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Reviewed, UniProtKB/Swiss-Prot Q08639 (TFDP1_MOUSE)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Transcription factor Dp-1
Alternative name(s):
    E2F dimerization partner 1
    DRTF1-polypeptide 1
Gene names
Name: Tfdp1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 which is composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and 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 By similarity.

Subcellular location

Nucleus.

Developmental stage

In the intestinal epithelium, first expressed in undifferentiated and mesenchymal tissues, levels increasing by 12.5 dpc in the epithelial compartment. With epithelial differentiation at 15.5 dpc, Its expression increases substantially in the intervillus epithelium with lower levels in the mesenchyme. At later stages, expression continues in the intervillus epithelium. Also found at lower levels in the developing villi. In the developing brain, highest levels found between 11.5 and 13.5 dpc in the ventricular region. In the developing retina, it is expressed both in retinoblast and ganglion cell layers from 14.5 dpc to 6 days after birth. In other developing tissues, its expression is highest in the thymus. Also present in kidney, lung, liver, heart and chondrocytes. Weakly expressed in skeletal muscle and absent from choroid plexus. Ref.4 Ref.5

Post-translational modification

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

Sequence similarities

Belongs to the E2F/DP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Transcription factor Dp-1
PRO_0000219476

Regions

DNA binding113 – 19583 Potential
Region204 – 27774Dimerization Potential
Region214 – 24633DCB1
Region259 – 31557DCB2
Motif161 – 19535DEF box
Compositional bias250 – 2534Poly-Pro
Compositional bias395 – 41016Asp/Glu-rich (acidic; NCB domain)

Amino acid modifications

Modified residue231Phosphoserine; by CDK2 Potential
Modified residue1831Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08639-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FEEA090C781071B9

FASTA41045,231
        10         20         30         40         50         60 
MAKDASLIEA NGELKVFIDQ NLSPGKGVVS LVAVHPSTVN TLGKQLLPKT FGQSNVNITQ 

        70         80         90        100        110        120 
QVVIGTPQRP AASNTIVVGS PHTPNTHFVS QNQTSDSSPW SAGKRNRKGE KNGKGLRHFS 

       130        140        150        160        170        180 
MKVCEKVQRK GTTSYNEVAD ELVAEFSAAD NHILPNESAY DQKNIRRRVY DALNVLMAMN 

       190        200        210        220        230        240 
IISKEKKEIK WIGLPTNSAQ ECQNLEVERQ RRLERIKQKQ SQLQELILQQ IAFKNLVQRN 

       250        260        270        280        290        300 
RQAEQQARRP PPPNSVIHLP FIIVNTSRKT VIDCSISNDK FEYLFNFDNT FEIHDDIEVL 

       310        320        330        340        350        360 
KRMGMACGLE SGNCSAEDLK VARSLVPKAL EPYVTEMAQG SIGGVFVTTT GSTSNGTRLS 

       370        380        390        400        410 
ASDLSNGADG MLATSSNGSQ YSGSRVETPV SYVGEDDDDD DDFNENDEED 

« Hide

References

[1]"A new component of the transcription factor DRTF1/E2F."
Girling R., Partridge J.F., Bandara L.R., Burden N., Totty N.F., Hsuan J.J., La Thangue N.B.
Nature 362:83-87(1993) [PubMed: 8446173] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"A new component of the transcription factor DRTF1/E2F."
Girling R., Partridge J.F., Bandara L.R., Burden N., Totty N.F., Hsuan J.J., La Thangue N.B.
Nature 365:468-468(1993) [PubMed: 8413592] [Abstract]
Cited for: SEQUENCE REVISION TO 388-410.
[3]"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].
[4]"Expression patterns of the E2F family of transcription factors during murine epithelial development."
Dagnino L., Fry C.J., Bartley S.M., Farnham P., Gallie B.L., Phillips R.A.
Cell Growth Differ. 8:553-563(1997) [PubMed: 9149906] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[5]"Expression patterns of the E2F family of transcription factors during mouse nervous system development."
Dagnino L., Fry C.J., Bartley S.M., Farnham P., Gallie B.L., Phillips R.A.
Mech. Dev. 66:13-25(1997) [PubMed: 9376316] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

X72310 mRNA. Translation: CAA51056.1.
IPIIPI00122992.
PIRB48585.
RefSeqNP_033387.1.
UniGeneMm.925

3D structure databases

HSSPHSSP built from PDB template 1CF7 based on UniProtKB Q14188.
SMRQ08639. Positions 113-195, 199-346.
ModBaseSearch...

PTM databases

PhosphoSiteQ08639.

Proteomic databases

PRIDEQ08639.

Genome annotation databases

EnsemblENSMUSG00000038482. Mus musculus. [Contig view]
GeneID21781.
KEGGmmu:21781.

Organism-specific databases

MGIMGI:101934. Tfdp1.

Phylogenomic databases

HOGENOMQ08639.
HOVERGENQ08639.
OMAQ08639. PHTPSTH.

Gene expression databases

ArrayExpressQ08639.
BgeeQ08639.
CleanExMM_TFDP1.
GermOnlineENSMUSG00000038482. Mus musculus.

Family and domain databases

InterProIPR003316. E2F_TDP.
IPR014889. Transc_factor_DP_C.
IPR016556. Transcription_factor_DP_sub.
IPR015648. Transcrpt_fac_DP.
IPR011991. Wing_hlx_DNA_bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PANTHERPTHR12548. DP. 1 hit.
PfamPF08781. DP. 1 hit.
PF02319. E2F_TDP. 1 hit.
[Graphical view]
PIRSFPIRSF009404. Transcription_factor_DP. 1 hit.
ProtoNetSearch...

Other Resources

NextBio301122.
SOURCESearch...

Entry information

Entry nameTFDP1_MOUSE
AccessionPrimary (citable) accession number: Q08639
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents