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Q14186 (TFDP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor Dp-1
Alternative name(s):
DRTF1-polypeptide 1
Short name=DRTF1
E2F dimerization partner 1
Gene names
Name:TFDP1
Synonyms:DP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. The DP2/E2F complex functions in the control of cell-cycle progression from G1 to S phase. The E2F1/DP complex appears to mediate both cell proliferation and apoptosis.

Subunit structure

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. Ref.8 Ref.9

Subcellular location

Nucleus.

Tissue specificity

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

Induction

Down-regulated during differentiation.

Post-translational modification

Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase, inhibits E2F-mediated DNA binding and transactivation.

Miscellaneous

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

Sequence similarities

Belongs to the E2F/DP family.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

Notch signaling pathway

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

transcription factor complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein domain specific binding

Inferred from physical interaction PubMed 16360038. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

transcription factor binding

Inferred from physical interaction PubMed 16360038. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 410409Transcription factor Dp-1
PRO_0000219475

Regions

DNA binding113 – 19583 Potential
Region204 – 27774Dimerization Potential
Region211 – 327117Enhances binding of RB protein to E2F
Region214 – 24633DCB1
Region259 – 31557DCB2
Motif161 – 19535DEF box
Compositional bias250 – 2534Poly-Pro
Compositional bias394 – 41017Asp/Glu-rich (acidic; NCB domain)

Amino acid modifications

Modified residue21N-acetylalanine Ref.13
Modified residue31N6-acetyllysine Ref.13
Modified residue231Phosphoserine Ref.12 Ref.14 Ref.15

Natural variations

Natural variant4011D → N.
Corresponds to variant rs4150823 [ dbSNP | Ensembl ].
VAR_029293

Secondary structure

....................... 410
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14186 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3FEEFE1E49FD9ED0

FASTA41045,070
        10         20         30         40         50         60 
MAKDAGLIEA NGELKVFIDQ NLSPGKGVVS LVAVHPSTVN PLGKQLLPKT FGQSNVNIAQ 

        70         80         90        100        110        120 
QVVIGTPQRP AASNTLVVGS PHTPSTHFAS QNQPSDSSPW SAGKRNRKGE KNGKGLRHFS 

       130        140        150        160        170        180 
MKVCEKVQRK GTTSYNEVAD ELVAEFSAAD NHILPNESAY DQKNIRRRVY DALNVLMAMN 

       190        200        210        220        230        240 
IISKEKKEIK WIGLPTNSAQ ECQNLEVERQ RRLERIKQKQ SQLQELILQQ IAFKNLVQRN 

       250        260        270        280        290        300 
RHAEQQASRP PPPNSVIHLP FIIVNTSKKT VIDCSISNDK FEYLFNFDNT FEIHDDIEVL 

       310        320        330        340        350        360 
KRMGMACGLE SGSCSAEDLK MARSLVPKAL EPYVTEMAQG TVGGVFITTA GSTSNGTRFS 

       370        380        390        400        410 
ASDLTNGADG MLATSSNGSQ YSGSRVETPV SYVGEDDEED DDFNENDEDD 

« Hide

References

« Hide 'large scale' references
[1]"Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation."
Helin K., Wu C.-L., Fattaey A.R., Lees J.A., Dynlacht B.D., Ngwu C., Harlow E.
Genes Dev. 7:1850-1861(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[2]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[5]NIEHS SNPs program
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-410.
[6]"DP-1: a cell cycle-regulated and phosphorylated component of transcription factor DRTF1/E2F which is functionally important for recognition by pRb and the adenovirus E4 orf 6/7 protein."
Bandara L.R., Lam E.W.-F., Soerensen T.S., Zamanian M., Girling R., la Thangue N.B.
EMBO J. 13:3104-3114(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[7]"In vivo association of E2F and DP family proteins."
Wu C.-L., Zukerberg L.R., Ngwu C., Harlow E., Lees J.A.
Mol. Cell. Biol. 15:2536-2546(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; MAX; MGA; EUHMTASE1; BAT8; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
[9]"Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence."
Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.
Mol. Cell 26:539-551(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L23959 mRNA. Translation: AAA58440.1.
AL442125 Genomic DNA. Translation: CAI39789.1.
CH471085 Genomic DNA. Translation: EAX09216.1.
BC011685 mRNA. Translation: AAH11685.1.
AF550129 Genomic DNA. Translation: AAN46090.1.
PIRA48585.
RefSeqNP_009042.1. NM_007111.4.
XP_005268383.1. XM_005268326.1.
XP_005268384.1. XM_005268327.1.
UniGeneHs.79353.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AZEX-ray2.55A199-350[»]
ProteinModelPortalQ14186.
SMRQ14186. Positions 113-195, 199-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112885. 29 interactions.
DIPDIP-238N.
IntActQ14186. 14 interactions.
MINTMINT-3029193.
STRING9606.ENSP00000364519.

PTM databases

PhosphoSiteQ14186.

Polymorphism databases

DMDM3122926.

Proteomic databases

PaxDbQ14186.
PRIDEQ14186.

Protocols and materials databases

DNASU7027.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375370; ENSP00000364519; ENSG00000198176.
GeneID7027.
KEGGhsa:7027.
UCSCuc001vtw.3. human.

Organism-specific databases

CTD7027.
GeneCardsGC13P114239.
H-InvDBHIX0002608.
HIX0033825.
HGNCHGNC:11749. TFDP1.
HPACAB033605.
MIM189902. gene.
neXtProtNX_Q14186.
PharmGKBPA36464.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271896.
HOGENOMHOG000030696.
HOVERGENHBG009894.
InParanoidQ14186.
KOK04683.
OMAHPSTVNT.
OrthoDBEOG7C2R27.
PhylomeDBQ14186.
TreeFamTF314396.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_578. Apoptosis.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ14186.
BgeeQ14186.
CleanExHS_TFDP1.
GenevestigatorQ14186.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR028313. DP-1.
IPR003316. E2F_TDP.
IPR014889. Transc_factor_DP_C.
IPR015648. Transcrpt_fac_DP.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERPTHR12548. PTHR12548. 1 hit.
PTHR12548:SF4. PTHR12548:SF4. 1 hit.
PfamPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFPIRSF009404. Transcription_factor_DP. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTFDP1. human.
EvolutionaryTraceQ14186.
GeneWikiTFDP1.
GenomeRNAi7027.
NextBio27455.
PROQ14186.
SOURCESearch...

Entry information

Entry nameTFDP1_HUMAN
AccessionPrimary (citable) accession number: Q14186
Secondary accession number(s): Q5JSB4, Q8IZL5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM