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Overview

Uniprot IDO95433
Protein NameActivator of 90 kDa heat shock protein ATPase homolog 1
Gene NameAHSA1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
194 KAKPAPSKTQARPVG
203 QARPVGVKIPTCKIT
3 *****MAKWGEGDPR
55 QVQNEEGKCEVTEVS

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 (PubMed:27353360). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155)

Protein Sequence

10 MAKWGEGDPR 20 WIVEERADAT 30 NVNNWHWTER 40 DASNWSTDKL 50 KTLFLAVQVQ 60 NEEGKCEVTE 70 VSKLDGEASI 80 NNRKGKLIFF 90 YEWSVKLNWT 100 GTSKSGVQYK 110 GHVEIPNLSD 120 ENSVDEVEIS 130 VSLAKDEPDT 140 NLVALMKEEG 150 VKLLREAMGI 160 YISTLKTEFT 170 QGMILPTMNG 180 ESVDPVGQPA 190 LKTEERKAKP 200 APSKTQARPV 210 GVKIPTCKIT 220 LKETFLTSPE 230 ELYRVFTTQE 240 LVQAFTHAPA 250 TLEADRGGKF 260 HMVDGNVSGE 270 FTDLVPEKHI 280 VMKWRFKSWP 290 EGHFATITLT 300 FIDKNGETEL 310 CMEGRGIPAP 320 EEERTRQGWQ 330 RYYFEGIKQT FGYGARLF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0070062 extracellular exosome
Molecular Function GO:0001671 ATPase activator activity
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0051879 Hsp90 protein binding
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0051087 protein-folding chaperone binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0036506 maintenance of unfolded protein
Biological Process GO:0032781 positive regulation of ATP-dependent activity
Biological Process GO:0006457 protein folding

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[6] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.