Reviewed, UniProtKB/Swiss-Prot Q14186 (TFDP1_HUMAN)

Names and origin

Protein names

Recommended name:
Transcription factor Dp-1

Alternative name(s):
E2F dimerization partner 1
DRTF1-polypeptide 1
Short name=DRTF1

Gene names

Name:	TFDP1
Synonyms:	DP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Protein existence	Evidence 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 E2F-1/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.
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 E2F-1-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 process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Ref.1 Traceable author statement. Source: ProtInc cellular transcription Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc
Cellular component	transcription factor complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein domain specific binding Inferred from physical interaction. Source: UniProtKB transcription coactivator activity Ref.1 Traceable author statement. Source: ProtInc transcription factor activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 410

410

Transcription factor Dp-1

PRO_0000219475

Regions

DNA binding

113 – 195

83

Potential

Region

204 – 277

74

Dimerization Potential

Region

211 – 327

117

Enhances binding of RB protein to E2F

Region

214 – 246

33

DCB1

Region

259 – 315

57

DCB2

Motif

161 – 195

35

DEF box

Compositional bias

250 – 253

4

Poly-Pro

Compositional bias

394 – 410

17

Asp/Glu-rich (acidic; NCB domain)

Amino acid modifications

Modified residue

3

1

N6-acetyllysine Ref.15

Modified residue

23

1

Phosphoserine Ref.10 Ref.12 Ref.13 Ref.14

Modified residue

183

1

Phosphoserine Ref.11

Natural variations

Natural variant

401

1

D → N: dbSNP rs4150823.

VAR_029293

Secondary structure

1

.

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410

Helix Strand Turn

Details...

Helix

199 – 245

47

Beta strand

246 – 249

4

Helix

253 – 255

3

Beta strand

256 – 260

5

Beta strand

262 – 269

8

Beta strand

272 – 276

5

Beta strand

280 – 289

10

Beta strand

291 – 295

5

Helix

296 – 302

7

Turn

303 – 308

6

Helix

309 – 311

3

Helix

316 – 324

9

Helix

328 – 330

3

Helix

331 – 339

9

Sequences

	Sequence		Length	Mass (Da)
	Q14186-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3FEEFE1E49FD9ED0	FASTA	410	45,070
	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

References

	« Hide 'large scale' referencesShow '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: 8405995] [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. , 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: 15057823] [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. , 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: 15489334] [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: 8039504] [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: 7739537] [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: 12004135] [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: 17531812] [Abstract] Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
[10]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY.
[11]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, MASS SPECTROMETRY.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY.
[13]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY.
[14]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY. Tissue: T-cell.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00029095.

PIR

A48585.

RefSeq

NP_009042.1.

UniGene

Hs.79353

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AZE	X-ray	2.55	A	199-350	[»]

SMR

Q14186. Positions 113-195.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-238N.

IntAct

Q14186. 5 interactions.

STRING

Q14186.

PTM databases

PhosphoSite

Q14186.

Proteomic databases

PRIDE

Q14186.

Genome annotation databases

Ensembl

ENST00000375370; ENSP00000364519; ENSG00000198176; Homo sapiens. [Genome view]

GeneID

7027.

KEGG

hsa:7027.

UCSC

uc001vtw.1. human.

Organism-specific databases

CTD

7027.

GeneCards

GC13P113287.

H-InvDB

HIX0002608.
HIX0011480.
HIX0033825.

HGNC

HGNC:11749. TFDP1.

MIM

189902. gene.

PharmGKB

PA36464.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG444383.

HOVERGEN

HBG009894.

InParanoid

Q14186.

OMA

SSNDSHY.

OrthoDB

EOG9F4VW9.

PhylomeDB

Q14186.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpress

Q14186.

Bgee

Q14186.

CleanEx

HS_TFDP1.

Genevestigator

Q14186.

Family and domain databases

InterPro

IPR003316. E2F_TDP.
IPR014889. Transc_factor_DP_C.
IPR016556. Transcription_factor_DP_sub.
IPR015648. Transcrpt_fac_DP.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

PANTHER

PTHR12548. DP. 1 hit.

Pfam

PF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]

PIRSF

PIRSF009404. Transcription_factor_DP. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

27455.

SOURCE

Search...

Entry information

Entry name

TFDP1_HUMAN

Accession

Primary (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:	March 2, 2010
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.