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Protein

Ataxin-7

Gene

Atxn7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Necessary for microtubule cytoskeleton stabilization (By similarity).By similarity

GO - Molecular functioni

  • chromatin binding Source: MGI

GO - Biological processi

  • histone deubiquitination Source: MGI
  • microtubule cytoskeleton organization Source: MGI
  • negative regulation of insulin-like growth factor receptor signaling pathway Source: MGI
  • negative regulation of phosphorylation Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Ataxin-7
Alternative name(s):
Spinocerebellar ataxia type 7 protein homolog
Gene namesi
Name:Atxn7
Synonyms:Sca7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:2179277. Atxn7.

Subcellular locationi

  • Nucleus Curated
  • Nucleusnucleolus By similarity
  • Nucleus matrix By similarity
  • Cytoplasmcytoskeleton By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • microtubule cytoskeleton Source: MGI
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • STAGA complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 867867Ataxin-7PRO_0000064760Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei222 – 2221N6-acetyllysineCombined sources
Cross-linki243 – 243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Proteolytically cleaved.By similarity
Sumoylation has no effect on subcellular location or interaction with components of the STAGA complex.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ8R4I1.
PaxDbiQ8R4I1.
PRIDEiQ8R4I1.

PTM databases

PhosphoSiteiQ8R4I1.

Expressioni

Tissue specificityi

Widely expressed in adult tissues, with the highest expression in heart, brain, liver and kidney.

Gene expression databases

BgeeiQ8R4I1.
CleanExiMM_ATXN7.
GenevisibleiQ8R4I1. MM.

Interactioni

Subunit structurei

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 (By similarity). Interacts with alpha tubulin (By similarity).By similarity

Protein-protein interaction databases

BioGridi232871. 1 interaction.
DIPiDIP-29176N.
IntActiQ8R4I1. 2 interactions.
STRINGi10090.ENSMUSP00000022257.

Structurei

3D structure databases

ProteinModelPortaliQ8R4I1.
SMRiQ8R4I1. Positions 325-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini320 – 38768SCA7PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 234Poly-Ala
Compositional biasi25 – 317Poly-Gln
Compositional biasi158 – 1614Poly-Ser
Compositional biasi202 – 2054Poly-Ser
Compositional biasi393 – 46573Pro-richAdd
BLAST
Compositional biasi619 – 735117Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the ataxin-7 family.Curated
Contains 1 SCA7 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4140. Eukaryota.
ENOG4111ZIZ. LUCA.
GeneTreeiENSGT00530000063215.
HOVERGENiHBG004320.
InParanoidiQ8R4I1.
KOiK11318.
OMAiNSTNCHN.
OrthoDBiEOG7XSTDP.
TreeFamiTF331337.

Family and domain databases

InterProiIPR030706. ATXN7.
IPR013243. SCA7_dom.
[Graphical view]
PANTHERiPTHR15117:SF2. PTHR15117:SF2. 1 hit.
PfamiPF08313. SCA7. 1 hit.
[Graphical view]
PROSITEiPS51505. SCA7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R4I1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSERAADDVR GEPRRAAGGA AAARQQQQQP QPLQPQRQHP PLRRPRAEDG
60 70 80 90 100
GTGDTTTSAA AMATVGERRP LPSPEAMLGQ SWNLWVEASK LPGKDGTELD
110 120 130 140 150
ESFKEFGKNR EVMGLCREDM PIFGLCPAHD DFYLVVCNDC NQVVKPQAFQ
160 170 180 190 200
SHYERRHSSS SKPALAVPHT SVFSLLPSLS KSKGSGAGGS SRPPSGGVLC
210 220 230 240 250
ASSSSKLLRL PKEKLPLRGN MKPMHPVQQI KVPHGRVMTP SVKVEKMHPK
260 270 280 290 300
MDGTLLKSTV GPACPATMSS AVKPGLNCPS IPKPTLPSPG QILNGKGLPA
310 320 330 340 350
MPTLEKKSED SSNNRKFLNK RLSEREFDPD IHCGVIDLDT KKPCTRSLTC
360 370 380 390 400
KTHSLTQRRA VQGRRKRFDV LLAEHKNKAR EKELIRHDSQ QVPHPLRDPH
410 420 430 440 450
PTPPRTPQEP QLPAESKPFL ASKPKPQTPS LPRPPGCPAQ QGGSTPIDPP
460 470 480 490 500
PGQESPHPPL PATEPASRLS SEEGEGDDRE ESVEKLDCHY SGRHPQPASF
510 520 530 540 550
CTFGSRQIGR GYYVFDSRWN RLRCALNLMV EKHLNAQLWK KIPPVPCTTS
560 570 580 590 600
PVSARVPHRT NSVPTSQGGI SYLAATTVSA PPVLLSSTCI SPNSKSVPAH
610 620 630 640 650
GTTLNAQPAG SGAMDPVCSV QSRQVSASSS PPSTPSGLSS VPSSPLSRKP
660 670 680 690 700
QKWKPSKSIR PKESSALSTN CHNASSSTSG GSGKKRKNSS PLLVPSSSSS
710 720 730 740 750
SSSSSSSSHS VNSFRKNCVA HSGTPYLSTA PSSHSIGLNC VTNKTHSVSL
760 770 780 790 800
RHEQAGRGPA GVSSAEPIKR MSVMVNSSDS TLSLGPFIHQ ASELPVNPHS
810 820 830 840 850
HTPLDKLIGK KRKCSPGSST VGNSGSKPTK VAKLPAMNNV HMKHTGNISG
860
AQGLTNNSLL HQPKARP
Length:867
Mass (Da):92,697
Last modified:July 27, 2011 - v2
Checksum:iD12908CFD3257A4A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101R → H in AAL84238 (PubMed:12039035).Curated
Sequence conflicti176 – 1783LPS → FPP in AAL84238 (PubMed:12039035).Curated
Sequence conflicti232 – 2321V → A in AAL84238 (PubMed:12039035).Curated
Sequence conflicti626 – 6261S → L in AAL84238 (PubMed:12039035).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF455111 mRNA. Translation: AAL84238.1.
AK046679 mRNA. Translation: BAC32834.1.
AC116479 Genomic DNA. No translation available.
CCDSiCCDS26823.1.
RefSeqiNP_631973.3. NM_139227.4.
UniGeneiMm.133625.

Genome annotation databases

EnsembliENSMUST00000022257; ENSMUSP00000022257; ENSMUSG00000021738.
GeneIDi246103.
KEGGimmu:246103.
UCSCiuc007sgi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF455111 mRNA. Translation: AAL84238.1.
AK046679 mRNA. Translation: BAC32834.1.
AC116479 Genomic DNA. No translation available.
CCDSiCCDS26823.1.
RefSeqiNP_631973.3. NM_139227.4.
UniGeneiMm.133625.

3D structure databases

ProteinModelPortaliQ8R4I1.
SMRiQ8R4I1. Positions 325-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232871. 1 interaction.
DIPiDIP-29176N.
IntActiQ8R4I1. 2 interactions.
STRINGi10090.ENSMUSP00000022257.

PTM databases

PhosphoSiteiQ8R4I1.

Proteomic databases

MaxQBiQ8R4I1.
PaxDbiQ8R4I1.
PRIDEiQ8R4I1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022257; ENSMUSP00000022257; ENSMUSG00000021738.
GeneIDi246103.
KEGGimmu:246103.
UCSCiuc007sgi.2. mouse.

Organism-specific databases

CTDi6314.
MGIiMGI:2179277. Atxn7.

Phylogenomic databases

eggNOGiKOG4140. Eukaryota.
ENOG4111ZIZ. LUCA.
GeneTreeiENSGT00530000063215.
HOVERGENiHBG004320.
InParanoidiQ8R4I1.
KOiK11318.
OMAiNSTNCHN.
OrthoDBiEOG7XSTDP.
TreeFamiTF331337.

Miscellaneous databases

PROiQ8R4I1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R4I1.
CleanExiMM_ATXN7.
GenevisibleiQ8R4I1. MM.

Family and domain databases

InterProiIPR030706. ATXN7.
IPR013243. SCA7_dom.
[Graphical view]
PANTHERiPTHR15117:SF2. PTHR15117:SF2. 1 hit.
PfamiPF08313. SCA7. 1 hit.
[Graphical view]
PROSITEiPS51505. SCA7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression analysis of the murine homolog of the spinocerebellar ataxia type 7 (SCA7) gene."
    Stroem A.-L., Jonasson J., Hart P., Braennstroem T., Forsgren L., Holmberg M.
    Gene 285:91-99(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Adipose tissue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "Polyglutamine-expanded ataxin-7 antagonizes CRX function and induces cone-rod dystrophy in a mouse model of SCA7."
    La Spada A.R., Fu Y.-H., Sopher B.L., Libby R.T., Wang X., Li L.Y., Einum D.D., Huang J., Possin D.E., Smith A.C., Martinez R.A., Koszdin K.L., Treuting P.M., Ware C.B., Hurley J.B., Ptacek L.J., Chen S.
    Neuron 31:913-927(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRX.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiATX7_MOUSE
AccessioniPrimary (citable) accession number: Q8R4I1
Secondary accession number(s): E9QPX9, Q8BL17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.