| UniProt ID | DDIT3_MOUSE | |
|---|---|---|
| UniProt AC | P35639 | |
| Protein Name | DNA damage-inducible transcript 3 protein | |
| Gene Name | Ddit3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 168 | |
| Subcellular Localization | Cytoplasm. Nucleus. Present in the cytoplasm under non-stressed conditions and ER stress leads to its nuclear accumulation. | |
| Protein Description | Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes. Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes. Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L. Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity. Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response. Acts as a major regulator of postnatal neovascularization through regulation of endothelial nitric oxide synthase (NOS3)-related signaling.. | |
| Protein Sequence | MAAESLPFTLETVSSWELEAWYEDLQEVLSSDEIGGTYISSPGNEEEESKTFTTLDPASLAWLTEEPGPTEVTRTSQSPRSPDSSQSSMAQEEEEEEQGRTRKRKQSGQCPARPGKQRMKEKEQENERKVAQLAEENERLKQEIERLTREVETTRRALIDRMVSLHQA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 14 | Phosphorylation | PFTLETVSSWELEAW CCEEECCCCHHHHHH | 36.83 | 12876286 | |
| 15 | Phosphorylation | FTLETVSSWELEAWY CEEECCCCHHHHHHH | 21.89 | 12876286 | |
| 30 | Phosphorylation | EDLQEVLSSDEIGGT HHHHHHHHCCCCCCE | 40.70 | 12876286 | |
| 31 | Phosphorylation | DLQEVLSSDEIGGTY HHHHHHHCCCCCCEE | 34.79 | 12876286 | |
| 75 | Phosphorylation | GPTEVTRTSQSPRSP CCCCCEECCCCCCCC | 23.04 | 30635358 | |
| 76 | Phosphorylation | PTEVTRTSQSPRSPD CCCCEECCCCCCCCC | 25.93 | 30635358 | |
| 78 | Phosphorylation | EVTRTSQSPRSPDSS CCEECCCCCCCCCCC | 23.27 | 8650547 | |
| 81 | Phosphorylation | RTSQSPRSPDSSQSS ECCCCCCCCCCCCCH | 36.12 | 8650547 | |
| 84 | Phosphorylation | QSPRSPDSSQSSMAQ CCCCCCCCCCCHHHH | 33.39 | 26643407 | |
| 85 | Phosphorylation | SPRSPDSSQSSMAQE CCCCCCCCCCHHHHH | 41.27 | 26643407 | |
| 87 | Phosphorylation | RSPDSSQSSMAQEEE CCCCCCCCHHHHHHH | 24.83 | 26643407 | |
| 88 | Phosphorylation | SPDSSQSSMAQEEEE CCCCCCCHHHHHHHH | 15.53 | 26643407 | |
| 107 | Phosphorylation | RTRKRKQSGQCPARP HHHHHHHHCCCCCCC | 33.59 | 23684622 | |
| 120 | Ubiquitination | RPGKQRMKEKEQENE CCCHHHHHHHHHHHH | 68.75 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 14 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 15 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 30 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 31 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 78 | S | Phosphorylation | Kinase | MAPKAPK2 | P49138 | GPS |
| 78 | S | Phosphorylation | Kinase | MAPK1 | P63085 | GPS |
| 78 | S | Phosphorylation | Kinase | MAPK14 | P47811 | Uniprot |
| 81 | S | Phosphorylation | Kinase | MAPKAPK2 | P49138 | GPS |
| 81 | S | Phosphorylation | Kinase | MAPK14 | P47811 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DDIT3_MOUSE !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of DDIT3_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CERS2_MOUSE | Cers2 | physical | 20211142 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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