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Protein

Transcription factor Dp-1

Gene

TFDP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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
DNA bindingi113 – 195Sequence analysisAdd BLAST83

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • DNA binding transcription factor activity Source: ProtInc
  • protein domain specific binding Source: UniProtKB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • transcription coactivator activity Source: ProtInc
  • transcription factor binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding
Biological processCell cycle, Transcription, Transcription regulation

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

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor Dp-1
Alternative name(s):
DRTF1-polypeptide 1
Short name:
DRTF1
E2F dimerization partner 1
Gene namesi
Name:TFDP1
Synonyms:DP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

EuPathDBiHostDB:ENSG00000198176.12
HGNCiHGNC:11749 TFDP1
MIMi189902 gene
neXtProtiNX_Q14186

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi7027
OpenTargetsiENSG00000198176
PharmGKBiPA36464

Polymorphism and mutation databases

BioMutaiTFDP1
DMDMi3122926

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194751 – 410Transcription factor Dp-1Add BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N6-acetyllysineCombined sources1
Modified residuei23PhosphoserineCombined sources1

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

EPDiQ14186
MaxQBiQ14186
PaxDbiQ14186
PeptideAtlasiQ14186
PRIDEiQ14186

PTM databases

iPTMnetiQ14186
PhosphoSitePlusiQ14186

Expressioni

Tissue specificityi

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

Inductioni

Down-regulated during differentiation.

Gene expression databases

BgeeiENSG00000198176
CleanExiHS_TFDP1
ExpressionAtlasiQ14186 baseline and differential
GenevisibleiQ14186 HS

Organism-specific databases

HPAiCAB033605
HPA044754
HPA068909

Interactioni

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

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein domain specific binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112885, 46 interactors
CORUMiQ14186
DIPiDIP-238N
IntActiQ14186, 67 interactors
MINTiQ14186
STRINGi9606.ENSP00000364519

Structurei

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi199 – 247Combined sources49
Beta strandi253 – 260Combined sources8
Beta strandi262 – 267Combined sources6
Beta strandi272 – 276Combined sources5
Beta strandi280 – 289Combined sources10
Beta strandi291 – 295Combined sources5
Helixi296 – 303Combined sources8
Turni304 – 308Combined sources5
Helixi309 – 311Combined sources3
Helixi316 – 324Combined sources9
Helixi328 – 330Combined sources3
Helixi331 – 337Combined sources7

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...

Miscellaneous databases

EvolutionaryTraceiQ14186

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Motifi161 – 195DEF boxAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi250 – 253Poly-Pro4
Compositional biasi394 – 410Asp/Glu-rich (acidic; NCB domain)Add BLAST17

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiKOG2829 Eukaryota
ENOG410Y9QP LUCA
GeneTreeiENSGT00390000018222
HOGENOMiHOG000030696
HOVERGENiHBG009894
InParanoidiQ14186
KOiK04683
OMAiHPSTVNT
OrthoDBiEOG091G0AVY
PhylomeDBiQ14186
TreeFamiTF314396

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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
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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029293401D → N. Corresponds to variant dbSNP:rs4150823Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
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 [Q14186-2]
UniGeneiHs.79353

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiTFDP1_HUMAN
AccessioniPrimary (citable) accession number: Q14186
Secondary accession number(s): B4DLQ9, Q5JSB4, Q8IZL5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 176 of the entry and version 1 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

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