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Heat shock protein 90kDa beta (Grp94), member 1
Protein HSP90B1 PDB 1qy5.png
PDB rendering based on 1qy5.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols HSP90B1 ; ECGP; GP96; GRP94; HEL-S-125m; HEL35; TRA1
External IDs OMIM191175 MGI98817 HomoloGene2476 ChEMBL: 1075323 GeneCards: HSP90B1 Gene
RNA expression pattern
PBB GE HSP90B1 200599 s at tn.png
PBB GE HSP90B1 200598 s at tn.png
PBB GE HSP90B1 216449 x at tn.png
More reference expression data
Species Human Mouse
Entrez 7184 22027
Ensembl ENSG00000166598 ENSMUSG00000020048
UniProt P14625 P08113
RefSeq (mRNA) NM_003299 NM_011631
RefSeq (protein) NP_003290 NP_035761
Location (UCSC) Chr 12:
104.32 – 104.35 Mb
Chr 10:
86.69 – 86.71 Mb
PubMed search [1] [2]

Heat shock protein 90kDa beta member 1 (HSP90B1), known also as endoplasmin, gp96, grp94 and ERp99, is a chaperone protein that in humans is encoded by the HSP90B1 gene.[1][2]

HSP90B1 is an HSP90 paralogue that is found in the endoplasmic reticulum. It plays critical roles in folding proteins in the secretory pathway such as Toll-like receptors and integrins.[3][4] It has been implicated as an essential immune chaperone to regulate both innate and adaptive immunity.[5] Tumor-derived HSP90B1 (vitespen) has entered clinical trials for cancer immunotherapy.[6][7][8][9]


  1. ^ Maki RG, Old LJ, Srivastava PK (August 1990). "Human homologue of murine tumor rejection antigen gp96: 5'-regulatory and coding regions and relationship to stress-induced proteins". Proc. Natl. Acad. Sci. U.S.A. 87 (15): 5658–62. doi:10.1073/pnas.87.15.5658. PMC 54386. PMID 2377606. 
  2. ^ Chen B, Piel WH, Gui L, Bruford E, Monteiro A (December 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. 
  3. ^ Randow F, Seed B (2001). "Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability.". Nat. Cell Biol. 3 (10): 891–6. doi:10.1038/ncb1001-891. PMID 11584270. 
  4. ^ Yang Y et al. (2007). "Heat Shock Protein gp96 Is a Master Chaperone for Toll-like Receptors and Is Important in the Innate Function of Macrophages.". Immunity 26 (2): 215–226. doi:10.1016/j.immuni.2006.12.005. PMC 2847270. PMID 17275357.  ,
  5. ^ Schild H, Rammensee HG (August 2000). "gp96--the immune system's Swiss army knife". Nat. Immunol. 1 (2): 100–1. doi:10.1038/77770. PMID 11248798. 
  6. ^ Wood CG, Mulders P (August 2009). "Vitespen: a preclinical and clinical review". Future Oncol 5 (6): 763–74. doi:10.2217/fon.09.46. PMID 19663726. 
  7. ^ Tosti G, di Pietro A, Ferrucci PF, Testori A (November 2009). "HSPPC-96 vaccine in metastatic melanoma patients: from the state of the art to a possible future". Expert Rev Vaccines 8 (11): 1513–26. doi:10.1586/erv.09.108. PMID 19863242. 
  8. ^ "NCT00293423". ClinicalTrials.gov, United States National Institutes of Health. Retrieved 2010-04-10. GP96 Heat Shock Protein-Peptide Complex Vaccine in Treating Patients With Recurrent or Progressive Glioma 
  9. ^ Bloch, O.; Crane, C. A.; Fuks, Y.; Kaur, R.; Aghi, M. K.; Berger, M. S.; Butowski, N. A.; Chang, S. M.; Clarke, J. L.; McDermott, M. W.; Prados, M. D.; Sloan, A. E.; Bruce, J. N.; Parsa, A. T. (12 December 2013). "Heat-shock protein peptide complex-96 vaccination for recurrent glioblastoma: a phase II, single-arm trial". Neuro-Oncology. doi:10.1093/neuonc/not203. 

Further reading[edit]