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O15265

- ATX7_HUMAN

UniProt

O15265 - ATX7_HUMAN

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Protein
Ataxin-7
Gene
ATXN7, SCA7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. chromatin organization Source: Reactome
  3. histone deubiquitination Source: UniProtKB
  4. microtubule cytoskeleton organization Source: UniProtKB
  5. negative regulation of insulin-like growth factor receptor signaling pathway Source: Ensembl
  6. negative regulation of phosphorylation Source: Ensembl
  7. nucleus organization Source: ProtInc
  8. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  9. transcription, DNA-templated Source: UniProtKB-KW
  10. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Ataxin-7
Alternative name(s):
Spinocerebellar ataxia type 7 protein
Gene namesi
Name:ATXN7
Synonyms:SCA7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:10560. ATXN7.

Subcellular locationi

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.3 Publications
Isoform b : Cytoplasm 3 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. microtubule cytoskeleton Source: UniProtKB
  3. nuclear matrix Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi257 – 2571K → R: Almost completely abolishes sumoylation. 1 Publication
Mutagenesisi858 – 8581K → R: No effect on sumoylation. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration, Spinocerebellar ataxia

Organism-specific databases

MIMi164500. phenotype.
Orphaneti94147. Spinocerebellar ataxia type 7.
PharmGKBiPA34973.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 892892Ataxin-7
PRO_0000064759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki257 – 257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiO15265.
PaxDbiO15265.
PRIDEiO15265.

PTM databases

PhosphoSiteiO15265.

Miscellaneous databases

PMAP-CutDBO15265.

Expressioni

Tissue specificityi

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.

Gene expression databases

ArrayExpressiO15265.
BgeeiO15265.
CleanExiHS_ATXN7.
GenevestigatoriO15265.

Organism-specific databases

HPAiHPA034989.

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. Interacts with alpha tubulin.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGRNO004682EBI-708350,EBI-947482
CEP72Q9P2092EBI-708350,EBI-739498
His2B:CG33910P022832EBI-708350,EBI-188137From a different organism.
LTBP4Q8N2S12EBI-708350,EBI-947718
MATN2O003392EBI-708350,EBI-949020
MEGF6O750952EBI-708350,EBI-947597
MEGF8Q7Z7M02EBI-708350,EBI-947617
NOC2LQ9Y3T92EBI-708350,EBI-751547
NUP62P371982EBI-708350,EBI-347978
SIAH1Q8IUQ42EBI-708350,EBI-747107
SORBS1Q9BX6615EBI-708350,EBI-433642
TAF10Q129626EBI-708350,EBI-708376
TRRAPQ9Y4A56EBI-708350,EBI-399128

Protein-protein interaction databases

BioGridi112221. 82 interactions.
IntActiO15265. 60 interactions.
MINTiMINT-2862470.
STRINGi9606.ENSP00000381590.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni343 – 3453
Turni352 – 3543
Helixi369 – 3746
Beta strandi378 – 3803
Helixi382 – 39312

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KKRNMR-A330-401[»]
ProteinModelPortaliO15265.
SMRiO15265. Positions 339-397.

Miscellaneous databases

EvolutionaryTraceiO15265.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini334 – 40168SCA7
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 205Poly-Ala
Compositional biasi23 – 286Poly-Ala
Compositional biasi30 – 4920Gln-rich
Add
BLAST
Compositional biasi30 – 3910Poly-Gln
Compositional biasi40 – 6526Pro-rich
Add
BLAST
Compositional biasi40 – 456Poly-Pro
Compositional biasi51 – 555Poly-Pro
Compositional biasi171 – 21949Ser-rich
Add
BLAST
Compositional biasi171 – 1744Poly-Ser
Compositional biasi213 – 2197Poly-Ser
Compositional biasi402 – 48685Pro-rich
Add
BLAST
Compositional biasi640 – 851212Ser-rich
Add
BLAST
Compositional biasi647 – 6548Poly-Ser
Compositional biasi717 – 73014Poly-Ser
Add
BLAST
Compositional biasi840 – 8456Poly-Ser

Sequence similaritiesi

Belongs to the ataxin-7 family.
Contains 1 SCA7 domain.

Phylogenomic databases

eggNOGiNOG270433.
HOGENOMiHOG000252910.
HOVERGENiHBG004320.
KOiK11318.
OMAiNSTNCHN.
OrthoDBiEOG7XSTDP.
PhylomeDBiO15265.
TreeFamiTF331337.

Family and domain databases

InterProiIPR013243. SCA7_dom.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF08313. SCA7. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS51505. SCA7. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform a (identifier: O15265-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSERAADDVR GEPRRAAAAA GGAAAAAARQ QQQQQQQQQP PPPQPQRQQH    50
PPPPPRRTRP EDGGPGAAST SAAAMATVGE RRPLPSPEVM LGQSWNLWVE 100
ASKLPGKDGT ELDESFKEFG KNREVMGLCR EDMPIFGFCP AHDDFYLVVC 150
NDCNQVVKPQ AFQSHYERRH SSSSKPPLAV PPTSVFSFFP SLSKSKGGSA 200
SGSNRSSSGG VLSASSSSSK LLKSPKEKLQ LRGNTRPMHP IQQSRVPHGR 250
IMTPSVKVEK IHPKMDGTLL KSAVGPTCPA TVSSLVKPGL NCPSIPKPTL 300
PSPGQILNGK GLPAPPTLEK KPEDNSNNRK FLNKRLSERE FDPDIHCGVI 350
DLDTKKPCTR SLTCKTHSLT QRRAVQGRRK RFDVLLAEHK NKTREKELIR 400
HPDSQQPPQP LRDPHPAPPR TSQEPHQNPH GVIPSESKPF VASKPKPHTP 450
SLPRPPGCPA QQGGSAPIDP PPVHESPHPP LPATEPASRL SSEEGEGDDK 500
EESVEKLDCH YSGHHPQPAS FCTFGSRQIG RGYYVFDSRW NRLRCALNLM 550
VEKHLNAQLW KKIPPVPSTT SPISTRIPHR TNSVPTSQCG VSYLAAATVS 600
TSPVLLSSTC ISPNSKSVPA HGTTLNAQPA ASGAMDPVCS MQSRQVSSSS 650
SSPSTPSGLS SVPSSPMSRK PQKLKSSKSL RPKESSGNST NCQNASSSTS 700
GGSGKKRKNS SPLLVHSSSS SSSSSSSSHS MESFRKNCVA HSGPPYPSTV 750
TSSHSIGLNC VTNKANAVNV RHDQSGRGPP TGSPAESIKR MSVMVNSSDS 800
TLSLGPFIHQ SNELPVNSHG SFSHSHTPLD KLIGKKRKCS PSSSSINNSS 850
SKPTKVAKVP AVNNVHMKHT GTIPGAQGLM NSSLLHQPKA RP 892
Length:892
Mass (Da):95,451
Last modified:January 1, 1998 - v1
Checksum:i9AEA787D77103C5F
GO
Isoform b (identifier: O15265-2) [UniParc]FASTAAdd to Basket

Also known as: Ataxin-7b, SCA7b

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

Show »
Length:945
Mass (Da):101,112
Checksum:iB230F94D3D468D77
GO
Isoform 3 (identifier: O15265-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-166: MSERAADDVR...VKPQAFQSHY → MEGSKTPLQSSPSAQELKAPL

Note: No experimental confirmation available.

Show »
Length:747
Mass (Da):79,535
Checksum:iAE6215958E714C8E
GO

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti264 – 2641K → R.2 Publications
Corresponds to variant rs1053338 [ dbSNP | Ensembl ].
VAR_011823
Natural varianti573 – 5731I → V.
Corresponds to variant rs3733124 [ dbSNP | Ensembl ].
VAR_053779
Natural varianti663 – 6631P → S.
Corresponds to variant rs1053340 [ dbSNP | Ensembl ].
VAR_011824
Natural varianti862 – 8621V → M.2 Publications
Corresponds to variant rs3774729 [ dbSNP | Ensembl ].
VAR_020143

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 166166MSERA…FQSHY → MEGSKTPLQSSPSAQELKAP L in isoform 3.
VSP_044456Add
BLAST
Alternative sequencei888 – 8925PKARP → DISSPCLRTGISATSPQSPD LKSKGTSLTAENSTGRNNAD TFEDKLHLHSALWTPRCL in isoform b.
VSP_007695

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051P → H in AAC19162. 1 Publication
Sequence conflicti129 – 1291C → S in AAC19162. 1 Publication
Sequence conflicti888 – 8925PKARP → VGNGL in AAC39765. 1 Publication
Sequence conflicti888 – 8925PKARP → VGNGL in AAC19163. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43102.1. [O15265-1]
CCDS46861.2. [O15265-3]
CCDS54603.1. [O15265-2]
PIRiT09193.
RefSeqiNP_000324.1. NM_000333.3. [O15265-1]
NP_001121621.2. NM_001128149.2. [O15265-3]
NP_001170858.1. NM_001177387.1. [O15265-2]
UniGeneiHs.476595.

Genome annotation databases

EnsembliENST00000295900; ENSP00000295900; ENSG00000163635. [O15265-1]
ENST00000398590; ENSP00000381590; ENSG00000163635. [O15265-2]
ENST00000484332; ENSP00000428277; ENSG00000163635. [O15265-3]
ENST00000487717; ENSP00000420234; ENSG00000163635. [O15265-1]
ENST00000538065; ENSP00000439585; ENSG00000163635. [O15265-2]
GeneIDi6314.
KEGGihsa:6314.
UCSCiuc003dlv.3. human. [O15265-1]
uc011bfn.2. human. [O15265-3]
uc021wzy.1. human. [O15265-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Triplet repeat expansion

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS43102.1. [O15265-1 ]
CCDS46861.2. [O15265-3 ]
CCDS54603.1. [O15265-2 ]
PIRi T09193.
RefSeqi NP_000324.1. NM_000333.3. [O15265-1 ]
NP_001121621.2. NM_001128149.2. [O15265-3 ]
NP_001170858.1. NM_001177387.1. [O15265-2 ]
UniGenei Hs.476595.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KKR NMR - A 330-401 [» ]
ProteinModelPortali O15265.
SMRi O15265. Positions 339-397.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112221. 82 interactions.
IntActi O15265. 60 interactions.
MINTi MINT-2862470.
STRINGi 9606.ENSP00000381590.

PTM databases

PhosphoSitei O15265.

Proteomic databases

MaxQBi O15265.
PaxDbi O15265.
PRIDEi O15265.

Protocols and materials databases

DNASUi 6314.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295900 ; ENSP00000295900 ; ENSG00000163635 . [O15265-1 ]
ENST00000398590 ; ENSP00000381590 ; ENSG00000163635 . [O15265-2 ]
ENST00000484332 ; ENSP00000428277 ; ENSG00000163635 . [O15265-3 ]
ENST00000487717 ; ENSP00000420234 ; ENSG00000163635 . [O15265-1 ]
ENST00000538065 ; ENSP00000439585 ; ENSG00000163635 . [O15265-2 ]
GeneIDi 6314.
KEGGi hsa:6314.
UCSCi uc003dlv.3. human. [O15265-1 ]
uc011bfn.2. human. [O15265-3 ]
uc021wzy.1. human. [O15265-2 ]

Organism-specific databases

CTDi 6314.
GeneCardsi GC03P063825.
GeneReviewsi ATXN7.
HGNCi HGNC:10560. ATXN7.
HPAi HPA034989.
MIMi 164500. phenotype.
607640. gene.
neXtProti NX_O15265.
Orphaneti 94147. Spinocerebellar ataxia type 7.
PharmGKBi PA34973.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270433.
HOGENOMi HOG000252910.
HOVERGENi HBG004320.
KOi K11318.
OMAi NSTNCHN.
OrthoDBi EOG7XSTDP.
PhylomeDBi O15265.
TreeFami TF331337.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi ATXN7. human.
EvolutionaryTracei O15265.
GenomeRNAii 6314.
NextBioi 24505.
PMAP-CutDB O15265.
PROi O15265.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15265.
Bgeei O15265.
CleanExi HS_ATXN7.
Genevestigatori O15265.

Family and domain databases

InterProi IPR013243. SCA7_dom.
IPR015880. Znf_C2H2-like.
[Graphical view ]
Pfami PF08313. SCA7. 1 hit.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
PROSITEi PS51505. SCA7. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiATX7_HUMAN
AccessioniPrimary (citable) accession number: O15265
Secondary accession number(s): B4E207
, E9PHP9, O75328, O75329, Q9Y6P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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