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Conserved domains on  [gi|6681243|ref|NP_031917|]
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transcription factor E2F1 isoform a [Mus musculus]

Protein Classification

transcription factor E2F( domain architecture ID 10491895)

transcription factor E2F is involved in the regulation of cell proliferation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
 216-296 8.44e-34

Dimerization domain of E2F transcription factors; E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA-binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain.


:

Pssm-ID: 271137 [Multi-domain]  Cd Length: 104  Bit Score: 122.24  E-value: 8.44e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681243  216 DHLMHICTTQLQLLSEDSDTQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSSET---FQISLKSKQGPIDVFL 292
Cdd:cd14660  21 DELIRWCQQSLKNLTEDPENQKLAYVTYEDIRSIPSFKEQTVIAIKAPPGTTLEVPDPEEGmrsYQIHLKSTKGPIDVYL 100


                ....
gi 6681243  293 CPEE 296
Cdd:cd14660 101 CPKE 104
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 123-187 1.99e-31

E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor E2F and its dimerization partners TDP1 and TDP2, which stimulate E2F-dependent transcription. E2F binds to DNA as a homodimer or as a heterodimer in association with TDP1/2, the heterodimer having increased binding efficiency. The crystal structure of an E2F4-DP2-DNA complex shows that the DNA-binding domains of the E2F and DP proteins both have a fold related to the winged-helix DNA-binding motif. Recognition of the central c/gGCGCg/c sequence of the consensus DNA-binding site is symmetric, and amino acids that contact these bases are conserved among all known E2F and DP proteins.


:

Pssm-ID: 460530  Cd Length: 65  Bit Score: 114.45  E-value: 1.99e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6681243    123 YETSLNLTTKRFLELLSRSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLG 187
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESPDGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
 
Name Accession Description Interval E-value
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
 216-296 8.44e-34

Dimerization domain of E2F transcription factors; E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA-binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain.


Pssm-ID: 271137 [Multi-domain]  Cd Length: 104  Bit Score: 122.24  E-value: 8.44e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681243  216 DHLMHICTTQLQLLSEDSDTQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSSET---FQISLKSKQGPIDVFL 292
Cdd:cd14660  21 DELIRWCQQSLKNLTEDPENQKLAYVTYEDIRSIPSFKEQTVIAIKAPPGTTLEVPDPEEGmrsYQIHLKSTKGPIDVYL 100


                ....
gi 6681243  293 CPEE 296
Cdd:cd14660 101 CPKE 104
E2F_CC-MB pfam16421
E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain ...
 216-294 4.30e-32

E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain of E2F transcription factors. This domain forms a heterodimer with the corresponding domain of the DP transcription factor, the heterodimer binds the C-terminus of retinoblastoma protein.


Pssm-ID: 465115  Cd Length: 96  Bit Score: 117.30  E-value: 4.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681243    216 DHLMHICTTQLQLLSEDSDTQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVD--SSETFQISLKSKQGPIDVFLC 293
Cdd:pfam16421  16 DQLIRWLQQSLKNLTEDEKNQKLAYVTYQDIRSIPCFQEQTVIAIKAPPGTQLEVPDpdEEEQYQIHLKSTNGPIDVYLC 95


                  .
gi 6681243    294 P 294
Cdd:pfam16421  96 S 96
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 123-187 1.99e-31

E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor E2F and its dimerization partners TDP1 and TDP2, which stimulate E2F-dependent transcription. E2F binds to DNA as a homodimer or as a heterodimer in association with TDP1/2, the heterodimer having increased binding efficiency. The crystal structure of an E2F4-DP2-DNA complex shows that the DNA-binding domains of the E2F and DP proteins both have a fold related to the winged-helix DNA-binding motif. Recognition of the central c/gGCGCg/c sequence of the consensus DNA-binding site is symmetric, and amino acids that contact these bases are conserved among all known E2F and DP proteins.


Pssm-ID: 460530  Cd Length: 65  Bit Score: 114.45  E-value: 1.99e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6681243    123 YETSLNLTTKRFLELLSRSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLG 187
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESPDGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
 
Name Accession Description Interval E-value
E2F_DD cd14660
Dimerization domain of E2F transcription factors; E2F transcription factors are involved in ...
 216-296 8.44e-34

Dimerization domain of E2F transcription factors; E2F transcription factors are involved in the regulation of DNA synthesis, cell cycle progression, proliferation and apoptosis. It associates with the retinoblastoma (Rb) protein, negatively regulating the G1-S transition until cyclin-dependent kinases phosphorylate Rb, which causes E2F release. E2F forms heterodimers with DP, a distantly related protein. Heterodimerization enhances the Rb binding, DNA binding, and transactivation activities of E2Fs. In humans, there are at least six closely related E2F and two DP family members, all containing a DNA-binding domain, a coiled-coil (CC) region, and a marked-box domain. E2F1 to E2F5 also contain a C-terminal transactivation domain.


Pssm-ID: 271137 [Multi-domain]  Cd Length: 104  Bit Score: 122.24  E-value: 8.44e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681243  216 DHLMHICTTQLQLLSEDSDTQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVDSSET---FQISLKSKQGPIDVFL 292
Cdd:cd14660  21 DELIRWCQQSLKNLTEDPENQKLAYVTYEDIRSIPSFKEQTVIAIKAPPGTTLEVPDPEEGmrsYQIHLKSTKGPIDVYL 100


                ....
gi 6681243  293 CPEE 296
Cdd:cd14660 101 CPKE 104
E2F_CC-MB pfam16421
E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain ...
 216-294 4.30e-32

E2F transcription factor CC-MB domain; This is the coiled coil (CC) - marked box (MB) domain of E2F transcription factors. This domain forms a heterodimer with the corresponding domain of the DP transcription factor, the heterodimer binds the C-terminus of retinoblastoma protein.


Pssm-ID: 465115  Cd Length: 96  Bit Score: 117.30  E-value: 4.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681243    216 DHLMHICTTQLQLLSEDSDTQRLAYVTCQDLRSIADPAEQMVIVIKAPPETQLQAVD--SSETFQISLKSKQGPIDVFLC 293
Cdd:pfam16421  16 DQLIRWLQQSLKNLTEDEKNQKLAYVTYQDIRSIPCFQEQTVIAIKAPPGTQLEVPDpdEEEQYQIHLKSTNGPIDVYLC 95


                  .
gi 6681243    294 P 294
Cdd:pfam16421  96 S 96
E2F_TDP pfam02319
E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor ...
 123-187 1.99e-31

E2F/DP family winged-helix DNA-binding domain; This family contains the transcription factor E2F and its dimerization partners TDP1 and TDP2, which stimulate E2F-dependent transcription. E2F binds to DNA as a homodimer or as a heterodimer in association with TDP1/2, the heterodimer having increased binding efficiency. The crystal structure of an E2F4-DP2-DNA complex shows that the DNA-binding domains of the E2F and DP proteins both have a fold related to the winged-helix DNA-binding motif. Recognition of the central c/gGCGCg/c sequence of the consensus DNA-binding site is symmetric, and amino acids that contact these bases are conserved among all known E2F and DP proteins.


Pssm-ID: 460530  Cd Length: 65  Bit Score: 114.45  E-value: 1.99e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6681243    123 YETSLNLTTKRFLELLSRSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLG 187
Cdd:pfam02319   1 KDKSLGLLTQKFLELLLESPDGVIDLNEAAEELGVKKRRIYDITNVLEGLGLIEKKSKNKIKWIG 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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