AHSA1

AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast)

PDB rendering based on 1x53.

Available structures
PDB	1x53

Identifiers

Symbols

AHSA1; AHA1; C14orf3; p38

External IDs

OMIM: 608466 MGI: 2387603 HomoloGene: 8106 GeneCards: AHSA1 Gene

Gene Ontology
Molecular function	• ATPase activator activity • ATPase activator activity • protein binding • chaperone binding
Cellular component	• cytoplasm • cytoplasm • endoplasmic reticulum • cytosol
Biological process	• protein folding • response to stress • positive regulation of ATPase activity • positive regulation of ATPase activity
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
77.92 – 77.94 Mb

Chr 12:
88.61 – 88.61 Mb

PubMed search

[1]

[2]

Activator of 90 kDa heat shock protein ATPase homolog 1 is an enzyme that in humans is encoded by the AHSA1 gene.^[1]

Interactions

AHSA1 has been shown to interact with Heat shock protein 90kDa alpha (cytosolic), member A1.^[2]

References

^ "Entrez Gene: AHSA1 AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10598.
^ Panaretou, Barry; Siligardi Giuliano, Meyer Philippe, Maloney Alison, Sullivan Janis K, Singh Shradha, Millson Stefan H, Clarke Paul A, Naaby-Hansen Soren, Stein Rob, Cramer Rainer, Mollapour Mehdi, Workman Paul, Piper Peter W, Pearl Laurence H, Prodromou Chrisostomos (Dec. 2002). "Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1". Mol. Cell (United States) 10 (6): 1307–18. doi:10.1016/S1097-2765(02)00785-2. ISSN 1097-2765. PMID 12504007.

Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=16901.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310934.
Sevier CS, Machamer CE (2001). "p38: A novel protein that associates with the vesicular stomatitis virus glycoprotein". Biochem. Biophys. Res. Commun. 287 (2): 574–82. doi:10.1006/bbrc.2001.5621. PMID 11554768.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Panaretou B, Siligardi G, Meyer P, et al. (2003). "Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1". Mol. Cell 10 (6): 1307–18. doi:10.1016/S1097-2765(02)00785-2. PMID 12504007.
Heilig R, Eckenberg R, Petit JL, et al. (2003). "The DNA sequence and analysis of human chromosome 14". Nature 421 (6923): 601–7. doi:10.1038/nature01348. PMID 12508121.
Lotz GP, Lin H, Harst A, Obermann WM (2003). "Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone". J. Biol. Chem. 278 (19): 17228–35. doi:10.1074/jbc.M212761200. PMID 12604615.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Swick L, Kapatos G (2006). "A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions". J. Neurochem. 97 (5): 1447–55. doi:10.1111/j.1471-4159.2006.03836.x. PMC 2239266. PMID 16696853. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2239266.
Wang X, Venable J, LaPointe P, et al. (2006). "Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis". Cell 127 (4): 803–15. doi:10.1016/j.cell.2006.09.043. PMID 17110338.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.

PDB gallery

1x53: The solution structure of the C-terminal domain of human Activator of 90 kDa heat shock protein ATPase homolog 1

AHSA1

Interactions

References

Further reading