Search Results
Overview
| Uniprot ID | P31689 |
|---|---|
| Protein Name | DnaJ homolog subfamily A member 1 |
| Gene Name | DNAJA1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 130 | TRKLALQKNVICDKC |
| 136 | QKNVICDKCEGRGGK |
| 206 | RKIVREKKILEVHID |
| 296 | SHPGQIVKHGDIKCV |
| 317 | IYRRPYEKGRLIIEF |
| 32 | AYRKLALKYHPDKNP |
| 37 | ALKYHPDKNPNEGEK |
Function
Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as a 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 (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0098554 | cytoplasmic side of endoplasmic reticulum membrane |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0015630 | microtubule cytoskeleton |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0001671 | ATPase activator activity |
| Molecular Function | GO:0055131 | C3HC4-type RING finger domain binding |
| Molecular Function | GO:0001664 | G protein-coupled receptor binding |
| Molecular Function | GO:0030544 | Hsp70 protein binding |
| Molecular Function | GO:0050750 | low-density lipoprotein particle receptor binding |
| Molecular Function | GO:0051087 | protein-folding chaperone binding |
| Molecular Function | GO:0030957 | Tat protein binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:1903748 | negative regulation of establishment of protein localization to mitochondrion |
| Biological Process | GO:0043508 | negative regulation of JUN kinase activity |
| Biological Process | GO:1905259 | negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway |
| Biological Process | GO:0031397 | negative regulation of protein ubiquitination |
| Biological Process | GO:0043065 | positive regulation of apoptotic process |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0070585 | protein localization to mitochondrion |
| Biological Process | GO:0051223 | regulation of protein transport |
| Biological Process | GO:0009408 | response to heat |
| Biological Process | GO:0006986 | response to unfolded protein |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.