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HSP90B1

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(Redirected from Grp94) Protein-coding gene in the species Homo sapiens
HSP90B1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4NH9

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; HomoloGene: 2476; GeneCards: HSP90B1; OMA:HSP90B1 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)
Chromosome 12 (human)Genomic location for HSP90B1Genomic location for HSP90B1
Band12q23.3Start103,930,107 bp
End103,953,931 bp
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)
Chromosome 10 (mouse)Genomic location for HSP90B1Genomic location for HSP90B1
Band10 C1|10 43.05 cMStart86,526,073 bp
End86,541,373 bp
RNA expression pattern
Bgee
HumanMouse (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
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
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 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.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000166598Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000020048Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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". Proceedings of the National Academy of Sciences of the United States of America. 87 (15): 5658–62. Bibcode:1990PNAS...87.5658M. doi:10.1073/pnas.87.15.5658. PMC 54386. PMID 2377606.
  6. 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.
  7. Randow F, Seed B (October 2001). "Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability". Nature Cell Biology. 3 (10): 891–6. doi:10.1038/ncb1001-891. PMID 11584270. S2CID 26559580.
  8. Yang Y, Liu B, Dai J, Srivastava PK, Zammit DJ, Lefrançois L, Li Z (February 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): 215–26. doi:10.1016/j.immuni.2006.12.005. PMC 2847270. PMID 17275357.,
  9. Schild H, Rammensee HG (August 2000). "gp96--the immune system's Swiss army knife". Nature Immunology. 1 (2): 100–1. doi:10.1038/77770. PMID 11248798. S2CID 29571184.
  10. Wood CG, Mulders P (August 2009). "Vitespen: a preclinical and clinical review". Future Oncology. 5 (6): 763–74. doi:10.2217/fon.09.46. PMID 19663726.
  11. 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 Review of Vaccines. 8 (11): 1513–26. doi:10.1586/erv.09.108. PMID 19863242. S2CID 207223461.
  12. "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
  13. Bloch O, Crane CA, Fuks Y, Kaur R, Aghi MK, Berger MS, Butowski NA, Chang SM, Clarke JL, McDermott MW, Prados MD, Sloan AE, Bruce JN, Parsa AT (January 2014). "Heat-shock protein peptide complex-96 vaccination for recurrent glioblastoma: a phase II, single-arm trial". Neuro-Oncology. 16 (2): 274–9. doi:10.1093/neuonc/not203. PMC 3895386. PMID 24335700.
  14. Khandelwal A, Crowley VM, Blagg BS (October 2017). "Resorcinol-Based Grp94-Selective Inhibitors". ACS Medicinal Chemistry Letters. 8 (10): 1013–1018. doi:10.1021/acsmedchemlett.7b00193. PMC 5641966. PMID 29057043.

Further reading

PDB gallery
  • 1qy5: Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with the specific ligand NECA 1qy5: Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with the specific ligand NECA
  • 1qy8: Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with Radicicol 1qy8: Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with Radicicol
  • 1qye: Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine 1qye: Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine
  • 1u0y: N-Domain Of Grp94, with the Charged Domain, In Complex With the Novel Ligand N-Propyl Carboxyamido Adenosine 1u0y: N-Domain Of Grp94, with the Charged Domain, In Complex With the Novel Ligand N-Propyl Carboxyamido Adenosine
  • 1yt2: Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N APO CRYSTAL 1yt2: Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N APO CRYSTAL
Posttranslational modification
Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
(ubiquitylation)
Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E2 SUMO-conjugating enzyme
Other


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