HSP90B1

From Wikipedia, the free encyclopedia

Heat shock protein 90kDa beta (Grp94), member 1

PDB rendering based on 1qy5.

Available structures: 1qy5, 1qy8, 1qye, 1u0y, 1yt2

Identifiers

Symbol(s)

HSP90B1; ECGP; GP96; GRP94; TRA1

External IDs

OMIM: 191175 MGI: 98817 HomoloGene: 2476

Gene ontology
Molecular Function:	• RNA binding • calcium ion binding • ATP binding • virion binding • low-density lipoprotein receptor binding • unfolded protein binding
Cellular Component:	• endoplasmic reticulum • endoplasmic reticulum lumen • endoplasmic reticulum membrane • microsome • cytosol • perinuclear region of cytoplasm
Biological Process:	• response to hypoxia • protein folding • anti-apoptosis • protein transport • sequestering of calcium ion

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003299 (mRNA)
NP_003290 (protein)

NM_011631 (mRNA)
NP_035761 (protein)

Location

Chr 12: 102.85 - 102.87 Mb

Chr 10: 86.12 - 86.14 Mb

Pubmed search

[1]

[2]

Heat shock protein 90kDa beta (Grp94), member 1 is a human chaperone protein. HSP90B1 is the human gene encoding it.

[edit] Further reading

Li Z, Dai J, Zheng H, et al. (2002). "An integrated view of the roles and mechanisms of heat shock protein gp96-peptide complex in eliciting immune response.". Front. Biosci. 7: d731–51. PMID 11861214.
Kaul SC, Taira K, Pereira-Smith OM, Wadhwa R (2003). "Mortalin: present and prospective.". Exp. Gerontol. 37 (10-11): 1157–64. PMID 12470827.
Schaiff WT, Hruska KA, McCourt DW, et al. (1992). "HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells.". J. Exp. Med. 176 (3): 657–66. PMID 1512535.
Zolnierowicz S, Work C, Hutchison K, Fox IH (1990). "Partial separation of platelet and placental adenosine receptors from adenosine A2-like binding protein.". Mol. Pharmacol. 37 (4): 554–9. PMID 2325637.
Maki RG, Old LJ, Srivastava PK (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. PMID 2377606.
Hutchison KA, Nevins B, Perini F, Fox IH (1990). "Soluble and membrane-associated human low-affinity adenosine binding protein (adenotin): properties and homology with mammalian and avian stress proteins.". Biochemistry 29 (21): 5138–44. PMID 2378869.
Chang SC, Erwin AE, Lee AS (1989). "Glucose-regulated protein (GRP94 and GRP78) genes share common regulatory domains and are coordinately regulated by common trans-acting factors.". Mol. Cell. Biol. 9 (5): 2153–62. PMID 2546060.
Anderson SL, Shen T, Lou J, et al. (1994). "The endoplasmic reticular heat shock protein gp96 is transcriptionally upregulated in interferon-treated cells.". J. Exp. Med. 180 (4): 1565–9. PMID 7523574.
Bruneau N, Lombardo D (1995). "Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase.". J. Biol. Chem. 270 (22): 13524–33. PMID 7768954.
Chavany C, Mimnaugh E, Miller P, et al. (1996). "p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2.". J. Biol. Chem. 271 (9): 4974–7. PMID 8617772.
Kuznetsov G, Chen LB, Nigam SK (1997). "Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum.". J. Biol. Chem. 272 (5): 3057–63. PMID 9006956.
Hoshino T, Wang J, Devetten MP, et al. (1998). "Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression.". Blood 91 (11): 4379–86. PMID 9596688.
Linnik KM, Herscovitz H (1998). "Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state.". J. Biol. Chem. 273 (33): 21368–73. PMID 9694898.
Delom F, Lejeune PJ, Vinet L, et al. (1999). "Involvement of oxidative reactions and extracellular protein chaperones in the rescue of misassembled thyroglobulin in the follicular lumen.". Biochem. Biophys. Res. Commun. 255 (2): 438–43. doi:10.1006/bbrc.1999.0229. PMID 10049727.
Reddy RK, Lu J, Lee AS (1999). "The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis.". J. Biol. Chem. 274 (40): 28476–83. PMID 10497210.
Roher N, Sarno S, Miró F, et al. (2001). "The carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme.". FEBS Lett. 505 (1): 42–6. PMID 11557039.
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.
Vabulas RM, Braedel S, Hilf N, et al. (2002). "The endoplasmic reticulum-resident heat shock protein Gp96 activates dendritic cells via the Toll-like receptor 2/4 pathway.". J. Biol. Chem. 277 (23): 20847–53. doi:10.1074/jbc.M200425200. PMID 11912201.
Shin HJ, Kim SS, Cho YH, et al. (2002). "Host cell proteins binding to the encapsidation signal epsilon in hepatitis B virus RNA.". Arch. Virol. 147 (3): 471–91. PMID 11958450.