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HSPA1B

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heat shock 70kDa protein 1B
Identifiers
SymbolHSPA1B
NCBI gene3304
HGNC5233
OMIM603012
RefSeqNM_005346
UniProtP08107
Other data
LocusChr. 6 p21.3
Search for
StructuresSwiss-model
DomainsInterPro

Heat shock 70kDa protein 1B, also known as HSPA1B, is a human gene.[1] This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family.[2]

Function

In conjunction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins.[2][3]

Disease linkage

Patients with chronic hepatitis B or hepatitis C virus infection who harbor a HSPA1B-1267 single nucleotide polymorphism have a higher risk for developing hepatocellular carcinoma.[4]

See also

References

  1. ^ Milner CM, Campbell RD (1990). "Structure and expression of the three MHC-linked HSP70 genes". Immunogenetics. 32 (4): 242–51. doi:10.1007/BF00187095. PMID 1700760. S2CID 9531492.
  2. ^ a b "Entrez Gene: HSPA1A heat shock 70kDa protein 1B".
  3. ^ Ito Y, Ando A, Ando H, Ando J, Saijoh Y, Inoko H, Fujimoto H (August 1998). "Genomic structure of the spermatid-specific hsp70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man". J. Biochem. 124 (2): 347–53. doi:10.1093/oxfordjournals.jbchem.a022118. PMID 9685725.
  4. ^ Jeng JE, Tsai JF, Chuang LY, Ho MS, Lin ZY, Hsieh MY, Chen SC, Chuang WL, Wang LY, Yu ML, Dai CY, Chang JG (March 2008). "Heat shock protein A1B 1267 polymorphism is highly associated with risk and prognosis of hepatocellular carcinoma: a case-control study". Medicine (Baltimore). 87 (2): 87–98. doi:10.1097/MD.0b013e31816be95c. PMID 18344806. S2CID 26906991.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.