Heat shock protein 90kDa alpha (cytosolic), member A1

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Heat shock protein 90kDa alpha (cytosolic), class A member 1
Protein HSP90AA1 PDB 1byq.png
PDB rendering based on 1byq.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols HSP90AA1 ; EL52; HSP86; HSP89A; HSP90A; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; Hsp89; Hsp90; LAP-2; LAP2
External IDs OMIM140571 MGI96250 HomoloGene68464 ChEMBL: 3880 GeneCards: HSP90AA1 Gene
RNA expression pattern
PBB GE HSP90AA1 211969 at tn.png
PBB GE HSP90AA1 210211 s at tn.png
PBB GE HSP90AA1 211968 s at tn.png
More reference expression data
Species Human Mouse
Entrez 3320 15519
Ensembl ENSG00000080824 ENSMUSG00000021270
UniProt P07900 P07901
RefSeq (mRNA) NM_001017963 NM_010480
RefSeq (protein) NP_001017963 NP_034610
Location (UCSC) Chr 14:
102.55 – 102.61 Mb
Chr 12:
110.69 – 110.7 Mb
PubMed search [1] [2]

Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the HSP90AA1 gene.[1][2]


Heat shock protein 90kDa alpha (cytosolic), member A1 has been shown to interact with:


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  16. ^ a b Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF (1996). "A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor". Cell Stress Chaperones 1 (4): 237–50. doi:10.1379/1466-1268(1996)001<0237:APOMCI>2.3.CO;2. PMC 376461. PMID 9222609. 
  17. ^ Lee MO, Kim EO, Kwon HJ, Kim YM, Kang HJ, Kang H, Lee JE (2002). "Radicicol represses the transcriptional function of the estrogen receptor by suppressing the stabilization of the receptor by heat shock protein 90". Mol. Cell. Endocrinol. 188 (1-2): 47–54. doi:10.1016/S0303-7207(01)00753-5. PMID 11911945. 
  18. ^ Nair SC, Rimerman RA, Toran EJ, Chen S, Prapapanich V, Butts RN, Smith DF (1997). "Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor". Mol. Cell. Biol. 17 (2): 594–603. PMC 231784. PMID 9001212. 
  19. ^ Vaiskunaite R, Kozasa T, Voyno-Yasenetskaya TA (2001). "Interaction between the G alpha subunit of heterotrimeric G(12) protein and Hsp90 is required for G alpha(12) signaling". J. Biol. Chem. 276 (49): 46088–93. doi:10.1074/jbc.M108711200. PMID 11598136. 
  20. ^ a b Venema RC, Venema VJ, Ju H, Harris MB, Snead C, Jilling T, Dimitropoulou C, Maragoudakis ME, Catravas JD (2003). "Novel complexes of guanylate cyclase with heat shock protein 90 and nitric oxide synthase". Am. J. Physiol. Heart Circ. Physiol. 285 (2): H669–78. doi:10.1152/ajpheart.01025.2002. PMID 12676772. 
  21. ^ Xu W, Mimnaugh E, Rosser MF, Nicchitta C, Marcu M, Yarden Y, Neckers L (2001). "Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90". J. Biol. Chem. 276 (5): 3702–8. doi:10.1074/jbc.M006864200. PMID 11071886. 
  22. ^ Jeong JH, An JY, Kwon YT, Li LY, Lee YJ (2008). "Quercetin-induced ubiquitination and down-regulation of Her-2/neu". J. Cell. Biochem. 105 (2): 585–95. doi:10.1002/jcb.21859. PMC 2575035. PMID 18655187. 
  23. ^ Hu Y, Mivechi NF (2003). "HSF-1 interacts with Ral-binding protein 1 in a stress-responsive, multiprotein complex with HSP90 in vivo". J. Biol. Chem. 278 (19): 17299–306. doi:10.1074/jbc.M300788200. PMID 12621024. 
  24. ^ Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I (2000). "Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine". Cell 101 (2): 199–210. doi:10.1016/S0092-8674(00)80830-2. PMID 10786835. 
  25. ^ Johnson BD, Schumacher RJ, Ross ED, Toft DO (1998). "Hop modulates Hsp70/Hsp90 interactions in protein folding". J. Biol. Chem. 273 (6): 3679–86. doi:10.1074/jbc.273.6.3679. PMID 9452498. 
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  27. ^ Stepp DW, Ou J, Ackerman AW, Welak S, Klick D, Pritchard KA (2002). "Native LDL and minimally oxidized LDL differentially regulate superoxide anion in vascular endothelium in situ". Am. J. Physiol. Heart Circ. Physiol. 283 (2): H750–9. doi:10.1152/ajpheart.00029.2002. PMID 12124224. 
  28. ^ Jibard N, Meng X, Leclerc P, Rajkowski K, Fortin D, Schweizer-Groyer G, Catelli MG, Baulieu EE, Cadepond F (1999). "Delimitation of two regions in the 90-kDa heat shock protein (Hsp90) able to interact with the glucocorticosteroid receptor (GR)". Exp. Cell Res. 247 (2): 461–74. doi:10.1006/excr.1998.4375. PMID 10066374. 
  29. ^ Kanelakis KC, Shewach DS, Pratt WB (2002). "Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly". J. Biol. Chem. 277 (37): 33698–703. doi:10.1074/jbc.M204164200. PMID 12093808. 
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  33. ^ Stancato LF, Silverstein AM, Gitler C, Groner B, Pratt WB (1996). "Use of the thiol-specific derivatizing agent N-iodoacetyl-3-[125I]iodotyrosine to demonstrate conformational differences between the unbound and hsp90-bound glucocorticoid receptor hormone binding domain". J. Biol. Chem. 271 (15): 8831–6. doi:10.1074/jbc.271.15.8831. PMID 8621522. 
  34. ^ Wang C, Chen J (2003). "Phosphorylation and hsp90 binding mediate heat shock stabilization of p53". J. Biol. Chem. 278 (3): 2066–71. doi:10.1074/jbc.M206697200. PMID 12427754. 
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  38. ^ Sumanasekera WK, Tien ES, Turpey R, Vanden Heuvel JP, Perdew GH (2003). "Evidence that peroxisome proliferator-activated receptor alpha is complexed with the 90-kDa heat shock protein and the hepatitis virus B X-associated protein 2". J. Biol. Chem. 278 (7): 4467–73. doi:10.1074/jbc.M211261200. PMID 12482853. 
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  40. ^ Boudeau J, Deak M, Lawlor MA, Morrice NA, Alessi DR (2003). "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". Biochem. J. 370 (Pt 3): 849–57. doi:10.1042/BJ20021813. PMC 1223241. PMID 12489981. 
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Further reading[edit]