RCOR1_MOUSE
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 03-AUG-2022, entry version 170.
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).
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. {ECO:0000250,
CC ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:24227653}.
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};
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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.ENSMUSP00000082034; -.
DR iPTMnet; Q8CFE3; -.
DR PhosphoSitePlus; Q8CFE3; -.
DR EPD; Q8CFE3; -.
DR jPOST; Q8CFE3; -.
DR MaxQB; Q8CFE3; -.
DR PaxDb; Q8CFE3; -.
DR PRIDE; Q8CFE3; -.
DR ProteomicsDB; 254906; -.
DR ABCD; Q8CFE3; 1 sequenced antibody.
DR Antibodypedia; 4532; 272 antibodies from 32 providers.
DR DNASU; 217864; -.
DR Ensembl; ENSMUST00000084968; ENSMUSP00000082034; ENSMUSG00000037896.
DR GeneID; 217864; -.
DR KEGG; mmu:217864; -.
DR UCSC; uc007pck.1; mouse.
DR CTD; 23186; -.
DR MGI; MGI:106340; Rcor1.
DR VEuPathDB; HostDB:ENSMUSG00000037896; -.
DR eggNOG; KOG1194; Eukaryota.
DR GeneTree; ENSGT00940000155654; -.
DR InParanoid; Q8CFE3; -.
DR OrthoDB; 641792at2759; -.
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 113 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 258 other 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; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0070933; P:histone H4 deacetylation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
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 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 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
