Ahsa1
entrez
217737
canonical
uniprot
Q8BK64
canonical
ensembl
ENSMUSG00000021037
resolver
ensp
ENSMUSP00000021425
resolver
enst
ENSMUST00000021425
resolver
genesymbol
Ahsa1
resolver
uniprot
Q8R3E6
resolver
uniprot_entry
AHSA1_MOUSE
resolver
uniprot_sec
Q8R3E6
resolver
amino_acid_sequence
MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTEKLKTLFLAVRVENEEGKCEVTEVNKLDGEASINNRKGKLIFFYEWTIKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEDGVKLLREAVGIYISTLKTEFTQGMILPTVNGESVDPVGQPALKTETCKAKSAPSKSQAKPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
uniprot
proteins
function
FUNCTION: Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). {ECO:0000250|UniProtKB:O95433, ECO:0000269|PubMed:29127155}.
uniprot
proteins
mass_dalton
38117
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1. {ECO:0000305|PubMed:29127155}.
uniprot
proteins
protein_family
AHA1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22022502
uniprot
proteins
pubmed
29127155
uniprot
proteins
sequence_length
338
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O95433}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O95433}. Note=May transiently interact with the endoplasmic reticulum. {ECO:0000250|UniProtKB:O95433}.
uniprot
proteins