| UniProt ID | DDIT3_HUMAN | |
|---|---|---|
| UniProt AC | P35638 | |
| Protein Name | DNA damage-inducible transcript 3 protein | |
| Gene Name | DDIT3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 169 | |
| 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.. | |
| Protein Sequence | MAAESLPFSFGTLSSWELEAWYEDLQEVLSSDENGGTYVSPPGNEEEESKIFTTLDPASLAWLTEEEPEPAEVTSTSQSPHSPDSSQSSLAQEEEEEDQGRTRKRKQSGHSPARAGKQRMKEKEQENERKVAQLAEENERLKQEIERLTREVEATRRALIDRMVNLHQA | |
| 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 | PFSFGTLSSWELEAW CCCCCCCCCHHHHHH | 32.99 | 22817900 | |
| 15 | Phosphorylation | FSFGTLSSWELEAWY CCCCCCCCHHHHHHH | 27.90 | 22817900 | |
| 30 | Phosphorylation | EDLQEVLSSDENGGT HHHHHHHHCCCCCCE | 40.70 | 22817900 | |
| 31 | Phosphorylation | DLQEVLSSDENGGTY HHHHHHHCCCCCCEE | 44.79 | 22817900 | |
| 49 | Phosphorylation | PGNEEEESKIFTTLD CCCHHHHHCCEECCC | 34.04 | - | |
| 54 | Phosphorylation | EESKIFTTLDPASLA HHHCCEECCCHHHHH | 20.58 | - | |
| 64 | Phosphorylation | PASLAWLTEEEPEPA HHHHHHHCCCCCCCC | 30.56 | - | |
| 77 | Phosphorylation | PAEVTSTSQSPHSPD CCCCCCCCCCCCCCC | 28.55 | 22468782 | |
| 79 | Phosphorylation | EVTSTSQSPHSPDSS CCCCCCCCCCCCCCC | 25.09 | 8650547 | |
| 82 | Phosphorylation | STSQSPHSPDSSQSS CCCCCCCCCCCCCCH | 33.51 | 8650547 | |
| 88 | Phosphorylation | HSPDSSQSSLAQEEE CCCCCCCCHHHHHHH | 29.30 | 22468782 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 14 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 14 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 14 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 14 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 15 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 15 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 15 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 15 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 30 | S | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
| 30 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 30 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 30 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 30 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 31 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| 31 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 31 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 31 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 79 | S | Phosphorylation | Kinase | P38-SUBFAMILY | - | GPS |
| 79 | S | Phosphorylation | Kinase | P38_GROUP | - | PhosphoELM |
| 79 | S | Phosphorylation | Kinase | P38A | Q16539 | PSP |
| 82 | S | Phosphorylation | Kinase | P38-SUBFAMILY | - | GPS |
| 82 | S | Phosphorylation | Kinase | P38_GROUP | - | PhosphoELM |
| 82 | S | Phosphorylation | Kinase | P38A | Q16539 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DDIT3_HUMAN !! | ||||||
* 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_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 613488 | Myxoid liposarcoma (MXLIPO) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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