Reactome | UniProt:Q01094 E2F1

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UniProt:Q01094 E2F1 Show undefined attributes

chain	chain:1-437
checksum	003B3F654F0C60DF
comment	FUNCTION Transcription 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 (PubMed:10675335, PubMed:12717439, PubMed:17050006, PubMed:17704056, PubMed:18625225, PubMed:28992046). The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase (PubMed:10675335, PubMed:12717439, PubMed:17704056). E2F1 binds preferentially RB1 in a cell-cycle dependent manner (PubMed:10675335, PubMed:12717439, PubMed:17704056). It can mediate both cell proliferation and TP53/p53-dependent apoptosis (PubMed:8170954). Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:20176812). Directly activates transcription of PEG10 (PubMed:17050006, PubMed:18625225, PubMed:28992046). Positively regulates transcription of RRP1B (PubMed:20040599).ACTIVITY REGULATION BIRC2/c-IAP1 stimulates its transcriptional activity.SUBUNIT Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F1 complex binds specifically hypophosphorylated RB1, the interaction represses E2F1-driven transcription (PubMed:8336704). During the cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex, rendering E2F transcriptionally active. Viral oncoproteins, notably E1A, T-antigen and HPV E7, are capable of sequestering RB1, thus releasing the active complex. Interacts with TRRAP, which probably mediates its interaction with histone acetyltransferase complexes, leading to transcription activation. Binds TOPBP1 and EAPP. Interacts with ARID3A. Interacts with TRIM28; the interaction inhibits E2F1 acetylation through recruiting HDAC1 and represses its transcriptional activity. Interaction with KAT2B; the interaction acetylates E2F1 enhancing its DNA-binding and transcriptional activity. Interacts with BIRC2/c-IAP1 (via BIR domains). The complex TFDP1:E2F1 interacts with CEBPA; the interaction prevents CEBPA binding to target genes promoters and represses its transcriptional activity (PubMed:20176812). Interacts with RRP1B (PubMed:20040599). Interacts with HCFC1 (PubMed:23629655). Interacts with KMT2E; the interaction is probably indirect and is mediated via HCFC1 (PubMed:23629655). Interacts with DCAF5 and L3MBTL3; the interaction requires methylation at Lys-185 and is necessary to target E2F1 for ubiquitination by the CRL4-DCAF5 E3 ubiquitin ligase complex (PubMed:29691401).SUBUNIT (Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL123.INTERACTION Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase (PubMed:12717439, PubMed:7838523). Phosphorylation at Ser-364 by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis (PubMed:12717439). Phosphorylation at Ser-403 by GSK3B promotes interaction with USP11, leading to its deubiquitination and stabilization (PubMed:28992046).PTM Ubiquitinated via 'Lys-63'-linked ubiquitin, leading to its degradation (PubMed:28992046). Deubiquitinated by USP11 following phosphorylation by GSK3B, promoting its stability (PubMed:28992046).PTM Acetylation stimulates DNA-binding. Enhanced under stress conditions such as DNA damage and inhibited by retinoblastoma protein RB1. Regulated by KAP1/TRIM28 which recruits HDAC1 to E2F1 resulting in deacetylation. Acetylated by P/CAF/KAT2B.PTM Methylation at Lys-185 by SETD7 promotes E2F1 ubiquitin-dependent proteasomal degradation.SIMILARITY Belongs to the E2F/DP family.SEQUENCE CAUTION Extended N-terminus.
crossReference	[DatabaseIdentifier:11503887] ENSEMBL:ENSG00000101412 [DatabaseIdentifier:12436997] RefSeq:NP_005216.1 [DatabaseIdentifier:12294780] Pharos - Targets:Q01094 [DatabaseIdentifier:12257290] PRO:Q01094 [DatabaseIdentifier:12165849] PDB:9CB3 [DatabaseIdentifier:12142218] PDB:5M9O [DatabaseIdentifier:12213166] PDB:2AZE [DatabaseIdentifier:12224258] PDB:6ULS [DatabaseIdentifier:12162099] PDB:5M9N [DatabaseIdentifier:12224237] PDB:6G0P [DatabaseIdentifier:12191495] PDB:1H24 [DatabaseIdentifier:12215432] PDB:1O9K [DatabaseIdentifier:12134618] OpenTargets:ENSG00000101412 [DatabaseIdentifier:11615660] ENSEMBL:ENSP00000345571 [DatabaseIdentifier:11738359] ENSEMBL:ENST00000343380 [DatabaseIdentifier:11796951] GeneCards:E2F1 [DatabaseIdentifier:11849917] HPA:ENSG00000101412-E2F1
databaseName	UniProt
dbId	89561
description	recommendedName: fullName evidence="31"Transcription factor E2F1 shortName evidence="31"E2F-1 alternativeName: PBR3 alternativeName: fullName evidence="30"Retinoblastoma-associated protein 1 shortName evidence="30"RBAP-1 alternativeName: fullName evidence="29"Retinoblastoma-binding protein 3 shortName evidence="29"RBBP-3 alternativeName: pRB-binding protein E2F-1
displayName	UniProt:Q01094 E2F1
geneName	E2F1 RBBP3
identifier	Q01094
isSequenceChanged	false
keyword	3D-structure Acetylation Activator Apoptosis Cell cycle DNA-binding Host-virus interaction Methylation Nucleus Phosphoprotein Proteomics identification Reference proteome Transcription Transcription regulation Ubl conjugation
modified	[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
moleculeType	Protein
name	E2F1
otherIdentifier	11723713_at 1322_at 16918445 1869 2028_PM_s_at 2028_s_at 204947_PM_at 204947_at 3903124 3903125 3903126 3903147 3903148 3903149 3903150 3903151 3903153 3903154 3903155 3903157 3903158 3903159 3903161 3903162 3903163 3903164 8065710 A_23_P80032 GE60538 GO:0000077 GO:0000122 GO:0000228 GO:0000785 GO:0000976 GO:0000978 GO:0000981 GO:0000987 GO:0001216 GO:0003677 GO:0003700 GO:0005515 GO:0005634 GO:0005654 GO:0005667 GO:0005694 GO:0005737 GO:0005813 GO:0005815 GO:0006351 GO:0006355 GO:0006357 GO:0006915 GO:0007283 GO:0008630 GO:0010628 GO:0019805 GO:0019901 GO:0022414 GO:0030900 GO:0032496 GO:0032991 GO:0035189 GO:0043065 GO:0043276 GO:0043392 GO:0043565 GO:0045599 GO:0045892 GO:0045893 GO:0045944 GO:0046983 GO:0048146 GO:0048255 GO:0048856 GO:0051726 GO:0060090 GO:0060252 GO:0070345 GO:0071398 GO:0071456 GO:0071466 GO:0072332 GO:0090575 GO:0140297 GO:1990086 GO:1990090 GO:1990837 GO:2000045 HMNXSV003055600 ILMN_2051469 PH_hs_0005226 S49592_s_at TC20000773.hg U47677_at g12669910_3p_s_at
physicalEntity	[EntityWithAccessionedSequence:R-HSA-68639] E2F1 [nucleoplasm] - Homo sapiens [EntityWithAccessionedSequence:R-HSA-187911] p-E2F1 [nucleoplasm] - Homo sapiens
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:12083386] NCBI Gene:1869 E2F1 [ReferenceDNASequence:12759285] UCSC:Q01094 E2F1 [ReferenceDNASequence:12118782] OMIM:189971 E2F1 [ReferenceDNASequence:ensembl:ENSG00000101412] ENSEMBL:ENSG00000101412 E2F1 [ReferenceDNASequence:11369504] BioGPS Gene:1869 E2F1 [ReferenceDNASequence:11402318] COSMIC - genes:E2F1 E2F1 [ReferenceDNASequence:11426321] CTD Gene:1869 E2F1 [ReferenceDNASequence:11439784] dbSNP Gene:1869 E2F1 [ReferenceDNASequence:11828666] HGNC:3113 E2F1 [ReferenceDNASequence:11907704] KEGG:hsa:1869 E2F1 [ReferenceDNASequence:11999293] Monarch:1869 E2F1
referenceTranscript	[ReferenceRNASequence:12618507] RefSeq:NM_005225.3 E2F1
schemaClass	ReferenceGeneProduct
secondaryIdentifier	E2F1_HUMAN Q13143 Q92768
sequenceLength	437
species	[Species:48887] Homo sapiens
stId	uniprot:Q01094
url	http://purl.uniprot.org/uniprot/Q01094

Referrals

(referenceEntity)	[EntityWithAccessionedSequence:R-HSA-68639] E2F1 [nucleoplasm] [EntityWithAccessionedSequence:R-HSA-187911] p-E2F1 [nucleoplasm]
(referenceSequence)	[ModifiedResidue:187923] phosphorylated residue at unknown position
(interactor)	[UndirectedInteraction:11131871] UniProt:Q14188 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11146257] UniProt:P06400 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11149873] UniProt:Q14186 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11152603] UniProt:P31749 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11165555] UniProt:P09874 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11180859] UniProt:Q9Y618 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11195615] UniProt:P51532 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11199511] UniProt:Q8NEM0 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11220281] UniProt:Q92466 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11240285] UniProt:O14744 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11241003] UniProt:Q96EB6 <-> UniProt:Q01094 (IntAct) [UndirectedInteraction:11244461] UniProt:Q01094 <-> UniProt:P03129 (IntAct) [UndirectedInteraction:11244463] UniProt:Q01094 <-> UniProt:Q92547 (IntAct) [UndirectedInteraction:11244465] UniProt:Q01094 <-> UniProt:Q92830 (IntAct) [UndirectedInteraction:11244467] UniProt:Q01094 <-> UniProt:Q14684 (IntAct) [UndirectedInteraction:11244469] UniProt:Q01094 <-> UniProt:Q92831 (IntAct) [UndirectedInteraction:11244473] UniProt:Q01094 <-> UniProt:Q14201 (IntAct) [UndirectedInteraction:11244475] UniProt:Q01094 <-> UniProt:Q13547 (IntAct) [UndirectedInteraction:11244477] UniProt:Q01094 <-> UniProt:Q96JM7 (IntAct) [UndirectedInteraction:11244479] UniProt:Q01094 <-> UniProt:P28749 (IntAct) [UndirectedInteraction:11244481] UniProt:Q01094 <-> UniProt:P05067 (IntAct) [UndirectedInteraction:11244485] UniProt:Q01094 <-> IntAct:EBI-2549087 (IntAct) [UndirectedInteraction:11244489] UniProt:Q01094 <-> IntAct:EBI-5279495 (IntAct) [UndirectedInteraction:11244493] UniProt:Q01094 <-> IntAct:EBI-2549104 (IntAct) [UndirectedInteraction:11244497] UniProt:Q01094 <-> IntAct:EBI-2549096 (IntAct) [UndirectedInteraction:11244501] UniProt:Q01094 <-> IntAct:EBI-20620429 (IntAct) [UndirectedInteraction:11244503] UniProt:Q01094 <-> UniProt:Q96IZ0 (IntAct) [UndirectedInteraction:11244505] UniProt:Q01094 <-> UniProt:P42224 (IntAct) [UndirectedInteraction:11244507] UniProt:Q01094 <-> UniProt:Q923E4 (IntAct) [UndirectedInteraction:11244509] UniProt:Q01094 <-> UniProt:Q9UPP1 (IntAct) [UndirectedInteraction:11244511] UniProt:Q01094 <-> UniProt:Q86X55 (IntAct)