HSP90AB1

Heat shock protein 90kDa alpha (cytosolic), class B member 1
	; PDB rendering based on 1byq.
Available structures
PDB	1QZ2, 1UYM, 3NMQ, 3PRY
Identifiers
Symbols	HSP90AB1; D6S182; HSP90-BETA; HSP90B; HSPC2; HSPCB
External IDs	OMIM: 140572 MGI: 96247 HomoloGene: 74306 GeneCards: HSP90AB1 Gene
Gene Ontology
Molecular function	• nucleotide binding; • protein serine/threonine kinase activity; • protein binding; • ATP binding; • nitric-oxide synthase regulator activity; • TPR domain binding; • unfolded protein binding;
Cellular component	• intracellular; • cytoplasm; • mitochondrion; • cytosol; • signalosome; • melanosome;
Biological process	• placenta development; • protein folding; • response to stress; • response to unfolded protein; • axon guidance; • negative regulation of proteasomal ubiquitin-dependent protein catabolic process; • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; • innate immune response; • positive regulation of nitric oxide biosynthetic process; • regulation of interferon-gamma-mediated signaling pathway; • regulation of type I interferon-mediated signaling pathway;
	Sources: Amigo / QuickGO
Orthologs
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Heat shock protein HSP 90-beta is a protein that in humans is encoded by the HSP90AB1 gene.^[1]^[2]^[3]

[edit] References

^ Rebbe NF, Hickman WS, Ley TJ, Stafford DW, Hickman S (Oct 1989). "Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene". J Biol Chem 264 (25): 15006–11. PMID 2768249.
^ Chen B, Piel WH, Gui L, Bruford E, Monteiro A (Dec 2005). "The HSP90 family of genes in the human genome: insights into their divergence and evolution". Genomics 86 (6): 627–37. doi:10.1016/j.ygeno.2005.08.012. PMID 16269234.
^ "Entrez Gene: HSP90AB1 Heat shock protein 90kDa alpha (cytosolic), class B member 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3326.

[edit] Further reading

Hoffmann T, Hovemann B (1989). "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens.". Gene 74 (2): 491–501. doi:10.1016/0378-1119(88)90182-5. PMID 2469626.
Lees-Miller SP, Anderson CW (1989). "Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II.". J. Biol. Chem. 264 (5): 2431–7. PMID 2492519.
Rebbe NF, Ware J, Bertina RM, et al. (1987). "Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family.". Gene 53 (2–3): 235–45. doi:10.1016/0378-1119(87)90012-6. PMID 3301534.
Tang PZ, Gannon MJ, Andrew A, Miller D (1995). "Evidence for oestrogenic regulation of heat shock protein expression in human endometrium and steroid-responsive cell lines". Eur. J. Endocrinol. 133 (5): 598–605. doi:10.1530/eje.0.1330598. PMID 7581991.
Nemoto T, Ohara-Nemoto Y, Ota M, et al. (1995). "Mechanism of dimer formation of the 90-kDa heat-shock protein". Eur. J. Biochem. 233 (1): 1–8. doi:10.1111/j.1432-1033.1995.001_1.x. PMID 7588731.
Takahashi I, Tanuma R, Hirata M, Hashimoto K (1994). "A cosmid clone at the D6S182 locus on human chromosome 6p12 contains the 90-kDa heat shock protein beta gene (HSP90 beta)". Mamm. Genome 5 (2): 121–2. doi:10.1007/BF00292342. PMID 8180474.
Ji H, Reid GE, Moritz RL, et al. (1997). "A two-dimensional gel database of human colon carcinoma proteins". Electrophoresis 18 (3–4): 605–13. doi:10.1002/elps.1150180344. PMID 9150948.
Yano M, Naito Z, Yokoyama M, et al. (1999). "Expression of hsp90 and cyclin D1 in human breast cancer". Cancer Lett. 137 (1): 45–51. doi:10.1016/S0304-3835(98)00338-3. PMID 10376793.
Sato S, Fujita N, Tsuruo T (2000). "Modulation of Akt kinase activity by binding to Hsp90". Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10832–7. doi:10.1073/pnas.170276797. PMC 27109. PMID 10995457. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=27109.
Gisler SM, Stagljar I, Traebert M, et al. (2001). "Interaction of the type IIa Na/Pi cotransporter with PDZ proteins". J. Biol. Chem. 276 (12): 9206–13. doi:10.1074/jbc.M008745200. PMID 11099500.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a Catalog of Human Genes and Proteins: Sequencing and Analysis of 500 Novel Complete Protein Coding Human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=311072.
King FW, Wawrzynow A, Höhfeld J, Zylicz M (2002). "Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53". EMBO J. 20 (22): 6297–305. doi:10.1093/emboj/20.22.6297. PMC 125724. PMID 11707401. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125724.
Bouhouche-Chatelier L, Chadli A, Catelli MG (2002). "The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor". Cell Stress Chaperones 6 (4): 297–305. doi:10.1379/1466-1268(2001)006<0297:TNTATB>2.0.CO;2. PMC 434412. PMID 11795466. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=434412.
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.
Sato N, Yamamoto T, Sekine Y, et al. (2003). "Involvement of heat-shock protein 90 in the interleukin-6-mediated signaling pathway through STAT3". Biochem. Biophys. Res. Commun. 300 (4): 847–52. doi:10.1016/S0006-291X(02)02941-8. PMID 12559950.
Wu JM, Xiao L, Cheng XK, et al. (2004). "PKC epsilon is a unique regulator for hsp90 beta gene in heat shock response". J. Biol. Chem. 278 (51): 51143–9. doi:10.1074/jbc.M305537200. PMID 14532285.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Nagaraja GM, Kandpal RP (2004). "Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins". Biochem. Biophys. Res. Commun. 313 (3): 654–65. doi:10.1016/j.bbrc.2003.12.001. PMID 14697242.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.