Q64163 · TFDP2_MOUSE

  • Protein
    Transcription factor Dp-2
  • Gene
    Tfdp2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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 TFDP2: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. Blocks adipocyte differentiation by repressing CEBPA binding to its target gene promoters.

Features

Showing features for dna binding.

144650100150200250300350400
TypeIDPosition(s)Description
DNA binding129-210

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnuclear envelope
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componenttranscription regulator complex
Molecular FunctionDNA binding
Molecular FunctionDNA-binding transcription factor activity
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Biological Processnegative regulation of DNA-templated transcription
Biological Processregulation of cell cycle
Biological Processregulation of DNA-templated transcription
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Transcription factor Dp-2
  • Alternative names
    • Dp-3
    • E2F dimerization partner 2

Gene names

    • Name
      Tfdp2
    • Synonyms
      Dp2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q64163

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylthreonine
ChainPRO_00002194782-446Transcription factor Dp-2
Modified residue24Phosphoserine; by CDK2
Modified residue42Phosphoserine; by CDK2
Modified residue122Phosphoserine

Post-translational modification

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

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in all tissues examined. Highest levels in spleen and heart.

Interaction

Subunit

Component of the DRTF1/E2F 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. During the cell cycle, RB becomes phosphorylated in mid-to-late G1 phase, detaches from the DRTF1/E2F complex rendering E2F transcriptionally active. Interacts with GMCL (By similarity).
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 TFDP2:E2F1 interacts with CEBPA; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q64163-4E2f5 Q615022EBI-8077763, EBI-7225685
BINARY Q64163-4Ywhae P622596EBI-8077763, EBI-356480

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, motif, compositional bias.

TypeIDPosition(s)Description
Region60-82Interaction with CEBPA
Motif103-118Nuclear localization signal
Motif176-210DEF box
Region219-292Dimerization
Region229-261DCB1
Region274-330DCB2
Compositional bias404-426Polar residues
Region404-446Disordered
Compositional bias430-446Acidic residues

Sequence similarities

Belongs to the E2F/DP family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative splicing. Additional isoforms seem to exist.

Q64163-1

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.

  • Name
    Alpha
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    446
  • Mass (Da)
    49,098
  • Last updated
    2000-05-30 v2
  • Checksum
    0E6E87AE8B82EE8A
MTAKNVGLPSTNAKLRGFIDQNFSPSKGNISLVAFPVSSTNSPTKILPKTLGPINVNVGPQMIISTPQRIANSGSVLIGNPYTPAPAMVTQTHIAEAAGWVPSDRKRAREFIDSDFSESKRSKKGDKNGKGLRHFSMKVCEKVQRKGTTSYNEVADELVSEFTNSNNHLAADSAYDQENIRRRVYDALNVLMAMNIISSLPTGKKRNQVDCNSAQECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNQGPPAVNSTIQLPFIIINTSRKTVIDCSISSDKFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCSLEDLKIARSLVPKALEGYITDISTGPSWLNQGLLLNSTQSVSNLDPTTGATVPQSSVNQGLCLDAEVALATGQLPASNSHQSSSAASHFSESRGETPCSFNDEDEEDEEEDPSSPE

Q64163-2

  • Name
    Beta
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q64163-3

Q64163-4

  • Name
    Delta
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 11 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9PWL5E9PWL5_MOUSETfdp2310
Q8BHD2Q8BHD2_MOUSETfdp2385
F6QG91F6QG91_MOUSETfdp2386
A0A087WNL4A0A087WNL4_MOUSETfdp2117
A0A087WPS0A0A087WPS0_MOUSETfdp2203
A0A087WPU8A0A087WPU8_MOUSETfdp2446
J3QK26J3QK26_MOUSETfdp2359
A0A087WQV5A0A087WQV5_MOUSETfdp2112
A0A087WRW3A0A087WRW3_MOUSETfdp239
A0A087WSK4A0A087WSK4_MOUSETfdp2369
A0A1B0GXK0A0A1B0GXK0_MOUSETfdp2368

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0013551-61in isoform Beta, isoform Gamma and isoform Delta
Alternative sequenceVSP_001356103-118in isoform Beta and isoform Gamma
Alternative sequenceVSP_001357173in isoform Gamma
Compositional bias404-426Polar residues
Compositional bias430-446Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
S79780
EMBL· GenBank· DDBJ
AAB35506.2
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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