E2F6_MOUSE
ID E2F6_MOUSE Reviewed; 272 AA.
AC O54917; Q8K456;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Transcription factor E2F6 {ECO:0000305};
DE Short=E2F-6 {ECO:0000303|PubMed:18667754};
DE AltName: Full=E2F-binding site-modulating activity protein {ECO:0000303|PubMed:9403682};
DE Short=EMA {ECO:0000303|PubMed:9403682};
GN Name=E2f6 {ECO:0000303|PubMed:18667754, ECO:0000312|MGI:MGI:1354159};
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 [MRNA], AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=9403682; DOI=10.1038/37507;
RA Morkel M., Wenkel J., Bannister A.J., Kouzarides T., Hagemeier C.;
RT "An E2F-like repressor of transcription.";
RL Nature 390:567-568(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RA Salih M., Tuana B.S.;
RT "Characterization of the complete mouse E2F6 gene.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=18667754; DOI=10.1095/biolreprod.108.067645;
RA Kehoe S.M., Oka M., Hankowski K.E., Reichert N., Garcia S., McCarrey J.R.,
RA Gaubatz S., Terada N.;
RT "A conserved E2F6-binding element in murine meiosis-specific gene
RT promoters.";
RL Biol. Reprod. 79:921-930(2008).
CC -!- FUNCTION: Inhibitor of E2F-dependent transcription (PubMed:9403682).
CC Binds DNA cooperatively with DP proteins through the E2 recognition
CC site, 5'-TTTC[CG]CGC-3' (PubMed:9403682, PubMed:18667754). Has a
CC preference for the 5'-TTTCCCGC-3' E2F recognition site
CC (PubMed:9403682). E2F6 lacks the transcriptional activation and pocket
CC protein binding domains (PubMed:9403682). Appears to regulate a subset
CC of E2F-dependent genes whose products are required for entry into the
CC cell cycle but not for normal cell cycle progression (By similarity).
CC Represses expression of some meiosis-specific genes, including
CC SLC25A31/ANT4 (PubMed:18667754). May silence expression via the
CC recruitment of a chromatin remodeling complex containing histone H3-K9
CC methyltransferase activity. Overexpression delays the exit of cells
CC from the S-phase (By similarity). {ECO:0000250|UniProtKB:O75461,
CC ECO:0000269|PubMed:18667754, ECO:0000269|PubMed:9403682}.
CC -!- SUBUNIT: Forms heterodimers with DP family members TFDP1 or TFDP2.
CC Component of the DRTF1/E2F transcription factor complex. Part of the
CC E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3,
CC BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Component of some
CC MLL1/MLL complex, at least composed of the core components KMT2A/MLL1,
CC ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10.
CC {ECO:0000250|UniProtKB:O75461}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75461}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; AF032131; AAC53521.1; -; mRNA.
DR EMBL; AF487711; AAM45941.1; -; Genomic_DNA.
DR EMBL; AC157352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36409.1; -.
DR RefSeq; NP_150373.2; NM_033270.2.
DR AlphaFoldDB; O54917; -.
DR SMR; O54917; -.
DR BioGRID; 206042; 6.
DR DIP; DIP-59331N; -.
DR IntAct; O54917; 1.
DR STRING; 10090.ENSMUSP00000020908; -.
DR iPTMnet; O54917; -.
DR PhosphoSitePlus; O54917; -.
DR PaxDb; O54917; -.
DR PeptideAtlas; O54917; -.
DR PRIDE; O54917; -.
DR ProteomicsDB; 277701; -.
DR Antibodypedia; 12671; 337 antibodies from 36 providers.
DR DNASU; 50496; -.
DR Ensembl; ENSMUST00000020908; ENSMUSP00000020908; ENSMUSG00000057469.
DR GeneID; 50496; -.
DR KEGG; mmu:50496; -.
DR UCSC; uc007nce.2; mouse.
DR CTD; 1876; -.
DR MGI; MGI:1354159; E2f6.
DR VEuPathDB; HostDB:ENSMUSG00000057469; -.
DR eggNOG; KOG2577; Eukaryota.
DR GeneTree; ENSGT00940000155734; -.
DR HOGENOM; CLU_032091_4_0_1; -.
DR InParanoid; O54917; -.
DR OMA; VEQNHSN; -.
DR OrthoDB; 1087250at2759; -.
DR PhylomeDB; O54917; -.
DR TreeFam; TF105566; -.
DR Reactome; R-MMU-8953750; Transcriptional Regulation by E2F6.
DR BioGRID-ORCS; 50496; 3 hits in 73 CRISPR screens.
DR ChiTaRS; E2f6; mouse.
DR PRO; PR:O54917; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O54917; protein.
DR Bgee; ENSMUSG00000057469; Expressed in vastus lateralis and 249 other tissues.
DR ExpressionAtlas; O54917; baseline and differential.
DR Genevisible; O54917; MM.
DR GO; GO:0005662; C:DNA replication factor A complex; IC:MGI.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IGI:MGI.
DR CDD; cd14660; E2F_DD; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR015633; E2F.
DR InterPro; IPR037241; E2F-DP_heterodim.
DR InterPro; IPR032198; E2F_CC-MB.
DR InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR InterPro; IPR015635; Transcription_factor_E2F6.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12081; PTHR12081; 1.
DR PANTHER; PTHR12081:SF19; PTHR12081:SF19; 1.
DR Pfam; PF16421; E2F_CC-MB; 1.
DR Pfam; PF02319; E2F_TDP; 1.
DR SMART; SM01372; E2F_TDP; 1.
DR SUPFAM; SSF144074; SSF144074; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..272
FT /note="Transcription factor E2F6"
FT /id="PRO_0000219473"
FT DNA_BIND 50..129
FT /evidence="ECO:0000255"
FT REGION 1..62
FT /note="Binding to corepressors"
FT /evidence="ECO:0000305"
FT REGION 130..222
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 143..164
FT /note="Leucine-zipper"
FT REGION 173..272
FT /note="Transcription repression"
FT /evidence="ECO:0000250"
FT REGION 242..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 95..129
FT /note="DEF box"
FT COMPBIAS 242..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 97
FT /note="G -> S (in Ref. 1; AAC53521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 30852 MW; B99641329C00CD08 CRC64;
MSQQRTARRQ PSLLVDPAQE TVRRRCRDPI NVENLLPSKI RINLEENVQY VSMRKALKVK
RPRFDVSLVY LTRKFMDLVR SAPGGILDLN KVATKLGVRK RRVYDITNVL DGIELVEKKS
KNHIRWIGSD LNNFGAAPQQ KKLQAELSDL SAMEDALDEL IKDCAQQLLE LTDDKENERL
AYVTYQDIHG IQAFHEQIVI AVKAPEETRL DVPAPREDSI TVHIRSTKGP IDVYLCEVEQ
NHSNGKTNDG IGASPSKSSH PQCPEKEDEP PQ
