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O15265 (ATX7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Necessary for microtubule cytoskeleton stabilization. Ref.14

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. Interacts with alpha tubulin. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14

Subcellular location

Isoform a: Nucleus. Nucleusnucleolus. Nucleus matrix. Cytoplasmcytoskeleton. Note: In addition to a diffuse distribution throughout the nucleus, it is associated with the nuclear matrix and the nucleolus. It is able to shuttle between the nucleus and cytoplasm. Ref.6 Ref.11 Ref.14

Isoform b: Cytoplasm Ref.6 Ref.11 Ref.14.

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 fragmentsmay 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. Ref.13

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

Spinocerebellar ataxia 7 (SCA7) [MIM:164500]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

Sequence similarities

Belongs to the ataxin-7 family.

Contains 1 SCA7 domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
Triplet repeat expansion
   DiseaseDisease mutation
Neurodegeneration
Spinocerebellar ataxia
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin organization

Traceable author statement. Source: Reactome

histone deubiquitination

Inferred from direct assay Ref.12. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from mutant phenotype Ref.14. Source: UniProtKB

negative regulation of insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of phosphorylation

Inferred from electronic annotation. Source: Ensembl

nucleus organization

Traceable author statement Ref.6. Source: ProtInc

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

visual perception

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay Ref.14. Source: UniProtKB

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 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
Isoform 3 (identifier: O15265-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-166: MSERAADDVR...VKPQAFQSHY → MEGSKTPLQSSPSAQELKAPL
Note: No experimental confirmation available.

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

Cross-link257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13

Natural variations

Alternative sequence1 – 166166MSERA…FQSHY → MEGSKTPLQSSPSAQELKAP L in isoform 3.
VSP_044456
Alternative sequence888 – 8925PKARP → DISSPCLRTGISATSPQSPD LKSKGTSLTAENSTGRNNAD TFEDKLHLHSALWTPRCL in isoform b.
VSP_007695
Natural variant2641K → R. Ref.2 Ref.3
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 Ref.3
Corresponds to variant rs3774729 [ dbSNP | Ensembl ].
VAR_020143

Experimental info

Mutagenesis2571K → R: Almost completely abolishes sumoylation. Ref.13
Mutagenesis8581K → R: No effect on sumoylation. Ref.13
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

........... 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
Isoform 3 [UniParc].

Checksum: AE6215958E714C8E
Show »

FASTA74779,535

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] [Europe PMC] [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] [Europe PMC] [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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANTS ARG-264 AND MET-862.
Tissue: Trachea.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS A AND B).
Tissue: Testis.
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SORBS1.
[8]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMC1.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRRAP; GCN5L2 AND TAF10.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE STAGA COMPLEX.
[11]"Ataxin-7 can export from the nucleus via a conserved exportin-dependent signal."
Taylor J., Grote S.K., Xia J., Vandelft M., Graczyk J., Ellerby L.M., La Spada A.R., Truant R.
J. Biol. Chem. 281:2730-2739(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN STAGA COMPLEX.
[13]"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] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-257, MUTAGENESIS OF LYS-257 AND LYS-858.
[14]"Ataxin-7 associates with microtubules and stabilizes the cytoskeletal network."
Nakamura Y., Tagawa K., Oka T., Sasabe T., Ito H., Shiwaku H., La Spada A.R., Okazawa H.
Hum. Mol. Genet. 21:1099-1110(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ALPHA TUBULIN, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

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.
AK304062 mRNA. Translation: BAG64969.1.
AC012557 Genomic DNA. No translation available.
AC104162 Genomic DNA. No translation available.
AA398030 mRNA. No translation available.
CCDSCCDS43102.1. [O15265-1]
CCDS46861.2. [O15265-3]
CCDS54603.1. [O15265-2]
PIRT09193.
RefSeqNP_000324.1. NM_000333.3. [O15265-1]
NP_001121621.2. NM_001128149.2. [O15265-3]
NP_001170858.1. NM_001177387.1. [O15265-2]
UniGeneHs.476595.

3D structure databases

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

Protein-protein interaction databases

BioGrid112221. 82 interactions.
IntActO15265. 60 interactions.
MINTMINT-2862470.
STRING9606.ENSP00000381590.

PTM databases

PhosphoSiteO15265.

Proteomic databases

MaxQBO15265.
PaxDbO15265.
PRIDEO15265.

Protocols and materials databases

DNASU6314.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295900; ENSP00000295900; ENSG00000163635. [O15265-1]
ENST00000398590; ENSP00000381590; ENSG00000163635. [O15265-2]
ENST00000484332; ENSP00000428277; ENSG00000163635. [O15265-3]
ENST00000487717; ENSP00000420234; ENSG00000163635. [O15265-1]
ENST00000538065; ENSP00000439585; ENSG00000163635. [O15265-2]
GeneID6314.
KEGGhsa:6314.
UCSCuc003dlv.3. human. [O15265-1]
uc011bfn.2. human. [O15265-3]
uc021wzy.1. human. [O15265-2]

Organism-specific databases

CTD6314.
GeneCardsGC03P063825.
GeneReviewsATXN7.
HGNCHGNC:10560. ATXN7.
HPAHPA034989.
MIM164500. phenotype.
607640. gene.
neXtProtNX_O15265.
Orphanet94147. Spinocerebellar ataxia type 7.
PharmGKBPA34973.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270433.
HOGENOMHOG000252910.
HOVERGENHBG004320.
KOK11318.
OMANSTNCHN.
OrthoDBEOG7XSTDP.
PhylomeDBO15265.
TreeFamTF331337.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressO15265.
BgeeO15265.
CleanExHS_ATXN7.
GenevestigatorO15265.

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

ChiTaRSATXN7. human.
EvolutionaryTraceO15265.
GenomeRNAi6314.
NextBio24505.
PMAP-CutDBO15265.
PROO15265.
SOURCESearch...

Entry information

Entry nameATX7_HUMAN
AccessionPrimary (citable) accession number: O15265
Secondary accession number(s): B4E207 expand/collapse secondary AC list , E9PHP9, O75328, O75329, Q9Y6P8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 138 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

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