ATX7_HUMAN
ID ATX7_HUMAN Reviewed; 892 AA.
AC O15265; B4E207; E9PHP9; O75328; O75329; Q9Y6P8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Ataxin-7;
DE AltName: Full=Spinocerebellar ataxia type 7 protein;
GN Name=ATXN7; Synonyms=SCA7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), INVOLVEMENT IN SCA7, AND
RP POLYMORPHISM.
RC TISSUE=Lymphoblast;
RX PubMed=9288099; DOI=10.1038/ng0997-65;
RA David G., Abbas N., Stevanin G., Duerr A., Yvert G., Cancel G., Weber C.,
RA Imbert G., Saudou F., Antoniou E., Drabkin H., Gemmill R., Giunti P.,
RA Benomar A., Wood N., Ruberg M., Agid Y., Mandel J.-L., Brice A.;
RT "Cloning of the SCA7 gene reveals a highly unstable CAG repeat expansion.";
RL Nat. Genet. 17:65-70(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), NUCLEOTIDE SEQUENCE [GENOMIC DNA]
RP OF 1-131, POLYMORPHISM, AND VARIANTS ARG-264 AND MET-862.
RC TISSUE=Colon;
RX PubMed=9425224; DOI=10.1093/hmg/7.2.177;
RA Del-Favero J., Krols L., Michalik A., Theuns J., Loefgren A., Goossens D.,
RA Wehnert A., Van den Bossche D., Van Zand K., Backhovens H.,
RA van Regenmorter N., Martin J.-J., Van Broeckhoven C.;
RT "Molecular genetic analysis of autosomal dominant cerebellar ataxia with
RT retinal degeneration (ADCA type II) caused by CAG triplet repeat
RT expansion.";
RL Hum. Mol. Genet. 7:177-186(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS ARG-264
RP AND MET-862.
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP ALTERNATIVE SPLICING (ISOFORMS A AND B).
RC TISSUE=Testis;
RX PubMed=12533095; DOI=10.1001/archneur.60.1.97;
RA Einum D.D., Clark A.M., Townsend J.J., Ptacek L.J., Fu Y.H.;
RT "A novel central nervous system-enriched spinocerebellar ataxia type 7 gene
RT product.";
RL Arch. Neurol. 60:97-103(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10441328; DOI=10.1093/hmg/8.9.1657;
RA Kaytor M.D., Duvick L.A., Skinner P.J., Koob M.D., Ranum L.P., Orr H.T.;
RT "Nuclear localization of the spinocerebellar ataxia type 7 protein, ataxin-
RT 7.";
RL Hum. Mol. Genet. 8:1657-1664(1999).
RN [7]
RP INTERACTION WITH SORBS1.
RX PubMed=11371513; DOI=10.1093/hmg/10.11.1201;
RA Lebre A.-S., Jamot L., Takahashi J., Spassky N., Leprince C., Ravise N.,
RA Zander C., Fujigasaki H., Kussel-Andermann P., Duyckaerts C., Camonis J.H.,
RA Brice A.;
RT "Ataxin-7 interacts with a Cbl-associated protein that it recruits into
RT neuronal intranuclear inclusions.";
RL Hum. Mol. Genet. 10:1201-1213(2001).
RN [8]
RP INTERACTION WITH PSMC1.
RX PubMed=11734547; DOI=10.1093/hmg/10.24.2821;
RA Matilla A., Gorbea C., Einum D.D., Townsend J., Michalik A.,
RA van Broeckhoven C., Jensen C.C., Murphy K.J., Ptacek L.J., Fu Y.H.;
RT "Association of ataxin-7 with the proteasome subunit S4 of the 19S
RT regulatory complex.";
RL Hum. Mol. Genet. 10:2821-2831(2001).
RN [9]
RP INTERACTION WITH TRRAP; GCN5L2 AND TAF10.
RX PubMed=15115762; DOI=10.1093/hmg/ddh139;
RA Helmlinger D., Hardy S., Sasorith S., Klein F., Robert F., Weber C.,
RA Miguet L., Potier N., Van-Dorsselaer A., Wurtz J.M., Mandel J.L., Tora L.,
RA Devys D.;
RT "Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing
RT complexes.";
RL Hum. Mol. Genet. 13:1257-1265(2004).
RN [10]
RP IDENTIFICATION IN THE STAGA COMPLEX.
RX PubMed=15932940; DOI=10.1073/pnas.0503505102;
RA Palhan V.B., Chen S., Peng G.H., Tjernberg A., Gamper A.M., Fan Y.,
RA Chait B.T., La Spada A.R., Roeder R.G.;
RT "Polyglutamine-expanded ataxin-7 inhibits STAGA histone acetyltransferase
RT activity to produce retinal degeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8472-8477(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=16314424; DOI=10.1074/jbc.m506751200;
RA Taylor J., Grote S.K., Xia J., Vandelft M., Graczyk J., Ellerby L.M.,
RA La Spada A.R., Truant R.;
RT "Ataxin-7 can export from the nucleus via a conserved exportin-dependent
RT signal.";
RL J. Biol. Chem. 281:2730-2739(2006).
RN [12]
RP IDENTIFICATION IN STAGA COMPLEX.
RX PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G.,
RA Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT coactivates nuclear receptors, and counteracts heterochromatin silencing.";
RL Mol. Cell 29:92-101(2008).
RN [13]
RP SUMOYLATION AT LYS-257, AND MUTAGENESIS OF LYS-257 AND LYS-858.
RX PubMed=19843541; DOI=10.1093/hmg/ddp478;
RA Janer A., Werner A., Takahashi-Fujigasaki J., Daret A., Fujigasaki H.,
RA Takada K., Duyckaerts C., Brice A., Dejean A., Sittler A.;
RT "SUMOylation attenuates the aggregation propensity and cellular toxicity of
RT the polyglutamine expanded ataxin-7.";
RL Hum. Mol. Genet. 19:181-195(2010).
RN [14]
RP FUNCTION, INTERACTION WITH ALPHA TUBULIN, AND SUBCELLULAR LOCATION.
RX PubMed=22100762; DOI=10.1093/hmg/ddr539;
RA Nakamura Y., Tagawa K., Oka T., Sasabe T., Ito H., Shiwaku H.,
RA La Spada A.R., Okazawa H.;
RT "Ataxin-7 associates with microtubules and stabilizes the cytoskeletal
RT network.";
RL Hum. Mol. Genet. 21:1099-1110(2012).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-257, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Acts as component of the STAGA transcription coactivator-HAT
CC complex. Mediates the interaction of STAGA complex with the CRX and is
CC involved in CRX-dependent gene activation. Necessary for microtubule
CC cytoskeleton stabilization. {ECO:0000269|PubMed:22100762}.
CC -!- SUBUNIT: Component of the STAGA transcription coactivator-HAT complex,
CC at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L,
CC TAD1L, TAF10, TAF12, TRRAP, TAF9 and ATXN7. The STAGA core complex is
CC associated with a subcomplex required for histone deubiquitination
CC composed of ATXN7L3, ENY2 and USP22. Interacts with SORBS1, PSMC1 and
CC CRX. Interacts with TRRAP, GCN5L2 and TAF10. Interacts with alpha
CC tubulin. {ECO:0000269|PubMed:11371513, ECO:0000269|PubMed:11734547,
CC ECO:0000269|PubMed:15115762, ECO:0000269|PubMed:15932940,
CC ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:22100762}.
CC -!- INTERACTION:
CC O15265; O00468: AGRN; NbExp=2; IntAct=EBI-708350, EBI-947482;
CC O15265; Q9P209: CEP72; NbExp=2; IntAct=EBI-708350, EBI-739498;
CC O15265; Q8N2S1: LTBP4; NbExp=2; IntAct=EBI-708350, EBI-947718;
CC O15265; O00339: MATN2; NbExp=2; IntAct=EBI-708350, EBI-949020;
CC O15265; O75095: MEGF6; NbExp=2; IntAct=EBI-708350, EBI-947597;
CC O15265; Q7Z7M0: MEGF8; NbExp=2; IntAct=EBI-708350, EBI-947617;
CC O15265; Q9Y3T9: NOC2L; NbExp=2; IntAct=EBI-708350, EBI-751547;
CC O15265; P37198: NUP62; NbExp=2; IntAct=EBI-708350, EBI-347978;
CC O15265; Q8IUQ4: SIAH1; NbExp=2; IntAct=EBI-708350, EBI-747107;
CC O15265; Q9BX66: SORBS1; NbExp=15; IntAct=EBI-708350, EBI-433642;
CC O15265; Q12962: TAF10; NbExp=7; IntAct=EBI-708350, EBI-708376;
CC O15265; Q9Y4A5: TRRAP; NbExp=7; IntAct=EBI-708350, EBI-399128;
CC O15265; P02283: His2B:CG33910; Xeno; NbExp=2; IntAct=EBI-708350, EBI-188137;
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Nucleus. Nucleus, nucleolus. Nucleus
CC matrix. Cytoplasm, cytoskeleton. Note=In addition to a diffuse
CC distribution throughout the nucleus, it is associated with the nuclear
CC matrix and the nucleolus. It is able to shuttle between the nucleus and
CC cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform b]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a; Synonyms=Ataxin-7a;
CC IsoId=O15265-1; Sequence=Displayed;
CC Name=b; Synonyms=Ataxin-7b, SCA7b;
CC IsoId=O15265-2; Sequence=VSP_007695;
CC Name=3;
CC IsoId=O15265-3; Sequence=VSP_044456;
CC -!- TISSUE SPECIFICITY: Isoform a and isoform b are expressed in CNS, but
CC isoform a is expressed predominantly in the peripherical tissues.
CC Isoform b is also highly expressed in the frontal lobe, skeletal muscle
CC and spinal cord and is expressed at a lower level in the lung,
CC lymphoblast and intestine.
CC -!- PTM: Proteolytically cleaved. The cleavage may be involved in SCA7
CC degeneration: the isoform fragments may exert distinct toxic influences
CC that could contribute to selective neurodegeneration.
CC -!- PTM: Sumoylation decreases the aggregation propensity and cellular
CC toxicity of forms with an expanded poly-Gln region but has no effect on
CC subcellular location or interaction with components of the STAGA
CC complex. {ECO:0000269|PubMed:19843541}.
CC -!- POLYMORPHISM: The poly-Gln region of ATXN7 is highly polymorphic (4 to
CC 18 repeats) in the normal population and is expanded to about 38-130
CC repeats in SCA7 patients. Intermediate alleles with 28 to 35 repeats
CC are prone to further expansion. {ECO:0000269|PubMed:9288099,
CC ECO:0000269|PubMed:9425224}.
CC -!- DISEASE: Spinocerebellar ataxia 7 (SCA7) [MIM:164500]: Spinocerebellar
CC ataxia is a clinically and genetically heterogeneous group of
CC cerebellar disorders. Patients show progressive incoordination of gait
CC and often poor coordination of hands, speech and eye movements, due to
CC degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. SCA7 belongs to the autosomal dominant
CC cerebellar ataxias type II (ADCA II) which are characterized by
CC cerebellar ataxia with retinal degeneration and pigmentary macular
CC dystrophy. {ECO:0000269|PubMed:9288099}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ataxin-7 family. {ECO:0000305}.
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DR EMBL; AJ000517; CAA04154.1; -; mRNA.
DR EMBL; AF032102; AAC19162.1; -; Genomic_DNA.
DR EMBL; AF032103; AAC19163.1; -; mRNA.
DR EMBL; AF032105; AAC39765.1; -; mRNA.
DR EMBL; AK304062; BAG64969.1; -; mRNA.
DR EMBL; AC012557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AA398030; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS43102.1; -. [O15265-1]
DR CCDS; CCDS46861.2; -. [O15265-3]
DR CCDS; CCDS54603.1; -. [O15265-2]
DR PIR; T09193; T09193.
DR RefSeq; NP_000324.1; NM_000333.3. [O15265-1]
DR RefSeq; NP_001121621.2; NM_001128149.2. [O15265-3]
DR RefSeq; NP_001170858.1; NM_001177387.1. [O15265-2]
DR PDB; 2KKR; NMR; -; A=330-401.
DR PDB; 7KTR; EM; 2.93 A; N=1-892.
DR PDB; 7KTS; EM; 19.09 A; N=1-892.
DR PDBsum; 2KKR; -.
DR PDBsum; 7KTR; -.
DR PDBsum; 7KTS; -.
DR AlphaFoldDB; O15265; -.
DR BMRB; O15265; -.
DR SMR; O15265; -.
DR BioGRID; 112221; 108.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR CORUM; O15265; -.
DR IntAct; O15265; 81.
DR MINT; O15265; -.
DR STRING; 9606.ENSP00000439585; -.
DR GlyGen; O15265; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; O15265; -.
DR PhosphoSitePlus; O15265; -.
DR SwissPalm; O15265; -.
DR BioMuta; ATXN7; -.
DR EPD; O15265; -.
DR jPOST; O15265; -.
DR MassIVE; O15265; -.
DR MaxQB; O15265; -.
DR PaxDb; O15265; -.
DR PeptideAtlas; O15265; -.
DR PRIDE; O15265; -.
DR ProteomicsDB; 20578; -.
DR ProteomicsDB; 48553; -. [O15265-1]
DR ProteomicsDB; 48554; -. [O15265-2]
DR TopDownProteomics; O15265-2; -. [O15265-2]
DR Antibodypedia; 7629; 168 antibodies from 32 providers.
DR DNASU; 6314; -.
DR Ensembl; ENST00000295900.10; ENSP00000295900.6; ENSG00000163635.20. [O15265-1]
DR Ensembl; ENST00000484332.1; ENSP00000428277.1; ENSG00000163635.20. [O15265-3]
DR Ensembl; ENST00000487717.5; ENSP00000420234.1; ENSG00000163635.20. [O15265-1]
DR Ensembl; ENST00000522345.2; ENSP00000428067.2; ENSG00000163635.20. [O15265-2]
DR Ensembl; ENST00000674280.1; ENSP00000501377.1; ENSG00000163635.20. [O15265-1]
DR GeneID; 6314; -.
DR KEGG; hsa:6314; -.
DR MANE-Select; ENST00000674280.1; ENSP00000501377.1; NM_001377405.1; NP_001364334.1.
DR UCSC; uc003dlw.5; human. [O15265-1]
DR CTD; 6314; -.
DR DisGeNET; 6314; -.
DR GeneCards; ATXN7; -.
DR GeneReviews; ATXN7; -.
DR HGNC; HGNC:10560; ATXN7.
DR HPA; ENSG00000163635; Low tissue specificity.
DR MalaCards; ATXN7; -.
DR MIM; 164500; phenotype.
DR MIM; 607640; gene.
DR neXtProt; NX_O15265; -.
DR OpenTargets; ENSG00000163635; -.
DR Orphanet; 94147; Spinocerebellar ataxia type 7.
DR PharmGKB; PA34973; -.
DR VEuPathDB; HostDB:ENSG00000163635; -.
DR eggNOG; KOG4140; Eukaryota.
DR GeneTree; ENSGT00940000157279; -.
DR HOGENOM; CLU_014451_1_0_1; -.
DR InParanoid; O15265; -.
DR OMA; PFVHHQP; -.
DR OrthoDB; 693000at2759; -.
DR PhylomeDB; O15265; -.
DR TreeFam; TF331337; -.
DR PathwayCommons; O15265; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; O15265; -.
DR SIGNOR; O15265; -.
DR BioGRID-ORCS; 6314; 23 hits in 1086 CRISPR screens.
DR ChiTaRS; ATXN7; human.
DR EvolutionaryTrace; O15265; -.
DR GenomeRNAi; 6314; -.
DR Pharos; O15265; Tbio.
DR PRO; PR:O15265; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O15265; protein.
DR Bgee; ENSG00000163635; Expressed in mucosa of paranasal sinus and 204 other tissues.
DR ExpressionAtlas; O15265; baseline and differential.
DR Genevisible; O15265; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; IC:ComplexPortal.
DR GO; GO:0033276; C:transcription factor TFTC complex; IC:ComplexPortal.
DR GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:CACAO.
DR GO; GO:0006997; P:nucleus organization; TAS:ProtInc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR InterPro; IPR030706; ATXN7.
DR InterPro; IPR013243; SCA7_dom.
DR PANTHER; PTHR15117:SF2; PTHR15117:SF2; 1.
DR Pfam; PF08313; SCA7; 1.
DR PROSITE; PS51505; SCA7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Disease variant; Isopeptide bond; Neurodegeneration; Nucleus;
KW Reference proteome; Spinocerebellar ataxia; Transcription;
KW Transcription regulation; Triplet repeat expansion; Ubl conjugation.
FT CHAIN 1..892
FT /note="Ataxin-7"
FT /id="PRO_0000064759"
FT DOMAIN 334..401
FT /note="SCA7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00838"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..857
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 257
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..166
FT /note="MSERAADDVRGEPRRAAAAAGGAAAAAARQQQQQQQQQQPPPPQPQRQQHPP
FT PPPRRTRPEDGGPGAASTSAAAMATVGERRPLPSPEVMLGQSWNLWVEASKLPGKDGTE
FT LDESFKEFGKNREVMGLCREDMPIFGFCPAHDDFYLVVCNDCNQVVKPQAFQSHY ->
FT MEGSKTPLQSSPSAQELKAPL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044456"
FT VAR_SEQ 888..892
FT /note="PKARP -> DISSPCLRTGISATSPQSPDLKSKGTSLTAENSTGRNNADTFE
FT DKLHLHSALWTPRCL (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_007695"
FT VARIANT 264
FT /note="K -> R (in dbSNP:rs1053338)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9425224"
FT /id="VAR_011823"
FT VARIANT 573
FT /note="I -> V (in dbSNP:rs3733124)"
FT /id="VAR_053779"
FT VARIANT 663
FT /note="P -> S (in dbSNP:rs1053340)"
FT /id="VAR_011824"
FT VARIANT 862
FT /note="V -> M (in dbSNP:rs3774729)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9425224"
FT /id="VAR_020143"
FT MUTAGEN 257
FT /note="K->R: Almost completely abolishes sumoylation."
FT /evidence="ECO:0000269|PubMed:19843541"
FT MUTAGEN 858
FT /note="K->R: No effect on sumoylation."
FT /evidence="ECO:0000269|PubMed:19843541"
FT CONFLICT 105
FT /note="P -> H (in Ref. 2; AAC19162)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="C -> S (in Ref. 2; AAC19162)"
FT /evidence="ECO:0000305"
FT CONFLICT 888..892
FT /note="PKARP -> VGNGL (in Ref. 2; AAC39765/AAC19163)"
FT /evidence="ECO:0000305"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:2KKR"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:2KKR"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:2KKR"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:2KKR"
FT HELIX 382..393
FT /evidence="ECO:0007829|PDB:2KKR"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:7KTR"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:7KTR"
FT HELIX 541..557
FT /evidence="ECO:0007829|PDB:7KTR"
SQ SEQUENCE 892 AA; 95451 MW; 9AEA787D77103C5F CRC64;
MSERAADDVR GEPRRAAAAA GGAAAAAARQ QQQQQQQQQP PPPQPQRQQH PPPPPRRTRP
EDGGPGAAST SAAAMATVGE RRPLPSPEVM LGQSWNLWVE ASKLPGKDGT ELDESFKEFG
KNREVMGLCR EDMPIFGFCP AHDDFYLVVC NDCNQVVKPQ AFQSHYERRH SSSSKPPLAV
PPTSVFSFFP SLSKSKGGSA SGSNRSSSGG VLSASSSSSK LLKSPKEKLQ LRGNTRPMHP
IQQSRVPHGR IMTPSVKVEK IHPKMDGTLL KSAVGPTCPA TVSSLVKPGL NCPSIPKPTL
PSPGQILNGK GLPAPPTLEK KPEDNSNNRK FLNKRLSERE FDPDIHCGVI DLDTKKPCTR
SLTCKTHSLT QRRAVQGRRK RFDVLLAEHK NKTREKELIR HPDSQQPPQP LRDPHPAPPR
TSQEPHQNPH GVIPSESKPF VASKPKPHTP SLPRPPGCPA QQGGSAPIDP PPVHESPHPP
LPATEPASRL SSEEGEGDDK EESVEKLDCH YSGHHPQPAS FCTFGSRQIG RGYYVFDSRW
NRLRCALNLM VEKHLNAQLW KKIPPVPSTT SPISTRIPHR TNSVPTSQCG VSYLAAATVS
TSPVLLSSTC ISPNSKSVPA HGTTLNAQPA ASGAMDPVCS MQSRQVSSSS SSPSTPSGLS
SVPSSPMSRK PQKLKSSKSL RPKESSGNST NCQNASSSTS GGSGKKRKNS SPLLVHSSSS
SSSSSSSSHS MESFRKNCVA HSGPPYPSTV TSSHSIGLNC VTNKANAVNV RHDQSGRGPP
TGSPAESIKR MSVMVNSSDS TLSLGPFIHQ SNELPVNSHG SFSHSHTPLD KLIGKKRKCS
PSSSSINNSS SKPTKVAKVP AVNNVHMKHT GTIPGAQGLM NSSLLHQPKA RP
