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Q14186

- TFDP1_HUMAN

UniProt

Q14186 - TFDP1_HUMAN

Protein

Transcription factor Dp-1

Gene

TFDP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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. 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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi113 – 19583Sequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein domain specific binding Source: UniProtKB
    4. sequence-specific DNA binding transcription factor activity Source: ProtInc
    5. transcription coactivator activity Source: ProtInc
    6. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cell proliferation Source: ProtInc
    3. G1/S transition of mitotic cell cycle Source: Reactome
    4. gene expression Source: Reactome
    5. intrinsic apoptotic signaling pathway Source: Reactome
    6. mitotic cell cycle Source: Reactome
    7. Notch signaling pathway Source: Reactome
    8. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    9. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    10. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    11. transcription, DNA-templated Source: Reactome
    12. transcription initiation from RNA polymerase II promoter Source: Reactome
    13. transforming growth factor beta receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111214. G0 and Early G1.
    REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_1194. Activation of NOXA and translocation to mitochondria.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_121. Activation of PUMA and translocation to mitochondria.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_683. G1/S-Specific Transcription.
    REACT_821. Cyclin D associated events in G1.

    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
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:11749. TFDP1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. transcription factor complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36464.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 410409Transcription factor Dp-1PRO_0000219475Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei3 – 31N6-acetyllysine1 Publication
    Modified residuei23 – 231Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase, inhibits E2F-mediated DNA binding and transactivation.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14186.
    PaxDbiQ14186.
    PRIDEiQ14186.

    PTM databases

    PhosphoSiteiQ14186.

    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

    ArrayExpressiQ14186.
    BgeeiQ14186.
    CleanExiHS_TFDP1.
    GenevestigatoriQ14186.

    Organism-specific databases

    HPAiCAB033605.

    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 MYBL2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DVL1O146403EBI-749713,EBI-723489
    E2F1Q010949EBI-749713,EBI-448924
    NLKQ9UBE82EBI-749713,EBI-366978

    Protein-protein interaction databases

    BioGridi112885. 29 interactions.
    DIPiDIP-238N.
    IntActiQ14186. 14 interactions.
    MINTiMINT-3029193.
    STRINGi9606.ENSP00000364519.

    Structurei

    Secondary structure

    1
    410
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi199 – 24547
    Beta strandi246 – 2494
    Helixi253 – 2553
    Beta strandi256 – 2605
    Beta strandi262 – 2698
    Beta strandi272 – 2765
    Beta strandi280 – 28910
    Beta strandi291 – 2955
    Helixi296 – 3027
    Turni303 – 3086
    Helixi309 – 3113
    Helixi316 – 3249
    Helixi328 – 3303
    Helixi331 – 3399

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AZEX-ray2.55A199-350[»]
    ProteinModelPortaliQ14186.
    SMRiQ14186. Positions 113-195, 199-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14186.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni204 – 27774DimerizationSequence AnalysisAdd
    BLAST
    Regioni211 – 327117Enhances binding of RB protein to E2FAdd
    BLAST
    Regioni214 – 24633DCB1Add
    BLAST
    Regioni259 – 31557DCB2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi161 – 19535DEF boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi250 – 2534Poly-Pro
    Compositional biasi394 – 41017Asp/Glu-rich (acidic; NCB domain)Add
    BLAST

    Sequence similaritiesi

    Belongs to the E2F/DP family.Curated

    Phylogenomic databases

    eggNOGiNOG271896.
    HOGENOMiHOG000030696.
    HOVERGENiHBG009894.
    InParanoidiQ14186.
    KOiK04683.
    OMAiHPSTVNT.
    OrthoDBiEOG7C2R27.
    PhylomeDBiQ14186.
    TreeFamiTF314396.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR028313. DP-1.
    IPR003316. E2F_TDP.
    IPR014889. Transc_factor_DP_C.
    IPR015648. Transcrpt_fac_DP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PANTHERiPTHR12548. PTHR12548. 1 hit.
    PTHR12548:SF4. PTHR12548:SF4. 1 hit.
    PfamiPF08781. DP. 1 hit.
    PF02319. E2F_TDP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009404. Transcription_factor_DP. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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

    MAKDAGLIEA NGELKVFIDQ NLSPGKGVVS LVAVHPSTVN PLGKQLLPKT    50
    FGQSNVNIAQ QVVIGTPQRP AASNTLVVGS PHTPSTHFAS QNQPSDSSPW 100
    SAGKRNRKGE KNGKGLRHFS MKVCEKVQRK GTTSYNEVAD ELVAEFSAAD 150
    NHILPNESAY DQKNIRRRVY DALNVLMAMN IISKEKKEIK WIGLPTNSAQ 200
    ECQNLEVERQ RRLERIKQKQ SQLQELILQQ IAFKNLVQRN RHAEQQASRP 250
    PPPNSVIHLP FIIVNTSKKT VIDCSISNDK FEYLFNFDNT FEIHDDIEVL 300
    KRMGMACGLE SGSCSAEDLK MARSLVPKAL EPYVTEMAQG TVGGVFITTA 350
    GSTSNGTRFS ASDLTNGADG MLATSSNGSQ YSGSRVETPV SYVGEDDEED 400
    DDFNENDEDD 410
    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti401 – 4011D → N.
    Corresponds to variant rs4150823 [ dbSNP | Ensembl ].
    VAR_029293

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 103103MAKDA…PWSAG → MSTLPSKW in isoform 2. 1 PublicationVSP_056499Add
    BLAST
    Alternative sequencei358 – 3614Missing in isoform 2. 1 PublicationVSP_056500

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23959 mRNA. Translation: AAA58440.1.
    AK297114 mRNA. Translation: BAG59621.1.
    AL442125 Genomic DNA. Translation: CAI39789.1.
    CH471085 Genomic DNA. Translation: EAX09216.1.
    BC011685 mRNA. Translation: AAH11685.1.
    AF550129 Genomic DNA. Translation: AAN46090.1.
    CCDSiCCDS9538.1.
    PIRiA48585.
    RefSeqiNP_009042.1. NM_007111.4.
    XP_005268383.1. XM_005268326.1.
    XP_005268384.1. XM_005268327.1.
    XP_005268388.1. XM_005268331.1.
    UniGeneiHs.79353.

    Genome annotation databases

    EnsembliENST00000375370; ENSP00000364519; ENSG00000198176.
    ENST00000538138; ENSP00000443878; ENSG00000198176.
    GeneIDi7027.
    KEGGihsa:7027.
    UCSCiuc001vtw.3. human.

    Polymorphism databases

    DMDMi3122926.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23959 mRNA. Translation: AAA58440.1 .
    AK297114 mRNA. Translation: BAG59621.1 .
    AL442125 Genomic DNA. Translation: CAI39789.1 .
    CH471085 Genomic DNA. Translation: EAX09216.1 .
    BC011685 mRNA. Translation: AAH11685.1 .
    AF550129 Genomic DNA. Translation: AAN46090.1 .
    CCDSi CCDS9538.1.
    PIRi A48585.
    RefSeqi NP_009042.1. NM_007111.4.
    XP_005268383.1. XM_005268326.1.
    XP_005268384.1. XM_005268327.1.
    XP_005268388.1. XM_005268331.1.
    UniGenei Hs.79353.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AZE X-ray 2.55 A 199-350 [» ]
    ProteinModelPortali Q14186.
    SMRi Q14186. Positions 113-195, 199-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112885. 29 interactions.
    DIPi DIP-238N.
    IntActi Q14186. 14 interactions.
    MINTi MINT-3029193.
    STRINGi 9606.ENSP00000364519.

    PTM databases

    PhosphoSitei Q14186.

    Polymorphism databases

    DMDMi 3122926.

    Proteomic databases

    MaxQBi Q14186.
    PaxDbi Q14186.
    PRIDEi Q14186.

    Protocols and materials databases

    DNASUi 7027.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375370 ; ENSP00000364519 ; ENSG00000198176 .
    ENST00000538138 ; ENSP00000443878 ; ENSG00000198176 .
    GeneIDi 7027.
    KEGGi hsa:7027.
    UCSCi uc001vtw.3. human.

    Organism-specific databases

    CTDi 7027.
    GeneCardsi GC13P114239.
    H-InvDB HIX0002608.
    HIX0033825.
    HGNCi HGNC:11749. TFDP1.
    HPAi CAB033605.
    MIMi 189902. gene.
    neXtProti NX_Q14186.
    PharmGKBi PA36464.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271896.
    HOGENOMi HOG000030696.
    HOVERGENi HBG009894.
    InParanoidi Q14186.
    KOi K04683.
    OMAi HPSTVNT.
    OrthoDBi EOG7C2R27.
    PhylomeDBi Q14186.
    TreeFami TF314396.

    Enzyme and pathway databases

    Reactomei REACT_111214. G0 and Early G1.
    REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_1194. Activation of NOXA and translocation to mitochondria.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_121. Activation of PUMA and translocation to mitochondria.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_683. G1/S-Specific Transcription.
    REACT_821. Cyclin D associated events in G1.

    Miscellaneous databases

    ChiTaRSi TFDP1. human.
    EvolutionaryTracei Q14186.
    GeneWikii TFDP1.
    GenomeRNAii 7027.
    NextBioi 27455.
    PROi Q14186.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14186.
    Bgeei Q14186.
    CleanExi HS_TFDP1.
    Genevestigatori Q14186.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR028313. DP-1.
    IPR003316. E2F_TDP.
    IPR014889. Transc_factor_DP_C.
    IPR015648. Transcrpt_fac_DP.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    PANTHERi PTHR12548. PTHR12548. 1 hit.
    PTHR12548:SF4. PTHR12548:SF4. 1 hit.
    Pfami PF08781. DP. 1 hit.
    PF02319. E2F_TDP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009404. Transcription_factor_DP. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1), CHARACTERIZATION.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Muscle.
    6. NIEHS SNPs program
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-410.
    7. "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.
    8. "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.
    9. "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.
    10. "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.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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].
    13. "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.
    14. "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].
    15. "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.
    16. "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].

    Entry informationi

    Entry nameiTFDP1_HUMAN
    AccessioniPrimary (citable) accession number: Q14186
    Secondary accession number(s): B4DLQ9, Q5JSB4, Q8IZL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [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

    Miscellaneous

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

    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

    External Data

    Dasty 3