Reviewed,
UniProtKB/Swiss-Prot Q14186 (TFDP1_HUMAN)
Last modified
March 2, 2010.
Version 95.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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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 |
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| 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 | |
| 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
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 | |||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||
| 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
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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: 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. 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. 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. |
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 |
| ||||||||||||
| 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 |
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| 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. | ||||||||
Relevant documents
| Human chromosome 13 Human chromosome 13: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


