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O15265

- ATX7_HUMAN

UniProt

O15265 - ATX7_HUMAN

Protein

Ataxin-7

Gene

ATXN7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    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.

    GO - Cellular componenti

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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    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-7PRO_0000064759Add
    BLAST

    Amino acid modifications

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

    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

    1
    892
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15265.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini334 – 40168SCA7PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti105 – 1051P → H in AAC19162. (PubMed:9425224)Curated
    Sequence conflicti129 – 1291C → S in AAC19162. (PubMed:9425224)Curated
    Sequence conflicti888 – 8925PKARP → VGNGL in AAC39765. (PubMed:9425224)Curated
    Sequence conflicti888 – 8925PKARP → VGNGL in AAC19163. (PubMed:9425224)Curated

    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. 1 PublicationVSP_044456Add
    BLAST
    Alternative sequencei888 – 8925PKARP → DISSPCLRTGISATSPQSPD LKSKGTSLTAENSTGRNNAD TFEDKLHLHSALWTPRCL in isoform b. CuratedVSP_007695

    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]
    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 ]
    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

    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: October 1, 2014
    This is version 140 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