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 27-MAR-2024, entry version 205. 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. Interacts with SOX2 (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q8CFE3, 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}; 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; 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 PDB; 7ZRY; X-ray; 2.70 A; B=308-485. 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 PDBsum; 7ZRY; -. DR AlphaFoldDB; Q9UKL0; -. DR SASBDB; Q9UKL0; -. DR SMR; Q9UKL0; -. DR BioGRID; 116796; 498. DR CORUM; Q9UKL0; -. DR DIP; DIP-35263N; -. DR IntAct; Q9UKL0; 61. DR MINT; Q9UKL0; -. DR STRING; 9606.ENSP00000262241; -. DR BindingDB; Q9UKL0; -. DR ChEMBL; CHEMBL3137262; -. DR GlyGen; Q9UKL0; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000262241; -. DR PeptideAtlas; Q9UKL0; -. DR ProteomicsDB; 84814; -. DR Pumba; Q9UKL0; -. DR ABCD; Q9UKL0; 2 sequenced antibodies. DR Antibodypedia; 4532; 322 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 AGR; HGNC:17441; -. 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; HFFVSYR; -. DR OrthoDB; 3684011at2759; -. 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; 250 hits in 1194 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 202 other cell types or 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:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. 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 Gene3D; 1.20.58.1880; -; 1. DR Gene3D; 4.10.1240.50; -; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR IDEAL; IID00422; -. DR InterPro; IPR000949; ELM2_dom. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR049048; REST_helical. DR InterPro; IPR001005; SANT/Myb. DR InterPro; IPR017884; SANT_dom. DR PANTHER; PTHR16089:SF11; REST COREPRESSOR 1; 1. DR PANTHER; PTHR16089; REST COREPRESSOR COREST PROTEIN-RELATED; 1. DR Pfam; PF01448; ELM2; 1. DR Pfam; PF00249; Myb_DNA-binding; 2. DR Pfam; PF20878; REST_helical; 1. DR SMART; SM01189; ELM2; 1. DR SMART; SM00717; SANT; 2. DR SUPFAM; SSF46689; Homeodomain-like; 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 //