E2F6_BOVIN
ID E2F6_BOVIN Reviewed; 285 AA.
AC Q08DY6;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Transcription factor E2F6 {ECO:0000305};
DE Short=E2F-6 {ECO:0000250|UniProtKB:O54917};
GN Name=E2F6 {ECO:0000250|UniProtKB:O54917};
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=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibitor of E2F-dependent transcription. Binds DNA
CC cooperatively with DP proteins through the E2 recognition site, 5'-
CC TTTC[CG]CGC-3'. Has a preference for the 5'-TTTCCCGC-3' E2F recognition
CC site. E2F6 lacks the transcriptional activation and pocket protein
CC binding domains (By similarity). Appears to regulate a subset of E2F-
CC dependent genes whose products are required for entry into the cell
CC cycle but not for normal cell cycle progression (By similarity).
CC Represses expression of some meiosis-specific genes, including
CC SLC25A31/ANT4 (By similarity). 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:O54917,
CC ECO:0000250|UniProtKB:O75461}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC123506; AAI23507.1; -; mRNA.
DR RefSeq; NP_001070316.1; NM_001076848.1.
DR AlphaFoldDB; Q08DY6; -.
DR SMR; Q08DY6; -.
DR STRING; 9913.ENSBTAP00000028703; -.
DR PaxDb; Q08DY6; -.
DR PRIDE; Q08DY6; -.
DR Ensembl; ENSBTAT00000028703; ENSBTAP00000028703; ENSBTAG00000048286.
DR GeneID; 514085; -.
DR KEGG; bta:514085; -.
DR CTD; 1876; -.
DR VEuPathDB; HostDB:ENSBTAG00000048286; -.
DR VGNC; VGNC:28290; E2F6.
DR eggNOG; KOG2577; Eukaryota.
DR GeneTree; ENSGT00940000155734; -.
DR HOGENOM; CLU_032091_4_0_1; -.
DR InParanoid; Q08DY6; -.
DR OMA; VEQNHSN; -.
DR OrthoDB; 1087250at2759; -.
DR TreeFam; TF105566; -.
DR Reactome; R-BTA-8953750; Transcriptional Regulation by E2F6.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000048286; Expressed in biceps femoris and 103 other tissues.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
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; ISS: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:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
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; IEA:Ensembl.
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; Isopeptide bond; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..285
FT /note="Transcription factor E2F6"
FT /id="PRO_0000290583"
FT DNA_BIND 50..129
FT /evidence="ECO:0000255"
FT REGION 130..222
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 143..164
FT /note="Leucine-zipper"
FT REGION 173..285
FT /note="Transcription repression"
FT /evidence="ECO:0000250"
FT REGION 240..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 95..129
FT /note="DEF box"
FT COMPBIAS 240..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75461"
SQ SEQUENCE 285 AA; 32246 MW; 00F205365E941FEE CRC64;
MSQQRPARKL PSLLVDPAEE TVRRRCRDPI NVEGLLPSKI RINLEDNVQY VSMRKALKVK
RPRFDVSLVY LTRKFMDLVR SAPGGILDLN KVATKLGVRK RRVYDITNVL DGIDLVEKKS
KNHIRWIGSD LSNFGAVPQQ KKLQEELSDL SAMEDALDEL IKDCAQQLFE LTDDKENERL
AYVTYQDIHS IQAFHEQIVI AVKAPAETRL DVPAPKEDSI TVHIRSTKGP IDVYLCEVEQ
GSHSSNKTSD NVGTSSSKSK PLEHPQPEKE ENPPQQSEEV LEVSN
