Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor E2F1

Gene

E2F1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:20176812). Positively regulates transcription of RRP1B (PubMed:20040599).By similarity6 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

BIRC2/c-IAP1 stimulates its transcriptional activity.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi110 – 194Sequence analysisAdd BLAST85

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding
Biological processApoptosis, Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-111448 Activation of NOXA and translocation to mitochondria
R-HSA-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex
R-HSA-1362300 Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1
R-HSA-139915 Activation of PUMA and translocation to mitochondria
R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-539107 Activation of E2F1 target genes at G1/S
R-HSA-6804116 TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest
R-HSA-68689 CDC6 association with the ORC:origin complex
R-HSA-68911 G2 Phase
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69231 Cyclin D associated events in G1
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-8953750 Transcriptional Regulation by E2F6

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q01094

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q01094

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Transcription factor E2F1
Short name:
E2F-1
Alternative name(s):
PBR3
Retinoblastoma-associated protein 1
Short name:
RBAP-1
Retinoblastoma-binding protein 3
Short name:
RBBP-3
pRB-binding protein E2F-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:E2F1
Synonyms:RBBP3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000101412.12

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3113 E2F1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
189971 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q01094

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi117K → R: Abolishes acetylation; when associated with R-120 and R-125. 1 Publication1
Mutagenesisi120K → R: Abolishes acetylation; when associated with R-117 and R-125. 1 Publication1
Mutagenesisi125K → R: Abolishes acetylation; when associated with R-117 and R-120. 1 Publication1
Mutagenesisi132L → E: Abolishes interaction with and repression of CEBPA and inhibition of adipogenesis. 1 Publication1
Mutagenesisi364S → A: Abrogates in vitro phosphorylation by CHEK2 and CHEK2-dependent stabilization of E2F1 upon DNA damage. 1 Publication1
Mutagenesisi411Y → C: No retinoblastoma protein binding. No effect on interaction with and repression of CEBPA. 2 Publications1

Organism-specific databases

DisGeNET

More...
DisGeNETi
1869

Open Targets

More...
OpenTargetsi
ENSG00000101412

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA152

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4382

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
E2F1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
400928

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002194611 – 437Transcription factor E2F1Add BLAST437

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei117N6-acetyllysine1 Publication1
Modified residuei120N6-acetyllysine1 Publication1
Modified residuei125N6-acetyllysine1 Publication1
Modified residuei364Phosphoserine; by CHEK21 Publication1
Modified residuei375PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase. Phosphorylation at Ser-364 by CHEK2 stabilizes E2F1 upon DNA damage and regulates its effect on transcription and apoptosis.2 Publications
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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q01094

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q01094

PeptideAtlas

More...
PeptideAtlasi
Q01094

PRoteomics IDEntifications database

More...
PRIDEi
Q01094

ProteomicsDB human proteome resource

More...
ProteomicsDBi
57915

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01094

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q01094

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000101412 Expressed in 165 organ(s), highest expression level in secondary oocyte

CleanEx database of gene expression profiles

More...
CleanExi
HS_E2F1

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q01094 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB000329
CAB019308
HPA008003
HPA029735

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the DRTF1/E2F transcription factor complex. Forms heterodimers with DP family members. The E2F1 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. 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).By similarity12 Publications
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL123.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
108201, 120 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-155 RB1-E2F1-TFDP1 transcription repressor complex
CPX-1971 E2F1-DP1 transcription factor complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q01094

Database of interacting proteins

More...
DIPi
DIP-24227N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q01094

Protein interaction database and analysis system

More...
IntActi
Q01094, 45 interactors

Molecular INTeraction database

More...
MINTi
Q01094

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000345571

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q01094

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q01094

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q01094

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni67 – 108Cyclin A:CDK2 binding1 PublicationAdd BLAST42
Regioni89 – 191Interaction with BIRC2/c-IAP11 PublicationAdd BLAST103
Regioni153 – 174Leucine-zipperAdd BLAST22
Regioni192 – 382Required for interaction with TRIM281 PublicationAdd BLAST191
Regioni195 – 284DimerizationSequence analysisAdd BLAST90
Regioni368 – 437TransactivationAdd BLAST70
Regioni409 – 426RB1 binding1 PublicationAdd BLAST18

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi158 – 194DEF boxAdd BLAST37

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2577 Eukaryota
ENOG410XNYI LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000159472

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000232045

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG002227

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q01094

KEGG Orthology (KO)

More...
KOi
K17454

Identification of Orthologs from Complete Genome Data

More...
OMAi
VRCQDLR

Database of Orthologous Groups

More...
OrthoDBi
EOG091G087U

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q01094

TreeFam database of animal gene trees

More...
TreeFami
TF105566

Family and domain databases

Conserved Domains Database

More...
CDDi
cd14660 E2F_DD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015633 E2F
IPR037241 E2F-DP_heterodim
IPR032198 E2F_CC-MB
IPR003316 E2F_WHTH_DNA-bd_dom
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

The PANTHER Classification System

More...
PANTHERi
PTHR12081 PTHR12081, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16421 E2F_CC-MB, 1 hit
PF02319 E2F_TDP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01372 E2F_TDP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF144074 SSF144074, 1 hit
SSF46785 SSF46785, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q01094-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALAGAPAGG PCAPALEALL GAGALRLLDS SQIVIISAAQ DASAPPAPTG
60 70 80 90 100
PAAPAAGPCD PDLLLFATPQ APRPTPSAPR PALGRPPVKR RLDLETDHQY
110 120 130 140 150
LAESSGPARG RGRHPGKGVK SPGEKSRYET SLNLTTKRFL ELLSHSADGV
160 170 180 190 200
VDLNWAAEVL KVQKRRIYDI TNVLEGIQLI AKKSKNHIQW LGSHTTVGVG
210 220 230 240 250
GRLEGLTQDL RQLQESEQQL DHLMNICTTQ LRLLSEDTDS QRLAYVTCQD
260 270 280 290 300
LRSIADPAEQ MVMVIKAPPE TQLQAVDSSE NFQISLKSKQ GPIDVFLCPE
310 320 330 340 350
ETVGGISPGK TPSQEVTSEE ENRATDSATI VSPPPSSPPS SLTTDPSQSL
360 370 380 390 400
LSLEQEPLLS RMGSLRAPVD EDRLSPLVAA DSLLEHVRED FSGLLPEEFI
410 420 430
SLSPPHEALD YHFGLEEGEG IRDLFDCDFG DLTPLDF
Length:437
Mass (Da):46,920
Last modified:July 1, 1993 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i003B3F654F0C60DF
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB24289 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti89 – 111KRRLD…PARGR → RTPGTPRRQRRLCPPRRPGR APC in AAD14150 (PubMed:7958836).CuratedAdd BLAST23
Sequence conflicti313S → Y in AAC50719 (PubMed:8964493).Curated1
Sequence conflicti322N → T in AAC50719 (PubMed:8964493).Curated1
Sequence conflicti329T → N in AAC50719 (PubMed:8964493).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_048907200G → S. Corresponds to variant dbSNP:rs35385772Ensembl.1
Natural variantiVAR_013607252R → H1 PublicationCorresponds to variant dbSNP:rs3213172Ensembl.1
Natural variantiVAR_013608276V → M1 PublicationCorresponds to variant dbSNP:rs3213173Ensembl.1
Natural variantiVAR_013609311T → N1 PublicationCorresponds to variant dbSNP:rs3213174Ensembl.1
Natural variantiVAR_013610393G → S1 PublicationCorresponds to variant dbSNP:rs3213176Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M96577 mRNA Translation: AAA35782.1
U47677, U47675, U47676 Genomic DNA Translation: AAC50719.1
S49592 mRNA Translation: AAB24289.1 Different initiation.
AF516106 Genomic DNA Translation: AAM47604.1
AL121906 Genomic DNA No translation available.
BC050369 mRNA Translation: AAH50369.1
BC058902 mRNA Translation: AAH58902.1
S74230 Genomic DNA Translation: AAD14150.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13224.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC4929

NCBI Reference Sequences

More...
RefSeqi
NP_005216.1, NM_005225.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.654393

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000343380; ENSP00000345571; ENSG00000101412

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1869

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1869

UCSC genome browser

More...
UCSCi
uc002wzu.5 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96577 mRNA Translation: AAA35782.1
U47677, U47675, U47676 Genomic DNA Translation: AAC50719.1
S49592 mRNA Translation: AAB24289.1 Different initiation.
AF516106 Genomic DNA Translation: AAM47604.1
AL121906 Genomic DNA No translation available.
BC050369 mRNA Translation: AAH50369.1
BC058902 mRNA Translation: AAH58902.1
S74230 Genomic DNA Translation: AAD14150.1
CCDSiCCDS13224.1
PIRiJC4929
RefSeqiNP_005216.1, NM_005225.2
UniGeneiHs.654393

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H24X-ray2.50E87-95[»]
1O9KX-ray2.60P/Q/R/S409-426[»]
2AZEX-ray2.55B200-301[»]
5M9NX-ray1.95C104-120[»]
5M9OX-ray1.45B108-116[»]
ProteinModelPortaliQ01094
SMRiQ01094
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108201, 120 interactors
ComplexPortaliCPX-155 RB1-E2F1-TFDP1 transcription repressor complex
CPX-1971 E2F1-DP1 transcription factor complex
CORUMiQ01094
DIPiDIP-24227N
ELMiQ01094
IntActiQ01094, 45 interactors
MINTiQ01094
STRINGi9606.ENSP00000345571

Chemistry databases

ChEMBLiCHEMBL4382

PTM databases

iPTMnetiQ01094
PhosphoSitePlusiQ01094

Polymorphism and mutation databases

BioMutaiE2F1
DMDMi400928

Proteomic databases

MaxQBiQ01094
PaxDbiQ01094
PeptideAtlasiQ01094
PRIDEiQ01094
ProteomicsDBi57915

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343380; ENSP00000345571; ENSG00000101412
GeneIDi1869
KEGGihsa:1869
UCSCiuc002wzu.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1869
DisGeNETi1869
EuPathDBiHostDB:ENSG00000101412.12

GeneCards: human genes, protein and diseases

More...
GeneCardsi
E2F1
HGNCiHGNC:3113 E2F1
HPAiCAB000329
CAB019308
HPA008003
HPA029735
MIMi189971 gene
neXtProtiNX_Q01094
OpenTargetsiENSG00000101412
PharmGKBiPA152

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2577 Eukaryota
ENOG410XNYI LUCA
GeneTreeiENSGT00940000159472
HOGENOMiHOG000232045
HOVERGENiHBG002227
InParanoidiQ01094
KOiK17454
OMAiVRCQDLR
OrthoDBiEOG091G087U
PhylomeDBiQ01094
TreeFamiTF105566

Enzyme and pathway databases

ReactomeiR-HSA-111448 Activation of NOXA and translocation to mitochondria
R-HSA-113501 Inhibition of replication initiation of damaged DNA by RB1/E2F1
R-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex
R-HSA-1362300 Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1
R-HSA-139915 Activation of PUMA and translocation to mitochondria
R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559585 Oncogene Induced Senescence
R-HSA-539107 Activation of E2F1 target genes at G1/S
R-HSA-6804116 TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest
R-HSA-68689 CDC6 association with the ORC:origin complex
R-HSA-68911 G2 Phase
R-HSA-69202 Cyclin E associated events during G1/S transition
R-HSA-69231 Cyclin D associated events in G1
R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
R-HSA-8953750 Transcriptional Regulation by E2F6
SignaLinkiQ01094
SIGNORiQ01094

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
E2F1 human
EvolutionaryTraceiQ01094

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
E2F1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1869

Protein Ontology

More...
PROi
PR:Q01094

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000101412 Expressed in 165 organ(s), highest expression level in secondary oocyte
CleanExiHS_E2F1
GenevisibleiQ01094 HS

Family and domain databases

CDDicd14660 E2F_DD, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR015633 E2F
IPR037241 E2F-DP_heterodim
IPR032198 E2F_CC-MB
IPR003316 E2F_WHTH_DNA-bd_dom
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR12081 PTHR12081, 1 hit
PfamiView protein in Pfam
PF16421 E2F_CC-MB, 1 hit
PF02319 E2F_TDP, 1 hit
SMARTiView protein in SMART
SM01372 E2F_TDP, 1 hit
SUPFAMiSSF144074 SSF144074, 1 hit
SSF46785 SSF46785, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiE2F1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q01094
Secondary accession number(s): Q13143, Q92768
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: December 5, 2018
This is version 217 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again