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O15265 (ATX7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 16, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ataxin-7
Alternative name(s):
Spinocerebellar ataxia type 7 protein
Gene names
Name:ATXN7
Synonyms:SCA7
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length892 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 structure

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 deubiquitination composed of ATXN7L3, ENY2 and USP22. Interacts with SORBS1, PSMC1 and CRX. Interacts with TRRAP, GCN5L2 and TAF10. Ref.5 Ref.6 Ref.7

Subcellular location

Isoform a: 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. Ref.4

Isoform b: Cytoplasm Ref.4.

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.

Post-translational modification

Proteolytically cleaved. The cleavage may be involved in SCA7 degeneration: the isoform fragments may exert distinct toxic influences that could contribute to selective neurodegeneration.

Sumoylation decreases the aggregation propensity and cellular toxicity of forms with an expanded poly-Gln region but has no effect on subcellular location or interaction with components of the STAGA complex.

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.

Involvement in 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. Ref.1

Sequence similarities

Belongs to the ataxin-7 family.

Contains 1 SCA7 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TAF10Q129626EBI-708350,EBI-708376
TRRAPQ9Y4A56EBI-708350,EBI-399128

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform a (identifier: O15265-1)

Also known as: Ataxin-7a;

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.
Isoform b (identifier: O15265-2)

Also known as: Ataxin-7b; SCA7b;

The sequence of this isoform differs from the canonical sequence as follows:
     888-892: PKARP → DISSPCLRTGISATSPQSPDLKSKGTSLTAENSTGRNNADTFEDKLHLHSALWTPRCL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 892892Ataxin-7
PRO_0000064759

Regions

Domain334 – 40168SCA7
Compositional bias16 – 205Poly-Ala
Compositional bias23 – 286Poly-Ala
Compositional bias30 – 4920Gln-rich
Compositional bias30 – 3910Poly-Gln
Compositional bias40 – 6526Pro-rich
Compositional bias40 – 456Poly-Pro
Compositional bias51 – 555Poly-Pro
Compositional bias171 – 21949Ser-rich
Compositional bias171 – 1744Poly-Ser
Compositional bias213 – 2197Poly-Ser
Compositional bias402 – 48685Pro-rich
Compositional bias640 – 851212Ser-rich
Compositional bias647 – 6548Poly-Ser
Compositional bias717 – 73014Poly-Ser
Compositional bias840 – 8456Poly-Ser

Amino acid modifications

Modified residue8401Phosphoserine Ref.8
Modified residue8491Phosphoserine Ref.8
Modified residue8541Phosphothreonine Ref.8
Cross-link257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Natural variations

Alternative sequence888 – 8925PKARP → DISSPCLRTGISATSPQSPD LKSKGTSLTAENSTGRNNAD TFEDKLHLHSALWTPRCL in isoform b.
VSP_007695
Natural variant2641K → R. Ref.2
Corresponds to variant rs1053338 [ dbSNP | Ensembl ].
VAR_011823
Natural variant5731I → V.
Corresponds to variant rs3733124 [ dbSNP | Ensembl ].
VAR_053779
Natural variant6631P → S.
Corresponds to variant rs1053340 [ dbSNP | Ensembl ].
VAR_011824
Natural variant8621V → M. Ref.2
Corresponds to variant rs3774729 [ dbSNP | Ensembl ].
VAR_020143

Experimental info

Mutagenesis2571K → R: Almost completely abolishes sumoylation. Ref.11
Mutagenesis8581K → R: No effect on sumoylation. Ref.11
Sequence conflict1051P → H in AAC19162. Ref.2
Sequence conflict1291C → S in AAC19162. Ref.2
Sequence conflict888 – 8925PKARP → VGNGL in AAC39765. Ref.2
Sequence conflict888 – 8925PKARP → VGNGL in AAC19163. Ref.2

Secondary structure

1 ....... 892
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform a (Ataxin-7a) [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9AEA787D77103C5F

FASTA89295,451
        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

« Hide

Isoform b (Ataxin-7b) (SCA7b) [UniParc].

Checksum: B230F94D3D468D77
Show »

FASTA945101,112

References

« Hide 'large scale' references
[1]"Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion."
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.
Nat. Genet. 17:65-70(1997) [PubMed: 9288099] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), INVOLVEMENT IN SCA7.
Tissue: Lymphoblast.
[2]"Molecular genetic analysis of autosomal dominant cerebellar ataxia with retinal degeneration (ADCA type II) caused by CAG triplet repeat expansion."
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.
Hum. Mol. Genet. 7:177-186(1998) [PubMed: 9425224] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131, POLYMORPHISM, VARIANTS ARG-264 AND MET-862.
Tissue: Colon.
[3]"A novel central nervous system-enriched spinocerebellar ataxia type 7 gene product."
Einum D.D., Clark A.M., Townsend J.J., Ptacek L.J., Fu Y.H.
Arch. Neurol. 60:97-103(2003) [PubMed: 12533095] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS A AND B).
Tissue: Testis.
[4]"Nuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-7."
Kaytor M.D., Duvick L.A., Skinner P.J., Koob M.D., Ranum L.P., Orr H.T.
Hum. Mol. Genet. 8:1657-1664(1999) [PubMed: 10441328] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"Ataxin-7 interacts with a Cbl-associated protein that it recruits into neuronal intranuclear inclusions."
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.
Hum. Mol. Genet. 10:1201-1213(2001) [PubMed: 11371513] [Abstract]
Cited for: INTERACTION WITH SORBS1.
[6]"Association of ataxin-7 with the proteasome subunit S4 of the 19S regulatory complex."
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.
Hum. Mol. Genet. 10:2821-2831(2001) [PubMed: 11734547] [Abstract]
Cited for: INTERACTION WITH PSMC1.
[7]"Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing complexes."
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.
Hum. Mol. Genet. 13:1257-1265(2004) [PubMed: 15115762] [Abstract]
Cited for: INTERACTION WITH TRRAP; GCN5L2 AND TAF10.
[8]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-840; SER-849 AND THR-854, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Polyglutamine-expanded ataxin-7 inhibits STAGA histone acetyltransferase activity to produce retinal degeneration."
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.
Proc. Natl. Acad. Sci. U.S.A. 102:8472-8477(2005) [PubMed: 15932940] [Abstract]
Cited for: IDENTIFICATION IN THE STAGA COMPLEX.
[10]"A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
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.
Mol. Cell 29:92-101(2008) [PubMed: 18206972] [Abstract]
Cited for: IDENTIFICATION IN STAGA COMPLEX.
[11]"SUMOylation attenuates the aggregation propensity and cellular toxicity of the polyglutamine expanded ataxin-7."
Janer A., Werner A., Takahashi-Fujigasaki J., Daret A., Fujigasaki H., Takada K., Duyckaerts C., Brice A., Dejean A., Sittler A.
Hum. Mol. Genet. 19:181-195(2010) [PubMed: 19843541] [Abstract]
Cited for: SUMOYLATION AT LYS-257, MUTAGENESIS OF LYS-257 AND LYS-858.
+Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ000517 mRNA. Translation: CAA04154.1.
AF032102 Genomic DNA. Translation: AAC19162.1.
AF032103 mRNA. Translation: AAC19163.1.
AF032105 mRNA. Translation: AAC39765.1.
AA398030 mRNA. No translation available.
IPIIPI00005743.
IPI00332082.
PIRT09193.
RefSeqNP_000324.1. NM_000333.3.
NP_001170858.1. NM_001177387.1.
UniGeneHs.729041.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KKRNMR-A330-401[»]
ProteinModelPortalO15265.
SMRO15265. Positions 339-397.
ModBaseSearch...

Protein-protein interaction databases

IntActO15265. 8 interactions.
MINTMINT-2862470.
STRINGO15265.

PTM databases

PhosphoSiteO15265.

Proteomic databases

PRIDEO15265.

Protocols and materials databases

DNASU6314.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295900; ENSP00000295900; ENSG00000163635.
ENST00000487717; ENSP00000420234; ENSG00000163635.
GeneID6314.
KEGGhsa:6314.
UCSCuc003dlv.3. human.
uc021wzy.1. human.

Organism-specific databases

CTD6314.
GeneCardsGC03P063825.
H-InvDBHIX0030703.
HGNCHGNC:10560. ATXN7.
HPAHPA034989.
MIM164500. phenotype.
607640. gene.
neXtProtNX_O15265.
Orphanet94147. Autosomal dominant spinocerebellar ataxia type 7.
PharmGKBPA34973.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270433.
GeneTreeENSGT00530000063215.
HOGENOMHOG000252910.
HOVERGENHBG004320.
KOK11318.
OMAGAMDPVC.
OrthoDBEOG4DV5KV.

Gene expression databases

ArrayExpressO15265.
BgeeO15265.
CleanExHS_ATXN7.
GenevestigatorO15265.
GermOnlineENSG00000163635. Homo sapiens.

Family and domain databases

InterProIPR013243. SCA7_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF08313. SCA7. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS51505. SCA7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO15265.
NextBio24505.
PMAP-CutDBO15265.
SOURCESearch...

Entry information

Entry nameATX7_HUMAN
AccessionPrimary (citable) accession number: O15265
Secondary accession number(s): O75328, O75329, Q9Y6P8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: May 16, 2012
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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