RCOR2_MOUSE
ID RCOR2_MOUSE Reviewed; 523 AA.
AC Q8C796; Q9JMK4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=REST corepressor 2;
DE AltName: Full=M-CoREST;
GN Name=Rcor2;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-523, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11578870; DOI=10.1016/s0925-4773(01)00477-4;
RA Tontsch S., Zach O., Bauer H.-C.;
RT "Identification and localization of M-CoREST (1A13), a mouse homologue of
RT the human transcriptional co-repressor CoREST, in the developing mouse
RT CNS.";
RL Mech. Dev. 108:165-169(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-479, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May act as a component of a corepressor complex that
CC represses transcription. {ECO:0000305}.
CC -!- INTERACTION:
CC Q8C796; P70288: Hdac2; NbExp=2; IntAct=EBI-3043949, EBI-302251;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- TISSUE SPECIFICITY: Predominantly, but not exclusively, expressed in
CC neural tissue. Strongly expressed in neural domains of the developing
CC brain of the developing mouse CNS. {ECO:0000269|PubMed:11578870}.
CC -!- DEVELOPMENTAL STAGE: During early development (7 dpc to 8.5 dpc), it is
CC uniformly distributed, with a higher expression in the presumptive
CC neural tissue (head region) while it is not expressed in the heart.
CC From 9 dpc on, it becomes increasingly restricted to the developing
CC brain and spinal cord. With the exception of the floor plate, it is
CC expressed in many cell clusters in the neural tube at that stage.
CC Expressed in dorsal root ganglia and in the neural retina (sensory
CC layer of the retina) of embryos from 11 dpc on throughout development.
CC During mid-gestation, it is particularly expressed in neural tissue
CC thereby shifting to the intermediate and distal layers of the expanding
CC intraneural domains. From late gestational stages on, pronounced
CC expression is detectable only in selected areas of the brain such as
CC the retrospinal cortex. Expressed in neural cell layers in the
CC hypothalamic region at postnatal day 5. In adult brains, it is
CC expressed in many neural cells of the differentiated cortex. Expression
CC is also observed in non-neural tissue such as the developing limbs
CC where it becomes restricted to the interdigital areas. Strongly
CC expressed in the odontoblast layer of the developing teeth and the
CC maxillary bone. In the cerebellum, it is already expressed before the
CC lobules form. At 14 dpc, it is uniformly distributed in the cerebellar
CC rudiment. When lobulation becomes evident, expression is detectable
CC only in the proliferating granule cells of the outermost layer
CC (external granular layer). {ECO:0000269|PubMed:11578870}.
CC -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB93943.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK052295; BAC34922.1; -; mRNA.
DR EMBL; BC055719; AAH55719.1; -; mRNA.
DR EMBL; X83587; CAB93943.1; ALT_INIT; mRNA.
DR CCDS; CCDS29522.2; -.
DR RefSeq; NP_001307483.1; NM_001320554.1.
DR RefSeq; NP_473389.2; NM_054048.4.
DR AlphaFoldDB; Q8C796; -.
DR SMR; Q8C796; -.
DR BioGRID; 222597; 31.
DR DIP; DIP-59754N; -.
DR IntAct; Q8C796; 7.
DR MINT; Q8C796; -.
DR STRING; 10090.ENSMUSP00000063335; -.
DR iPTMnet; Q8C796; -.
DR PhosphoSitePlus; Q8C796; -.
DR EPD; Q8C796; -.
DR jPOST; Q8C796; -.
DR MaxQB; Q8C796; -.
DR PaxDb; Q8C796; -.
DR PeptideAtlas; Q8C796; -.
DR PRIDE; Q8C796; -.
DR ProteomicsDB; 253187; -.
DR Antibodypedia; 15236; 109 antibodies from 22 providers.
DR DNASU; 104383; -.
DR Ensembl; ENSMUST00000066646; ENSMUSP00000063335; ENSMUSG00000024968.
DR GeneID; 104383; -.
DR KEGG; mmu:104383; -.
DR UCSC; uc008gkn.1; mouse.
DR CTD; 283248; -.
DR MGI; MGI:1859854; Rcor2.
DR VEuPathDB; HostDB:ENSMUSG00000024968; -.
DR eggNOG; KOG1194; Eukaryota.
DR GeneTree; ENSGT00940000154196; -.
DR InParanoid; Q8C796; -.
DR OMA; ASQYRHH; -.
DR OrthoDB; 641792at2759; -.
DR PhylomeDB; Q8C796; -.
DR TreeFam; TF106450; -.
DR BioGRID-ORCS; 104383; 4 hits in 62 CRISPR screens.
DR ChiTaRS; Rcor2; mouse.
DR PRO; PR:Q8C796; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8C796; protein.
DR Bgee; ENSMUSG00000024968; Expressed in ventricular zone and 151 other tissues.
DR ExpressionAtlas; Q8C796; baseline and differential.
DR Genevisible; Q8C796; MM.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
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 Coiled coil; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..523
FT /note="REST corepressor 2"
FT /id="PRO_0000226777"
FT DOMAIN 44..129
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 130..181
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 327..378
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 283..314
FT /evidence="ECO:0000255"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ40"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ40"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ40"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FWT8"
FT MOD_RES 479
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ40"
SQ SEQUENCE 523 AA; 57908 MW; 46A563C1CC11A7E4 CRC64;
MPSVMEKPSA GSGILSRSRA KTAPNGGQPH SEDDSSEEEH SHDSMIRVGT NYQAVIPECK
PESPARYSNK ELKGMLVWSP NHCVSDAKLD KYIAMAKEKH GYNIEQALGM LLWHKHDVEK
SLADLANFTP FPDEWTVEDK VLFEQAFGFH GKCFQRIQQM LPDKVIPSLV KYYYSWKKTR
SRTSVMDRQA RRLGGRKDKE DSDELEEGRG AVSEGEPDTG DPKREPLPSR PLNARPGPGK
KEVQISQYRH HPLRTRRRPP KGMYLSPEGL TAVSGSPDLA NLTLRGLDSQ LISLKRQVQS
MKQTNSSLRQ ALEGGIDPLR PPEANTKFNS RWTTDEQLLA VQAIRRYGKD FGAIAEVIGN
KTLTQVKTFF VSYRRRFNLE EVLQEWEAEQ DGAPAAPVPT EEARRGAPVP ATALEEDDEV
QITSVSTSVP RSVPPAPPPP PPPTSLSQPP PLLRPPLPTA PTLLRQPPPL QQGRFLQPRL
APNQPPPPLI RPALAASRHS ARPGPQPPPT LVGAPLEPPA PSL
