HSPA1L
entrez
3305
canonical
uniprot
P34931
canonical
ensembl
ENSG00000204390
resolver
ensembl
ENSG00000206383
resolver
ensembl
ENSG00000234258
resolver
ensembl
ENSG00000236251
resolver
ensp
ENSP00000364805
resolver
ensp
ENSP00000372881
resolver
ensp
ENSP00000396486
resolver
ensp
ENSP00000408347
resolver
ensp
ENSP00000549347
resolver
ensp
ENSP00000549348
resolver
ensp
ENSP00000549349
resolver
ensp
ENSP00000549350
resolver
ensp
ENSP00000549351
resolver
ensp
ENSP00000624533
resolver
enst
ENST00000375654
resolver
enst
ENST00000383390
resolver
enst
ENST00000417601
resolver
enst
ENST00000456772
resolver
enst
ENST00000879288
resolver
enst
ENST00000879289
resolver
enst
ENST00000879290
resolver
enst
ENST00000879291
resolver
enst
ENST00000879292
resolver
enst
ENST00000954474
resolver
genesymbol
HSPA1L
resolver
hgnc
HGNC:5234
resolver
uniprot
A0A1U9X7W7
resolver
uniprot
A6NNB0
resolver
uniprot
B0UXW8
resolver
uniprot
O75634
resolver
uniprot
Q2HXR3
resolver
uniprot
Q8NE72
resolver
uniprot
Q96QC9
resolver
uniprot
Q9UQM1
resolver
uniprot_entry
A0A1U9X7W7_HUMAN
resolver
uniprot_entry
HS71L_HUMAN
resolver
uniprot_sec
A6NNB0
resolver
uniprot_sec
B0UXW8
resolver
uniprot_sec
O75634
resolver
uniprot_sec
Q2HXR3
resolver
uniprot_sec
Q8NE72
resolver
uniprot_sec
Q96QC9
resolver
uniprot_sec
Q9UQM1
resolver
amino_acid_sequence
MATAKGIAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPQNTVFDAKRLIGRKFNDPVVQADMKLWPFQVINEGGKPKVLVSYKGENKAFYPEEISSMVLTKLKETAEAFLGHPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDKGGQGERHVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVSHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQANLEIDSLYEGIDFYTSITRARFEELCADLFRGTLEPVEKALRDAKMDKAKIHDIVLVGGSTRIPKVQRLLQDYFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSEKVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFDLTGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKVNKITITNDKGRLSKEEIERMVLDAEKYKAEDEVQREKIAAKNALESYAFNMKSVVSDEGLKGKISESDKNKILDKCNELLSWLEVNQLAEKDEFDHKRKELEQMCNPIITKLYQGGCTGPACGTGYVPGRPATGPTIEEVD
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). Positive regulator of PRKN translocation to damaged mitochondria (PubMed:24270810). {ECO:0000269|PubMed:24270810, ECO:0000303|PubMed:26865365}.
uniprot
proteins
mass_dalton
70375
uniprot
proteins
mutagenesis
MUTAGEN 73; /note="K->E: No rescue of PRKN translocation deficit in knockout cells."; /evidence="ECO:0000269|PubMed:24270810"; MUTAGEN 396; /note="L->D: No rescue of PRKN translocation deficit in knockout cells."; /evidence="ECO:0000269|PubMed:24270810"; MUTAGEN 638..641; /note="Missing: No rescue of PRKN translocation deficit in knockout cells."; /evidence="ECO:0000269|PubMed:24270810
uniprot
proteins
protein_family
Heat shock protein 70 family
uniprot
proteins
pubmed
1356099
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1700760
uniprot
proteins
pubmed
20072699
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24270810
uniprot
proteins
pubmed
26865365
uniprot
proteins
pubmed
9685725
uniprot
proteins
sequence_length
641
uniprot
proteins