ID ATX1_MOUSE Reviewed; 791 AA. AC P54254; Q8C866; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 2. DT 27-MAR-2024, entry version 182. DE RecName: Full=Ataxin-1; DE AltName: Full=Spinocerebellar ataxia type 1 protein homolog; GN Name=Atxn1; Synonyms=Sca1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=C57BL/6 X CBA; TISSUE=Brain, Retina, and Thymus; RX PubMed=8789437; DOI=10.1093/hmg/5.1.33; RA Banfi S., Servadio A., Chung M.-Y., Capozzoli F., Duvick L.A., Elde R., RA Zoghbi H.Y., Orr H.T.; RT "Cloning and developmental expression analysis of the murine homolog of the RT spinocerebellar ataxia type 1 gene (Sca1)."; RL Hum. Mol. Genet. 5:33-40(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryonic head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NMRI; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-771. RX PubMed=9778246; DOI=10.1016/s0092-8674(00)81781-x; RA Klement I.A., Skinner P.J., Kaytor M.D., Yi H., Hersch S.M., Clark H.B., RA Zoghbi H.Y., Orr H.T.; RT "Ataxin-1 nuclear localization and aggregation: role in polyglutamine- RT induced disease in SCA1 transgenic mice."; RL Cell 95:41-53(1998). RN [5] RP INTERACTION WITH ANP32A. RX PubMed=9353121; DOI=10.1038/40159; RA Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y.; RT "The cerebellar leucine-rich acidic nuclear protein interacts with ataxin- RT 1."; RL Nature 389:974-978(1997). RN [6] RP DISEASE MODEL, AND UBIQUITINATION. RX PubMed=10624951; DOI=10.1016/s0896-6273(00)81035-1; RA Cummings C.J., Reinstein E., Sun Y., Antalffy B., Jiang Y., Ciechanover A., RA Orr H.T., Beaudet A.L., Zoghbi H.Y.; RT "Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency RT while accelerating polyglutamine-induced pathology in SCA1 mice."; RL Neuron 24:879-892(1999). RN [7] RP DISEASE MODEL. RX PubMed=12086639; DOI=10.1016/s0896-6273(02)00733-x; RA Watase K., Weeber E.J., Xu B., Antalffy B., Yuva-Paylor L., Hashimoto K., RA Kano M., Atkinson R., Sun Y., Armstrong D.L., Sweatt J.D., Orr H.T., RA Paylor R., Zoghbi H.Y.; RT "A long CAG repeat in the mouse Sca1 locus replicates SCA1 features and RT reveals the impact of protein solubility on selective neurodegeneration."; RL Neuron 34:905-919(2002). RN [8] RP INTERACTION WITH CIC. RX PubMed=17190598; DOI=10.1016/j.cell.2006.11.038; RA Lam Y.C., Bowman A.B., Jafar-Nejad P., Lim J., Richman R., Fryer J.D., RA Hyun E.D., Duvick L.A., Orr H.T., Botas J., Zoghbi H.Y.; RT "ATAXIN-1 interacts with the repressor Capicua in its native complex to RT cause SCA1 neuropathology."; RL Cell 127:1335-1347(2006). RN [9] RP INTERACTION WITH ATXN1L. RX PubMed=17322884; DOI=10.1038/ng1977; RA Bowman A.B., Lam Y.C., Jafar-Nejad P., Chen H.-K., Richman R., Samaco R.C., RA Fryer J.D., Kahle J.J., Orr H.T., Zoghbi H.Y.; RT "Duplication of Atxn1l suppresses SCA1 neuropathology by decreasing RT incorporation of polyglutamine-expanded ataxin-1 into native complexes."; RL Nat. Genet. 39:373-379(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-87; SER-213; THR-218 RP AND SER-229, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and RC Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [11] RP DISEASE MODEL, AND INDUCTION. RX PubMed=25768905; DOI=10.1016/j.cell.2015.02.012; RA Gennarino V.A., Singh R.K., White J.J., De Maio A., Han K., Kim J.Y., RA Jafar-Nejad P., di Ronza A., Kang H., Sayegh L.S., Cooper T.A., Orr H.T., RA Sillitoe R.V., Zoghbi H.Y.; RT "Pumilio1 haploinsufficiency leads to SCA1-like neurodegeneration by RT increasing wild-type Ataxin1 levels."; RL Cell 160:1087-1098(2015). RN [12] RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND IDENTIFICATION IN A RP COMPLEX WITH CIC AND ATXN1L. RX PubMed=28288114; DOI=10.1038/ng.3808; RA Lu H.C., Tan Q., Rousseaux M.W., Wang W., Kim J.Y., Richman R., Wan Y.W., RA Yeh S.Y., Patel J.M., Liu X., Lin T., Lee Y., Fryer J.D., Han J., RA Chahrour M., Finnell R.H., Lei Y., Zurita-Jimenez M.E., Ahimaz P., RA Anyane-Yeboa K., Van Maldergem L., Lehalle D., Jean-Marcais N., RA Mosca-Boidron A.L., Thevenon J., Cousin M.A., Bro D.E., Lanpher B.C., RA Klee E.W., Alexander N., Bainbridge M.N., Orr H.T., Sillitoe R.V., RA Ljungberg M.C., Liu Z., Schaaf C.P., Zoghbi H.Y.; RT "Disruption of the ATXN1-CIC complex causes a spectrum of neurobehavioral RT phenotypes in mice and humans."; RL Nat. Genet. 49:527-536(2017). CC -!- FUNCTION: Chromatin-binding factor that repress Notch signaling in the CC absence of Notch intracellular domain by acting as a CBF1 corepressor. CC Binds to the HEY promoter and might assist, along with NCOR2, RBPJ- CC mediated repression (By similarity). May be involved in RNA metabolism CC (By similarity). In concert with CIC and ATXN1L, involved in brain CC development (PubMed:28288114). {ECO:0000250|UniProtKB:P54253, CC ECO:0000269|PubMed:28288114}. CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with PQBP1, UBQLN4 and CC USP7 (By similarity). Interacts with ANP32A (PubMed:9353121). Interacts CC with CIC (PubMed:17190598). Directly interacts with RBPJ; this CC interaction is disrupted in the presence of Notch intracellular domain. CC Interacts with ATXN1L; competes with ATXN1L for RBPJ-binding CC (PubMed:17322884). Found in a complex with CIC and ATXN1L CC (PubMed:28288114). {ECO:0000250|UniProtKB:P54253, CC ECO:0000269|PubMed:17190598, ECO:0000269|PubMed:17322884, CC ECO:0000269|PubMed:28288114, ECO:0000269|PubMed:9353121}. CC -!- INTERACTION: CC P54254; Q924A2: Cic; NbExp=2; IntAct=EBI-1169713, EBI-8412165; CC P54254; Q8CHK4: Kat5; NbExp=2; IntAct=EBI-1169713, EBI-1169948; CC P54254; P51448: Rora; NbExp=3; IntAct=EBI-1169713, EBI-1169722; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54253}. Nucleus CC {ECO:0000269|PubMed:9778246}. Note=Colocalizes with USP7 in the CC nucleus. {ECO:0000250|UniProtKB:P54253}. CC -!- TISSUE SPECIFICITY: Expressed in the cortex and hypothalamus (at CC protein level). Widely expressed. In brain, the pattern of distribution CC is limited to neuron populations. {ECO:0000269|PubMed:28288114, CC ECO:0000269|PubMed:8789437}. CC -!- DEVELOPMENTAL STAGE: Transient expression burst in Purkinje cells as CC the cerebellar cortex becomes functional (postnatal day 14), and in CC mesenchymal cells of the developing intervertebral disks of the spinal CC column. {ECO:0000269|PubMed:8789437}. CC -!- INDUCTION: Atxn1 protein levels are directly regulated by Pum1 protein: CC Pum1 acts by binding to the 3'-UTR of Atxn1 mRNA, affecting Atxn1 mRNA CC stability and leading to reduced Atxn1 protein levels. CC {ECO:0000269|PubMed:25768905}. CC -!- DOMAIN: The AXH domain is required for interaction with CIC. CC {ECO:0000269|PubMed:17190598}. CC -!- PTM: Ubiquitinated by UBE3A, leading to its degradation by the CC proteasome. The presence of poly-Gln repeats in trangenic models CC developed to replicate phenotypes of the spinocerebellar ataxia 1 CC disease (SCA1) impair ubiquitination and degradation, leading to CC accumulation of Atxn1 in neurons and subsequent toxicity. CC {ECO:0000269|PubMed:10624951}. CC -!- PTM: Sumoylation is dependent on nuclear localization and CC phosphorylation at Ser-751. {ECO:0000250|UniProtKB:P54253}. CC -!- POLYMORPHISM: The murine poly-Gln region is very limited in comparison CC to human ATXN1 and is not polymorphic. {ECO:0000269|PubMed:10624951, CC ECO:0000269|PubMed:12086639}. CC -!- DISRUPTION PHENOTYPE: Mice with conditional knockouts of either ATXN1- CC ATXN1L or CIC in the developing forebrain exhibit intellectual CC disability, hyperactivity, social-behavioral deficits and reduced CC thickness of upper cortical layers. {ECO:0000269|PubMed:28288114}. CC -!- MISCELLANEOUS: Different transgenic mouse, containing a poly-Gln region CC insertion in position 199 have been developed to replicate phenotypes CC of the spinocerebellar ataxia 1 disease (SCA1) in human CC (PubMed:10624951, PubMed:12086639). Heterozygous mice with a poly-Gln CC of 92 residues [92Q] develop the ataxia typical of human SCA1. However, CC they show only the phenotype associated with dysfunctional Purkinje CC cells and usually live a normal lifespan (PubMed:10624951). CC Heterozygous mice with a poly-Gln of 154 residues [154Q] develop a CC progressive neurological disorder that resembles human SCA1, with motor CC incoordination, cognitive deficits, wasting, and premature death, CC accompanied by Purkinje cell loss and age-related hippocampal synaptic CC dysfunction (PubMed:12086639). Phenotypes are caused by an accumulation CC of Atxn1 in neurons, exerting toxicity. The expanded poly-Gln tract CC causes stabilization of Atxn1 and impairs its ubiquitination and CC subsequent degradation, increasing its abundance in neurons CC (PubMed:10624951). {ECO:0000269|PubMed:10624951, CC ECO:0000269|PubMed:12086639, ECO:0000269|PubMed:25768905}. CC -!- SIMILARITY: Belongs to the ATXN1 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; X83542; CAA58533.1; -; mRNA. DR EMBL; AK048268; BAC33290.1; -; mRNA. DR EMBL; BC058178; AAH58178.1; -; mRNA. DR CCDS; CCDS26483.1; -. DR RefSeq; NP_001186233.1; NM_001199304.1. DR RefSeq; NP_001186234.1; NM_001199305.1. DR RefSeq; NP_033150.2; NM_009124.6. DR RefSeq; XP_011242683.1; XM_011244381.2. DR RefSeq; XP_011242685.1; XM_011244383.2. DR RefSeq; XP_011242687.1; XM_011244385.2. DR RefSeq; XP_011242688.1; XM_011244386.2. DR RefSeq; XP_011242689.1; XM_011244387.2. DR RefSeq; XP_011242690.1; XM_011244388.1. DR RefSeq; XP_011242691.1; XM_011244389.2. DR RefSeq; XP_011242692.1; XM_011244390.2. DR RefSeq; XP_011242693.1; XM_011244391.2. DR RefSeq; XP_011242694.1; XM_011244392.1. DR RefSeq; XP_011242695.1; XM_011244393.1. DR RefSeq; XP_017170951.1; XM_017315462.1. DR RefSeq; XP_017170952.1; XM_017315463.1. DR AlphaFoldDB; P54254; -. DR BMRB; P54254; -. DR SMR; P54254; -. DR BioGRID; 203083; 665. DR CORUM; P54254; -. DR DIP; DIP-6004N; -. DR IntAct; P54254; 4. DR STRING; 10090.ENSMUSP00000137439; -. DR GlyGen; P54254; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P54254; -. DR PhosphoSitePlus; P54254; -. DR EPD; P54254; -. DR jPOST; P54254; -. DR MaxQB; P54254; -. DR PaxDb; 10090-ENSMUSP00000137439; -. DR ProteomicsDB; 277204; -. DR Pumba; P54254; -. DR ABCD; P54254; 2 sequenced antibodies. DR Antibodypedia; 1922; 907 antibodies from 42 providers. DR DNASU; 20238; -. DR Ensembl; ENSMUST00000091628.11; ENSMUSP00000089217.4; ENSMUSG00000046876.17. DR Ensembl; ENSMUST00000167708.4; ENSMUSP00000129890.3; ENSMUSG00000046876.17. DR GeneID; 20238; -. DR KEGG; mmu:20238; -. DR UCSC; uc011yyv.2; mouse. DR AGR; MGI:104783; -. DR CTD; 6310; -. DR MGI; MGI:104783; Atxn1. DR VEuPathDB; HostDB:ENSMUSG00000046876; -. DR eggNOG; KOG4053; Eukaryota. DR GeneTree; ENSGT00390000005939; -. DR InParanoid; P54254; -. DR OMA; HHQGGTH; -. DR OrthoDB; 2882425at2759; -. DR PhylomeDB; P54254; -. DR BioGRID-ORCS; 20238; 6 hits in 77 CRISPR screens. DR ChiTaRS; Atxn1; mouse. DR PRO; PR:P54254; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; P54254; Protein. DR Bgee; ENSMUSG00000046876; Expressed in dorsal striatum and 222 other cell types or tissues. DR ExpressionAtlas; P54254; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0042405; C:nuclear inclusion body; IDA:MGI. DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0098794; C:postsynapse; IEA:GOC. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0034046; F:poly(G) binding; ISS:UniProtKB. DR GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB. DR GO; GO:0031208; F:POZ domain binding; IPI:MGI. DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:MGI. DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI. DR GO; GO:0007420; P:brain development; IMP:UniProtKB. DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI. DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI. DR GO; GO:0007612; P:learning; IMP:UniProtKB. DR GO; GO:0048286; P:lung alveolus development; IGI:MGI. DR GO; GO:0007613; P:memory; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IMP:MGI. DR GO; GO:0042326; P:negative regulation of phosphorylation; IMP:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0051168; P:nuclear export; ISS:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IMP:MGI. DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0035176; P:social behavior; IMP:UniProtKB. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0008542; P:visual learning; IMP:MGI. DR InterPro; IPR020997; Ataxin-1_N. DR InterPro; IPR043404; ATAXIN1-like. DR InterPro; IPR003652; Ataxin_AXH_dom. DR InterPro; IPR036096; Ataxin_AXH_dom_sf. DR PANTHER; PTHR13392; ATAXIN 1; 1. DR PANTHER; PTHR13392:SF5; ATAXIN-1; 1. DR Pfam; PF12547; ATXN-1_C; 1. DR Pfam; PF08517; AXH; 1. DR SMART; SM00536; AXH; 1. DR SUPFAM; SSF102031; AXH domain; 1. DR PROSITE; PS51148; AXH; 1. DR Genevisible; P54254; MM. PE 1: Evidence at protein level; KW Cytoplasm; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; RNA-binding; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..791 FT /note="Ataxin-1" FT /id="PRO_0000064752" FT DOMAIN 538..669 FT /note="AXH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00496" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 187..240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 298..402 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 470..580 FT /note="Self-association" FT /evidence="ECO:0000250|UniProtKB:P54253" FT REGION 514..791 FT /note="Interaction with USP7" FT /evidence="ECO:0000250|UniProtKB:P54253" FT REGION 516..742 FT /note="RNA-binding" FT /evidence="ECO:0000250|UniProtKB:P54253" FT REGION 736..774 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 770..773 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:9778246" FT COMPBIAS 219..235 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 345..389 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 741..766 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 213 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 218 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 751 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P54253" FT CROSSLNK 16 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250|UniProtKB:P54253" FT CROSSLNK 193 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250|UniProtKB:P54253" FT CROSSLNK 585 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250|UniProtKB:P54253" FT CROSSLNK 672 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250|UniProtKB:P54253" FT CROSSLNK 721 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250|UniProtKB:P54253" FT MUTAGEN 771 FT /note="K->T: Abolishes nuclear localization. Inhibits FT development of ataxia." FT /evidence="ECO:0000269|PubMed:9778246" FT CONFLICT 8 FT /note="S -> T (in Ref. 1; CAA58533)" FT /evidence="ECO:0000305" FT CONFLICT 77 FT /note="H -> L (in Ref. 1; CAA58533)" FT /evidence="ECO:0000305" FT CONFLICT 393..395 FT /note="HLG -> APR (in Ref. 1; CAA58533)" FT /evidence="ECO:0000305" FT CONFLICT 477 FT /note="T -> M (in Ref. 1; CAA58533)" FT /evidence="ECO:0000305" FT CONFLICT 519 FT /note="A -> S (in Ref. 1; CAA58533)" FT /evidence="ECO:0000305" FT CONFLICT 587 FT /note="D -> H (in Ref. 1; CAA58533)" FT /evidence="ECO:0000305" FT CONFLICT 687 FT /note="A -> V (in Ref. 1; CAA58533)" FT /evidence="ECO:0000305" FT CONFLICT 749 FT /note="R -> RR (in Ref. 1; CAA58533)" FT /evidence="ECO:0000305" SQ SEQUENCE 791 AA; 83793 MW; 1F87A5D65527D550 CRC64; MKSNQERSNE CLPPKKREIP ATSRPSEEKA TALPSDNHCV EGVAWLPSTP GIRGHGGGRH GSAGTSGEHG LQGMGLHKAL SAGLDYSPPS APRSVPTANT LPTVYPPPQS GTPVSPVQYA HLSHTFQFIG SSQYSGPYAG FIPSQLISPS GNPVTSAVAS AAGATTPSQR SQLEAYSTLL ANMGSLSQAP GHKVEPPPQQ HLSRAAGLVN PGSPPPPTQQ NQYIHISSSP QSSGRATSPP PIPVHLHPHQ TMIPHTLTLG PSSQVVVQYS DAGGHFVPRE STKKAESSRL QQAMQAKEVL NGEMEKSRRY GASSSVELSL GKASSKSVPH PYESRHVVVH PSPADYSSRD TSGVRGSVMV LPNSSTPSAD LEAQQTTHRE ASPSTLNDKS GLHLGKPGHR SYALSPHTVI QTTHSASEPL PVGLPATAFY AGTQPPVIGY LSGQQQAITY AGGLPQHLVI PGNQPLLIPV GSPDMDTPGA ASAIVTSSPQ FAAVPHTFVT TALPKSENFN PEALVTQAAY PAMVQAQIHL PVVQSVASPT TASPTLPPYF MKGSIIQLAN GELKKVEDLK TEDFIQSAEI SNDLKIDSST VERIEESHSP GVAVIQFAVG EHRAQVSVEV LVEYPFFVFG QGWSSCCPER TSQLFDLPCS KLSVGDVCIS LTLKNLKNGS VKKGQPVDPA SVLLKQAKTD SLAGSRHRYA EQENGINQGS AQVLSENGEL KFPEKIGLPA APFLSKIEPS KPTATRKRRW SAPETRKLEK SEDEPPLTLP KPSLIPQEVK ICIEGRSNVG K //