| UniProt ID | DAPK3_RAT | |
|---|---|---|
| UniProt AC | O88764 | |
| Protein Name | Death-associated protein kinase 3 | |
| Gene Name | Dapk3 | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 448 | |
| Subcellular Localization | Nucleus . Nucleus, PML body . Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center . Chromosome, centromere . Cytoplasm, cytoskeleton . Predominantly localized to the nucleus. Relocates to the cytoplasm on binding PAWR where the complex | |
| Protein Description | Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation; in vitro phosphorylates PAWR. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition (By similarity). Phosphorylates STAT3 and enhances its transcriptional activity (By similarity). Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis.. | |
| Protein Sequence | MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRVAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR | |
| 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 |
|---|---|---|---|---|---|
| 51 | Phosphorylation | IKKRRLPSSRRGVSR HHHCCCCCCCCCCCH | 40.86 | 26022182 | |
| 52 | Phosphorylation | KKRRLPSSRRGVSRE HHCCCCCCCCCCCHH | 24.85 | 26022182 | |
| 180 | Phosphorylation | EFKNIFGTPEFVAPE CHHHHHCCCCCCCCC | 14.64 | - | |
| 225 | Phosphorylation | LGETKQETLTNISAV CCCCCCHHHHHCEEE | 36.07 | - | |
| 265 | Phosphorylation | KDPKRRMTIAQSLEH CCHHHCCCHHHHHHH | 16.02 | - | |
| 304 | Phosphorylation | LREYSLKSHSSMPRN HHHHHCCCCCCCCCC | 33.62 | 23984901 | |
| 306 | Phosphorylation | EYSLKSHSSMPRNTS HHHCCCCCCCCCCCC | 35.11 | 23984901 | |
| 307 | Phosphorylation | YSLKSHSSMPRNTSY HHCCCCCCCCCCCCH | 27.64 | 23984901 | |
| 312 | Phosphorylation | HSSMPRNTSYASFER CCCCCCCCCHHHHHH | 25.13 | 23984901 | |
| 313 | Phosphorylation | SSMPRNTSYASFERF CCCCCCCCHHHHHHH | 23.42 | 23984901 | |
| 314 | Phosphorylation | SMPRNTSYASFERFS CCCCCCCHHHHHHHH | 12.29 | 23984901 | |
| 316 | Phosphorylation | PRNTSYASFERFSRV CCCCCHHHHHHHHHH | 21.29 | 23984901 | |
| 321 | Phosphorylation | YASFERFSRVLEDVA HHHHHHHHHHHHHHH | 27.92 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 265 | T | Phosphorylation | Kinase | ROCK1 | Q63644 | Uniprot |
| 304 | S | Phosphorylation | Kinase | DAPK1 | - | Uniprot |
| 306 | S | Phosphorylation | Kinase | DAPK1 | - | Uniprot |
| 307 | S | Phosphorylation | Kinase | DAPK1 | - | Uniprot |
| 313 | S | Phosphorylation | Kinase | DAPK1 | - | Uniprot |
| 321 | S | Phosphorylation | Kinase | DAPK1 | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 180 | T | Phosphorylation |
| - |
| 225 | T | Phosphorylation |
| - |
| 265 | T | Phosphorylation |
| - |
* 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 DAPK3_RAT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PAWR_RAT | Pawr | physical | 10580117 | |
| ATF4_RAT | Atf4 | physical | 10580117 | |
| TPM1_RAT | Tpm1 | physical | 10580117 | |
| AATF_RAT | Aatf | physical | 10580117 | |
| ATF4_RAT | Atf4 | physical | 10602480 | |
| TPM1_RAT | Tpm1 | physical | 10602480 | |
| AATF_RAT | Aatf | physical | 10602480 | |
| PAWR_RAT | Pawr | physical | 10602480 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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