Search Results
Overview
| Uniprot ID | P63039 |
|---|---|
| Protein Name | 60 kDa heat shock protein, mitochondrial |
| Gene Name | Hspd1 |
| Organism | Rattus norvegicus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 125 | VLARSIAKEGFEKIS |
| 133 | EGFEKISKGANPVEI |
| 191 | NIISDAMKKVGRKGV |
| 202 | RKGVITVKDGKTLND |
| 233 | PYFINTSKGQKCEFQ |
| 250 | YVLLSEKKISSVQSI |
| 292 | TLVLNRLKVGLQVVA |
| 364 | LLKGKGDKAHIEKRI |
| 396 | KLNERLAKLSDGVAV |
| 417 | SDVEVNEKKDRVTDA |
| 469 | KIGIEIIKRALKIPA |
| 473 | EIIKRALKIPAMTIA |
| 523 | KGIIDPTKVVRTALL |
| 72 | EQSWGSPKVTKDGVT |
| 75 | WGSPKVTKDGVTVAK |
| 91 | IDLKDKYKNIGAKLV |
Function
Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005769 | early endosome |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0031985 | Golgi cisterna |
| Cellular Component | GO:0046696 | lipopolysaccharide receptor complex |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0140494 | migrasome |
| Cellular Component | GO:0030061 | mitochondrial crista |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005782 | peroxisomal matrix |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0030141 | secretory granule |
| Cellular Component | GO:0097225 | sperm midpiece |
| Cellular Component | GO:0042588 | zymogen granule |
| Molecular Function | GO:0034186 | apolipoprotein A-I binding |
| Molecular Function | GO:0034185 | apolipoprotein binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0140662 | ATP-dependent protein folding chaperone |
| Cellular Component | GO:0005905 | clathrin-coated pit |
| Cellular Component | GO:0030135 | coated vesicle |
| Molecular Function | GO:0140608 | cysteine-type endopeptidase activator activity |
| Molecular Function | GO:0003725 | double-stranded RNA binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0008035 | high-density lipoprotein particle binding |
| Molecular Function | GO:0016853 | isomerase activity |
| Molecular Function | GO:0001530 | lipopolysaccharide binding |
| Molecular Function | GO:0140030 | modification-dependent protein binding |
| Molecular Function | GO:0002039 | p53 binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0051087 | protein-folding chaperone binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0006458 | 'de novo' protein folding |
| Biological Process | GO:0008637 | apoptotic mitochondrial changes |
| Biological Process | GO:0042113 | B cell activation |
| Biological Process | GO:0042100 | B cell proliferation |
| Biological Process | GO:0034605 | cellular response to heat |
| Biological Process | GO:0098761 | cellular response to interleukin-7 |
| Biological Process | GO:0048291 | isotype switching to IgG isotypes |
| Biological Process | GO:0034514 | mitochondrial unfolded protein response |
| Biological Process | GO:0002755 | MyD88-dependent toll-like receptor signaling pathway |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0071866 | negative regulation of apoptotic process in bone marrow cell |
| Biological Process | GO:1900118 | negative regulation of execution phase of apoptosis |
| Biological Process | GO:0043524 | negative regulation of neuron apoptotic process |
| Biological Process | GO:1903427 | negative regulation of reactive oxygen species biosynthetic process |
| Biological Process | GO:1900119 | positive regulation of execution phase of apoptosis |
| Biological Process | GO:0032727 | positive regulation of interferon-alpha production |
| Biological Process | GO:0032733 | positive regulation of interleukin-10 production |
| Biological Process | GO:0032735 | positive regulation of interleukin-12 production |
| Biological Process | GO:0032755 | positive regulation of interleukin-6 production |
| Biological Process | GO:0043032 | positive regulation of macrophage activation |
| Biological Process | GO:0050870 | positive regulation of T cell activation |
| Biological Process | GO:0002842 | positive regulation of T cell mediated immune response to tumor cell |
| Biological Process | GO:0032760 | positive regulation of tumor necrosis factor production |
| Biological Process | GO:0032729 | positive regulation of type II interferon production |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0045041 | protein import into mitochondrial intermembrane space |
| Biological Process | GO:0042026 | protein refolding |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0014823 | response to activity |
| Biological Process | GO:0033198 | response to ATP |
| Biological Process | GO:0042220 | response to cocaine |
| Biological Process | GO:0009409 | response to cold |
| Biological Process | GO:0043627 | response to estrogen |
| Biological Process | GO:0051384 | response to glucocorticoid |
| Biological Process | GO:0042542 | response to hydrogen peroxide |
| Biological Process | GO:0001666 | response to hypoxia |
| Biological Process | GO:0002931 | response to ischemia |
| Biological Process | GO:0032496 | response to lipopolysaccharide |
| Biological Process | GO:1904638 | response to resveratrol |
| Biological Process | GO:0006986 | response to unfolded protein |
| Biological Process | GO:0009410 | response to xenobiotic stimulus |
| Biological Process | GO:0042110 | T cell activation |
Reference
[1] Yao Y, Bade R, Li G, Zhang A, Zhao H et al.. Global-Scale Profiling of Differential Expressed Lysine-Lactylated Proteins in the Cerebral Endothelium of Cerebral Ischemia-Reperfusion Injury Rats.. Cell Mol Neurobiol 43(5):1989-2004. 2023 Jul. PMID: 36030297.
[2] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.
[3] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.