AHSA1 (original) (raw)

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Protein-coding gene in the species Homo sapiens

AHSA1

Available structuresPDBOrtholog search: PDBe RCSB List of PDB id codes1X53
Identifiers
Aliases	AHSA1, AHA1, C14orf3, p38, hAha1, activator of Hsp90 ATPase activity 1
External IDs	OMIM: 608466; MGI: 2387603; HomoloGene: 8106; GeneCards: AHSA1; OMA:AHSA1 - orthologs
Gene location (Human)Chr.Chromosome 14 (human)[1]Band14q24.3Start77,457,870 bp [1]End77,469,472 bp [1]
Gene location (Mouse)Chr.Chromosome 12 (mouse)[2]Band12\|12 D2Start87,313,253 bp [2]End87,320,772 bp [2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inoocyteright testissecondary oocyteleft testisright uterine tubeventricular zoneganglionic eminencemuscle of thighC1 segmentBrodmann area 9Top expressed inotic vesiclesacculeotic placodezygoteepiblastmandibular prominenceembryomaxillary prominencefetal liver hematopoietic progenitor celldentate gyrus of hippocampal formation granule cellMore reference expression data BioGPS More reference expression data
Gene ontologyMolecular function ATPase activator activity chaperone binding protein binding cadherin binding Hsp90 protein binding Cellular component extracellular exosome endoplasmic reticulum cytoplasm cytosol Biological process response to stress positive regulation of ATP-dependent activity Sources:Amigo / QuickGO
OrthologsSpeciesHuman MouseEntrez 10598 217737 Ensembl ENSG00000100591 ENSMUSG00000021037 UniProt O95433 Q8BK64RefSeq (mRNA)NM_012111 NM_001321441 NM_146036RefSeq (protein)NP_001308370 NP_036243 NP_666148Location (UCSC)Chr 14: 77.46 – 77.47 Mb Chr 12: 87.31 – 87.32 Mb PubMed search[3][4]
Wikidata
View/Edit Human View/Edit Mouse

Activator of 90 kDa heat shock protein ATPase homolog 1 is an enzyme that in humans is encoded by the AHSA1 gene.[5]

AHSA1 has been shown to interact with Heat shock protein 90kDa alpha (cytosolic), member A1.[6]

^ a b c GRCh38: Ensembl release 89: ENSG00000100591 – Ensembl, May 2017
^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021037 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: AHSA1 AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast)".
^ Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C (Dec 2002). "Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1" (PDF). Mol. Cell. 10 (6): 1307–18. doi:10.1016/S1097-2765(02)00785-2. PMID 12504007.

Human AHSA1 genome location and AHSA1 gene details page in the UCSC Genome Browser.
Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL (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. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (2000). "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.
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.
Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C (2002). "Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1" (PDF). Mol. Cell. 10 (6): 1307–18. doi:10.1016/S1097-2765(02)00785-2. PMID 12504007.
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.
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.
Wang X, Venable J, LaPointe P, Hutt DM, Koulov AV, Coppinger J, Gurkan C, Kellner W, Matteson J, Plutner H, Riordan JR, Kelly JW, Yates JR, Balch WE (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. S2CID 1457851.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (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.