RCOR2_HUMAN
ID RCOR2_HUMAN Reviewed; 523 AA.
AC Q8IZ40; Q96FP3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=REST corepressor 2;
GN Name=RCOR2;
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=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-514.
RC 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-35 AND SER-36, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-88, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: May act as a component of a corepressor complex that
CC represses transcription. {ECO:0000305}.
CC -!- INTERACTION:
CC Q8IZ40; O60341: KDM1A; NbExp=3; IntAct=EBI-723853, EBI-710124;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10608.1; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence={ECO:0000305};
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DR EMBL; AP003780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010608; AAH10608.1; ALT_SEQ; mRNA.
DR EMBL; BC023587; AAH23587.1; -; mRNA.
DR CCDS; CCDS8052.1; -.
DR RefSeq; NP_775858.2; NM_173587.3.
DR AlphaFoldDB; Q8IZ40; -.
DR SMR; Q8IZ40; -.
DR BioGRID; 129510; 28.
DR IntAct; Q8IZ40; 11.
DR STRING; 9606.ENSP00000301459; -.
DR iPTMnet; Q8IZ40; -.
DR PhosphoSitePlus; Q8IZ40; -.
DR BioMuta; RCOR2; -.
DR DMDM; 147744586; -.
DR EPD; Q8IZ40; -.
DR jPOST; Q8IZ40; -.
DR MassIVE; Q8IZ40; -.
DR MaxQB; Q8IZ40; -.
DR PaxDb; Q8IZ40; -.
DR PeptideAtlas; Q8IZ40; -.
DR PRIDE; Q8IZ40; -.
DR ProteomicsDB; 71276; -.
DR Antibodypedia; 15236; 109 antibodies from 22 providers.
DR DNASU; 283248; -.
DR Ensembl; ENST00000301459.5; ENSP00000301459.4; ENSG00000167771.6.
DR GeneID; 283248; -.
DR KEGG; hsa:283248; -.
DR MANE-Select; ENST00000301459.5; ENSP00000301459.4; NM_173587.4; NP_775858.2.
DR UCSC; uc001nyc.3; human.
DR CTD; 283248; -.
DR DisGeNET; 283248; -.
DR GeneCards; RCOR2; -.
DR HGNC; HGNC:27455; RCOR2.
DR HPA; ENSG00000167771; Low tissue specificity.
DR neXtProt; NX_Q8IZ40; -.
DR OpenTargets; ENSG00000167771; -.
DR PharmGKB; PA134876257; -.
DR VEuPathDB; HostDB:ENSG00000167771; -.
DR eggNOG; KOG1194; Eukaryota.
DR GeneTree; ENSGT00940000154196; -.
DR HOGENOM; CLU_026741_3_1_1; -.
DR InParanoid; Q8IZ40; -.
DR OMA; ASQYRHH; -.
DR OrthoDB; 641792at2759; -.
DR PhylomeDB; Q8IZ40; -.
DR TreeFam; TF106450; -.
DR PathwayCommons; Q8IZ40; -.
DR SignaLink; Q8IZ40; -.
DR BioGRID-ORCS; 283248; 41 hits in 1097 CRISPR screens.
DR ChiTaRS; RCOR2; human.
DR GenomeRNAi; 283248; -.
DR Pharos; Q8IZ40; Tbio.
DR PRO; PR:Q8IZ40; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8IZ40; protein.
DR Bgee; ENSG00000167771; Expressed in ganglionic eminence and 154 other tissues.
DR Genevisible; Q8IZ40; HS.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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_0000226776"
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..264
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 501..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5FWT8"
FT MOD_RES 479
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8C796"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 514
FT /note="T -> A (in dbSNP:rs320108)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025516"
FT CONFLICT 422
FT /note="I -> T (in Ref. 2; AAH23587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 523 AA; 58012 MW; EA9E53BC578B5A2E CRC64;
MPSVMEKPSA GSGILSRSRA KTVPNGGQPH SEDDSSEEEH SHDSMIRVGT NYQAVIPECK
PESPARYSNK ELKGMLVWSP NHCVSDAKLD KYIAMAKEKH GYNIEQALGM LLWHKHDVEK
SLADLANFTP FPDEWTVEDK VLFEQAFGFH GKCFQRIQQM LPDKLIPSLV KYYYSWKKTR
SRTSVMDRQA RRLGGRKDKE DSDELEEGRG GVSEGEPDPA DPKREPLPSR PLNARPGPGK
KEVQVSQYRH HPLRTRRRPP KGMYLSPEGL TAVSGSPDLA NLTLRGLDSQ LISLKRQVQS
MKQTNSSLRQ ALEGGIDPLR PPEANTKFNS RWTTDEQLLA VQAIRRYGKD FGAIAEVIGN
KTLTQVKTFF VSYRRRFNLE EVLQEWEAEQ DGAPGAPVPM EEARRGAPLP APALEEDDEV
QITSVSTSVP RSVPPAPPPP PPPTSLSQPP PLLRPPLPTA PTLLRQPPPL QQGRFLQPRL
APNQPPPPLI RPALAAPRHS ARPGPQPPPT LIGTPLEPPA PSL
