Harmonizome 3.0

E2F transcription factor 6 pseudogene 3

E2F transcription factor 6 pseudogene 2

E2F transcription factor 6 pseudogene 1

E2F transcription factor 6 pseudogene 4

E2F transcription factor 3 pseudogene 2

E2F transcription factor 3 pseudogene 1

ubiquitin-conjugating enzyme E2F (putative) pseudogene

transcription factor Dp-2 (E2F dimerization partner 2)

The gene is a member of the transcription factor DP family. The encoded protein forms heterodimers with the E2F transcription factors resulting in transcriptional activation of cell cycle regulated genes. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2010]

ubiquitin-conjugating enzyme E2F (putative) pseudogene 1

E2F transcription factor 4, p107/p130-binding pseudogene 1

ubiquitin-conjugating enzyme E2F (putative) pseudogene

ubiquitin-conjugating enzyme E2F (putative)

Enables NEDD8 conjugating enzyme activity. Involved in protein neddylation. Predicted to be active in cytosol and nucleus. [provided by Alliance of Genome Resources, Mar 2025]

E2F transcription factor 7

Enables DNA-binding transcription repressor activity; cis-regulatory region sequence-specific DNA binding activity; and identical protein binding activity. Involved in DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; regulation of transcription by RNA polymerase II; and sprouting angiogenesis. Located in nuclear speck. [provided by Alliance of Genome Resources, Mar 2025]

E2F transcription factor 6

This gene encodes a member of a family of transcription factors that play a crucial role in the control of the cell cycle. The protein encoded by this gene lacks the transactivation and tumor suppressor protein association domains found in other family members, and contains a modular suppression domain that functions in the inhibition of transcription. It interacts in a complex with chromatin modifying factors. There are pseudogenes for this gene on chromosomes 22 and X. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2013]

E2F transcription factor 5, p130-binding

The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionarily conserved domains that are present in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein is differentially phosphorylated and is expressed in a wide variety of human tissues. It has higher identity to E2F4 than to other family members. Both this protein and E2F4 interact with tumor suppressor proteins p130 and p107, but not with pRB. Alternative splicing results in multiple variants encoding different isoforms. [provided by RefSeq, Jul 2008]

E2F transcription factor 4, p107/p130-binding

The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein binds to all three of the tumor suppressor proteins pRB, p107 and p130, but with higher affinity to the last two. It plays an important role in the suppression of proliferation-associated genes, and its gene mutation and increased expression may be associated with human cancer. [provided by RefSeq, Jul 2008]

E2F transcription factor 3

This gene encodes a member of a small family of transcription factors that function through binding of DP interaction partner proteins. The encoded protein recognizes a specific sequence motif in DNA and interacts directly with the retinoblastoma protein (pRB) to regulate the expression of genes involved in the cell cycle. Altered copy number and activity of this gene have been observed in a number of human cancers. There are pseudogenes for this gene on chromosomes 2 and 17. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2013]

E2F transcription factor 2

The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F1 and E2F3, have an additional cyclin binding domain. This protein binds specifically to retinoblastoma protein pRB in a cell-cycle dependent manner, and it exhibits overall 46% amino acid identity to E2F1. [provided by RefSeq, Jul 2008]

E2F transcription factor 1

The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. This protein binds preferentially to retinoblastoma protein pRB in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent/independent apoptosis. [provided by RefSeq, Jul 2008]

E2F transcription factor 8

This gene encodes a member of a family of transcription factors which regulate the expression of genes required for progression through the cell cycle. The encoded protein regulates progression from G1 to S phase by ensuring the nucleus divides at the proper time. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Jan 2012]

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the E2F-associated phosphoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the rb-e2f complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From CORUM Protein Complexes

proteins in the S-phase-specific E2F-p107 complex protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the E2F-6 complex protein complex from the CORUM Protein Complexes dataset.

From CORUM Protein Complexes

proteins in the pRB-E2F-1 complex protein complex from the CORUM Protein Complexes dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term e2f in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Cellular Component Annotations 2015

proteins localized to the rb-e2f complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the E2F Family protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the E2F/DP family, winged-helix DNA-binding domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From MotifMap Predicted Transcription Factor Targets

target genes of the E2F transcription factor predicted using known transcription factor binding site motifs from the MotifMap Predicted Transcription Factor Targets dataset.

From PID Pathways

proteins participating in the E2F transcription factor network pathway from the PID Pathways dataset.

From Reactome Pathways 2014

proteins participating in the E2F-enabled inhibition of pre-replication complex formation pathway from the Reactome Pathways dataset.

From Reactome Pathways 2014

proteins participating in the E2F mediated regulation of DNA replication pathway from the Reactome Pathways dataset.

From GO Cellular Component Annotations 2023

proteins localized to the Rb-E2F complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From Reactome Pathways 2024

proteins participating in the E2F mediated regulation of DNA replication pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the E2F-enabled inhibition of pre-replication complex formation pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Transcription of E2F targets under negative control by DREAM complex pathway from the Reactome Pathways 2024 dataset.

From Reactome Pathways 2024

proteins participating in the Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 pathway from the Reactome Pathways 2024 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the Rb-E2F complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Rb-E2F complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Rb-E2F complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From Biocarta Pathways

proteins participating in the pkc-catalyzed phosphorylation of inhibitory phosphoprotein of myosin phosphatase pathway from the Biocarta Pathways dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term phosphoprotein in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of phosphoprotein phosphatase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of phosphoprotein phosphatase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of phosphoprotein phosphatase activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphoprotein binding molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the phosphoprotein phosphatase activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Casein kinase substrate, phosphoprotein PP28 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the U2A'/phosphoprotein 32 family A, C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Golgi phosphoprotein 3 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Dopamine/cAMP-regulated neuronal phosphoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Astrocytic phosphoprotein PEA-15 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Nuclear phosphoprotein p8, DNA binding protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Secreted phosphoprotein 24 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Vasodilator-stimulated phosphoprotein protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the M-phase phosphoprotein 6 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the M-phase phosphoprotein 9 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the MKI67 FHA domain-interacting nucleolar phosphoprotein, FHA Ki67 binding protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of phosphoprotein phosphatase activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of phosphoprotein phosphatase activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of phosphoprotein phosphatase activity biological process from the curated GO Biological Process Annotations 2023 dataset.