AHSA1

AHSA1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1X53
Identifiers
Aliases	AHSA1 , AHA1, C14orf3, p38, hAha1, activator of Hsp90 ATPase activity 1
External IDs	OMIM: 608466 MGI: 2387603 HomoloGene: 8106 GeneCards: AHSA1
Gene location (Human)
Chr.	Chromosome 14 (human)
End	77,469,472 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	87,273,998 bp
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• ATPase activator activity ; • chaperone binding ; • GO:0001948 protein binding ; • cadherin binding ; • Hsp90 protein binding ;
Cellular component	• extracellular exosome ; • endoplasmic reticulum ; • cytoplasm ; • cytosol ;
Biological process	• response to stress ; • positive regulation of ATPase activity ;
	Sources:Amigo / QuickGO
Orthologs
	10598
	217737
	ENSG00000100591
	ENSMUSG00000021037
	O95433
	Q8BK64
	NM_012111 ; NM_001321441
	NM_146036
	NP_001308370 ; NP_036243
	NP_666148
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 19, 2021

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

Interactions

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

Related Research Articles

Hsp90 Heat shock proteins with a molecular mass around 90kDa

Hsp90 is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs.

Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene.

PRA1 family protein 3 is a protein that in humans is encoded by the ARL6IP5 gene.

Vacuolar protein sorting-associated protein 4A is a protein that in humans is encoded by the VPS4A gene.

Hsp70-binding protein 1 is a protein that in humans is encoded by the HSPBP1 gene.

Mediator of RNA polymerase II transcription subunit 4 also known as mediator complex subunit 4 (MED4), a component of Mediator or vitamin D3 receptor-interacting protein complex 36 kDa component (DRIP36) is a protein that in humans is encoded by the MED4 gene.

V-type proton ATPase subunit H is an enzyme that in humans is encoded by the ATP6V1H gene.

V-type proton ATPase subunit G 1 is an enzyme that in humans is encoded by the ATP6V1G1 gene.

The ATP5MF gene encodes the ATP synthase subunit f, mitochondrial enzyme in humans.

ATP-binding cassette sub-family B member 7, mitochondrial is a protein that in humans is encoded by the ABCB7 gene.

Eukaryotic translation initiation factor 4E type 2 is a protein that in humans is encoded by the EIF4E2 gene. It belongs to the eukaryotic translation initiation factor 4E family.

Splicing factor 3B, 14 kDa subunit, also known as SF3B14, is a human gene.

Ergosterol biosynthetic protein 28 is a protein that in humans is encoded by the ERG28 gene.

Ras-related protein Rab-10 is a protein that in humans is encoded by the RAB10 gene.

Chromodomain-helicase-DNA-binding protein 1-like (ALC1) is an enzyme that in humans is encoded by the CHD1L gene. It has been implicated in chromatin remodeling and DNA relaxation process required for DNA replication, repair and transcription. The ALC1 comprises ATPase domain and macro domain. On the basis of homology within the ATPase domain, ALC1 belongs to Snf2 family.

Elongator complex protein 5 (ELP5) also known as dermal papilla-derived protein 6 (DERP6) is a protein that in humans is encoded by the ELP5 gene.

39S ribosomal protein L33, mitochondrial is a protein that in humans is encoded by the MRPL33 gene.

AHSA2 also known as AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast) is a human gene which encodes a protein which acts as co-chaperone of Hsp90. AHSA2 and the related AHSA1 belongs to the AHA family of stress-regulated proteins that bind directly to Hsp90 and are required for Hsp90-dependent activation of client proteins.

The GHKL domain is an evolutionary conserved protein domain.

The chaperone code refers to post-translational modifications of molecular chaperones that control protein folding. Whilst the genetic code specifies how DNA makes proteins, and the histone code regulates histone-DNA interactions, the chaperone code controls how proteins are folded to produce a functional proteome.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000100591 - Ensembl, May 2017
1 2 3 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.

External links

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. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100591 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000021037 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: AHSA1 AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast)".

[pmid12504007-6] 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.

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AHSA1

Contents

Interactions

Related Research Articles

References

External links

Further reading