Search Results
Overview
| Uniprot ID | A0A4X1T4G7 |
|---|---|
| Protein Name | Activator of 90 kDa heat shock protein ATPase homolog 1 |
| Gene Name | AHSA1 |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 203 | QARPVGVKIPTCKIT |
| 94 | LNWTGTSKSGVQYKG |
Function
Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins
Protein Sequence
10
MAKWGEGDPR
20
WIVEERADAT
30
NVNNWHWTER
40
DASNWSTDKL
50
KTLFLAVRVQ
60
NEEGKCEVTE
70
VNKLDGEASI
80
NNRKGKLIFF
90
YEWSIKLNWT
100
GTSKSGVQYK
110
GHVDIPNLSD
120
ENSVDEVEIS
130
VSLAKDEPDT
140
NLVALMKEEG
150
VRLLREAMGI
160
YISTLKTEFT
170
QGMILPTMNG
180
ESVDPAGQPA
190
LKTEERKAKS
200
APSKTQARPV
210
GVKIPTCKIT
220
LRETFLTSPE
230
ELYRVFTNQE
240
LVQAFTHAPA
250
MLEADKGGKF
260
HLVDGNVSGE
270
FTDLVPEKHI
280
VMKWRFKSWP
290
EGHFATITLT
300
FIDKNGETEL
310
CMEGRGVPAP
320
EEERTRQGWQ
330
RYYFEGIKQT
FGYGARLF
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Molecular Function | GO:0001671 | ATPase activator activity |
| Molecular Function | GO:0051879 | Hsp90 protein binding |
| Molecular Function | GO:0044183 | protein folding chaperone |
| Molecular Function | GO:0051087 | protein-folding chaperone binding |
| Biological Process | GO:0036506 | maintenance of unfolded protein |
| Biological Process | GO:0006457 | protein folding |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.