Primary information |
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ID | 12601 |
Uniprot ID | P0DMV8 |
Description | Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 1) (HSP70-1) (HSP70.1) |
Organism | Homo sapiens |
Txonomy | Eukaryota; Opisthokonta; Metazoa; Eumetazoa; Bilateria; Deuterostomia; Chordata; Craniata; Vertebrata; Gnathostomata (jawed vertebrates); Teleostomi; Euteleostomi; Sarcopterygii; Dipnotetrapodomorpha; Tetrapoda; Amniota; Mammalia; Theria; Eutheria; Boreoeutheria; Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini; Hominoidea (apes); Hominidae (great apes); Homininae; Homo; Homo sapiens (Human) |
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 | KAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD |
Sequence map | 12-41 |
PDB ID | 1HJO; 1S3X; 1XQS; 2E88; 2E8A; 2LMG; 3A8Y; 3ATU; 3ATV; 3AY9; 3D2E; 3D2F; 3JXU; 3LOF; 3Q49; 4IO8; 4J8F |
Drugpedia | NA |
Receptor | NA |
Domain | The N-terminal nucleotide binding domain (NBD) (al |
Pharmaceutical Use | NA
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