RCOR1_HUMAN
ID RCOR1_HUMAN Reviewed; 485 AA.
AC Q9UKL0; J3KN32; Q15044; Q6P2I9; Q86VG5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=REST corepressor 1;
DE AltName: Full=Protein CoREST;
GN Name=RCOR1; Synonyms=KIAA0071, RCOR;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-298.
RC TISSUE=Lymph;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 4-485, INTERACTION WITH REST, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=10449787; DOI=10.1073/pnas.96.17.9873;
RA Andres M.E., Burger C., Peral-Rubio M.J., Battaglioli E., Anderson M.E.,
RA Grimes J., Dallman J., Ballas N., Mandel G.;
RT "CoREST: a functional corepressor required for regulation of neural-
RT specific gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9873-9878(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-485.
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH REST.
RX PubMed=10734093; DOI=10.1074/jbc.275.13.9461;
RA Grimes J.A., Nielsen S.J., Battaglioli E., Miska E.A., Speh J.C.,
RA Berry D.L., Atouf F., Holdener B.C., Mandel G., Kouzarides T.;
RT "The co-repressor mSin3A is a functional component of the REST-CoREST
RT repressor complex.";
RL J. Biol. Chem. 275:9461-9467(2000).
RN [7]
RP FUNCTION, AND INTERACTION WITH HDAC1 AND HDAC2.
RX PubMed=11516394; DOI=10.1016/s0896-6273(01)00371-3;
RA Ballas N., Battaglioli E., Atouf F., Andres M.E., Chenoweth J.,
RA Anderson M.E., Burger C., Moniwa M., Davie J.R., Bowers W.J.,
RA Federoff H.J., Rose D.W., Rosenfeld M.G., Brehm P., Mandel G.;
RT "Regulation of neuronal traits by a novel transcriptional complex.";
RL Neuron 31:353-365(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE BHC COMPLEX
RP WITH HDAC1 AND KDM1A.
RX PubMed=11102443; DOI=10.1074/jbc.m007372200;
RA Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
RA Howard B.H.;
RT "Stable histone deacetylase complexes distinguished by the presence of SANT
RT domain proteins CoREST/kiaa0071 and Mta-L1.";
RL J. Biol. Chem. 276:6817-6824(2001).
RN [9]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP BHC COMPLEX WITH HDAC1; HDAC2 AND KDM1A.
RX PubMed=11171972; DOI=10.1073/pnas.98.4.1454;
RA You A., Tong J.K., Grozinger C.M., Schreiber S.L.;
RT "CoREST is an integral component of the CoREST-human histone deacetylase
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1454-1458(2001).
RN [10]
RP INTERACTION WITH SMARCE1.
RX PubMed=12192000; DOI=10.1074/jbc.m205691200;
RA Battaglioli E., Andres M.E., Rose D.W., Chenoweth J.G., Rosenfeld M.G.,
RA Anderson M.E., Mandel G.;
RT "REST repression of neuronal genes requires components of the hSWI.SNF
RT complex.";
RL J. Biol. Chem. 277:41038-41045(2002).
RN [11]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; KDM1A AND PHF21A.
RX PubMed=12032298; DOI=10.1073/pnas.112008599;
RA Hakimi M.-A., Bochar D.A., Chenoweth J., Lane W.S., Mandel G.,
RA Shiekhattar R.;
RT "A core-BRAF35 complex containing histone deacetylase mediates repression
RT of neuronal-specific genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7420-7425(2002).
RN [12]
RP FUNCTION.
RX PubMed=12399542; DOI=10.1126/science.1076469;
RA Lunyak V.V., Burgess R., Prefontaine G.G., Nelson C., Sze S.-H.,
RA Chenoweth J., Schwartz P., Pevzner P.A., Glass C., Mandel G.,
RA Rosenfeld M.G.;
RT "Corepressor-dependent silencing of chromosomal regions encoding neuronal
RT genes.";
RL Science 298:1747-1752(2002).
RN [13]
RP ERRATUM OF PUBMED:12399542.
RA Lunyak V.V., Burgess R., Prefontaine G.G., Nelson C., Sze S.-H.,
RA Chenoweth J., Schwartz P., Pevzner P.A., Glass C., Mandel G.,
RA Rosenfeld M.G.;
RL Science 299:1663-1663(2003).
RN [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP BHC COMPLEX WITH GSE1; GTF2I; HDAC1; HDAC2; HMG20B; KDM1A; PHF21A; ZMYM2;
RP ZMYM3 AND ZNF217.
RX PubMed=12493763; DOI=10.1074/jbc.m208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [15]
RP FUNCTION, DOMAIN, AND INTERACTION WITH KDM1A.
RX PubMed=16140033; DOI=10.1016/j.molcel.2005.08.027;
RA Shi Y.-J., Matson C., Lan F., Iwase S., Baba T., Shi Y.;
RT "Regulation of LSD1 histone demethylase activity by its associated
RT factors.";
RL Mol. Cell 19:857-864(2005).
RN [16]
RP FUNCTION, AND INTERACTION WITH KDM1A.
RX PubMed=16079794; DOI=10.1038/nature04021;
RA Lee M.G., Wynder C., Cooch N., Shiekhattar R.;
RT "An essential role for CoREST in nucleosomal histone 3 lysine 4
RT demethylation.";
RL Nature 437:432-435(2005).
RN [17]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH HSV-1 ICP0
RP (MICROBIAL INFECTION).
RX PubMed=15897453; DOI=10.1073/pnas.0502658102;
RA Gu H., Liang Y., Mandel G., Roizman B.;
RT "Components of the REST/CoREST/histone deacetylase repressor complex are
RT disrupted, modified, and translocated in HSV-1-infected cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7571-7576(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-260, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-260, AND
RP IDENTIFICATION BY 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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-260 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122; LYS-297 AND LYS-466, 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 [27]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 289-485 IN COMPLEX WITH KDM1A.
RX PubMed=16885027; DOI=10.1016/j.molcel.2006.07.012;
RA Yang M., Gocke C.B., Luo X., Borek D., Tomchick D.R., Machius M.,
RA Otwinowski Z., Yu H.;
RT "Structural basis for CoREST-dependent demethylation of nucleosomes by the
RT human LSD1 histone demethylase.";
RL Mol. Cell 23:377-387(2006).
CC -!- FUNCTION: Essential component of the BHC complex, a corepressor complex
CC that represses transcription of neuron-specific genes in non-neuronal
CC cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts
CC by deacetylating and demethylating specific sites on histones, thereby
CC acting as a chromatin modifier. In the BHC complex, it serves as a
CC molecular beacon for the recruitment of molecular machinery, including
CC MeCP2 and SUV39H1, that imposes silencing across a chromosomal
CC interval. Plays a central role in demethylation of Lys-4 of histone H3
CC by promoting demethylase activity of KDM1A on core histones and
CC nucleosomal substrates. It also protects KDM1A from the proteasome.
CC Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone
CC deacetylase (HDAC) recruitment, a number of genes implicated in
CC multilineage blood cell development and controls hematopoietic
CC differentiation. {ECO:0000269|PubMed:11171972,
CC ECO:0000269|PubMed:11516394, ECO:0000269|PubMed:12032298,
CC ECO:0000269|PubMed:12399542, ECO:0000269|PubMed:12493763,
CC ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16140033}.
CC -!- SUBUNIT: Interacts directly with GFI1 and GFI1B in a
CC RCOR/GFI/KDM1A/HDAC complex. Interacts with INMS1 (By similarity).
CC Component of a BHC histone deacetylase complex that contains HDAC1,
CC HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC
CC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC Interacts with REST. Interacts with the SMARCE1/BAF57, suggesting that
CC the BHC complex may recruit the ATP-dependent chromatin-remodeling SWI-
CC SNF complex. {ECO:0000250, ECO:0000269|PubMed:10449787,
CC ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:11102443,
CC ECO:0000269|PubMed:11171972, ECO:0000269|PubMed:11516394,
CC ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:12192000,
CC ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:16079794,
CC ECO:0000269|PubMed:16140033, ECO:0000269|PubMed:16885027}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus HSV-1 ICP0
CC protein; the interaction leads to the disruption of the BHC complex,
CC thereby preventing the BHC complex from repressing transcription of
CC viral genes. {ECO:0000269|PubMed:15897453}.
CC -!- INTERACTION:
CC Q9UKL0; Q13547: HDAC1; NbExp=11; IntAct=EBI-926563, EBI-301834;
CC Q9UKL0; O60341: KDM1A; NbExp=7; IntAct=EBI-926563, EBI-710124;
CC Q9UKL0; O60341-1: KDM1A; NbExp=6; IntAct=EBI-926563, EBI-15599570;
CC Q9UKL0; Q969G3-1: SMARCE1; NbExp=2; IntAct=EBI-926563, EBI-455091;
CC Q9UKL0; Q969G3-2: SMARCE1; NbExp=4; IntAct=EBI-926563, EBI-455096;
CC Q9UKL0; Q92618: ZNF516; NbExp=6; IntAct=EBI-926563, EBI-2799490;
CC Q9UKL0; P08393: ICP0; Xeno; NbExp=2; IntAct=EBI-926563, EBI-6148881;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:10734093,
CC ECO:0000269|PubMed:15897453}. Note=Upon infection by HSV-1, it is
CC partially translocated into the cytoplasm in an HSV-1-dependent manner.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10449787}.
CC -!- DOMAIN: The SANT domains may bridge the nucleosomal substrates and the
CC demethylase KDM1A. {ECO:0000269|PubMed:16140033}.
CC -!- PTM: Phosphorylated by HSV-1 protein kinases in case of infection.
CC {ECO:0000269|PubMed:15897453}.
CC -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51003.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH64495.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH64495.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AL132801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81793.1; -; Genomic_DNA.
DR EMBL; BC051003; AAH51003.1; ALT_INIT; mRNA.
DR EMBL; BC064495; AAH64495.1; ALT_SEQ; mRNA.
DR EMBL; AF155595; AAF01498.1; -; mRNA.
DR EMBL; D31888; BAA06686.1; -; mRNA.
DR CCDS; CCDS9974.2; -.
DR RefSeq; NP_055971.2; NM_015156.3.
DR PDB; 2IW5; X-ray; 2.57 A; B=289-485.
DR PDB; 2UXN; X-ray; 2.72 A; B=289-485.
DR PDB; 2UXX; X-ray; 2.74 A; B=289-485.
DR PDB; 2V1D; X-ray; 3.10 A; B=308-485.
DR PDB; 2X0L; X-ray; 3.00 A; B=311-443.
DR PDB; 2XAF; X-ray; 3.25 A; B=4-485.
DR PDB; 2XAG; X-ray; 3.10 A; B=4-485.
DR PDB; 2XAH; X-ray; 3.10 A; B=4-485.
DR PDB; 2XAJ; X-ray; 3.30 A; B=4-485.
DR PDB; 2XAQ; X-ray; 3.20 A; B=4-485.
DR PDB; 2XAS; X-ray; 3.20 A; B=4-485.
DR PDB; 2Y48; X-ray; 3.00 A; B=308-485.
DR PDB; 3ZMS; X-ray; 2.96 A; B=4-485.
DR PDB; 3ZMT; X-ray; 3.10 A; B=4-485.
DR PDB; 3ZMU; X-ray; 3.20 A; B=4-485.
DR PDB; 3ZMV; X-ray; 3.00 A; B=4-485.
DR PDB; 3ZMZ; X-ray; 3.00 A; B=4-485.
DR PDB; 3ZN0; X-ray; 2.80 A; B=4-485.
DR PDB; 3ZN1; X-ray; 3.10 A; B=4-485.
DR PDB; 4BAY; X-ray; 3.10 A; B=311-443.
DR PDB; 4KUM; X-ray; 3.05 A; B=289-485.
DR PDB; 4UV8; X-ray; 2.80 A; B=4-485.
DR PDB; 4UV9; X-ray; 3.00 A; B=4-485.
DR PDB; 4UVA; X-ray; 2.90 A; B=4-485.
DR PDB; 4UVB; X-ray; 2.80 A; B=4-485.
DR PDB; 4UVC; X-ray; 3.10 A; B=4-485.
DR PDB; 4UXN; X-ray; 2.85 A; B=4-485.
DR PDB; 4XBF; X-ray; 2.80 A; B=311-443.
DR PDB; 5H6Q; X-ray; 2.53 A; B=311-443.
DR PDB; 5H6R; X-ray; 2.60 A; B=311-443.
DR PDB; 5L3B; X-ray; 3.30 A; B=4-485.
DR PDB; 5L3C; X-ray; 3.31 A; B=4-485.
DR PDB; 5L3D; X-ray; 2.60 A; B=4-485.
DR PDB; 5L3E; X-ray; 2.80 A; B=308-485.
DR PDB; 5L3F; X-ray; 3.50 A; B=308-485.
DR PDB; 5L3G; X-ray; 3.10 A; B=308-485.
DR PDB; 5LBQ; X-ray; 3.30 A; B=308-485.
DR PDB; 5LGN; X-ray; 3.20 A; B=311-443.
DR PDB; 5LGT; X-ray; 3.00 A; B=308-485.
DR PDB; 5LGU; X-ray; 3.20 A; B=308-485.
DR PDB; 5LHG; X-ray; 3.34 A; B=4-485.
DR PDB; 5LHH; X-ray; 3.05 A; B=4-485.
DR PDB; 5LHI; X-ray; 3.40 A; B=4-485.
DR PDB; 5X60; X-ray; 2.69 A; B=311-443.
DR PDB; 5YJB; X-ray; 2.96 A; B=311-443.
DR PDB; 6K3E; X-ray; 2.87 A; B=311-443.
DR PDB; 6KGK; X-ray; 2.70 A; B=311-443.
DR PDB; 6KGL; X-ray; 2.70 A; B=311-443.
DR PDB; 6KGM; X-ray; 2.62 A; B=311-443.
DR PDB; 6KGN; X-ray; 2.62 A; B=311-443.
DR PDB; 6S35; X-ray; 3.10 A; B=308-485.
DR PDB; 6TE1; X-ray; 3.11 A; B=4-485.
DR PDB; 6TUY; X-ray; 2.60 A; B=1-485.
DR PDB; 6VYP; X-ray; 4.99 A; L/N/l/n=289-443.
DR PDB; 6W4K; X-ray; 2.93 A; B=312-443.
DR PDB; 6WC6; X-ray; 3.10 A; B=311-443.
DR PDB; 7CDC; X-ray; 2.64 A; B=311-443.
DR PDB; 7CDD; X-ray; 2.76 A; B=311-443.
DR PDB; 7CDE; X-ray; 2.68 A; B=311-443.
DR PDB; 7CDF; X-ray; 2.68 A; B=311-443.
DR PDB; 7CDG; X-ray; 2.80 A; B=311-443.
DR PDBsum; 2IW5; -.
DR PDBsum; 2UXN; -.
DR PDBsum; 2UXX; -.
DR PDBsum; 2V1D; -.
DR PDBsum; 2X0L; -.
DR PDBsum; 2XAF; -.
DR PDBsum; 2XAG; -.
DR PDBsum; 2XAH; -.
DR PDBsum; 2XAJ; -.
DR PDBsum; 2XAQ; -.
DR PDBsum; 2XAS; -.
DR PDBsum; 2Y48; -.
DR PDBsum; 3ZMS; -.
DR PDBsum; 3ZMT; -.
DR PDBsum; 3ZMU; -.
DR PDBsum; 3ZMV; -.
DR PDBsum; 3ZMZ; -.
DR PDBsum; 3ZN0; -.
DR PDBsum; 3ZN1; -.
DR PDBsum; 4BAY; -.
DR PDBsum; 4KUM; -.
DR PDBsum; 4UV8; -.
DR PDBsum; 4UV9; -.
DR PDBsum; 4UVA; -.
DR PDBsum; 4UVB; -.
DR PDBsum; 4UVC; -.
DR PDBsum; 4UXN; -.
DR PDBsum; 4XBF; -.
DR PDBsum; 5H6Q; -.
DR PDBsum; 5H6R; -.
DR PDBsum; 5L3B; -.
DR PDBsum; 5L3C; -.
DR PDBsum; 5L3D; -.
DR PDBsum; 5L3E; -.
DR PDBsum; 5L3F; -.
DR PDBsum; 5L3G; -.
DR PDBsum; 5LBQ; -.
DR PDBsum; 5LGN; -.
DR PDBsum; 5LGT; -.
DR PDBsum; 5LGU; -.
DR PDBsum; 5LHG; -.
DR PDBsum; 5LHH; -.
DR PDBsum; 5LHI; -.
DR PDBsum; 5X60; -.
DR PDBsum; 5YJB; -.
DR PDBsum; 6K3E; -.
DR PDBsum; 6KGK; -.
DR PDBsum; 6KGL; -.
DR PDBsum; 6KGM; -.
DR PDBsum; 6KGN; -.
DR PDBsum; 6S35; -.
DR PDBsum; 6TE1; -.
DR PDBsum; 6TUY; -.
DR PDBsum; 6VYP; -.
DR PDBsum; 6W4K; -.
DR PDBsum; 6WC6; -.
DR PDBsum; 7CDC; -.
DR PDBsum; 7CDD; -.
DR PDBsum; 7CDE; -.
DR PDBsum; 7CDF; -.
DR PDBsum; 7CDG; -.
DR AlphaFoldDB; Q9UKL0; -.
DR SASBDB; Q9UKL0; -.
DR SMR; Q9UKL0; -.
DR BioGRID; 116796; 179.
DR CORUM; Q9UKL0; -.
DR DIP; DIP-35263N; -.
DR IntAct; Q9UKL0; 59.
DR MINT; Q9UKL0; -.
DR STRING; 9606.ENSP00000262241; -.
DR BindingDB; Q9UKL0; -.
DR ChEMBL; CHEMBL3137262; -.
DR GlyGen; Q9UKL0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKL0; -.
DR PhosphoSitePlus; Q9UKL0; -.
DR BioMuta; RCOR1; -.
DR DMDM; 74762776; -.
DR EPD; Q9UKL0; -.
DR jPOST; Q9UKL0; -.
DR MassIVE; Q9UKL0; -.
DR MaxQB; Q9UKL0; -.
DR PaxDb; Q9UKL0; -.
DR PeptideAtlas; Q9UKL0; -.
DR PRIDE; Q9UKL0; -.
DR ProteomicsDB; 84814; -.
DR ABCD; Q9UKL0; 2 sequenced antibodies.
DR Antibodypedia; 4532; 272 antibodies from 32 providers.
DR DNASU; 23186; -.
DR Ensembl; ENST00000262241.7; ENSP00000262241.5; ENSG00000089902.10.
DR GeneID; 23186; -.
DR KEGG; hsa:23186; -.
DR MANE-Select; ENST00000262241.7; ENSP00000262241.5; NM_015156.4; NP_055971.2.
DR UCSC; uc001ymb.5; human.
DR CTD; 23186; -.
DR DisGeNET; 23186; -.
DR GeneCards; RCOR1; -.
DR HGNC; HGNC:17441; RCOR1.
DR HPA; ENSG00000089902; Low tissue specificity.
DR MIM; 607675; gene.
DR neXtProt; NX_Q9UKL0; -.
DR OpenTargets; ENSG00000089902; -.
DR PharmGKB; PA34305; -.
DR VEuPathDB; HostDB:ENSG00000089902; -.
DR eggNOG; KOG1194; Eukaryota.
DR GeneTree; ENSGT00940000155654; -.
DR InParanoid; Q9UKL0; -.
DR OMA; WHKHDLN; -.
DR OrthoDB; 641792at2759; -.
DR PhylomeDB; Q9UKL0; -.
DR TreeFam; TF106450; -.
DR PathwayCommons; Q9UKL0; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9UKL0; -.
DR SIGNOR; Q9UKL0; -.
DR BioGRID-ORCS; 23186; 242 hits in 1115 CRISPR screens.
DR ChiTaRS; RCOR1; human.
DR EvolutionaryTrace; Q9UKL0; -.
DR GeneWiki; RCOR1; -.
DR GenomeRNAi; 23186; -.
DR Pharos; Q9UKL0; Tbio.
DR PRO; PR:Q9UKL0; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UKL0; protein.
DR Bgee; ENSG00000089902; Expressed in secondary oocyte and 201 other tissues.
DR ExpressionAtlas; Q9UKL0; baseline and differential.
DR GO; GO:1990391; C:DNA repair complex; IDA:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0070933; P:histone H4 deacetylation; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00167; SANT; 1.
DR DisProt; DP02523; -.
DR IDEAL; IID00422; -.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Coiled coil; Host-virus interaction;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..485
FT /note="REST corepressor 1"
FT /id="PRO_0000226773"
FT DOMAIN 103..189
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 190..241
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 381..432
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..257
FT /note="Interaction with HDAC1"
FT /evidence="ECO:0000269|PubMed:11516394"
FT REGION 244..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..384
FT /note="Interaction with KDM1A"
FT /evidence="ECO:0000269|PubMed:16885027"
FT REGION 442..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 244..273
FT /evidence="ECO:0000255"
FT COILED 334..369
FT /evidence="ECO:0000255"
FT COMPBIAS 49..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 466
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5LHI"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:5H6Q"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:5H6R"
FT HELIX 333..365
FT /evidence="ECO:0007829|PDB:5H6Q"
FT TURN 366..372
FT /evidence="ECO:0007829|PDB:5H6Q"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:5H6Q"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:7CDD"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:5H6Q"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:2XAQ"
FT HELIX 417..426
FT /evidence="ECO:0007829|PDB:5H6Q"
FT TURN 427..432
FT /evidence="ECO:0007829|PDB:5H6Q"
FT HELIX 433..441
FT /evidence="ECO:0007829|PDB:5H6Q"
SQ SEQUENCE 485 AA; 53327 MW; 77E90FB0EFD514B2 CRC64;
MPAMVEKGPE VSGKRRGRNN AAASASAAAA SAAASAACAS PAATAASGAA ASSASAAAAS
AAAAPNNGQN KSLAAAAPNG NSSSNSWEEG SSGSSSDEEH GGGGMRVGPQ YQAVVPDFDP
AKLARRSQER DNLGMLVWSP NQNLSEAKLD EYIAIAKEKH GYNMEQALGM LFWHKHNIEK
SLADLPNFTP FPDEWTVEDK VLFEQAFSFH GKTFHRIQQM LPDKSIASLV KFYYSWKKTR
TKTSVMDRHA RKQKREREES EDELEEANGN NPIDIEVDQN KESKKEVPPT ETVPQVKKEK
HSTQAKNRAK RKPPKGMFLS QEDVEAVSAN ATAATTVLRQ LDMELVSVKR QIQNIKQTNS
ALKEKLDGGI EPYRLPEVIQ KCNARWTTEE QLLAVQAIRK YGRDFQAISD VIGNKSVVQV
KNFFVNYRRR FNIDEVLQEW EAEHGKEETN GPSNQKPVKS PDNSIKMPEE EDEAPVLDVR
YASAS
