| UniProt ID | DNJA1_RAT | |
|---|---|---|
| UniProt AC | P63036 | |
| Protein Name | DnaJ homolog subfamily A member 1 | |
| Gene Name | Dnaja1 | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 397 | |
| Subcellular Localization |
Membrane Lipid-anchor. Cytoplasm . Microsome . Mitochondrion . Nucleus . Cytoplasm, perinuclear region. Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria. |
|
| Protein Description | Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. [PubMed: 10816573] | |
| Protein Sequence | MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLADSKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS | |
| 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 |
|---|---|---|---|---|---|
| 37 | Succinylation | ALKYHPDKNPNEGEK HHHHCCCCCCCCCHH | 77.93 | 26843850 | |
| 66 | Acetylation | KKRELYDKGGEQAIK HCHHHHHCHHHHHHH | 56.08 | 22902405 | |
| 83 | Phosphorylation | GAGGGFGSPMDIFDM CCCCCCCCHHHHHHH | 18.13 | 25403869 | |
| 112 | Phosphorylation | KNVVHQLSVTLEDLY CCCEEEEECCHHHHH | 13.39 | 23984901 | |
| 114 | Phosphorylation | VVHQLSVTLEDLYNG CEEEEECCHHHHHCC | 22.51 | 23984901 | |
| 119 | Phosphorylation | SVTLEDLYNGATRKL ECCHHHHHCCHHHHH | 24.71 | - | |
| 175 | Phosphorylation | GMVQQIQSVCMECQG HHHHHHHHHHHHCCC | 20.93 | 16641100 | |
| 296 | Acetylation | SHPGQIVKHGDIKCV CCCCCEEECCCEEEE | 43.42 | 22902405 | |
| 335 | Phosphorylation | FPENGFLSPDKLSLL CCCCCCCCHHHHHHH | 28.88 | 29779826 | |
| 340 | Phosphorylation | FLSPDKLSLLEKLLP CCCHHHHHHHHHHCC | 36.33 | 28432305 | |
| 381 | Phosphorylation | RHYNGEAYEDDEHHP HHCCCCCCCCCCCCC | 18.65 | - | |
| 394 | Farnesylation | HPRGGVQCQTS---- CCCCCCCCCCC---- | 4.41 | - | |
| 394 | Methylation | HPRGGVQCQTS---- CCCCCCCCCCC---- | 4.41 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of DNJA1_RAT !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DNJA1_RAT !! | ||||||
* 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 DNJA1_RAT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of DNJA1_RAT !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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