| Primary information |
|---|
| ID | 12697 |
| Uniprot ID | P0DMW0 |
| Description | Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2) |
| Organism | Rattus norvegicus |
| Txonomy | Eukaryota; Opisthokonta; Metazoa; Eumetazoa; Bilateria; Deuterostomia; Chordata; Craniata; Vertebrata; Gnathostomata (jawed vertebrates); Teleostomi; Euteleostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Mammalia; Theria; Eutheria; Boreoeutheria; Euarchontoglires; Glires (Rodents and rabbits); Rodentia; Myomorpha (mice and others); Muroidea; Muridae; Murinae; Rattus; Rattus norvegicus (Rat) |
| Subcellular Location | Cytoplasm |
| Developmental Stage | NA |
| Similarity | Belongs to the heat shock protein 70 family. |
| Tissue Specificity | NA |
| Post Translational Modification | In response to cellular stress; acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will |
| 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. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle; but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form; it has a low affinity for substrate proteins. However; upon hydro |
| Length | 641 |
| Molecular Weight | 70 |
| Name | Heat shock 70 kDa protein 1A |
| Sequence | KKTAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVVNDGDKPKVQVNYKGENRSFYPEEISSMVLTKMKEIAEAYLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRGTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTRDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAERYKAEDEVQRERVAAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDSNTLAEKEEFVHKREELERVCNPIISGLYQGAGAPGAGGFGAQAPKGGSGSGPTIEEVD |
| Sequence map | 12-41 |
| PDB ID | NA |
| Drugpedia | NA |
| Receptor | NA |
| Domain | The N-terminal nucleotide binding domain (NBD) (al |
| Pharmaceutical Use | NA
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