strandi606 – 62015
    Beta strandi626 – 6338
    Turni634 – 6374
    Beta strandi638 – 6458
    Beta strandi650 – 6523
    Turni653 – 6553
    Beta strandi656 – 6605
    Helixi662 – 6698
    Beta strandi673 – 6753
    Beta strandi681 – 6877

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP54253.
    SMRiP54253. Positions 573-693.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54253.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini562 – 693132AXHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni494 – 604111Self-associationAdd
    BLAST
    Regioni538 – 815278Interaction with USP7Add
    BLAST
    Regioni540 – 766227RNA-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi794 – 7974Nuclear localization signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi197 – 22529Poly-GlnAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the ATXN1 family.Curated
    Contains 1 AXH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG306883.
    HOGENOMiHOG000034225.
    HOVERGENiHBG004319.
    OMAiHRSYALS.
    OrthoDBiEOG7SBNQX.
    PhylomeDBiP54253.
    TreeFamiTF350643.

    Family and domain databases

    InterProiIPR013723. Ataxin-1_HBP1.
    IPR003652. Ataxin_AXH_dom.
    IPR020997. Capicua_tscrpt_rep_mod.
    [Graphical view]
    PfamiPF12547. ATXN-1_C. 1 hit.
    PF08517. AXH. 1 hit.
    [Graphical view]
    SMARTiSM00536. AXH. 1 hit.
    [Graphical view]
    SUPFAMiSSF102031. SSF102031. 1 hit.
    PROSITEiPS51148. AXH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. Align

    Note: At least 2 isoforms are produced.

    Isoform 1 (identifier: P54253-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MKSNQERSNE CLPPKKREIP ATSRSSEEKA PTLPSDNHRV EGTAWLPGNP    50
    GGRGHGGGRH GPAGTSVELG LQQGIGLHKA LSTGLDYSPP SAPRSVPVAT 100
    TLPAAYATPQ PGTPVSPVQY AHLPHTFQFI GSSQYSGTYA SFIPSQLIPP 150
    TANPVTSAVA SAAGATTPSQ RSQLEAYSTL LANMGSLSQT PGHKAEQQQQ 200
    QQQQQQQQHQ HQQQQQQQQQ QQQQQHLSRA PGLITPGSPP PAQQNQYVHI 250
    SSSPQNTGRT ASPPAIPVHL HPHQTMIPHT LTLGPPSQVV MQYADSGSHF 300
    VPREATKKAE SSRLQQAIQA KEVLNGEMEK SRRYGAPSSA DLGLGKAGGK 350
    SVPHPYESRH VVVHPSPSDY SSRDPSGVRA SVMVLPNSNT PAADLEVQQA 400
    THREASPSTL NDKSGLHLGK PGHRSYALSP HTVIQTTHSA SEPLPVGLPA 450
    TAFYAGTQPP VIGYLSGQQQ AITYAGSLPQ HLVIPGTQPL LIPVGSTDME 500
    ASGAAPAIVT SSPQFAAVPH TFVTTALPKS ENFNPEALVT QAAYPAMVQA 550
    QIHLPVVQSV ASPAAAPPTL PPYFMKGSII QLANGELKKV EDLKTEDFIQ 600
    SAEISNDLKI DSSTVERIED SHSPGVAVIQ FAVGEHRAQV SVEVLVEYPF 650
    FVFGQGWSSC CPERTSQLFD LPCSKLSVGD VCISLTLKNL KNGSVKKGQP 700
    VDPASVLLKH SKADGLAGSR HRYAEQENGI NQGSAQMLSE NGELKFPEKM 750
    GLPAAPFLTK IEPSKPAATR KRRWSAPESR KLEKSEDEPP LTLPKPSLIP 800
    QEVKICIEGR SNVGK 815
    Length:815
    Mass (Da):86,923
    Last modified:September 23, 2008 - v2
    Checksum:i657876F8FD19ECB2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti211 – 2111H → HQ in CAA55793. (PubMed:7951322)Curated

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti209 – 2091H → Q.
    Corresponds to variant rs11969612 [ dbSNP | Ensembl ].
    VAR_046616
    Natural varianti753 – 7531P → S.
    Corresponds to variant rs16885 [ dbSNP | Ensembl ].
    VAR_046617

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79204 mRNA. Translation: CAA55793.1.
    AL009031 Genomic DNA. Translation: CAA15622.1.
    BC117125 mRNA. Translation: AAI17126.1.
    S82497 Genomic DNA. Translation: AAD14401.1.
    CCDSiCCDS34342.1. [P54253-1]
    PIRiS46268.
    RefSeqiNP_000323.2. NM_000332.3. [P54253-1]
    NP_001121636.1. NM_001128164.1. [P54253-1]
    UniGeneiHs.434961.

    Genome annotation databases

    EnsembliENST00000244769; ENSP00000244769; ENSG00000124788. [P54253-1]
    ENST00000436367; ENSP00000416360; ENSG00000124788. [P54253-1]
    GeneIDi6310.
    KEGGihsa:6310.
    UCSCiuc003nbt.3. human. [P54253-1]

    Polymorphism databases

    DMDMi206729854.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, Triplet repeat expansion

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Ataxin-1 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79204 mRNA. Translation: CAA55793.1 .
    AL009031 Genomic DNA. Translation: CAA15622.1 .
    BC117125 mRNA. Translation: AAI17126.1 .
    S82497 Genomic DNA. Translation: AAD14401.1 .
    CCDSi CCDS34342.1. [P54253-1 ]
    PIRi S46268.
    RefSeqi NP_000323.2. NM_000332.3. [P54253-1 ]
    NP_001121636.1. NM_001128164.1. [P54253-1 ]
    UniGenei Hs.434961.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OA8 X-ray 1.70 A/B/C/D 562-693 [» ]
    2M41 NMR - B 566-688 [» ]
    4APT X-ray 2.50 A/B/C/D 566-688 [» ]
    4AQP X-ray 2.45 A/B/C/D 566-688 [» ]
    4J2J X-ray 2.50 A/B/C 562-688 [» ]
    4J2L X-ray 3.15 A/B 562-688 [» ]
    ProteinModelPortali P54253.
    SMRi P54253. Positions 573-693.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112217. 249 interactions.
    DIPi DIP-35353N.
    IntActi P54253. 242 interactions.
    MINTi MINT-266093.
    STRINGi 9606.ENSP00000244769.

    PTM databases

    PhosphoSitei P54253.

    Polymorphism databases

    DMDMi 206729854.

    Proteomic databases

    MaxQBi P54253.
    PaxDbi P54253.
    PRIDEi P54253.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244769 ; ENSP00000244769 ; ENSG00000124788 . [P54253-1 ]
    ENST00000436367 ; ENSP00000416360 ; ENSG00000124788 . [P54253-1 ]
    GeneIDi 6310.
    KEGGi hsa:6310.
    UCSCi uc003nbt.3. human. [P54253-1 ]

    Organism-specific databases

    CTDi 6310.
    GeneCardsi GC06M016299.
    GeneReviewsi ATXN1.
    H-InvDB HIX0032878.
    HGNCi HGNC:10548. ATXN1.
    HPAi HPA008335.
    MIMi 164400. phenotype.
    601556. gene.
    neXtProti NX_P54253.
    Orphaneti 98755. Spinocerebellar ataxia type 1.
    PharmGKBi PA34958.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG306883.
    HOGENOMi HOG000034225.
    HOVERGENi HBG004319.
    OMAi HRSYALS.
    OrthoDBi EOG7SBNQX.
    PhylomeDBi P54253.
    TreeFami TF350643.

    Miscellaneous databases

    ChiTaRSi ATXN1. human.
    EvolutionaryTracei P54253.
    GeneWikii Ataxin_1.
    GenomeRNAii 6310.
    NextBioi 24497.
    PROi P54253.
    SOURCEi Search...

    Gene expression databases

    Bgeei P54253.
    CleanExi HS_ATXN1.
    Genevestigatori P54253.

    Family and domain databases

    InterProi IPR013723. Ataxin-1_HBP1.
    IPR003652. Ataxin_AXH_dom.
    IPR020997. Capicua_tscrpt_rep_mod.
    [Graphical view ]
    Pfami PF12547. ATXN-1_C. 1 hit.
    PF08517. AXH. 1 hit.
    [Graphical view ]
    SMARTi SM00536. AXH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF102031. SSF102031. 1 hit.
    PROSITEi PS51148. AXH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiATX1_HUMAN
    AccessioniPrimary (citable) accession number: P54253
    Secondary accession number(s): Q17S02, Q9UJG2, Q9Y4J1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 143 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3