HSPA6
entrez
3310
canonical
uniprot
P17066
canonical
ensembl
ENSG00000173110
resolver
ensp
ENSP00000310219
resolver
enst
ENST00000309758
resolver
genesymbol
HSPA6
resolver
genesymbol_syn
HSP70B'
resolver
hgnc
HGNC:5239
resolver
uniprot
A0A384NKX5
resolver
uniprot
B3KSM6
resolver
uniprot
Q1HBA8
resolver
uniprot
Q8IYK7
resolver
uniprot
Q9BT95
resolver
uniprot_entry
A0A384NKX5_HUMAN
resolver
uniprot_entry
B3KSM6_HUMAN
resolver
uniprot_entry
HSP76_HUMAN
resolver
uniprot_sec
Q1HBA8
resolver
uniprot_sec
Q8IYK7
resolver
uniprot_sec
Q9BT95
resolver
amino_acid_sequence
MQAPRELAVGIDLGTTYSCVGVFQQGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPHNTVFDAKRLIGRKFADTTVQSDMKHWPFRVVSEGGKPKVRVCYRGEDKTFYPEEISSMVLSKMKETAEAYLGQPVKHAVITVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDRRGAGERNVLIFDLGGGTFDVSVLSIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHGKDLSGNKRALRRLRTACERAKRTLSSSTQATLEIDSLFEGVDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDVVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAVLMGDKCEKVQDLLLLDVAPLSLGLETAGGVMTTLIQRNATIPTKQTQTFTTYSDNQPGVFIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILSVTATDRSTGKANKITITNDKGRLSKEEVERMVHEAEQYKAEDEAQRDRVAAKNSLEAHVFHVKGSLQEESLRDKIPEEDRRKMQDKCREVLAWLEHNQLAEKEEYEHQKRELEQICRPIFSRLYGGPGVPGGSSCGTQARQGDPSTGPIIEEVD
uniprot
proteins
function
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 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 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 (PubMed:26865365). {ECO:0000303|PubMed:26865365}.
uniprot
proteins
mass_dalton
71028
uniprot
proteins
mutagenesis
MUTAGEN 563; /note="K->R: Complete loss of in vitro methylation by METTL21A."; /evidence="ECO:0000269|PubMed:23921388
uniprot
proteins
protein_family
Heat shock protein 70 family
uniprot
proteins
pubmed
1346391
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
20072699
uniprot
proteins
pubmed
2327978
uniprot
proteins
pubmed
23921388
uniprot
proteins
pubmed
26865365
uniprot
proteins
pubmed
3184191
uniprot
proteins
sequence_length
643
uniprot
proteins