ID RCOR1_MOUSE Reviewed; 480 AA. AC Q8CFE3; K3W4P9; Q3V092; Q8BK28; Q8CHI2; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2017, sequence version 3. DT 27-MAR-2024, entry version 179. DE RecName: Full=REST corepressor 1; DE AltName: Full=Protein CoREST; GN Name=Rcor1; Synonyms=D12Wsu95e, Kiaa0071; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-120 AND 252-480. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 66-480. RC STRAIN=NMRI; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-480. RC TISSUE=Brain; RX PubMed=12465718; DOI=10.1093/dnares/9.5.179; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I. RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 9:179-188(2002). RN [5] RP DEVELOPMENTAL STAGE. 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 [6] RP FUNCTION. RX PubMed=15907476; DOI=10.1016/j.cell.2005.03.013; RA Ballas N., Grunseich C., Lu D.D., Speh J.C., Mandel G.; RT "REST and its corepressors mediate plasticity of neuronal gene chromatin RT throughout neurogenesis."; RL Cell 121:645-657(2005). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY AS A COMPONENT OF A GFI-RCOR-KDM1A-HDAC RP COMPLEX, INTERACTION WITH GFI1 AND GFI1B, AND FUNCTION. RX PubMed=17707228; DOI=10.1016/j.molcel.2007.06.039; RA Saleque S., Kim J., Rooke H.M., Orkin S.H.; RT "Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b RT is mediated by the cofactors CoREST and LSD1."; RL Mol. Cell 27:562-572(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 AND SER-454, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [11] RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=20346398; DOI=10.1016/j.mcn.2010.03.006; RA Ravanpay A.C., Hansen S.J., Olson J.M.; RT "Transcriptional inhibition of REST by NeuroD2 during neuronal RT differentiation."; RL Mol. Cell. Neurosci. 44:178-189(2010). RN [12] RP INTERACTION WITH INMS1. RX PubMed=24227653; DOI=10.1242/dev.097642; RA Welcker J.E., Hernandez-Miranda L.R., Paul F.E., Jia S., Ivanov A., RA Selbach M., Birchmeier C.; RT "Insm1 controls development of pituitary endocrine cells and requires a RT SNAG domain for function and for recruitment of histone-modifying RT factors."; RL Development 140:4947-4958(2013). RN [13] RP INTERACTION WITH SOX2. RX PubMed=30442713; DOI=10.1074/jbc.ra118.005336; RA Zhang C., Leng F., Saxena L., Hoang N., Yu J., Alejo S., Lee L., Qi D., RA Lu F., Sun H., Zhang H.; RT "Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and CRL4- RT DCAF5 ubiquitin ligase."; RL J. Biol. Chem. 294:476-489(2019). 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:15907476, CC ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:20346398}. CC -!- SUBUNIT: Component of a BHC histone deacetylase complex that contains CC HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The CC BHC 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 (By similarity). Interacts directly with GFI1 and GFI1B in CC a RCOR/GFI/KDM1A/HDAC complex. Interacts with INMS1. Interacts with CC SOX2 (PubMed:30442713). {ECO:0000250, ECO:0000269|PubMed:17707228, CC ECO:0000269|PubMed:24227653, ECO:0000269|PubMed:30442713}. CC -!- INTERACTION: CC Q8CFE3; Q6ZQ88: Kdm1a; NbExp=2; IntAct=EBI-2337309, EBI-1216284; CC Q8CFE3; Q06219: Nr4a2; NbExp=5; IntAct=EBI-2337309, EBI-2337255; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, CC ECO:0000255|PROSITE-ProRule:PRU00624}. CC -!- TISSUE SPECIFICITY: Expressed in the external germinal layer (EGL) and CC internal granular layer (IGL) of the cerebellum and in Purkinje cells CC (at protein level). {ECO:0000269|PubMed:20346398}. CC -!- DEVELOPMENTAL STAGE: At embryonic day 8.5, it is highly expressed in CC the head mesenchyme, but neither in the somites nor in the presomitic CC mesoderm. By day 11.5 it is expressed fairly ubiquitously throughout CC the embryo. {ECO:0000269|PubMed:10734093}. CC -!- INDUCTION: Down-regulated by the transcriptional repressor ZEB1 during CC NEUROD2-induced neurogenesis. {ECO:0000269|PubMed:20346398}. CC -!- DOMAIN: The SANT domains may bridge the nucleosomal substrates and the CC demethylase KDM1A. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH42731.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AC122023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC153152; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK077445; BAC36804.1; -; mRNA. DR EMBL; AK133352; BAE21612.1; -; mRNA. DR EMBL; BY729958; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC042731; AAH42731.1; ALT_INIT; mRNA. DR EMBL; AB093210; BAC41394.1; -; mRNA. DR CCDS; CCDS49179.2; -. DR RefSeq; NP_932140.1; NM_198023.2. DR RefSeq; XP_006515823.1; XM_006515760.3. DR AlphaFoldDB; Q8CFE3; -. DR SMR; Q8CFE3; -. DR BioGRID; 229971; 5. DR CORUM; Q8CFE3; -. DR DIP; DIP-48899N; -. DR IntAct; Q8CFE3; 8. DR MINT; Q8CFE3; -. DR STRING; 10090.ENSMUSP00000112089; -. DR GlyGen; Q8CFE3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8CFE3; -. DR PhosphoSitePlus; Q8CFE3; -. DR EPD; Q8CFE3; -. DR jPOST; Q8CFE3; -. DR MaxQB; Q8CFE3; -. DR PaxDb; 10090-ENSMUSP00000082034; -. DR ProteomicsDB; 254906; -. DR Pumba; Q8CFE3; -. DR ABCD; Q8CFE3; 1 sequenced antibody. DR Antibodypedia; 4532; 322 antibodies from 32 providers. DR DNASU; 217864; -. DR Ensembl; ENSMUST00000084968.14; ENSMUSP00000082034.8; ENSMUSG00000037896.18. DR GeneID; 217864; -. DR KEGG; mmu:217864; -. DR UCSC; uc007pck.1; mouse. DR AGR; MGI:106340; -. DR CTD; 23186; -. DR MGI; MGI:106340; Rcor1. DR VEuPathDB; HostDB:ENSMUSG00000037896; -. DR eggNOG; KOG1194; Eukaryota. DR GeneTree; ENSGT00940000155654; -. DR InParanoid; Q8CFE3; -. DR OrthoDB; 3684011at2759; -. DR PhylomeDB; Q8CFE3; -. DR TreeFam; TF106450; -. DR Reactome; R-MMU-3214815; HDACs deacetylate histones. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR BioGRID-ORCS; 217864; 7 hits in 119 CRISPR screens. DR ChiTaRS; Rcor1; mouse. DR PRO; PR:Q8CFE3; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; Q8CFE3; Protein. DR Bgee; ENSMUSG00000037896; Expressed in hair follicle and 262 other cell types or tissues. DR ExpressionAtlas; Q8CFE3; baseline and differential. DR GO; GO:1990391; C:DNA repair complex; ISO:MGI. DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central. DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0019899; F:enzyme binding; IPI:MGI. DR GO; GO:0003714; F:transcription corepressor activity; IDA:GO_Central. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB. DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd00167; SANT; 1. DR Gene3D; 1.20.58.1880; -; 1. DR Gene3D; 4.10.1240.50; -; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. 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 Chromatin regulator; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..480 FT /note="REST corepressor 1" FT /id="PRO_0000226774" FT DOMAIN 97..183 FT /note="ELM2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512" FT DOMAIN 184..235 FT /note="SANT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT DOMAIN 375..426 FT /note="SANT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624" FT REGION 1..105 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 72..251 FT /note="Interaction with HDAC1" FT /evidence="ECO:0000250|UniProtKB:Q9UKL0" FT REGION 238..308 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 290..378 FT /note="Interaction with KDM1A" FT /evidence="ECO:0000250|UniProtKB:Q9UKL0" FT REGION 436..466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 238..265 FT /evidence="ECO:0000255" FT COILED 328..363 FT /evidence="ECO:0000255" FT COMPBIAS 57..92 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 271..296 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 121 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9UKL0" FT MOD_RES 254 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES 454 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 116 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9UKL0" FT CROSSLNK 291 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9UKL0" FT CROSSLNK 460 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9UKL0" FT CONFLICT 444 FT /note="N -> Y (in Ref. 2; BAC36804/BAE21612)" FT /evidence="ECO:0000305" SQ SEQUENCE 480 AA; 52715 MW; 7FA2AEA127EA297A CRC64; MPAMVEKGPE VSGKRRGRNT AASAASAAAS AASAAASAAA SAGTASASAA AAASAAAAPN NGQNKSLAAA APNGNSGSNS WEEGSSGSSS DEEHGGGGMR VGPQYQAAVP DFDPAKLARR SQERDNLGML VWSPNQSLSE AKLDEYIAIA KEKHGYNMEQ ALGMLFWHKH NIEKSLADLP NFTPFPDEWT VEDKVLFEQA FSFHGKTFHR IQQMLPDKSI ASLVKFYYSW KKTRTKTSVM DRHARKQKRE REESEDELEE TNGSNPVDIE IDPNKESKKE VPPTETVPQV KKEKHSTQAK NRAKRKPPKG MFLSQEDVEA VSANATAATT VLRQLDMELV SIKRQIQNIK QTNSALKEKL DGGIEPYRLP EVIQKCNARW TTEEQLLAVQ AIRKYGRDFQ AISDVIGNKS VVQVKNFFVN YRRRFNIDEV LQEWEAEHGK DETNGPANQK PVKSPESSIK IPEEEDEAAS VLDVRYASAS //