EED_BOVIN
ID EED_BOVIN Reviewed; 441 AA.
AC Q3SZ25;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Polycomb protein EED;
GN Name=EED;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2
CC complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading
CC to transcriptional repression of the affected target gene. Also
CC recognizes 'Lys-26' trimethylated histone H1 with the effect of
CC inhibiting PRC2 complex methyltransferase activity on nucleosomal
CC histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite
CC effect, enabling the propagation of this repressive mark (By
CC similarity). The PRC2/EED-EZH2 complex may also serve as a recruiting
CC platform for DNA methyltransferases, thereby linking two epigenetic
CC repression systems (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the PRC2/EED-EZH2 complex, which includes EED,
CC EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2 (By similarity). The
CC minimum components required for methyltransferase activity of the
CC PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12. Component of the
CC PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2
CC (By similarity). The PRC2 complex may also interact with DNMT1, DNMT3A,
CC DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the SUZ12
CC subunit (By similarity). Interacts with HDAC, HDAC2, histone H1,
CC KMT2A/MLL1 and YY1 (By similarity). May interact with ITGA4, ITGAE and
CC ITGB7 (By similarity). Interacts with CDYL. Interacts with ARNTL/BMAL1
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The WD repeat domain mediates recognition of trimethylated
CC histone peptides at the consensus sequence Ala-Arg-Lys-Ser. This is
CC achieved through an aromatic cage encircling the methyllysine, and
CC involving Phe-97, Tyr-148 and Tyr-365 (By similarity). {ECO:0000250}.
CC -!- PTM: Methylated. Binding to histone H1 'Lys-26' promotes mono-, di-,
CC and trimethylation of internal lysines (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat ESC family. {ECO:0000305}.
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DR EMBL; BC103217; AAI03218.1; -; mRNA.
DR RefSeq; NP_001035584.1; NM_001040494.2.
DR AlphaFoldDB; Q3SZ25; -.
DR SMR; Q3SZ25; -.
DR STRING; 9913.ENSBTAP00000010324; -.
DR PaxDb; Q3SZ25; -.
DR PRIDE; Q3SZ25; -.
DR Ensembl; ENSBTAT00000010324; ENSBTAP00000010324; ENSBTAG00000007847.
DR GeneID; 404183; -.
DR KEGG; bta:404183; -.
DR CTD; 8726; -.
DR VEuPathDB; HostDB:ENSBTAG00000007847; -.
DR VGNC; VGNC:28332; EED.
DR eggNOG; KOG1034; Eukaryota.
DR GeneTree; ENSGT00510000047334; -.
DR HOGENOM; CLU_032683_1_0_1; -.
DR InParanoid; Q3SZ25; -.
DR OMA; WSYDSVT; -.
DR OrthoDB; 1191277at2759; -.
DR TreeFam; TF314451; -.
DR Reactome; R-BTA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-BTA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-BTA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-BTA-8943724; Regulation of PTEN gene transcription.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000007847; Expressed in pharyngeal tonsil and 108 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; ISS:UniProtKB.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037352; Polycomb_EED.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10253:SF5; PTHR10253:SF5; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromatin regulator; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT CHAIN 2..441
FT /note="Polycomb protein EED"
FT /id="PRO_0000343724"
FT REPEAT 91..134
FT /note="WD 1"
FT REPEAT 142..185
FT /note="WD 2"
FT REPEAT 188..228
FT /note="WD 3"
FT REPEAT 234..275
FT /note="WD 4"
FT REPEAT 304..341
FT /note="WD 5"
FT REPEAT 359..399
FT /note="WD 6"
FT REPEAT 408..441
FT /note="WD 7"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..441
FT /note="Interaction with EZH2"
FT /evidence="ECO:0000250"
FT COMPBIAS 41..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q921E6"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 66
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 66
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 66
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 197
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 197
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 197
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 268
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 268
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 268
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 284
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 284
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
FT MOD_RES 284
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75530"
SQ SEQUENCE 441 AA; 50226 MW; B4DA10D346BCA05F CRC64;
MSEREVSTVP AGTDMPAAKK QKLSSDENSN PDLSGDENDD AVSIESGTNT ERPDTPTNTP
NAPGRKSWGK GKWKSKKCKY SFKCVNSLKE DHNQPLFGVQ FNWHSKEGDP LVFATVGSNR
VTLYECHSQG EIRLLQSYVD ADADENFYTC AWTYDSNTSH PLLAVAGSRG IIRIINPITM
QCIKHYVGHG NAINELKFHP RDPNLLLSVS KDHALRLWNI QTDTLVAIFG GVEGHRDEVL
SADYDLLGEK IMSCGMDHSL KLWRINSKRM MNAIKESYDY NPNKTNRPFI SQKIHFPDFS
TRDIHRNYVD CVRWLGDLIL SKSCENAIVC WKPGKMEDDI DKIKPSESNV TILGRFDYSQ
CDIWYMRFSM DFWQKMLALG NQVGKLYVWD LEVEDPHKAK CTTLTHHKCG AAIRQTSFSR
DSSILIAVCD DASIWRWDRL R
