Search Results
Overview
| Uniprot ID | P14659 |
|---|---|
| Protein Name | Heat shock-related 70 kDa protein 2 |
| Gene Name | Hspa2 |
| Organism | Rattus norvegicus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 72 | TNTIFDAKRLIGRKF |
Function
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0036128 | CatSper complex |
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0001673 | male germ cell nucleus |
| Cellular Component | GO:0072687 | meiotic spindle |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0000795 | synaptonemal complex |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0097718 | disordered domain specific binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0051861 | glycolipid binding |
| Molecular Function | GO:0031072 | heat shock protein binding |
| Molecular Function | GO:0044183 | protein folding chaperone |
| Molecular Function | GO:0051087 | protein-folding chaperone binding |
| Molecular Function | GO:0048156 | tau protein binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0007141 | male meiosis I |
| Biological Process | GO:0007140 | male meiotic nuclear division |
| Biological Process | GO:0090084 | negative regulation of inclusion body assembly |
| Biological Process | GO:0010971 | positive regulation of G2/M transition of mitotic cell cycle |
| Biological Process | GO:0001934 | positive regulation of protein phosphorylation |
| Biological Process | GO:0042026 | protein refolding |
| Biological Process | GO:0009409 | response to cold |
| Biological Process | GO:0009408 | response to heat |
| Biological Process | GO:0007286 | spermatid development |
| Biological Process | GO:0007283 | spermatogenesis |
| Biological Process | GO:0070194 | synaptonemal complex disassembly |
Reference
[1] 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.
[2] 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.