Hspa1l
entrez
24963
canonical
uniprot
P55063
canonical
ensembl
ENSRNOG00000047966
resolver
ensembl
ENSRNOG00055007902
resolver
ensembl
ENSRNOG00060004760
resolver
ensembl
ENSRNOG00065031164
resolver
ensp
ENSRNOP00000063974
resolver
ensp
ENSRNOP00000106918
resolver
ensp
ENSRNOP00000110573
resolver
ensp
ENSRNOP00055010671
resolver
ensp
ENSRNOP00060005964
resolver
ensp
ENSRNOP00065044175
resolver
enst
ENSRNOT00000074223
resolver
enst
ENSRNOT00000126760
resolver
enst
ENSRNOT00000144895
resolver
enst
ENSRNOT00055013295
resolver
enst
ENSRNOT00060007951
resolver
enst
ENSRNOT00065053730
resolver
genesymbol
Hspa1l
resolver
genesymbol_syn
Hsp70-3
resolver
uniprot
Q32P36
resolver
uniprot
Q6MG67
resolver
uniprot_entry
HS71L_RAT
resolver
uniprot_sec
Q32P36
resolver
uniprot_sec
Q6MG67
resolver
amino_acid_sequence
MAANKGMAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQSDMKLWPFQVINEAGKPKVLVSYKGEKKAFYPEEISSMVLTKMKETAEAFLGHSVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGSHGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKSLRDAKMDKAKIHDIVLVGGSTRIPKVQKLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKVQDLLLLDVAPLSLGLETAGGVMTVLIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTRDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDANGILNVTAMDKSTGKANKITITNDKGRLSKEEIERMVQEAERYKAEDEGQREKIAAKNALESYAFNMKSAVGDEGLKDKISESDKKKILDKCSEVLSWLEANQLAEKEEFDHKRKELENMCNPIITKLYQSGCTGPTCAPGYTPGRAATGPTIEEVD
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. Positive regulator of PRKN translocation to damaged mitochondria. {ECO:0000250|UniProtKB:P34931}.
uniprot
proteins
mass_dalton
70549
uniprot
proteins
protein_family
Heat shock protein 70 family
uniprot
proteins
pubmed
15060004
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
7927536
uniprot
proteins
sequence_length
641
uniprot
proteins