HSP90B1

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.^[5][6]

HSP90B1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4NH9
Identifiers
Aliases	HSP90B1, 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 IDs	OMIM: 191175; MGI: 98817; HomoloGene: 2476; GeneCards: HSP90B1; OMA:HSP90B1 - orthologs
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q23.3 Start 103,930,107 bp[1] End 103,953,931 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 C1|10 43.05 cM Start 86,526,073 bp[2] End 86,541,373 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of thyroid gland left lobe of thyroid gland corpus epididymis pericardium islet of Langerhans anterior pituitary tendon of biceps brachii pylorus Achilles tendon caput epididymis Top expressed in tail of embryo genital tubercle migratory enteric neural crest cell medullary collecting duct abdominal wall dermis spermatocyte renal corpuscle supraoptic nucleus seminal vesicula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding calcium ion binding unfolded protein binding low-density lipoprotein particle receptor binding protein binding RNA binding protein phosphatase binding ATP binding Cellular component cytosol endocytic vesicle lumen endoplasmic reticulum lumen endoplasmic reticulum membrane membrane focal adhesion extracellular matrix melanosome plasma membrane endoplasmic reticulum chaperone complex extracellular region midbody endoplasmic reticulum perinuclear region of cytoplasm extracellular exosome nucleus protein-containing complex collagen-containing extracellular matrix Biological process response to hypoxia response to stress protein folding in endoplasmic reticulum negative regulation of apoptotic process receptor-mediated endocytosis response to endoplasmic reticulum stress toll-like receptor signaling pathway regulation of phosphoprotein phosphatase activity ATF6-mediated unfolded protein response actin rod assembly retrograde protein transport, ER to cytosol sequestering of calcium ion protein folding ubiquitin-dependent ERAD pathway protein transport cellular response to ATP post-translational protein modification cytokine-mediated signaling pathway Sources:Amigo / QuickGO
Orthologs 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: 103.93 – 103.95 Mb Chr 10: 86.53 – 86.54 Mb PubMed search [3] [4]
Wikidata
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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.^[7][8] It has been implicated as an essential immune chaperone to regulate both innate and adaptive immunity.^[9] Tumor-derived HSP90B1 (vitespen) has entered clinical trials for cancer immunotherapy.^{[10][11][12][13]}

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.^[14]