RERE_HUMAN
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 03-AUG-2022, entry version 191.
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};
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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; 81.
DR DIP; DIP-47606N; -.
DR IntAct; Q9P2R6; 37.
DR MINT; Q9P2R6; -.
DR STRING; 9606.ENSP00000338629; -.
DR CarbonylDB; Q9P2R6; -.
DR GlyGen; Q9P2R6; 3 sites, 2 O-linked glycans (3 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; Q9P2R6; -.
DR PeptideAtlas; Q9P2R6; -.
DR PRIDE; Q9P2R6; -.
DR ProteomicsDB; 83883; -. [Q9P2R6-1]
DR ProteomicsDB; 83884; -. [Q9P2R6-2]
DR Antibodypedia; 13215; 162 antibodies from 24 providers.
DR DNASU; 473; -.
DR Ensembl; ENST00000337907.7; ENSP00000338629.3; ENSG00000142599.19. [Q9P2R6-1]
DR Ensembl; ENST00000400908.7; ENSP00000383700.2; ENSG00000142599.19. [Q9P2R6-1]
DR Ensembl; ENST00000476556.5; ENSP00000422246.1; ENSG00000142599.19. [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 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; HAYPGYA; -.
DR PhylomeDB; Q9P2R6; -.
DR TreeFam; TF328554; -.
DR PathwayCommons; Q9P2R6; -.
DR SignaLink; Q9P2R6; -.
DR SIGNOR; Q9P2R6; -.
DR BioGRID-ORCS; 473; 27 hits in 1104 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 205 other tissues.
DR ExpressionAtlas; Q9P2R6; baseline and differential.
DR Genevisible; Q9P2R6; HS.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
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; cd00202; ZnF_GATA; 1.
DR Gene3D; 2.30.30.490; -; 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 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; SSF46689; SSF46689; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
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; unknown pathological
FT significance; dbSNP:rs765016528)"
FT /evidence="ECO:0000269|PubMed:27087320"
FT /id="VAR_077007"
FT VARIANT 1156
FT /note="G -> R (in NEDBEH; unknown pathological
FT significance; dbSNP:rs766951273)"
FT /evidence="ECO:0000269|PubMed:27087320"
FT /id="VAR_077008"
FT VARIANT 1262
FT /note="P -> R (in NEDBEH; unknown pathological
FT significance; dbSNP:rs878853270)"
FT /evidence="ECO:0000269|PubMed:27087320"
FT /id="VAR_077009"
FT VARIANT 1431
FT /note="H -> Q (in NEDBEH; unknown pathological
FT significance; 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
