Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcription factor Dp-1

Gene

TFDP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. 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).1 Publication

Regions

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

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:11749. TFDP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36464.

Polymorphism and mutation databases

BioMutaiTFDP1.
DMDMi3122926.

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 – 231Phosphoserine3 Publications

Post-translational modificationi

Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase, inhibits E2F-mediated DNA binding and transactivation.1 Publication

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

BgeeiQ14186.
CleanExiHS_TFDP1.
ExpressionAtlasiQ14186. baseline and differential.
GenevestigatoriQ14186.

Organism-specific databases

HPAiCAB033605.
HPA044754.

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).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DVL1O146403EBI-749713,EBI-723489
E2F1Q010949EBI-749713,EBI-448924
E2F6O754616EBI-749713,EBI-749694
NLKQ9UBE82EBI-749713,EBI-366978

Protein-protein interaction databases

BioGridi112885. 34 interactions.
DIPiDIP-238N.
IntActiQ14186. 15 interactions.
MINTiMINT-3029193.
STRINGi9606.ENSP00000364519.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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
Regioni105 – 12723Interaction with CEBPA1 PublicationAdd
BLAST
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.
GeneTreeiENSGT00390000018222.
HOGENOMiHOG000030696.
HOVERGENiHBG009894.
InParanoidiQ14186.
KOiK04683.
OMAiHPSTVNT.
OrthoDBiEOG7C2R27.
PhylomeDBiQ14186.
TreeFamiTF314396.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR028313. DP-1.
IPR003316. E2F_WHTH_DNA-bd_dom.
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. 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)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:
EMBLi
GenBanki
DDBJi
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. [Q14186-1]
PIRiA48585.
RefSeqiNP_009042.1. NM_007111.4. [Q14186-1]
XP_005268383.1. XM_005268326.1. [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.3. human. [Q14186-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q14186-1]
PIRiA48585.
RefSeqiNP_009042.1. NM_007111.4. [Q14186-1]
XP_005268383.1. XM_005268326.1. [Q14186-1]
XP_005268384.1. XM_005268327.1. [Q14186-1]
XP_005268388.1. XM_005268331.1. [Q14186-2]
UniGeneiHs.79353.

3D structure databases

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

Protein-protein interaction databases

BioGridi112885. 34 interactions.
DIPiDIP-238N.
IntActiQ14186. 15 interactions.
MINTiMINT-3029193.
STRINGi9606.ENSP00000364519.

PTM databases

PhosphoSiteiQ14186.

Polymorphism and mutation databases

BioMutaiTFDP1.
DMDMi3122926.

Proteomic databases

MaxQBiQ14186.
PaxDbiQ14186.
PRIDEiQ14186.

Protocols and materials databases

DNASUi7027.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375370; ENSP00000364519; ENSG00000198176. [Q14186-1]
GeneIDi7027.
KEGGihsa:7027.
UCSCiuc001vtw.3. human. [Q14186-1]

Organism-specific databases

CTDi7027.
GeneCardsiGC13P114239.
H-InvDBHIX0002608.
HIX0033825.
HGNCiHGNC:11749. TFDP1.
HPAiCAB033605.
HPA044754.
MIMi189902. gene.
neXtProtiNX_Q14186.
PharmGKBiPA36464.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG271896.
GeneTreeiENSGT00390000018222.
HOGENOMiHOG000030696.
HOVERGENiHBG009894.
InParanoidiQ14186.
KOiK04683.
OMAiHPSTVNT.
OrthoDBiEOG7C2R27.
PhylomeDBiQ14186.
TreeFamiTF314396.

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.

Miscellaneous databases

ChiTaRSiTFDP1. human.
EvolutionaryTraceiQ14186.
GeneWikiiTFDP1.
GenomeRNAii7027.
NextBioi27455.
PROiQ14186.
SOURCEiSearch...

Gene expression databases

BgeeiQ14186.
CleanExiHS_TFDP1.
ExpressionAtlasiQ14186. baseline and differential.
GenevestigatoriQ14186.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR028313. DP-1.
IPR003316. E2F_WHTH_DNA-bd_dom.
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Repression of transcriptional activity of C/EBPalpha by E2F-dimerization partner complexes."
    Zaragoza K., Begay V., Schuetz A., Heinemann U., Leutz A.
    Mol. Cell. Biol. 30:2293-2304(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CEBPA.
  16. "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.
  17. "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: May 27, 2015
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.