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 27-MAR-2024, entry version 210. DE RecName: Full=Ataxin-7 {ECO:0000303|PubMed:10441328}; DE AltName: Full=Spinocerebellar ataxia type 7 protein {ECO:0000303|PubMed:9288099}; GN Name=ATXN7; Synonyms=SCA7 {ECO:0000303|PubMed:9288099}; 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), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. 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 FUNCTION, AND 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 PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASP-266 AND ASP-344. RX PubMed=17646170; DOI=10.1074/jbc.m705265200; RA Young J.E., Gouw L., Propp S., Sopher B.L., Taylor J., Lin A., Hermel E., RA Logvinova A., Chen S.F., Chen S., Bredesen D.E., Truant R., Ptacek L.J., RA La Spada A.R., Ellerby L.M.; RT "Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity RT and transcriptional dysregulation."; RL J. Biol. Chem. 282:30150-30160(2007). RN [13] RP FUNCTION, AND 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 [14] 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 [15] 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 [16] 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 a component of the STAGA transcription coactivator- CC HAT complex (PubMed:15932940, PubMed:18206972). Mediates the CC interaction of STAGA complex with the CRX and is involved in CRX- CC dependent gene activation (PubMed:15932940, PubMed:18206972). Necessary CC for microtubule cytoskeleton stabilization (PubMed:22100762). CC {ECO:0000269|PubMed:15932940, ECO:0000269|PubMed:18206972, CC 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 (PubMed:15932940, CC PubMed:18206972). The STAGA core complex is associated with a CC subcomplex required for histone deubiquitination composed of ATXN7L3, CC ENY2 and USP22 (PubMed:15932940, PubMed:18206972). Interacts with CC SORBS1, PSMC1 and CRX (PubMed:11371513, PubMed:11734547). Interacts CC with TRRAP, GCN5L2 and TAF10 (PubMed:15115762). Interacts with alpha CC tubulin (PubMed:22100762). {ECO:0000269|PubMed:11371513, CC ECO:0000269|PubMed:11734547, ECO:0000269|PubMed:15115762, CC ECO:0000269|PubMed:15932940, ECO:0000269|PubMed:18206972, CC 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 CC {ECO:0000269|PubMed:12533095, ECO:0000269|PubMed:16314424, CC ECO:0000269|PubMed:22100762}. Nucleus, nucleolus CC {ECO:0000269|PubMed:10441328}. Nucleus matrix CC {ECO:0000269|PubMed:10441328}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:22100762}. Note=In addition to a diffuse CC distribution throughout the nucleus, it is associated with the nuclear CC matrix and the nucleolus (PubMed:10441328). It is able to shuttle CC between the nucleus and cytoplasm (PubMed:16314424). CC {ECO:0000269|PubMed:10441328, ECO:0000269|PubMed:16314424}. CC -!- SUBCELLULAR LOCATION: [Isoform b]: Cytoplasm CC {ECO:0000269|PubMed:12533095}. 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]: Isoform a is expressed in CNS, but is CC expressed predominantly in the peripherical tissues. CC {ECO:0000269|PubMed:12533095}. CC -!- TISSUE SPECIFICITY: [Isoform b]: Isoform b is expressed in CNS CC (PubMed:12533095). Also highly expressed in the frontal lobe, skeletal CC muscle and spinal cord and is expressed at a lower level in the lung, CC lymphoblast and intestine (PubMed:12533095). CC {ECO:0000269|PubMed:12533095}. CC -!- PTM: Proteolytically cleaved by caspase-7 (CASP7) (PubMed:17646170). CC The cleavage may be involved in SCA7 degeneration: the isoform CC fragments may exert distinct toxic influences that could contribute to CC selective neurodegeneration (PubMed:17646170). CC {ECO:0000269|PubMed:17646170}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8H7G; EM; 3.70 A; L=1-892. DR PDBsum; 2KKR; -. DR PDBsum; 7KTR; -. DR PDBsum; 7KTS; -. DR PDBsum; 8H7G; -. DR AlphaFoldDB; O15265; -. DR BMRB; O15265; -. DR EMDB; EMD-23027; -. DR EMDB; EMD-23028; -. DR EMDB; EMD-34520; -. DR SMR; O15265; -. DR BioGRID; 112221; 114. 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.ENSP00000295900; -. DR GlyCosmos; O15265; 1 site, 2 glycans. 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; 9606-ENSP00000439585; -. DR PeptideAtlas; O15265; -. DR ProteomicsDB; 20578; -. DR ProteomicsDB; 48553; -. [O15265-1] DR ProteomicsDB; 48554; -. [O15265-2] DR Pumba; O15265; -. DR TopDownProteomics; O15265-2; -. [O15265-2] DR Antibodypedia; 7629; 186 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 AGR; HGNC:10560; -. 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; NNVHTKH; -. DR OrthoDB; 1385477at2759; -. 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; 25 hits in 1170 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 206 other cell types or tissues. DR ExpressionAtlas; O15265; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0033276; C:transcription factor TFTC complex; NAS:ComplexPortal. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB. 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 DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal. DR GO; GO:0043484; P:regulation of RNA splicing; NAS: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 Gene3D; 6.10.140.670; -; 1. DR InterPro; IPR013243; SCA7_dom. DR PANTHER; PTHR15117; ATAXIN 7 RELATED; 1. DR PANTHER; PTHR15117:SF2; ATAXIN-7; 1. DR Pfam; PF08313; SCA7; 1. DR PROSITE; PS51505; SCA7; 1. DR Genevisible; O15265; HS. 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 SITE 266..267 FT /note="Cleavage; by caspase-7" FT /evidence="ECO:0000269|PubMed:17646170" FT SITE 344..345 FT /note="Cleavage; by caspase-7" FT /evidence="ECO:0000269|PubMed:17646170" FT CROSSLNK 257 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000269|PubMed:19843541" 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 266 FT /note="D->N: Abolished cleavage by caspase-7 and attenuates FT formation of protein aggregates in SCA7 degeneration; when FT associated with N-344." FT /evidence="ECO:0000269|PubMed:17646170" FT MUTAGEN 344 FT /note="D->N: Abolished cleavage by caspase-7 and attenuates FT formation of protein aggregates in SCA7 degeneration; when FT associated with N-266." FT /evidence="ECO:0000269|PubMed:17646170" 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 //