ATX1_MOUSE
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 03-AUG-2022, entry version 173.
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 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; 662.
DR CORUM; P54254; -.
DR DIP; DIP-6004N; -.
DR IntAct; P54254; 4.
DR STRING; 10090.ENSMUSP00000137439; -.
DR iPTMnet; P54254; -.
DR PhosphoSitePlus; P54254; -.
DR EPD; P54254; -.
DR jPOST; P54254; -.
DR MaxQB; P54254; -.
DR PaxDb; P54254; -.
DR PRIDE; P54254; -.
DR ProteomicsDB; 277204; -.
DR ABCD; P54254; 2 sequenced antibodies.
DR Antibodypedia; 1922; 857 antibodies from 42 providers.
DR DNASU; 20238; -.
DR Ensembl; ENSMUST00000091628; ENSMUSP00000089217; ENSMUSG00000046876.
DR Ensembl; ENSMUST00000167708; ENSMUSP00000129890; ENSMUSG00000046876.
DR GeneID; 20238; -.
DR KEGG; mmu:20238; -.
DR UCSC; uc011yyv.2; mouse.
DR CTD; 6310; -.
DR MGI; MGI:104783; Atxn1.
DR VEuPathDB; HostDB:ENSMUSG00000046876; -.
DR eggNOG; KOG4053; Eukaryota.
DR GeneTree; ENSGT00390000005939; -.
DR InParanoid; P54254; -.
DR OMA; ENHRADN; -.
DR OrthoDB; 249631at2759; -.
DR PhylomeDB; P54254; -.
DR BioGRID-ORCS; 20238; 6 hits in 72 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 219 other tissues.
DR ExpressionAtlas; P54254; baseline and differential.
DR Genevisible; P54254; MM.
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:0008022; F:protein C-terminus binding; ISS:UniProtKB.
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:0048856; P:anatomical structure development; IBA:GO_Central.
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: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:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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 InterPro; IPR040172; ATXN1.
DR PANTHER; PTHR13392; PTHR13392; 1.
DR PANTHER; PTHR13392:SF5; PTHR13392:SF5; 1.
DR Pfam; PF12547; ATXN-1_C; 1.
DR Pfam; PF08517; AXH; 1.
DR SMART; SM00536; AXH; 1.
DR SUPFAM; SSF102031; SSF102031; 1.
DR PROSITE; PS51148; AXH; 1.
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
