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Protein

Transcription factor Dp

Gene

Dp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication at the chorion loci. During development, the complex represses transcription of developmentally controlled E2F target genes. Can stimulate E2F-dependent transcription.1 Publication

GO - Molecular functioni

  • DNA binding Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: FlyBase
  • transcription factor binding Source: FlyBase

GO - Biological processi

  • dorsal/ventral axis specification, ovarian follicular epithelium Source: FlyBase
  • eggshell chorion gene amplification Source: FlyBase
  • endomitotic cell cycle Source: FlyBase
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: FlyBase
  • mitotic cell cycle Source: FlyBase
  • nurse cell apoptotic process Source: FlyBase
  • oogenesis Source: FlyBase
  • positive regulation of gene expression Source: FlyBase
  • positive regulation of nurse cell apoptotic process Source: FlyBase
  • regulation of cell cycle Source: FlyBase
  • regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-113510. E2F mediated regulation of DNA replication.
R-DME-1538133. G0 and Early G1.
R-DME-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-DME-69205. G1/S-Specific Transcription.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor Dp
Gene namesi
Name:Dp
ORF Names:CG4654
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0011763. Dp.

Subcellular locationi

GO - Cellular componenti

  • Myb complex Source: FlyBase
  • nucleus Source: FlyBase
  • Rb-E2F complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Transcription factor DpPRO_0000219479Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei398 – 3981Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ24318.

PTM databases

iPTMnetiQ24318.

Expressioni

Gene expression databases

BgeeiQ24318.
ExpressionAtlasiQ24318. differential.
GenevisibleiQ24318. DM.

Interactioni

Subunit structurei

Heterodimer of E2f and Dp. Cooperate to give sequence-specific DNA binding and optimal trans-activation. Component of the DREAM complex at least composed of Myb, Caf1, mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, Rpd3 and l3mbt.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RbfQ244723EBI-530830,EBI-145741

GO - Molecular functioni

  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi62224. 25 interactions.
IntActiQ24318. 10 interactions.
MINTiMINT-939136.
STRINGi7227.FBpp0086853.

Structurei

3D structure databases

ProteinModelPortaliQ24318.
SMRiQ24318. Positions 167-245, 255-392.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the E2F/DP family.Curated

Phylogenomic databases

eggNOGiKOG2829. Eukaryota.
ENOG410Y9QP. LUCA.
GeneTreeiENSGT00390000018222.
InParanoidiQ24318.
KOiK09394.
OMAiTNDKSEY.
OrthoDBiEOG7C2R27.
PhylomeDBiQ24318.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003316. 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.
PfamiPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFiPIRSF009404. Transcription_factor_DP. 1 hit.
SMARTiSM01138. DP. 1 hit.
SM01372. E2F_TDP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q24318-1) [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
MAHSTGGTVK TDEVNFFFRN EHGQISKMLK PAQNKSEMEG GKPVAVVYAT
60 70 80 90 100
GSSARNSGSA SGIGNVGRMG AFSQMGSQGQ FIRLQDNGLS IPKTEAGTTY
110 120 130 140 150
TTVSAQKTSG AGSGHYDLPL KGDRYVKFTP NPIKMKSKLH AIQSNSLHSM
160 170 180 190 200
SASSSSVQRK RKPDKAGKGL RHFSMKVCEK VEEKGKTTYN EVADDLVSEE
210 220 230 240 250
MKNNAYDNNC DQKNIRRRVY DALNVLMAIN VISKDKKEIR WIGLPANSTE
260 270 280 290 300
TFLALEEENC QRRERIKQKN EMLREMIMQH VAFKGLVERN KRNESQGVVP
310 320 330 340 350
SPNASIQLPF IIVNTHKSTK INCSVTNDKS EYIFKFDKTF EMHDDIEVLK
360 370 380 390 400
RMGFLLGLDK GECTPENIER VKSWVPPNLA KYVEAYGTGK TGENMYESDD
410 420 430 440
EDNEFNGYLE SANESQGFAQ HSAQHTTDGE FKLEMDDDEL DDDID
Length:445
Mass (Da):49,750
Last modified:June 21, 2005 - v2
Checksum:i87F4DBB26CFE4E42
GO
Isoform B (identifier: Q24318-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-22: MAHSTGGTVKTDEVNFFFRNEH → MCISETKEPPHLPISNSA

Show »
Length:441
Mass (Da):49,179
Checksum:iAAD836B2A83E8EC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171D → G in AAO24938 (Ref. 4) Curated
Sequence conflicti343 – 3431H → L in AAB87765 (PubMed:9271122).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2222MAHST…FRNEH → MCISETKEPPHLPISNSA in isoform B. 1 PublicationVSP_014146Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58403.1.
AE013599 Genomic DNA. Translation: AAM68602.1.
AY069526 mRNA. Translation: AAL39671.1.
BT003183 mRNA. Translation: AAO24938.1.
BT056266 mRNA. Translation: ACL68713.1.
X79708 mRNA. Translation: CAA56147.2.
AF011362 Genomic DNA. Translation: AAB87765.1.
PIRiB55745.
RefSeqiNP_477039.1. NM_057691.4. [Q24318-1]
NP_725267.1. NM_165974.3. [Q24318-2]
UniGeneiDm.6412.

Genome annotation databases

EnsemblMetazoaiFBtr0087740; FBpp0086853; FBgn0011763. [Q24318-1]
GeneIDi36461.
KEGGidme:Dmel_CG4654.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF58403.1.
AE013599 Genomic DNA. Translation: AAM68602.1.
AY069526 mRNA. Translation: AAL39671.1.
BT003183 mRNA. Translation: AAO24938.1.
BT056266 mRNA. Translation: ACL68713.1.
X79708 mRNA. Translation: CAA56147.2.
AF011362 Genomic DNA. Translation: AAB87765.1.
PIRiB55745.
RefSeqiNP_477039.1. NM_057691.4. [Q24318-1]
NP_725267.1. NM_165974.3. [Q24318-2]
UniGeneiDm.6412.

3D structure databases

ProteinModelPortaliQ24318.
SMRiQ24318. Positions 167-245, 255-392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62224. 25 interactions.
IntActiQ24318. 10 interactions.
MINTiMINT-939136.
STRINGi7227.FBpp0086853.

PTM databases

iPTMnetiQ24318.

Proteomic databases

PaxDbiQ24318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087740; FBpp0086853; FBgn0011763. [Q24318-1]
GeneIDi36461.
KEGGidme:Dmel_CG4654.

Organism-specific databases

CTDi13450.
FlyBaseiFBgn0011763. Dp.

Phylogenomic databases

eggNOGiKOG2829. Eukaryota.
ENOG410Y9QP. LUCA.
GeneTreeiENSGT00390000018222.
InParanoidiQ24318.
KOiK09394.
OMAiTNDKSEY.
OrthoDBiEOG7C2R27.
PhylomeDBiQ24318.

Enzyme and pathway databases

ReactomeiR-DME-113510. E2F mediated regulation of DNA replication.
R-DME-1538133. G0 and Early G1.
R-DME-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-DME-69205. G1/S-Specific Transcription.

Miscellaneous databases

GenomeRNAii36461.
PROiQ24318.

Gene expression databases

BgeeiQ24318.
ExpressionAtlasiQ24318. differential.
GenevisibleiQ24318. DM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR003316. 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.
PfamiPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFiPIRSF009404. Transcription_factor_DP. 1 hit.
SMARTiSM01138. DP. 1 hit.
SM01372. E2F_TDP. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
    Tissue: Embryo.
  5. "DNA-binding and trans-activation properties of Drosophila E2F and DP proteins."
    Dynlacht B.D., Brook A., Dembski M., Yenush L., Dyson N.
    Proc. Natl. Acad. Sci. U.S.A. 91:6359-6363(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-445.
    Tissue: Eye imaginal disk.
  6. "Mutations in Drosophila DP and E2F distinguish G1-S progression from an associated transcriptional program."
    Royzman I., Whittaker A.J., Orr-Weaver T.L.
    Genes Dev. 11:1999-2011(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 83-445.
  7. "Native E2F/RBF complexes contain Myb-interacting proteins and repress transcription of developmentally controlled E2F target genes."
    Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S., Stevaux O., Aasland R., White-Cooper H., Dyson N., Brehm A.
    Cell 119:181-193(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE DREAM COMPLEX.
  8. "Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor complex."
    Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J., Botchan M.R.
    Genes Dev. 18:2929-2940(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
  9. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiTFDP_DROME
AccessioniPrimary (citable) accession number: Q24318
Secondary accession number(s): B8A3X4
, O17472, O44080, Q86PE0, Q8ML56, Q9V6M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 21, 2005
Last modified: June 8, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.