HSP90B1

HSP90B1
Identifiers
AliasesHSP90B1, ECGP, GP96, GRP94, HEL-S-125m, HEL35, TRA1, heat shock protein 90kDa beta family member 1, heat shock protein 90 beta family member 1
External IDsOMIM: 191175; MGI: 98817; GeneCards: HSP90B1
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003299

NM_011631

RefSeq (protein)

NP_003290

NP_035761

Location (UCSC)Chr 12: 103.93 – 103.95 MbChr 10: 86.53 – 86.54 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

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

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. It has been implicated as an essential immune chaperone to regulate both innate and adaptive immunity. Tumor-derived HSP90B1 (vitespen) has entered clinical trials for cancer immunotherapy.

grp94 has been shown to be a target for treatment of a plethora of diseases such as glaucoma, multiple myeloma, and metastatic cancer. grp94 includes 5 distinct amino acids in its primary sequence which creates 2 unique sub-pockets, S1 and S2. These sub-pockets have been utilized in current research in order to inhibit the chaperone since its client proteins seem to be up-regulated in cancer cells.