P54253 (ATX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ataxin-1

Alternative name(s):
Spinocerebellar ataxia type 1 protein

Gene names

Name:	ATXN1
Synonyms:	ATX1, SCA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	815 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism Triplet repeat expansion
Disease	Neurodegeneration Spinocerebellar ataxia
Ligand	DNA-binding RNA-binding
Molecular function	Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA processing Non-traceable author statement PubMed 15615787. Source: UniProtKB adult locomotory behavior Inferred from electronic annotation. Source: Compara cell death Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of insulin-like growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of phosphorylation Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent 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: Compara regulation of excitatory postsynaptic membrane potential Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay PubMed 7647801. Source: UniProtKB 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
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW poly(G) RNA binding Inferred from direct assay Ref.7. Source: UniProtKB poly(U) RNA binding Inferred from direct assay Ref.7. Source: UniProtKB protein self-association Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-930964,EBI-930964
ARID5A	Q03989	3	EBI-930964,EBI-948603
ATXN2	Q99700	4	EBI-930964,EBI-697691
C1orf94	Q6P1W5	3	EBI-930964,EBI-946029
CCNK	O75909	2	EBI-930964,EBI-739806
CFL1	P23528	5	EBI-930964,EBI-352733
CIC	Q96RK0	5	EBI-930964,EBI-945857
COIL	P38432	6	EBI-930975,EBI-945751
CPSF7	Q8N684	2	EBI-930964,EBI-746909
CRK	P46108	3	EBI-930964,EBI-886
DAZAP2	Q15038	2	EBI-930964,EBI-724310
ELP5	Q8TE02	2	EBI-930964,EBI-946189
GPATCH8	Q9UKJ3	4	EBI-930964,EBI-948259
HIVEP1	P15822	6	EBI-930964,EBI-722264
HSFX1	Q9UBD0	3	EBI-930964,EBI-947253
IST1	P53990	2	EBI-930964,EBI-945994
KAT5	Q92993	3	EBI-930964,EBI-399080
KLHL12	Q53G59	2	EBI-930964,EBI-740929
METTL17	Q9H7H0	5	EBI-930964,EBI-749353
NUDT21	O43809	2	EBI-930964,EBI-355720
PLEKHA5	Q9HAU0	2	EBI-930964,EBI-945934
PRRC2A	P48634	4	EBI-930964,EBI-347545
RBFOX1	Q9NWB1	2	EBI-930964,EBI-945906
RBFOX2	O43251	7	EBI-930964,EBI-746056
RBPMS	Q93062	3	EBI-930964,EBI-740322
RCN1	Q15293	3	EBI-930964,EBI-948278
SIX5	Q8N196	4	EBI-930964,EBI-946167
SYBU	Q9NX95	3	EBI-930964,EBI-948293
TBC1D5	Q92609	2	EBI-930964,EBI-742381
TRAF2	Q12933	2	EBI-930964,EBI-355744
TRIM32	Q13049	2	EBI-930964,EBI-742790
U2AF2	P26368	4	EBI-930964,EBI-742339
UBQLN4	Q9NRR5	6	EBI-930964,EBI-711226
USP54	Q70EL1	3	EBI-930964,EBI-946185
VSTM2L	Q96N03	3	EBI-930964,EBI-948213
YY1AP1	Q9H869	4	EBI-930964,EBI-946122
ZC3H10	Q96K80	4	EBI-930964,EBI-742550
ZHX1	Q9UKY1	5	EBI-930964,EBI-347767
ZNF488	Q96MN9	3	EBI-930964,EBI-948288

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 815

815

Ataxin-1

PRO_0000064751

Regions

Domain

562 – 693

132

AXH

Region

494 – 604

111

Self-association

Region

538 – 815

278

Interaction with USP7

Region

540 – 766

227

RNA-binding

Motif

794 – 797

4

Nuclear localization signal By similarity

Compositional bias

197 – 225

29

Poly-Gln

Amino acid modifications

Modified residue

238

1

Phosphoserine Ref.15

Modified residue

775

1

Phosphoserine Ref.11

Cross-link

16

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Cross-link

194

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Cross-link

609

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Cross-link

696

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Cross-link

745

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Natural variant

209

1

H → Q.
Corresponds to variant rs11969612 [ dbSNP | Ensembl ].

VAR_046616

Natural variant

753

1

P → S.
Corresponds to variant rs16885 [ dbSNP | Ensembl ].

VAR_046617

Experimental info

Mutagenesis

16

1

K → R: Sumoylation reduced to 40% of wild-type. Ref.13

Mutagenesis

194

1

K → R: Sumoylation reduced to 46% of wild-type. Ref.13

Mutagenesis

420

1

K → R: No effect on sumoylation. Ref.13

Mutagenesis

529

1

K → R: Sumoylation reduced to 57% of wild-type. Ref.13

Mutagenesis

589

1

K → R: Sumoylation reduced to 53% of wild-type. Ref.13

Mutagenesis

594

1

K → R: Sumoylation reduced to 68% of wild-type. Ref.13

Mutagenesis

609

1

K → R: Sumoylation reduced to 43% of wild-type. Ref.13

Mutagenesis

691

1

K → R: No effect on sumoylation. Ref.13

Mutagenesis

696

1

K → R: Sumoylation reduced to 42% of wild-type. Ref.13

Mutagenesis

745

1

K → R: Sumoylation reduced to 44% of wild-type. Ref.13

Mutagenesis

775

1

S → A: Reduces phosphorylation but does not affect nuclear localization. Ref.11

Mutagenesis

784

1

K → R: Sumoylation reduced to 62% of wild-type. Ref.13

Sequence conflict

211

1

H → HQ in CAA55793. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

815

Helix Strand Turn

Details...

Helix

572 – 574

3

Beta strand

579 – 581

3

Beta strand

587 – 589

3

Helix

590 – 592

3

Helix

595 – 604

10

Beta strand

606 – 620

15

Beta strand

626 – 633

8

Turn

634 – 637

4

Beta strand

638 – 645

8

Beta strand

650 – 652

3

Turn

653 – 655

3

Beta strand

656 – 660

5

Helix

662 – 669

8

Beta strand

681 – 687

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 23, 2008. Version 2. Checksum: 657876F8FD19ECB2	FASTA	815	86,923
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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

GeneReviews

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.

IPI

IPI00903319.

PIR

S46268.

RefSeq

NP_000323.2. NM_000332.3.
NP_001121636.1. NM_001128164.1.

UniGene

Hs.434961.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OA8	X-ray	1.70	A/B/C/D	563-693	[»]
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	[»]

ProteinModelPortal

P54253.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35353N.

IntAct

P54253. 238 interactions.

MINT

MINT-266093.

STRING

9606.ENSP00000244769.

PTM databases

PhosphoSite

P54253.

Polymorphism databases

DMDM

206729854.

Proteomic databases

PaxDb

P54253.

PRIDE

P54253.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000244769; ENSP00000244769; ENSG00000124788.
ENST00000436367; ENSP00000416360; ENSG00000124788.
ENST00000450222; ENSP00000397260; ENSG00000124788.

GeneID

6310.

KEGG

hsa:6310.

UCSC

uc003nbt.3. human.

Organism-specific databases

CTD

6310.

GeneCards

GC06M016299.

H-InvDB

HIX0032878.

HGNC

HGNC:10548. ATXN1.

HPA

HPA008335.

MIM

164400. phenotype.
601556. gene.

neXtProt

NX_P54253.

Orphanet

98755. Spinocerebellar ataxia type 1.

PharmGKB

PA34958.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG306883.

HOGENOM

HOG000034225.

HOVERGEN

HBG004319.

OMA

GLDYSPP.

OrthoDB

EOG408N7X.

PhylomeDB

P54253.

Gene expression databases

Bgee

P54253.

CleanEx

HS_ATXN1.

Genevestigator

P54253.

GermOnline

ENSG00000124788. Homo sapiens.

Family and domain databases

InterPro

IPR013723. Ataxin-1_HBP1.
IPR003652. Ataxin_AXH_dom.
IPR020997. Capicua_tscrpt_rep_mod.
[Graphical view]

Pfam

PF12547. ATXN-1_C. 1 hit.
PF08517. AXH. 1 hit.
[Graphical view]

SMART

SM00536. AXH. 1 hit.
[Graphical view]

SUPFAM

SSF102031. Ataxin-1_HBP1. 1 hit.

PROSITE

PS51148. AXH. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

ATXN1. human.

EvolutionaryTrace

P54253.

GenomeRNAi

6310.

NextBio

24497.

SOURCE

Search...

Entry information

Entry name

ATX1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.