PlantTFDB
PlantRegMap/PlantTFDB v5.0
Plant Transcription Factor Database
Transcription Factor Information
Basic Information | Signature Domain | Sequence | 
Basic Information? help Back to Top
TF ID Cc00_g35310
Common NameGSCOC_T00007535001
Organism
Taxonomic ID
Taxonomic Lineage
cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Coffeeae; Coffea
Family E2F/DP
Protein Properties Length: 168aa    MW: 19275.3 Da    PI: 9.2339
Description E2F/DP family protein
Gene Model
Gene Model ID Type Source Coding Sequence
Cc00_g35310genomeCGSCView CDS
Signature Domain? help Back to Top
Signature Domain
No. Domain Score E-value Start End HMM Start HMM End
1E2F_TDP72.93.4e-232994171
      E2F_TDP  1 rkeksLrlltqkflkllekseegivtlnevakeLvsedvknkrRRiYDilNVLealnliekkekneirwkg 71
                 r+++sL+l t++f++l++++e+gi++lne+ak+L   ++  ++RRiYDi+ VL +++liek+ k+ irw g
  Cc00_g35310 29 RNDRSLGLQTKNFVNLIKHAEDGILDLNEAAKTL---EM--SKRRIYDITSVLGGIGLIEKELKSTIRWTG 94
                 789*******************************...99..****************************98 PP

Protein Features ? help Back to Top
3D Structure
Database Entry ID E-value Start End InterPro ID Description
Gene3DG3DSA:1.10.10.101.8E-242695IPR011991Winged helix-turn-helix DNA-binding domain
SuperFamilySSF467859.87E-152992IPR011991Winged helix-turn-helix DNA-binding domain
SMARTSM013724.2E-252994IPR003316E2F/DP family, winged-helix DNA-binding domain
PfamPF023191.6E-203194IPR003316E2F/DP family, winged-helix DNA-binding domain
SuperFamilySSF1440742.62E-899154No hitNo description
Gene Ontology ? help Back to Top
GO Term GO Category GO Description
GO:0006355Biological Processregulation of transcription, DNA-templated
GO:0005634Cellular Componentnucleus
GO:0005667Cellular Componenttranscription factor complex
GO:0003677Molecular FunctionDNA binding
GO:0003700Molecular Functiontranscription factor activity, sequence-specific DNA binding
Sequence ? help Back to Top
Protein Sequence    Length: 168 aa     Download sequence    Send to blast
MSGGNAYRSK VTPLTPLFNA KGGKARSCRN DRSLGLQTKN FVNLIKHAED GILDLNEAAK  60
TLEMSKRRIY DITSVLGGIG LIEKELKSTI RWTGLGASRQ PDLQAEVENL SMEERRLDDR  120
IRLEMQERLR DLSAINQKWL FVTFEDIKVV PCFQVLFYCF VVWQFLFS
3D Structure ? help Back to Top
Structure
PDB ID Evalue Query Start Query End Hit Start Hit End Description
1cf7_A8e-202897676PROTEIN (TRANSCRIPTION FACTOR E2F-4)
Search in ModeBase
Functional Description ? help Back to Top
Source Description
UniProtTranscription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The binding of retinoblastoma-related proteins represses transactivation. Regulates gene expression both positively and negatively. Activates the expression of E2FB. Involved in the control of cell-cycle progression from G1 to S phase. Stimulates cell proliferation and delays differentiation. {ECO:0000269|PubMed:11669580, ECO:0000269|PubMed:11786543, ECO:0000269|PubMed:11862494, ECO:0000269|PubMed:11889041, ECO:0000269|PubMed:11891240, ECO:0000269|PubMed:12913157, ECO:0000269|PubMed:15377755, ECO:0000269|PubMed:16514015, ECO:0000269|PubMed:19662336}.
Regulation -- PlantRegMap ? help Back to Top
Source Upstream Regulator Target Gene
PlantRegMapRetrieve-
Annotation -- Protein ? help Back to Top
Source Hit ID E-value Description
RefseqXP_027174750.15e-87transcription factor E2FA-like
SwissprotQ9FNY01e-44E2FA_ARATH; Transcription factor E2FA
TrEMBLA0A068VNG91e-121A0A068VNG9_COFCA; Uncharacterized protein (Fragment)
STRINGXP_010262959.11e-56(Nelumbo nucifera)
Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID E-value Description
AT2G36010.15e-41E2F transcription factor 3
Publications ? help Back to Top
  1. Magyar Z, et al.
    Arabidopsis E2FA stimulates proliferation and endocycle separately through RBR-bound and RBR-free complexes.
    EMBO J., 2012. 31(6): p. 1480-93
    [PMID:22307083]