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Protein

Ataxin-1

Gene

ATXN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.1 Publication

GO - Molecular functioni

  • chromatin binding Source: Ensembl
  • DNA binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • poly(G) binding Source: UniProtKB
  • poly(U) RNA binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein self-association Source: UniProtKB

GO - Biological processi

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 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:10548. ATXN1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • nuclear inclusion body Source: UniProtKB
  • nuclear matrix Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Spinocerebellar ataxia 1 (SCA1)3 Publications

The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by expansion of the polyglutamine tract to about 40-83 repeats, causing accumulation in neurons and exerting toxicity.

Disease descriptionSpinocerebellar 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.

See also OMIM:164400

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.

Polymorphism and mutation databases

BioMutaiATXN1.
DMDMi206729854.

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

Ubiquitinated by UBE3A, leading to its degradation by the proteasome. The presence of expanded poly-Gln repeats in spinocerebellar ataxia 1 (SCA1) patients impairs ubiquitination and degradation, leading to accumulation of ATXN1 in neurons and subsequent toxicity.By similarity
Phosphorylation at Ser-775 increases the pathogenicity of proteins with an expanded polyglutamine tract.1 Publication
Sumoylation is dependent on nuclear localization and phosphorylation at Ser-775. It is reduced in the presence of an expanded polyglutamine tract.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP54253.
PaxDbiP54253.
PRIDEiP54253.

PTM databases

PhosphoSiteiP54253.

Expressioni

Tissue specificityi

Widely expressed throughout the body.1 Publication

Inductioni

ATXN1 protein levels are directly regulated by PUM1 protein: PUM1 acts by binding to the 3'-UTR of ATXN1 mRNA, affecting ATXN1 mRNA stability and leading to reduced ATXN1 protein levels.1 Publication

Gene expression databases

BgeeiP54253.
CleanExiHS_ATXN1.
GenevisibleiP54253. HS.

Organism-specific databases

HPAiHPA008335.

Interactioni

Subunit structurei

Homooligomer (PubMed:9097953). Interacts with CIC (By similarity). Interacts with ANP32A, PQBP1, UBQLN4, ATXN1L, USP7 and ZNF804A (PubMed:9353121, PubMed:11001934, PubMed:12062018, PubMed:12093161, PubMed:16121196, PubMed:16713569). Directly interacts with RBPJ; this interaction is disrupted in the presence of Notch intracellular domain. Competes with ATXN1L for RBPJ-binding (PubMed:21475249).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-930964,EBI-930964
ARID5AQ039893EBI-930964,EBI-948603
ATXN2Q997004EBI-930964,EBI-697691
C1orf94Q6P1W56EBI-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
ESRP1Q6NXG13EBI-930964,EBI-10213520
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
PRR20CP864793EBI-930964,EBI-10172814
PRRC2AP486344EBI-930964,EBI-347545
RBFOX1Q9NWB12EBI-930964,EBI-945906
RBFOX2O4325110EBI-930964,EBI-746056
RBPJQ063307EBI-930964,EBI-632552
RBPMSQ930626EBI-930964,EBI-740322
RCN1Q152933EBI-930964,EBI-948278
RELQ048643EBI-930964,EBI-307352
SIX5Q8N1964EBI-930964,EBI-946167
SYBUQ9NX953EBI-930964,EBI-948293
TBC1D5Q926092EBI-930964,EBI-742381
TBX15Q96SF73EBI-930964,EBI-10191361
TRAF2Q129335EBI-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. 261 interactions.
DIPiDIP-35353N.
IntActiP54253. 246 interactions.
MINTiMINT-266093.
STRINGi9606.ENSP00000244769.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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-association1 PublicationAdd
BLAST
Regioni538 – 815278Interaction with USP71 PublicationAdd
BLAST
Regioni540 – 766227RNA-binding1 PublicationAdd
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.
GeneTreeiENSGT00390000005939.
HOGENOMiHOG000034225.
HOVERGENiHBG004319.
InParanoidiP54253.
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. AlignAdd to basket

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

        10         20         30         40         50
MKSNQERSNE CLPPKKREIP ATSRSSEEKA PTLPSDNHRV EGTAWLPGNP
60 70 80 90 100
GGRGHGGGRH GPAGTSVELG LQQGIGLHKA LSTGLDYSPP SAPRSVPVAT
110 120 130 140 150
TLPAAYATPQ PGTPVSPVQY AHLPHTFQFI GSSQYSGTYA SFIPSQLIPP
160 170 180 190 200
TANPVTSAVA SAAGATTPSQ RSQLEAYSTL LANMGSLSQT PGHKAEQQQQ
210 220 230 240 250
QQQQQQQQHQ HQQQQQQQQQ QQQQQHLSRA PGLITPGSPP PAQQNQYVHI
260 270 280 290 300
SSSPQNTGRT ASPPAIPVHL HPHQTMIPHT LTLGPPSQVV MQYADSGSHF
310 320 330 340 350
VPREATKKAE SSRLQQAIQA KEVLNGEMEK SRRYGAPSSA DLGLGKAGGK
360 370 380 390 400
SVPHPYESRH VVVHPSPSDY SSRDPSGVRA SVMVLPNSNT PAADLEVQQA
410 420 430 440 450
THREASPSTL NDKSGLHLGK PGHRSYALSP HTVIQTTHSA SEPLPVGLPA
460 470 480 490 500
TAFYAGTQPP VIGYLSGQQQ AITYAGSLPQ HLVIPGTQPL LIPVGSTDME
510 520 530 540 550
ASGAAPAIVT SSPQFAAVPH TFVTTALPKS ENFNPEALVT QAAYPAMVQA
560 570 580 590 600
QIHLPVVQSV ASPAAAPPTL PPYFMKGSII QLANGELKKV EDLKTEDFIQ
610 620 630 640 650
SAEISNDLKI DSSTVERIED SHSPGVAVIQ FAVGEHRAQV SVEVLVEYPF
660 670 680 690 700
FVFGQGWSSC CPERTSQLFD LPCSKLSVGD VCISLTLKNL KNGSVKKGQP
710 720 730 740 750
VDPASVLLKH SKADGLAGSR HRYAEQENGI NQGSAQMLSE NGELKFPEKM
760 770 780 790 800
GLPAAPFLTK IEPSKPAATR KRRWSAPESR KLEKSEDEPP LTLPKPSLIP
810
QEVKICIEGR SNVGK
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.1 Publication

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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Triplet repeat expansion

Cross-referencesi

Web resourcesi

Wikipedia

Ataxin-1 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi112217. 261 interactions.
DIPiDIP-35353N.
IntActiP54253. 246 interactions.
MINTiMINT-266093.
STRINGi9606.ENSP00000244769.

PTM databases

PhosphoSiteiP54253.

Polymorphism and mutation databases

BioMutaiATXN1.
DMDMi206729854.

Proteomic databases

MaxQBiP54253.
PaxDbiP54253.
PRIDEiP54253.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6310.
GeneCardsiGC06M016299.
GeneReviewsiATXN1.
H-InvDBHIX0032878.
HGNCiHGNC:10548. ATXN1.
HPAiHPA008335.
MIMi164400. phenotype.
601556. gene.
neXtProtiNX_P54253.
Orphaneti98755. Spinocerebellar ataxia type 1.
PharmGKBiPA34958.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG306883.
GeneTreeiENSGT00390000005939.
HOGENOMiHOG000034225.
HOVERGENiHBG004319.
InParanoidiP54253.
OMAiHRSYALS.
OrthoDBiEOG7SBNQX.
PhylomeDBiP54253.
TreeFamiTF350643.

Miscellaneous databases

ChiTaRSiATXN1. human.
EvolutionaryTraceiP54253.
GeneWikiiAtaxin_1.
GenomeRNAii6310.
NextBioi24497.
PROiP54253.
SOURCEiSearch...

Gene expression databases

BgeeiP54253.
CleanExiHS_ATXN1.
GenevisibleiP54253. HS.

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]
ProtoNetiSearch...

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 SPECIFICITY.
    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, POLYMORPHISM.
  5. "Expression analysis of the ataxin-1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals."
    Servadio A., Koshy B., Armstrong D., Antalffy B., Orr H.T., Zoghbi H.Y.
    Nat. Genet. 10:94-98(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SCA1, SUBCELLULAR LOCATION.
  6. "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: SUBUNIT.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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.
  18. "Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by increasing wild-type Ataxin1 levels."
    Gennarino V.A., Singh R.K., White J.J., De Maio A., Han K., Kim J.Y., Jafar-Nejad P., di Ronza A., Kang H., Sayegh L.S., Cooper T.A., Orr H.T., Sillitoe R.V., Zoghbi H.Y.
    Cell 160:1087-1098(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  19. "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: June 24, 2015
This is version 151 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.