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E2F1 (human)

Overview E2F1 a member of the E2F/DP 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. Binds DNA cooperatively with Dp transcription factors in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication.The Dp-1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. The E2F-1 complex binds specifically hypophosphorylated retinoblastoma protein RB1. During the cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex, rendering E2F transcriptionally active. Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase. It can mediate both cell proliferation and p53-dependent apoptosis. Note: This description may include information from UniProtKB. Protein type: Transcription factor; DNA binding protein Cellular Component: nucleoplasm; Rb-E2F complex; cytoplasm; nucleus Molecular Function: protein binding; DNA binding; sequence-specific DNA binding; transcription factor activity; transcription corepressor activity; transcription factor binding Biological Process: transcription, DNA-dependent; apoptosis; mRNA stabilization; positive regulation of transcription, DNA-dependent; negative regulation of transcription from RNA polymerase II promoter; G2 phase of mitotic cell cycle; cell proliferation; positive regulation of fibroblast proliferation; regulation of transcription, DNA-dependent; DNA damage checkpoint; forebrain development; positive regulation of transcription from RNA polymerase II promoter; spermatogenesis; mitotic cell cycle; G1 phase of mitotic cell cycle; negative regulation of transcription, DNA-dependent; G1/S transition of mitotic cell cycle Reference #:  Q01094 (UniProtKB) Alt. Names/Synonyms: E2F transcription factor 1; E2F-1; E2F1; PBR3; PRB-binding protein E2F-1; RBAP-1; RBAP1; RBBP-3; RBBP3; RBP3; Retinoblastoma-associated protein 1; Retinoblastoma-binding protein 3; Transcription factor E2F1 Gene Symbols: E2F1 Molecular weight: 46,920 Da Basal Isoelectric point: 4.79  Predict pI for various phosphorylation states CST Pathways:  Cell Cycle: G1/S Checkpoint  |  ErbB/HER Signaling Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below E2F1 1H24 - E=87-95 (human) 1O9K - P/Q/R/S=409-426 (human) 2AZE - B=200-301 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1H24 1O9K 2AZE  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
apoptosis, induced: S364‑p cell cycle regulation: S332‑p, S337‑p cell differentiation, altered: S403‑p, T433‑p transcription, altered: S364‑p, S403‑p transcription, inhibited: S375‑p intracellular localization: S364‑p, S403‑p, T433‑p molecular association, regulation: S332‑p, S337‑p protein degradation: S403‑p, T433‑p protein stabilization: S31‑p, S364‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
2	0		S31-p	ALRLLDSsQIVIISA
0	1		Y100	DLETDHQYLAESSGP
3	0		K117-a	GRGRHPGkGVkSPGE
3	0		K120-a	RHPGkGVkSPGEkSR
3	0		K125-a	GVkSPGEkSRYETSL
0	1		T135-p	YETSLNLttKRFLEL
0	1		T136-p	ETSLNLttKRFLELL
1	0		K185-m1	QLIAKKSkNHIQWLG
2	0		S332-p	TDSATIVsPPPSsPP
2	0		S337-p	IVsPPPSsPPSSLTT
3	0		S364-p	PLLSRMGsLRAPVDE
2	2		S375-p	PVDEDRLsPLVAADS
5	0		S403-p	PEEFISLsPPHEALD
3	0		T433-p	DCDFGDLtPLDF___

	mouse
S29	ALRLLDSSQIVIIST
Y95	DLETDHQYLAGSSGP
K112	GRGRHPGKGVKSPGE
K115	RHPGKGVKSPGEKSR
K120	GVKSPGEKSRYETSL
T130	YETSLNLTTKRFLEL
T131	ETSLNLTTKRFLELL
K180	QLIAKKSKNHIQWLG
G325	TADSGPAGPPPSPPS
P330	PAGPPPSPPSTSPAL
H357	AVLPRMGHLRVPMEE
S368	PMEEDQLSPLVAADS
S396	PGEFISLSPPHEALD
T426	DCDFGDLTPLDF___

	rat
S29	ALRLLDSSQIVIIST
Y98-p	DLETDHQyLAGSSGP
K115	GRGRHPGKGVKSPGE
K118	RHPGKGVKSPGEKSR
K123	GVKSPGEKSRYETSL
T133	YETSLNLTTKRFLEL
T134	ETSLNLTTKRFLELL
K183	QLIAKKSKNHIQWLG
G327	NADSGTAGPPPSPPS
P332	TAGPPPSPPSTSPTL
N359	AVLPRIGNLRAPMEE
S370	PMEEDRLSPLVAADS
S398	PGEFISLSPPHEAVD
T428	DCDFGDLTPLDF___

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