SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P54253

- ATX1_HUMAN

UniProt

P54253 - ATX1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ataxin-1
Gene
ATXN1, ATX1, SCA1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 C-terminus binding Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. protein self-association Source: UniProtKB

GO - Biological processi

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

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
Note: Colocalizes with USP7 in the nucleus.1 Publication

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
Complete GO annotation...

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

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-1
PRO_0000064751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki194 – 194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei238 – 2381Phosphoserine1 Publication
Cross-linki609 – 609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki696 – 696Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki745 – 745Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei775 – 7751Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication

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.8 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

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.

Miscellaneous databases

EvolutionaryTraceiP54253.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini562 – 693132AXH
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni494 – 604111Self-association
Add
BLAST
Regioni538 – 815278Interaction with USP7
Add
BLAST
Regioni540 – 766227RNA-binding
Add
BLAST

Motif

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

Compositional bias

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

Domaini

The AXH domain is required for interaction with CIC By similarity.1 Publication

Sequence similaritiesi

Belongs to the ATXN1 family.
Contains 1 AXH domain.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti211 – 2111H → HQ in CAA55793. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 142 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

Similar proteinsi