Q64163 · TFDP2_MOUSE
- ProteinTranscription factor Dp-2
- GeneTfdp2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids446 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 129-210 | |||||
Sequence: GKGLRHFSMKVCEKVQRKGTTSYNEVADELVSEFTNSNNHLAADSAYDQENIRRRVYDALNVLMAMNIISSLPTGKKRNQVD |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nuclear envelope | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | transcription regulator complex | |
Molecular Function | DNA binding | |
Molecular Function | DNA-binding transcription factor activity | |
Molecular Function | DNA-binding transcription factor activity, RNA polymerase II-specific | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | regulation of cell cycle | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription factor Dp-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ64163
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylthreonine | ||||
Sequence: T | ||||||
Chain | PRO_0000219478 | 2-446 | Transcription factor Dp-2 | |||
Sequence: TAKNVGLPSTNAKLRGFIDQNFSPSKGNISLVAFPVSSTNSPTKILPKTLGPINVNVGPQMIISTPQRIANSGSVLIGNPYTPAPAMVTQTHIAEAAGWVPSDRKRAREFIDSDFSESKRSKKGDKNGKGLRHFSMKVCEKVQRKGTTSYNEVADELVSEFTNSNNHLAADSAYDQENIRRRVYDALNVLMAMNIISSLPTGKKRNQVDCNSAQECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNQGPPAVNSTIQLPFIIINTSRKTVIDCSISSDKFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCSLEDLKIARSLVPKALEGYITDISTGPSWLNQGLLLNSTQSVSNLDPTTGATVPQSSVNQGLCLDAEVALATGQLPASNSHQSSSAASHFSESRGETPCSFNDEDEEDEEEDPSSPE | ||||||
Modified residue | 24 | Phosphoserine; by CDK2 | ||||
Sequence: S | ||||||
Modified residue | 42 | Phosphoserine; by CDK2 | ||||
Sequence: S | ||||||
Modified residue | 122 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation by E2F1-bound cyclin A-CDK2, in the S phase, inhibits E2F-mediated DNA binding and transactivation.
Keywords
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q64163-4 | E2f5 Q61502 | 2 | EBI-8077763, EBI-7225685 | |
BINARY | Q64163-4 | Ywhae P62259 | 6 | EBI-8077763, EBI-356480 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 60-82 | Interaction with CEBPA | ||||
Sequence: PQMIISTPQRIANSGSVLIGNPY | ||||||
Motif | 103-118 | Nuclear localization signal | ||||
Sequence: SDRKRAREFIDSDFSE | ||||||
Motif | 176-210 | DEF box | ||||
Sequence: DQENIRRRVYDALNVLMAMNIISSLPTGKKRNQVD | ||||||
Region | 219-292 | Dimerization | ||||
Sequence: NLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNQGPPAVNSTIQLPFIIINTSRKTVIDCSIS | ||||||
Region | 229-261 | DCB1 | ||||
Sequence: ERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQ | ||||||
Region | 274-330 | DCB2 | ||||
Sequence: LPFIIINTSRKTVIDCSISSDKFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCS | ||||||
Compositional bias | 404-426 | Polar residues | ||||
Sequence: LPASNSHQSSSAASHFSESRGET | ||||||
Region | 404-446 | Disordered | ||||
Sequence: LPASNSHQSSSAASHFSESRGETPCSFNDEDEEDEEEDPSSPE | ||||||
Compositional bias | 430-446 | Acidic residues | ||||
Sequence: FNDEDEEDEEEDPSSPE |
Sequence similarities
Belongs to the E2F/DP family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- NameAlpha
- Length446
- Mass (Da)49,098
- Last updated2000-05-30 v2
- Checksum0E6E87AE8B82EE8A
Q64163-2
- NameBeta
Q64163-3
- NameGamma
Q64163-4
- NameDelta
- Differences from canonical
- 1-61: Missing
Computationally mapped potential isoform sequences
There are 11 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PWL5 | E9PWL5_MOUSE | Tfdp2 | 310 | ||
Q8BHD2 | Q8BHD2_MOUSE | Tfdp2 | 385 | ||
F6QG91 | F6QG91_MOUSE | Tfdp2 | 386 | ||
A0A087WNL4 | A0A087WNL4_MOUSE | Tfdp2 | 117 | ||
A0A087WPS0 | A0A087WPS0_MOUSE | Tfdp2 | 203 | ||
A0A087WPU8 | A0A087WPU8_MOUSE | Tfdp2 | 446 | ||
J3QK26 | J3QK26_MOUSE | Tfdp2 | 359 | ||
A0A087WQV5 | A0A087WQV5_MOUSE | Tfdp2 | 112 | ||
A0A087WRW3 | A0A087WRW3_MOUSE | Tfdp2 | 39 | ||
A0A087WSK4 | A0A087WSK4_MOUSE | Tfdp2 | 369 | ||
A0A1B0GXK0 | A0A1B0GXK0_MOUSE | Tfdp2 | 368 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_001355 | 1-61 | in isoform Beta, isoform Gamma and isoform Delta | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001356 | 103-118 | in isoform Beta and isoform Gamma | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_001357 | 173 | in isoform Gamma | |||
Sequence: S → SQ | ||||||
Compositional bias | 404-426 | Polar residues | ||||
Sequence: LPASNSHQSSSAASHFSESRGET | ||||||
Compositional bias | 430-446 | Acidic residues | ||||
Sequence: FNDEDEEDEEEDPSSPE |
Keywords
- Coding sequence diversity
- Technical term