UniProt ID | DNJ19_ARATH | |
---|---|---|
UniProt AC | Q9LZK5 | |
Protein Name | DnaJ protein ERDJ3B | |
Gene Name | ERDJ3B | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 346 | |
Subcellular Localization | Endoplasmic reticulum lumen . | |
Protein Description | Regulates protein folding in the endoplasmic reticulum (ER) lumen. Forms a complex in the ER with SDF2 and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity.. | |
Protein Sequence | MAIRWSELCIVLFALSYAICVLAGKSYYDVLQVPKGASDEQIKRAYRKLALKYHPDKNQGNEEATRKFAEINNAYEVLSDEEKREIYNKYGEEGLKQFSANGGRGGGGGGMNMQDIFSSFFGGGSMEEEEKVVKGDDVIVELEATLEDLYMGGSMKVWREKNVIKPAPGKRKCNCRNEVYHRQIGPGMFQQMTEQVCDKCPNVKYEREGYFVTVDIEKGMKDGEEVSFYEDGEPILDGDPGDLKFRIRTAPHARFRRDGNDLHMNVNITLVEALVGFEKSFKHLDDHEVDISSKGITKPKEVKKFKGEGMPLHYSTKKGNLFVTFEVLFPSSLTDDQKKKIKEVFA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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 DNJ19_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DNJ19_ARATH !! |
* 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 DNJ19_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SUMO3_ARATH | SUMO3 | physical | 20855607 | |
SUMO1_ARATH | SUMO1 | physical | 20855607 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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