AHSA1

From Wikipedia, the free encyclopedia

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

PDB rendering based on 1x53.

Available structures: 1x53

Identifiers

Symbol(s)

AHSA1; p38; AHA1; C14orf3

External IDs

OMIM: 608466 MGI: 2387603 HomoloGene: 8106

Gene ontology
Molecular Function:	• ATPase activator activity • chaperone activator activity • chaperone binding
Cellular Component:	• cytoplasm • endoplasmic reticulum
Biological Process:	• protein folding • response to stress

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012111 (mRNA)
NP_036243 (protein)

NM_146036 (mRNA)
NP_666148 (protein)

Location

Chr 14: 76.99 - 77.01 Mb

Chr 12: 88.16 - 88.16 Mb

Pubmed search

[1]

[2]

AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast), also known as AHSA1, is a human gene.^[1]

[edit] References

^ Entrez Gene: AHSA1 AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast).

[edit] Further reading

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. PMID 10931946.
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. PMID 11042152.
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. PMID 12477932.
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. 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. PMID 15489334.
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. PMID 16696853.
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: 89. doi:10.1038/msb4100134. PMID 17353931.