E2F1_CHICK
ID E2F1_CHICK Reviewed; 403 AA.
AC Q90977;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Transcription factor E2F1 {ECO:0000303|PubMed:7478572};
DE Short=E2F-1 {ECO:0000303|PubMed:7478572};
GN Name=E2F1 {ECO:0000303|PubMed:7478572};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7478572;
RA Pasteau S., Loiseau L., Arnaud L., Trembleau A., Brun G.;
RT "Isolation and characterization of a chicken homolog of the E2F-1
RT transcription factor.";
RL Oncogene 11:1475-1486(1995).
CC -!- FUNCTION: Transcription activator that binds DNA cooperatively with DP
CC proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in
CC the promoter region of a number of genes whose products are involved in
CC cell cycle regulation or in DNA replication. The DRTF1/E2F complex
CC functions in the control of cell-cycle progression from G1 to S phase.
CC E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can
CC mediate both cell proliferation and TP53/p53-dependent apoptosis.
CC Blocks adipocyte differentiation by binding to specific promoters
CC repressing CEBPA binding to its target gene promoters. Positively
CC regulates transcription of RRP1B. {ECO:0000250|UniProtKB:Q01094,
CC ECO:0000250|UniProtKB:Q61501}.
CC -!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Forms
CC heterodimers with DP family members. The E2F1 complex binds
CC specifically hypophosphorylated retinoblastoma protein RB1. During the
CC cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase,
CC detaches from the DRTF1/E2F complex, rendering E2F transcriptionally
CC active. Viral oncoproteins, notably E1A, T-antigen and HPV E7, are
CC capable of sequestering RB1, thus releasing the active complex.
CC {ECO:0000250|UniProtKB:Q01094}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q01094}.
CC -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR EMBL; X89245; CAA61533.1; -; mRNA.
DR PIR; S58345; S58345.
DR RefSeq; NP_990550.1; NM_205219.1.
DR AlphaFoldDB; Q90977; -.
DR SMR; Q90977; -.
DR STRING; 9031.ENSGALP00000042464; -.
DR PaxDb; Q90977; -.
DR GeneID; 396142; -.
DR KEGG; gga:396142; -.
DR CTD; 1869; -.
DR VEuPathDB; HostDB:geneid_396142; -.
DR eggNOG; KOG2577; Eukaryota.
DR InParanoid; Q90977; -.
DR OrthoDB; 1087250at2759; -.
DR PhylomeDB; Q90977; -.
DR PRO; PR:Q90977; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:InterPro.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; 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; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12081; PTHR12081; 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 Activator; Cell cycle; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..403
FT /note="Transcription factor E2F1"
FT /id="PRO_0000219460"
FT DNA_BIND 87..171
FT /evidence="ECO:0000255"
FT REGION 44..85
FT /note="Cyclin A/CDK2 binding"
FT /evidence="ECO:0000255"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..151
FT /note="Leucine-zipper"
FT REGION 172..261
FT /note="Dimerization"
FT /evidence="ECO:0000255"
FT REGION 335..403
FT /note="Transactivation"
FT /evidence="ECO:0000255"
FT REGION 375..392
FT /note="Retinoblastoma protein RB1 binding"
FT /evidence="ECO:0000255"
FT MOTIF 135..171
FT /note="DEF box"
SQ SEQUENCE 403 AA; 43552 MW; 78EEA320537C33ED CRC64;
MATAGGAAGL AALLGGASPH LLIVSASEEP AGGCRPDADL LLFATPQPSR PGPAPRRPAL
GRPPVKRKLN LETDHQYIAE SLPAARGRAR IPGRGAKSPG EKSRYETSLN LTTKRFLELL
SQSPDGVVDL NWAAEVLKVQ KRRIYDITNV LEGIQLITKK SKNNIQWLGS QVAAGASSRQ
RLLEKELRDL QAAERQLDDL IQTCTVRLRL LTEDPSNQHA AYVTCQDLRS IVDPSEQMVM
VIKAPPETQL QVSDPGEAFQ VSVRSTQGPI DVFLCPEDSS GVCSPVKSPF KAPAEELSPG
SSQQRASPLL HSAQDVNMLL PEALLPGTAL PTKCPTEDVS LSPLASMDTL LEHGKDDFPG
FLADEFIALS PPQPQDYHFG LEEGEGISEL FDCDFGDFTH LDF