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Protein

Transcription factor Dp-1

Gene

TFDP1

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

Can stimulate E2F-dependent transcription. Binds DNA cooperatively with E2F family members 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:8405995, PubMed:7739537). The E2F1:DP complex appears to mediate both cell proliferation and apoptosis. Blocks adipocyte differentiation by repressing CEBPA binding to its target gene promoters (PubMed:20176812).3 Publications

Miscellaneous

E2F/DP transactivation can be mediated by several cofactors including TBP, TFIIH, MDM2 and CBP.

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 bindingi113 – 195Sequence analysisAdd BLAST83

<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 processCell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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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-1538133 G0 and Early G1
R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
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-6804114 TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
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

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q14186

<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 Dp-1
Alternative name(s):
DRTF1-polypeptide 1
Short name:
DRTF1
E2F dimerization partner 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:TFDP1
Synonyms:DP1
<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 13

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000198176.12

Human Gene Nomenclature Database

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HGNCi
HGNC:11749 TFDP1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
189902 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q14186

<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

Cytoplasm, 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

Organism-specific databases

DisGeNET

More...
DisGeNETi
7027

Open Targets

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OpenTargetsi
ENSG00000198176

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36464

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TFDP1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
3122926

<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_00002194751 – 410Transcription factor Dp-1Add BLAST410

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 residuei3N6-acetyllysineCombined sources1
Modified residuei23PhosphoserineCombined 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

Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase, inhibits E2F-mediated DNA binding and transactivation.1 Publication
Ubiquitinated by the BCR(KBTBD5) complex, leading to its subsequent degradation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q14186

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q14186

MaxQB - The MaxQuant DataBase

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MaxQBi
Q14186

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

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PaxDbi
Q14186

PeptideAtlas

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PeptideAtlasi
Q14186

PRoteomics IDEntifications database

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PRIDEi
Q14186

ProteomicsDB human proteome resource

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ProteomicsDBi
59904

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q14186

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

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PhosphoSitePlusi
Q14186

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highest levels in muscle. Also expressed in brain, placenta, liver and kidney. Lower levels in lung and pancreas. Not detected in heart.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated during differentiation.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000198176 Expressed in 235 organ(s), highest expression level in trabecular bone tissue

CleanEx database of gene expression profiles

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CleanExi
HS_TFDP1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q14186 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q14186 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB033605
HPA044754
HPA068909

<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 E2F:DP transcription factor complex. Forms heterodimers with E2F family members. The complex can interact with hypophosphorylated retinoblastoma protein RB1 and related proteins (RBL1 and RBL2) that inhibit the E2F transactivation domain. This repression involves recruitment of histone deacetylase (HDAC). During the cell cycle, from mid-to-late G1 phase, RB family members become phosphorylated, detach from the DRTF1/E2F complex to render E2F transcriptionally active. Viral oncoproteins, notably E1A, T-antigen and HPV E7, are capable of sequestering RB protein, thus releasing the active complex. Part of the E2F6.com-1 complex in G0 phase is composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 YAF2. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. The complex TFDP1:E2F1 interacts with CEBPA; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (PubMed:20176812).5 Publications

<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)

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BioGridi
112885, 73 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-155 RB1-E2F1-TFDP1 transcription repressor complex
CPX-175 RB1-E2F2-TFDP1 transcription repressor complex
CPX-1971 E2F1-DP1 transcription factor complex
CPX-1972 E2F2-DP1 transcription factor complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q14186

Database of interacting proteins

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DIPi
DIP-238N

Protein interaction database and analysis system

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IntActi
Q14186, 67 interactors

Molecular INTeraction database

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MINTi
Q14186

STRING: functional protein association networks

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STRINGi
9606.ENSP00000364519

<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

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AZEX-ray2.55A199-350[»]
5GOWNMR-A392-410[»]
5TUUX-ray2.25A199-350[»]
5TUVX-ray2.90A/D199-350[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q14186

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

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SMRi
Q14186

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q14186

<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>Regioni105 – 127Interaction with CEBPA1 PublicationAdd BLAST23
Regioni204 – 277DimerizationSequence analysisAdd BLAST74
Regioni211 – 327Enhances binding of RB protein to E2FAdd BLAST117
Regioni214 – 246DCB1Add BLAST33
Regioni259 – 315DCB2Add BLAST57

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>Motifi161 – 195DEF boxAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi250 – 253Poly-Pro4
Compositional biasi394 – 410Asp/Glu-rich (acidic; NCB domain)Add BLAST17

<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

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eggNOGi
KOG2829 Eukaryota
ENOG410Y9QP LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154652

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000030696

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG009894

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q14186

KEGG Orthology (KO)

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KOi
K04683

Identification of Orthologs from Complete Genome Data

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OMAi
LEVGKCS

Database of Orthologous Groups

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OrthoDBi
1185408at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q14186

TreeFam database of animal gene trees

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TreeFami
TF314396

Family and domain databases

Conserved Domains Database

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CDDi
cd14458 DP_DD, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.10, 1 hit
1.20.140.80, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR028313 DP-1
IPR037241 E2F-DP_heterodim
IPR003316 E2F_WHTH_DNA-bd_dom
IPR038168 TF_DP_C_sf
IPR014889 Transc_factor_DP_C
IPR015648 Transcrpt_fac_DP
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

The PANTHER Classification System

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PANTHERi
PTHR12548 PTHR12548, 1 hit
PTHR12548:SF4 PTHR12548:SF4, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF08781 DP, 1 hit
PF02319 E2F_TDP, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF009404 Transcription_factor_DP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01138 DP, 1 hit
SM01372 E2F_TDP, 1 hit

Superfamily database of structural and functional annotation

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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>Sequences (2+)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q14186-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAKDAGLIEA NGELKVFIDQ NLSPGKGVVS LVAVHPSTVN PLGKQLLPKT
60 70 80 90 100
FGQSNVNIAQ QVVIGTPQRP AASNTLVVGS PHTPSTHFAS QNQPSDSSPW
110 120 130 140 150
SAGKRNRKGE KNGKGLRHFS MKVCEKVQRK GTTSYNEVAD ELVAEFSAAD
160 170 180 190 200
NHILPNESAY DQKNIRRRVY DALNVLMAMN IISKEKKEIK WIGLPTNSAQ
210 220 230 240 250
ECQNLEVERQ RRLERIKQKQ SQLQELILQQ IAFKNLVQRN RHAEQQASRP
260 270 280 290 300
PPPNSVIHLP FIIVNTSKKT VIDCSISNDK FEYLFNFDNT FEIHDDIEVL
310 320 330 340 350
KRMGMACGLE SGSCSAEDLK MARSLVPKAL EPYVTEMAQG TVGGVFITTA
360 370 380 390 400
GSTSNGTRFS ASDLTNGADG MLATSSNGSQ YSGSRVETPV SYVGEDDEED
410
DDFNENDEDD
Length:410
Mass (Da):45,070
Last modified:November 1, 1996 - 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:i3FEEFE1E49FD9ED0
GO
Isoform 2 (identifier: Q14186-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: MAKDAGLIEA...PSDSSPWSAG → MSTLPSKW
     358-361: Missing.

Note: No experimental confirmation available.
Show »
Length:311
Mass (Da):34,921
Checksum:i09377262F3D36A99
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5JSB5Q5JSB5_HUMAN
Transcription factor Dp-1
TFDP1
235Annotation score:

Annotation score:2 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>
Q5JSB6Q5JSB6_HUMAN
Transcription factor Dp-1
TFDP1
158Annotation score:

Annotation score:2 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>
F5H452F5H452_HUMAN
Transcription factor Dp-1
TFDP1
119Annotation score:

Annotation score:1 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>

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_029293401D → N. Corresponds to variant dbSNP:rs4150823Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0564991 – 103MAKDA…PWSAG → MSTLPSKW in isoform 2. 1 PublicationAdd BLAST103
Alternative sequenceiVSP_056500358 – 361Missing in isoform 2. 1 Publication4

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L23959 mRNA Translation: AAA58440.1
AK297114 mRNA Translation: BAG59621.1
AL442125 Genomic DNA No translation available.
CH471085 Genomic DNA Translation: EAX09216.1
BC011685 mRNA Translation: AAH11685.1
AF550129 Genomic DNA Translation: AAN46090.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS9538.1 [Q14186-1]

Protein sequence database of the Protein Information Resource

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PIRi
A48585

NCBI Reference Sequences

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RefSeqi
NP_009042.1, NM_007111.4 [Q14186-1]
XP_005268384.1, XM_005268327.1 [Q14186-1]
XP_005268388.1, XM_005268331.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.79353

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000375370; ENSP00000364519; ENSG00000198176 [Q14186-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
7027

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:7027

UCSC genome browser

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UCSCi
uc001vtw.4 human [Q14186-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23959 mRNA Translation: AAA58440.1
AK297114 mRNA Translation: BAG59621.1
AL442125 Genomic DNA No translation available.
CH471085 Genomic DNA Translation: EAX09216.1
BC011685 mRNA Translation: AAH11685.1
AF550129 Genomic DNA Translation: AAN46090.1
CCDSiCCDS9538.1 [Q14186-1]
PIRiA48585
RefSeqiNP_009042.1, NM_007111.4 [Q14186-1]
XP_005268384.1, XM_005268327.1 [Q14186-1]
XP_005268388.1, XM_005268331.1
UniGeneiHs.79353

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AZEX-ray2.55A199-350[»]
5GOWNMR-A392-410[»]
5TUUX-ray2.25A199-350[»]
5TUVX-ray2.90A/D199-350[»]
ProteinModelPortaliQ14186
SMRiQ14186
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112885, 73 interactors
ComplexPortaliCPX-155 RB1-E2F1-TFDP1 transcription repressor complex
CPX-175 RB1-E2F2-TFDP1 transcription repressor complex
CPX-1971 E2F1-DP1 transcription factor complex
CPX-1972 E2F2-DP1 transcription factor complex
CORUMiQ14186
DIPiDIP-238N
IntActiQ14186, 67 interactors
MINTiQ14186
STRINGi9606.ENSP00000364519

PTM databases

iPTMnetiQ14186
PhosphoSitePlusiQ14186

Polymorphism and mutation databases

BioMutaiTFDP1
DMDMi3122926

Proteomic databases

EPDiQ14186
jPOSTiQ14186
MaxQBiQ14186
PaxDbiQ14186
PeptideAtlasiQ14186
PRIDEiQ14186
ProteomicsDBi59904

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
7027
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375370; ENSP00000364519; ENSG00000198176 [Q14186-1]
GeneIDi7027
KEGGihsa:7027
UCSCiuc001vtw.4 human [Q14186-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7027
DisGeNETi7027
EuPathDBiHostDB:ENSG00000198176.12

GeneCards: human genes, protein and diseases

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GeneCardsi
TFDP1

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0002608
HIX0033825
HGNCiHGNC:11749 TFDP1
HPAiCAB033605
HPA044754
HPA068909
MIMi189902 gene
neXtProtiNX_Q14186
OpenTargetsiENSG00000198176
PharmGKBiPA36464

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2829 Eukaryota
ENOG410Y9QP LUCA
GeneTreeiENSGT00940000154652
HOGENOMiHOG000030696
HOVERGENiHBG009894
InParanoidiQ14186
KOiK04683
OMAiLEVGKCS
OrthoDBi1185408at2759
PhylomeDBiQ14186
TreeFamiTF314396

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-1538133 G0 and Early G1
R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
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-6804114 TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
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
SIGNORiQ14186

Miscellaneous databases

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

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ChiTaRSi
TFDP1 human
EvolutionaryTraceiQ14186

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
TFDP1

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

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GenomeRNAii
7027

Protein Ontology

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PROi
PR:Q14186

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000198176 Expressed in 235 organ(s), highest expression level in trabecular bone tissue
CleanExiHS_TFDP1
ExpressionAtlasiQ14186 baseline and differential
GenevisibleiQ14186 HS

Family and domain databases

CDDicd14458 DP_DD, 1 hit
Gene3Di1.10.10.10, 1 hit
1.20.140.80, 1 hit
InterProiView protein in InterPro
IPR028313 DP-1
IPR037241 E2F-DP_heterodim
IPR003316 E2F_WHTH_DNA-bd_dom
IPR038168 TF_DP_C_sf
IPR014889 Transc_factor_DP_C
IPR015648 Transcrpt_fac_DP
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR12548 PTHR12548, 1 hit
PTHR12548:SF4 PTHR12548:SF4, 1 hit
PfamiView protein in Pfam
PF08781 DP, 1 hit
PF02319 E2F_TDP, 1 hit
PIRSFiPIRSF009404 Transcription_factor_DP, 1 hit
SMARTiView protein in SMART
SM01138 DP, 1 hit
SM01372 E2F_TDP, 1 hit
SUPFAMiSSF144074 SSF144074, 1 hit
SSF46785 SSF46785, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiTFDP1_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: Q14186
Secondary accession number(s): B4DLQ9, Q5JSB4, Q8IZL5
<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 15, 1998
Last sequence update: November 1, 1996
Last modified: January 16, 2019
This is version 183 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
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