[1]	NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN SCA7. TISSUE=Lymphoblast; DOI=10.1038/ng0997-65; PubMed=9288099 [NCBI, ExPASy, EBI, Israel, Japan] David G., Abbas N., Stevanin G., Duerr A., Yvert G., Cancel G., Weber C., Imbert G., Saudou F., Antoniou E., Drabkin H., Gemmill R., Giunti P., Benomar A., Wood N., Ruberg M., Agid Y., Mandel J.-L., Brice A.; "Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion."; Nat. Genet. 17:65-70(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], POLYMORPHISM, AND VARIANT MET-862. TISSUE=Colon; DOI=10.1093/hmg/7.2.177; PubMed=9425224 [NCBI, ExPASy, EBI, Israel, Japan] Del-Favero J., Krols L., Michalik A., Theuns J., Loefgren A., Goossens D., Wehnert A., Van den Bossche D., Van Zand K., Backhovens H., van Regenmorter N., Martin J.-J., Van Broeckhoven C.; "Molecular genetic analysis of autosomal dominant cerebellar ataxia with retinal degeneration (ADCA type II) caused by CAG triplet repeat expansion."; Hum. Mol. Genet. 7:177-186(1998).
[3]	ALTERNATIVE SPLICING (ISOFORMS A AND B). TISSUE=Testis; PubMed=12533095 [NCBI, ExPASy, EBI, Israel, Japan] Einum D.D., Clark A.M., Townsend J.J., Ptacek L.J., Fu Y.H.; "A novel central nervous system-enriched spinocerebellar ataxia type 7 gene product."; Arch. Neurol. 60:97-103(2003).
[4]	SUBCELLULAR LOCATION. DOI=10.1093/hmg/8.9.1657; PubMed=10441328 [NCBI, ExPASy, EBI, Israel, Japan] Kaytor M.D., Duvick L.A., Skinner P.J., Koob M.D., Ranum L.P., Orr H.T.; "Nuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-7."; Hum. Mol. Genet. 8:1657-1664(1999).
[5]	INTERACTION WITH SORBS1. DOI=10.1093/hmg/10.11.1201; PubMed=11371513 [NCBI, ExPASy, EBI, Israel, Japan] Lebre A.-S., Jamot L., Takahashi J., Spassky N., Leprince C., Ravise N., Zander C., Fujigasaki H., Kussel-Andermann P., Duyckaerts C., Camonis J.H., Brice A.; "Ataxin-7 interacts with a Cbl-associated protein that it recruits into neuronal intranuclear inclusions."; Hum. Mol. Genet. 10:1201-1213(2001).
[6]	INTERACTION WITH PSMC1. DOI=10.1093/hmg/10.24.2821; PubMed=11734547 [NCBI, ExPASy, EBI, Israel, Japan] Matilla A., Gorbea C., Einum D.D., Townsend J., Michalik A., van Broeckhoven C., Jensen C.C., Murphy K.J., Ptacek L.J., Fu Y.H.; "Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex."; Hum. Mol. Genet. 10:2821-2831(2001).
[7]	INTERACTION WITH TRRAP; GCN5L2 AND TAF10. DOI=10.1093/hmg/ddh139; PubMed=15115762 [NCBI, ExPASy, EBI, Israel, Japan] Helmlinger D., Hardy S., Sasorith S., Klein F., Robert F., Weber C., Miguet L., Potier N., Van-Dorsselaer A., Wurtz J.M., Mandel J.L., Tora L., Devys D.; "Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexes."; Hum. Mol. Genet. 13:1257-1265(2004).
[8]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840; SER-849 AND THR-854, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[9]	IDENTIFICATION IN THE STAGA COMPLEX. DOI=10.1073/pnas.0503505102; PubMed=15932940 [NCBI, ExPASy, EBI, Israel, Japan] Palhan V.B., Chen S., Peng G.H., Tjernberg A., Gamper A.M., Fan Y., Chait B.T., La Spada A.R., Roeder R.G.; "Polyglutamine-expanded ataxin-7 inhibits STAGA histone acetyltransferase activity to produce retinal degeneration."; Proc. Natl. Acad. Sci. U.S.A. 102:8472-8477(2005).
[10]	IDENTIFICATION IN STAGA COMPLEX. DOI=10.1016/j.molcel.2007.12.011; PubMed=18206972 [NCBI, ExPASy, EBI, Israel, Japan] Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.; "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."; Mol. Cell 29:92-101(2008).

Comments

FUNCTION: Involved in neurodegeneration. Acts as component of the STAGA transcription coactivator-HAT complex. Mediates the interaction of STAGA complex with the CRX and is involved in CRX-dependent gene activation.
SUBUNIT: Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP, TAF9 and ATXN7. The STAGA core complex is associated with a subcomplex required for histone deubiquitinylation composed of ATXN7L3, ENY2 and USP22. Interacts with SORBS1, PSMC1 and CRX. Interacts with TRRAP, GCN5L2 and TAF10.
INTERACTION:
Q9Y4A5:TRRAP; NbExp=1; IntAct=EBI-708350, EBI-399128;
SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Nucleus matrix. Note=In addition to a diffuse distribution throughout the nucleus, it is associated with the nuclear matrix and the nucleolus.
SUBCELLULAR LOCATION: Isoform b: Cytoplasm.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	a
Synonyms	Ataxin-7a
Isoform ID	O15265-1
Note: Nuclear.
This is the isoform sequence displayed in this entry.

Name	b
Synonyms	Ataxin-7b, SCA7b
Isoform ID	O15265-2
Note: Cytoplasmic.
Features which should be applied to build the isoform sequence: VSP_007695.

TISSUE SPECIFICITY: Isoform a and isoform b are expressed in CNS, but isoform a is expressed predominantly in the peripherical tissues. Isoform b is also highly expressed in the frontal lobe, skeletal muscle and spinal cord and is expressed at a lower level in the lung, lymphoblast and intestine.
PTM: Proteolytically cleaved. The cleavage may be involved in SCA7 degeneration: the isoform fragments may exert distinct toxic influences that could contribute to selective neurodegeneration.
POLYMORPHISM: The poly-Gln region of ATXN7 is highly polymorphic (4 to 18 repeats) in the normal population and is expanded to about 38-130 repeats in SCA7 patients. Intermediate alleles with 28 to 35 repeats are prone to further expansion.
DISEASE: Defects in ATXN7 are the cause of spinocerebellar ataxia type 7 (SCA7) [MIM:164500]; also known as olivopontocerebellar atrophy III (OPCA III or OPCA3) or olivopontocerebellar atrophy with retinal degeneration. 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 degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA7 belongs to the autosomal dominant cerebellar ataxias type II (ADCA II) which are characterized by cerebellar ataxia with retinal degeneration and pigmentary macular dystrophy.
SIMILARITY: Belongs to the ataxin-7 family.
SIMILARITY: Contains 1 SCA7 domain.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ATXN7";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ000517; CAA04154.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF032105; AAC39765.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF032102; AAC19162.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF032103; AAC19163.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AA398030; -; NOT_ANNOTATED_CDS; mRNA.	[EMBL / GenBank / DDBJ]

IPI

IPI00005743; -.
IPI00332082; -.

T09193; T09193.

NP_000324.1; -.

3D structure databases

ModBase

O15265.

Protein-protein interaction databases

IntAct

O15265; 8.

PTM databases

PhosphoSite

O15265; -.

Organism-specific databases

GC03P063825; -.

HIX0030703; -.

HGNC:10560; ATXN7.

164500; phenotype. [NCBI / EBI]
607640; gene. [NCBI / EBI]

Orphanet

94147; Ataxia, spinocerebellar, autosomal dominant, type 7.
99; Autosomal dominant cerebellar ataxia.

PharmGKB

PA34973; -.

Gene expression databases

O15265; -.

O15265; -.

HS_ATXN7; -.

ENSG00000163635; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0016363;	Cellular component: nuclear matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005730;	Cellular component: nucleolus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0008219;	Biological process: cell death (inferred from electronic annotation from UniProtKB-KW).
GO:0016578;	Biological process: histone deubiquitination (inferred from direct assay from UniProtKB).
GO:0006997;	Biological process: nucleus organization (traceable author statement from ProtInc).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
GO:0007601;	Biological process: visual perception (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR013243; SCA7.
IPR015880; Znf_C2H2-like.
Graphical view of domain structure.

Pfam

PF08313; SCA7; 1.
Pfam graphical view of domain structure.

SMART

SM00355; ZnF_C2H2; 1.
SMART graphical view of domain structure.

Proteomic databases

PRIDE

O15265; -.

Genome annotation databases

Ensembl

ENSG00000163635; Homo sapiens. [Contig view]

GeneID

6314; -.

KEGG

hsa:6314; -.

Phylogenomic databases

HOGENOM

O15265; -.

HOVERGEN

O15265; -.

OMA

O15265; HSMESFR.

Other

24505; -.

O15265; -.

ATXN7; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Cytoplasm; Disease mutation; Neurodegeneration; Nucleus; Phosphoprotein; Polymorphism; Spinocerebellar ataxia; Transcription; Transcription regulation; Triplet repeat expansion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 892`	`892`	`Ataxin-7.`	`PRO_0000064759`
`DOMAIN`	`317 397`	`81`	`SCA7.`
`COMPBIAS`	`16 20`	`5`	`Poly-Ala.`
`COMPBIAS`	`23 28`	`6`	`Poly-Ala.`
`COMPBIAS`	`30 49`	`20`	`Gln-rich.`
`COMPBIAS`	`30 39`	`10`	`Poly-Gln.`
`COMPBIAS`	`40 65`	`26`	`Pro-rich.`
`COMPBIAS`	`40 45`	`6`	`Poly-Pro.`
`COMPBIAS`	`51 55`	`5`	`Poly-Pro.`
`COMPBIAS`	`171 219`	`49`	`Ser-rich.`
`COMPBIAS`	`171 174`	`4`	`Poly-Ser.`
`COMPBIAS`	`213 219`	`7`	`Poly-Ser.`
`COMPBIAS`	`402 486`	`85`	`Pro-rich.`
`COMPBIAS`	`640 851`	`212`	`Ser-rich.`
`COMPBIAS`	`647 654`	`8`	`Poly-Ser.`
`COMPBIAS`	`717 730`	`14`	`Poly-Ser.`
`COMPBIAS`	`840 845`	`6`	`Poly-Ser.`
`MOD_RES`	`840 840`		`Phosphoserine.`
`MOD_RES`	`849 849`		`Phosphoserine.`
`MOD_RES`	`854 854`		`Phosphothreonine.`
`VAR_SEQ`	`888 892`		`PKARP -> DISSPCLRTGISATSPQSPDLKSKGTSLTAENSTGRNNAD` `TFEDKLHLHSALWTPRCL (in isoform b).`	`VSP_007695`
`VARIANT`	`264 264`	`1`	`K -> R (in dbSNP:rs1053338 [NCBI]).`	`VAR_011823`
`VARIANT`	`573 573`	`1`	`I -> V (in dbSNP:rs3733124 [NCBI]).`	`VAR_053779`
`VARIANT`	`663 663`	`1`	`P -> S (in dbSNP:rs1053340 [NCBI]).`	`VAR_011824`
`VARIANT`	`862 862`	`1`	`V -> M (in dbSNP:rs3774729 [NCBI]).`	`VAR_020143`
`CONFLICT`	`105 105`		`P -> H (in Ref. 2; AAC19162).`
`CONFLICT`	`129 129`		`C -> S (in Ref. 2; AAC19162).`
`CONFLICT`	`888 892`		`PKARP -> VGNGL (in Ref. 2; AAC39765/AAC19163).`

Sequence information

Length: 892 AA [This is the length of the unprocessed precursor]

Molecular weight: 95451 Da [This is the MW of the unprocessed precursor]

CRC64: 9AEA787D77103C5F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSERAADDVR GEPRRAAAAA GGAAAAAARQ QQQQQQQQQP PPPQPQRQQH PPPPPRRTRP 

        70         80         90        100        110        120 
EDGGPGAAST SAAAMATVGE RRPLPSPEVM LGQSWNLWVE ASKLPGKDGT ELDESFKEFG 

       130        140        150        160        170        180 
KNREVMGLCR EDMPIFGFCP AHDDFYLVVC NDCNQVVKPQ AFQSHYERRH SSSSKPPLAV 

       190        200        210        220        230        240 
PPTSVFSFFP SLSKSKGGSA SGSNRSSSGG VLSASSSSSK LLKSPKEKLQ LRGNTRPMHP 

       250        260        270        280        290        300 
IQQSRVPHGR IMTPSVKVEK IHPKMDGTLL KSAVGPTCPA TVSSLVKPGL NCPSIPKPTL 

       310        320        330        340        350        360 
PSPGQILNGK GLPAPPTLEK KPEDNSNNRK FLNKRLSERE FDPDIHCGVI DLDTKKPCTR 

       370        380        390        400        410        420 
SLTCKTHSLT QRRAVQGRRK RFDVLLAEHK NKTREKELIR HPDSQQPPQP LRDPHPAPPR 

       430        440        450        460        470        480 
TSQEPHQNPH GVIPSESKPF VASKPKPHTP SLPRPPGCPA QQGGSAPIDP PPVHESPHPP 

       490        500        510        520        530        540 
LPATEPASRL SSEEGEGDDK EESVEKLDCH YSGHHPQPAS FCTFGSRQIG RGYYVFDSRW 

       550        560        570        580        590        600 
NRLRCALNLM VEKHLNAQLW KKIPPVPSTT SPISTRIPHR TNSVPTSQCG VSYLAAATVS 

       610        620        630        640        650        660 
TSPVLLSSTC ISPNSKSVPA HGTTLNAQPA ASGAMDPVCS MQSRQVSSSS SSPSTPSGLS 

       670        680        690        700        710        720 
SVPSSPMSRK PQKLKSSKSL RPKESSGNST NCQNASSSTS GGSGKKRKNS SPLLVHSSSS 

       730        740        750        760        770        780 
SSSSSSSSHS MESFRKNCVA HSGPPYPSTV TSSHSIGLNC VTNKANAVNV RHDQSGRGPP 

       790        800        810        820        830        840 
TGSPAESIKR MSVMVNSSDS TLSLGPFIHQ SNELPVNSHG SFSHSHTPLD KLIGKKRKCS 

       850        860        870        880        890 
PSSSSINNSS SKPTKVAKVP AVNNVHMKHT GTIPGAQGLM NSSLLHQPKA RP

O15265 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools