Search Results
Overview
| Uniprot ID | Q12931 |
|---|---|
| Protein Name | Heat shock protein 75 kDa, mitochondrial |
| Gene Name | TRAP1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 109 | ARSLYSEKEVFIREL |
| 126 | NASDALEKLRHKLVS |
| 324 | YVAQAHDKPRYTLHY |
| 369 | SVALYSRKVLIQTKA |
| 375 | RKVLIQTKATDILPK |
| 431 | KFFIDQSKKDAEKYA |
| 546 | LREFDKKKLISVETD |
| 598 | GSRVTNVKVTLRLDT |
| 629 | LRMQQLAKTQEERAQ |
| 95 | HEFQAETKKLLDIVA |
| 96 | EFQAETKKLLDIVAR |
Function
Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005758 | mitochondrial intermembrane space |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0140662 | ATP-dependent protein folding chaperone |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0005164 | tumor necrosis factor receptor binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:1901856 | negative regulation of cellular respiration |
| Biological Process | GO:1903751 | negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide |
| Biological Process | GO:1903427 | negative regulation of reactive oxygen species biosynthetic process |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0009386 | translational attenuation |
Reference
[1] 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.
[2] 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.
[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.