ID RERE_HUMAN Reviewed; 1566 AA. AC Q9P2R6; O43393; O75046; O75359; Q5VXL9; Q6P6B9; Q9Y2W4; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 27-MAR-2024, entry version 200. DE RecName: Full=Arginine-glutamic acid dipeptide repeats protein; DE AltName: Full=Atrophin-1-like protein; DE AltName: Full=Atrophin-1-related protein; GN Name=RERE; Synonyms=ARG, ARP, ATN1L, KIAA0458; 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 1), INTERACTION WITH ATN1, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=10814707; DOI=10.1093/hmg/9.9.1433; RA Yanagisawa H., Bundo M., Miyashita T., Okamura-Oho Y., Tadokoro K., RA Tokunaga K., Yamada M.; RT "Protein binding of a DRPLA family through arginine-glutamic acid dipeptide RT repeats is enhanced by extended polyglutamine."; RL Hum. Mol. Genet. 9:1433-1442(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RX PubMed=11331249; RA Waerner T., Gardellin P., Pfizenmaier K., Weith A., Kraut N.; RT "Human RERE is localized to nuclear promyelocytic leukemia oncogenic RT domains and enhances apoptosis."; RL Cell Growth Differ. 12:201-210(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2). RA Xia J.-H., Liu C.-Y., Ruan Q.-G., Wang D.-A., Deng H.-X.; RT "Cloning and localization of human atrophin-1 (DRPLA) related gene."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-1566 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9455484; DOI=10.1093/dnares/4.5.345; RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RT "Characterization of cDNA clones in size-fractionated cDNA libraries from RT human brain."; RL DNA Res. 4:345-349(1997). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 555-1566, TISSUE SPECIFICITY, AND CHROMOSOMAL RP TRANSLOCATION. RX PubMed=10729226; DOI=10.1006/geno.1999.6097; RA Amler L.C., Bauer A., Corvi R., Dihlmann S., Praml C., Cavenee W.K., RA Schwab M., Hampton G.M.; RT "Identification and characterization of novel genes located at the RT t(1;15)(p36.2;q24) translocation breakpoint in the neuroblastoma cell line RT NGP."; RL Genomics 64:195-202(2000). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-1106, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56 AND SER-642, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP INTERACTION WITH FAT1. RX PubMed=19131340; DOI=10.1074/jbc.m809333200; RA Hou R., Sibinga N.E.; RT "Atrophin proteins interact with the Fat1 cadherin and regulate migration RT and orientation in vascular smooth muscle cells."; RL J. Biol. Chem. 284:6955-6965(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675 AND SER-679, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-56; SER-642; SER-656; RP SER-675; SER-679 AND SER-1106, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120; SER-594; SER-600; RP SER-675; SER-679 AND SER-1266, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-613; SER-1106; RP SER-1113; THR-1119 AND TYR-1259, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-637, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [16] RP INVOLVEMENT IN NEDBEH, VARIANTS NEDBEH ILE-471; ARG-1156; ARG-1262 AND RP GLN-1431, AND CHARACTERIZATION OF VARIANT NEDBEH ARG-1156. RX PubMed=27087320; DOI=10.1016/j.ajhg.2016.03.002; RA Fregeau B., Kim B.J., Hernandez-Garcia A., Jordan V.K., Cho M.T., RA Schnur R.E., Monaghan K.G., Juusola J., Rosenfeld J.A., Bhoj E., RA Zackai E.H., Sacharow S., Baranano K., Bosch D.G., de Vries B.B., RA Lindstrom K., Schroeder A., James P., Kulch P., Lalani S.R., RA van Haelst M.M., van Gassen K.L., van Binsbergen E., Barkovich A.J., RA Scott D.A., Sherr E.H.; RT "De novo mutations of RERE cause a genetic syndrome with features that RT overlap those associated with proximal 1p36 deletions."; RL Am. J. Hum. Genet. 98:963-970(2016). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-560 AND LYS-637, AND RP IDENTIFICATION BY MASS 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). RN [18] RP STRUCTURE BY NMR OF 392-446. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SANT domain in arginine-glutamic acid dipeptide RT (RE) repeats."; RL Submitted (OCT-2007) to the PDB data bank. CC -!- FUNCTION: Plays a role as a transcriptional repressor during CC development. May play a role in the control of cell survival. CC Overexpression of RERE recruits BAX to the nucleus particularly to POD CC and triggers caspase-3 activation, leading to cell death. CC {ECO:0000269|PubMed:11331249}. CC -!- SUBUNIT: Interacts with HDAC1 (By similarity). Interacts with ATN1. CC Interaction with ATN1 is improved when the poly-Gln region of ATN1 is CC extended. Interacts with FAT1. {ECO:0000250, CC ECO:0000269|PubMed:10814707, ECO:0000269|PubMed:19131340}. CC -!- INTERACTION: CC Q9P2R6; P54259: ATN1; NbExp=3; IntAct=EBI-948076, EBI-945980; CC Q9P2R6; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-948076, EBI-744556; CC Q9P2R6; Q96KQ7: EHMT2; NbExp=3; IntAct=EBI-948076, EBI-744366; CC Q9P2R6; P60329: KRTAP12-4; NbExp=3; IntAct=EBI-948076, EBI-10176396; CC Q9P2R6; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-948076, EBI-11962084; CC Q9P2R6; P09234: SNRPC; NbExp=3; IntAct=EBI-948076, EBI-766589; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:10814707, CC ECO:0000269|PubMed:11331249}. Note=Localized in nuclear bodies of CC variables size. Colocalized with PML and BAX in nuclear PODs. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q9P2R6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P2R6-2; Sequence=VSP_016878; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in tumor cell lines. CC {ECO:0000269|PubMed:10729226, ECO:0000269|PubMed:10814707, CC ECO:0000269|PubMed:11331249}. CC -!- DOMAIN: The interaction with ATN1 is mediated by the coiled coil CC domain. CC -!- DISEASE: Note=A chromosomal aberration involving RERE is found in the CC neuroblastoma cell line NGP. Translocation t(1;15)(p36.2;q24). CC -!- DISEASE: Neurodevelopmental disorder with or without anomalies of the CC brain, eye, or heart (NEDBEH) [MIM:616975]: An autosomal dominant CC syndrome characterized by developmental delay, intellectual disability, CC brain anomalies, and neurological abnormalities including seizures, CC hypotonia, and behavioral problems such as autism spectrum disorders. CC Brain anomalies include abnormalities and/or thinning of the corpus CC callosum, diminished white matter volume, abnormal cerebellar vermis, CC and ventriculomegaly. Congenital defects of the eye, heart and CC genitourinary system are present in half of the patients. CC {ECO:0000269|PubMed:27087320}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAC31120.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAD27584.1; Type=Erroneous initiation; Evidence={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; AB036737; BAA95898.1; -; mRNA. DR EMBL; AF016005; AAC31120.1; ALT_FRAME; mRNA. DR EMBL; AF041104; AAC28264.1; -; Genomic_DNA. DR EMBL; AF041096; AAC28264.1; JOINED; Genomic_DNA. DR EMBL; AF041097; AAC28264.1; JOINED; Genomic_DNA. DR EMBL; AF041098; AAC28264.1; JOINED; Genomic_DNA. DR EMBL; AF041099; AAC28264.1; JOINED; Genomic_DNA. DR EMBL; AF041100; AAC28264.1; JOINED; Genomic_DNA. DR EMBL; AF041101; AAC28264.1; JOINED; Genomic_DNA. DR EMBL; AF041102; AAC28264.1; JOINED; Genomic_DNA. DR EMBL; AF041103; AAC28264.1; JOINED; Genomic_DNA. DR EMBL; AL356072; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL357713; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL096855; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB007927; BAA32303.3; -; mRNA. DR EMBL; AF118275; AAD27584.1; ALT_INIT; mRNA. DR CCDS; CCDS41243.1; -. [Q9P2R6-2] DR CCDS; CCDS95.1; -. [Q9P2R6-1] DR RefSeq; NP_001036146.1; NM_001042681.1. [Q9P2R6-1] DR RefSeq; NP_001036147.1; NM_001042682.1. [Q9P2R6-2] DR RefSeq; NP_036234.3; NM_012102.3. [Q9P2R6-1] DR RefSeq; XP_005263521.1; XM_005263464.2. DR RefSeq; XP_016856847.1; XM_017001358.1. DR RefSeq; XP_016856848.1; XM_017001359.1. DR PDB; 2YQK; NMR; -; A=392-441. DR PDBsum; 2YQK; -. DR AlphaFoldDB; Q9P2R6; -. DR SMR; Q9P2R6; -. DR BioGRID; 106963; 87. DR DIP; DIP-47606N; -. DR IntAct; Q9P2R6; 38. DR MINT; Q9P2R6; -. DR STRING; 9606.ENSP00000338629; -. DR CarbonylDB; Q9P2R6; -. DR GlyCosmos; Q9P2R6; 3 sites, 2 glycans. DR GlyGen; Q9P2R6; 7 sites, 2 O-linked glycans (7 sites). DR iPTMnet; Q9P2R6; -. DR PhosphoSitePlus; Q9P2R6; -. DR BioMuta; RERE; -. DR DMDM; 85540730; -. DR EPD; Q9P2R6; -. DR jPOST; Q9P2R6; -. DR MassIVE; Q9P2R6; -. DR MaxQB; Q9P2R6; -. DR PaxDb; 9606-ENSP00000338629; -. DR PeptideAtlas; Q9P2R6; -. DR ProteomicsDB; 83883; -. [Q9P2R6-1] DR ProteomicsDB; 83884; -. [Q9P2R6-2] DR Pumba; Q9P2R6; -. DR Antibodypedia; 13215; 182 antibodies from 24 providers. DR DNASU; 473; -. DR Ensembl; ENST00000337907.7; ENSP00000338629.3; ENSG00000142599.20. [Q9P2R6-1] DR Ensembl; ENST00000400908.7; ENSP00000383700.2; ENSG00000142599.20. [Q9P2R6-1] DR Ensembl; ENST00000465125.2; ENSP00000515651.1; ENSG00000142599.20. [Q9P2R6-2] DR Ensembl; ENST00000476556.5; ENSP00000422246.1; ENSG00000142599.20. [Q9P2R6-2] DR GeneID; 473; -. DR KEGG; hsa:473; -. DR MANE-Select; ENST00000400908.7; ENSP00000383700.2; NM_001042681.2; NP_001036146.1. DR UCSC; uc001apd.4; human. [Q9P2R6-1] DR AGR; HGNC:9965; -. DR CTD; 473; -. DR DisGeNET; 473; -. DR GeneCards; RERE; -. DR GeneReviews; RERE; -. DR HGNC; HGNC:9965; RERE. DR HPA; ENSG00000142599; Low tissue specificity. DR MalaCards; RERE; -. DR MIM; 605226; gene. DR MIM; 616975; phenotype. DR neXtProt; NX_Q9P2R6; -. DR OpenTargets; ENSG00000142599; -. DR Orphanet; 1606; 1p36 deletion syndrome. DR Orphanet; 494344; RERE-related neurodevelopmental syndrome. DR PharmGKB; PA34332; -. DR VEuPathDB; HostDB:ENSG00000142599; -. DR eggNOG; KOG2133; Eukaryota. DR GeneTree; ENSGT00940000153615; -. DR HOGENOM; CLU_005292_1_0_1; -. DR InParanoid; Q9P2R6; -. DR OMA; VMYLRAA; -. DR OrthoDB; 3349425at2759; -. DR PhylomeDB; Q9P2R6; -. DR TreeFam; TF328554; -. DR PathwayCommons; Q9P2R6; -. DR SignaLink; Q9P2R6; -. DR SIGNOR; Q9P2R6; -. DR BioGRID-ORCS; 473; 42 hits in 1187 CRISPR screens. DR ChiTaRS; RERE; human. DR EvolutionaryTrace; Q9P2R6; -. DR GeneWiki; RERE; -. DR GenomeRNAi; 473; -. DR Pharos; Q9P2R6; Tbio. DR PRO; PR:Q9P2R6; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9P2R6; Protein. DR Bgee; ENSG00000142599; Expressed in sural nerve and 207 other cell types or tissues. DR ExpressionAtlas; Q9P2R6; baseline and differential. DR GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:GO_Central. DR GO; GO:0003682; F:chromatin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl. DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central. DR GO; GO:0048755; P:branching morphogenesis of a nerve; IEA:Ensembl. DR GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IEA:Ensembl. DR GO; GO:0021691; P:cerebellar Purkinje cell layer maturation; IEA:Ensembl. DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl. DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl. DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IEA:Ensembl. DR CDD; cd04709; BAH_MTA; 1. DR CDD; cd11661; SANT_MTA3_like; 1. DR CDD; cd00202; ZnF_GATA; 1. DR Gene3D; 2.30.30.490; -; 1. DR Gene3D; 4.10.1240.50; -; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR002951; Atrophin-like. DR InterPro; IPR001025; BAH_dom. DR InterPro; IPR043151; BAH_sf. DR InterPro; IPR000949; ELM2_dom. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR001005; SANT/Myb. DR InterPro; IPR017884; SANT_dom. DR InterPro; IPR000679; Znf_GATA. DR PANTHER; PTHR13859:SF12; ARGININE-GLUTAMIC ACID DIPEPTIDE REPEATS PROTEIN; 1. DR PANTHER; PTHR13859; ATROPHIN-RELATED; 1. DR Pfam; PF03154; Atrophin-1; 1. DR Pfam; PF01426; BAH; 1. DR Pfam; PF01448; ELM2; 1. DR Pfam; PF00320; GATA; 1. DR SMART; SM00439; BAH; 1. DR SMART; SM01189; ELM2; 1. DR SMART; SM00717; SANT; 1. DR SMART; SM00401; ZnF_GATA; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS51038; BAH; 1. DR PROSITE; PS51156; ELM2; 1. DR PROSITE; PS51293; SANT; 1. DR Genevisible; Q9P2R6; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement; KW Coiled coil; Developmental protein; Disease variant; KW Intellectual disability; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..1566 FT /note="Arginine-glutamic acid dipeptide repeats protein" FT /id="PRO_0000083504" FT DOMAIN 103..283 FT /note="BAH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370" FT DOMAIN 284..387 FT /note="ELM2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512" FT DOMAIN 391..443 FT /note="SANT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT ZN_FING 507..532 FT /note="GATA-type" FT REGION 1..90 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 464..495 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 542..1133 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1162..1246 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1156..1211 FT /evidence="ECO:0000255" FT COMPBIAS 1..38 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 50..75 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 464..486 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 556..571 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 596..626 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 627..670 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 671..687 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 688..707 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 708..748 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 749..773 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 774..796 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 807..829 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 876..912 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 913..949 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 980..1065 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1162..1210 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 53 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 56 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 120 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 142 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80TZ9" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:24275569" FT MOD_RES 594 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 600 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 613 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 642 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 656 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 675 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 679 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1106 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 1113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1115 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80TZ9" FT MOD_RES 1119 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1158 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q80TZ9" FT MOD_RES 1259 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 560 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 637 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..554 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_016878" FT VARIANT 471 FT /note="V -> I (in NEDBEH; uncertain significance; FT dbSNP:rs765016528)" FT /evidence="ECO:0000269|PubMed:27087320" FT /id="VAR_077007" FT VARIANT 1156 FT /note="G -> R (in NEDBEH; uncertain significance; FT dbSNP:rs766951273)" FT /evidence="ECO:0000269|PubMed:27087320" FT /id="VAR_077008" FT VARIANT 1262 FT /note="P -> R (in NEDBEH; uncertain significance; FT dbSNP:rs878853270)" FT /evidence="ECO:0000269|PubMed:27087320" FT /id="VAR_077009" FT VARIANT 1431 FT /note="H -> Q (in NEDBEH; uncertain significance; FT dbSNP:rs869312871)" FT /evidence="ECO:0000269|PubMed:27087320" FT /id="VAR_077010" FT CONFLICT 65 FT /note="S -> G (in Ref. 1; BAA95898)" FT /evidence="ECO:0000305" FT CONFLICT 68 FT /note="A -> T (in Ref. 1; BAA95898)" FT /evidence="ECO:0000305" FT CONFLICT 114..115 FT /note="ES -> VC (in Ref. 1; BAA95898)" FT /evidence="ECO:0000305" FT CONFLICT 643 FT /note="P -> L (in Ref. 3; AAC31120)" FT /evidence="ECO:0000305" FT CONFLICT 921 FT /note="A -> G (in Ref. 1; BAA95898)" FT /evidence="ECO:0000305" FT CONFLICT 940 FT /note="P -> A (in Ref. 1; BAA95898)" FT /evidence="ECO:0000305" FT CONFLICT 957 FT /note="F -> L (in Ref. 6; AAD27584)" FT /evidence="ECO:0000305" FT CONFLICT 977 FT /note="T -> K (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 984 FT /note="H -> N (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 1009..1011 FT /note="QSQ -> RTR (in Ref. 6; AAD27584)" FT /evidence="ECO:0000305" FT CONFLICT 1117 FT /note="E -> D (in Ref. 6; AAD27584)" FT /evidence="ECO:0000305" FT CONFLICT 1272 FT /note="H -> Q (in Ref. 6; AAD27584)" FT /evidence="ECO:0000305" FT CONFLICT 1489..1490 FT /note="ML -> IV (in Ref. 1; BAA95898)" FT /evidence="ECO:0000305" FT CONFLICT 1529 FT /note="R -> K (in Ref. 6; AAD27584)" FT /evidence="ECO:0000305" FT CONFLICT 1536 FT /note="W -> C (in Ref. 6; AAD27584)" FT /evidence="ECO:0000305" FT CONFLICT 1543 FT /note="M -> R (in Ref. 6; AAD27584)" FT /evidence="ECO:0000305" FT HELIX 398..410 FT /evidence="ECO:0007829|PDB:2YQK" FT HELIX 415..421 FT /evidence="ECO:0007829|PDB:2YQK" FT HELIX 428..439 FT /evidence="ECO:0007829|PDB:2YQK" SQ SEQUENCE 1566 AA; 172424 MW; ECA4A22026E3E96F CRC64; MTADKDKDKD KEKDRDRDRD REREKRDKAR ESENSRPRRS CTLEGGAKNY AESDHSEDED NDNNSATAEE STKKNKKKPP KKKSRYERTD TGEITSYITE DDVVYRPGDC VYIESRRPNT PYFICSIQDF KLVHNSQACC RSPTPALCDP PACSLPVASQ PPQHLSEAGR GPVGSKRDHL LMNVKWYYRQ SEVPDSVYQH LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA LRGKCNISHF SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ PFPSPDGDTV TQHEELVWMP GVNDCDLLMY LRAARSMAAF AGMCDGGSTE DGCVAASRDD TTLNALNTLH ESGYDAGKAL QRLVKKPVPK LIEKCWTEDE VKRFVKGLRQ YGKNFFRIRK ELLPNKETGE LITFYYYWKK TPEAASSRAH RRHRRQAVFR RIKTRTASTP VNTPSRPPSS EFLDLSSASE DDFDSEDSEQ ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG ELPPIEKPVD PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPASPDGRTS PINEDIRSSG RNSPSAASTS SNDSKAETVK KSAKKVKEEA SSPLKSNKRQ REKVASDTEE ADRTSSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD PKDIDQDNRS TSPSIPSPQD NESDSDSSAQ QQMLQAQPPA LQAPTGVTPA PSSAPPGTPQ LPTPGPTPSA TAVPPQGSPT ASQAPNQPQA PTAPVPHTHI QQAPALHPQR PPSPHPPPHP SPHPPLQPLT GSAGQPSAPS HAQPPLHGQG PPGPHSLQAG PLLQHPGPPQ PFGLPPQASQ GQAPLGTSPA AAYPHTSLQL PASQSALQSQ QPPREQPLPP APLAMPHIKP PPTTPIPQLP APQAHKHPPH LSGPSPFSMN ANLPPPPALK PLSSLSTHHP PSAHPPPLQL MPQSQPLPSS PAQPPGLTQS QNLPPPPASH PPTGLHQVAP QPPFAQHPFV PGGPPPITPP TCPSTSTPPA GPGTSAQPPC SGAAASGGSI AGGSSCPLPT VQIKEEALDD AEEPESPPPP PRSPSPEPTV VDTPSHASQS ARFYKHLDRG YNSCARTDLY FMPLAGSKLA KKREEAIEKA KREAEQKARE EREREKEKEK ERERERERER EAERAAKASS SAHEGRLSDP QLSGPGHMRP SFEPPPTTIA AVPPYIGPDT PALRTLSEYA RPHVMSPTNR NHPFYMPLNP TDPLLAYHMP GLYNVDPTIR ERELREREIR EREIRERELR ERMKPGFEVK PPELDPLHPA ANPMEHFARH SALTIPPTAG PHPFASFHPG LNPLERERLA LAGPQLRPEM SYPDRLAAER IHAERMASLT SDPLARLQMF NVTPHHHQHS HIHSHLHLHQ QDPLHQGSAG PVHPLVDPLT AGPHLARFPY PPGTLPNPLL GQPPHEHEML RHPVFGTPYP RDLPGAIPPP MSAAHQLQAM HAQSAELQRL AMEQQWLHGH PHMHGGHLPS QEDYYSRLKK EGDKQL //