HSPA1A

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Heat shock 70kDa protein 1A
Protein HSPA1A PDB 1hjo.png
PDB rendering based on 1hjo.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols HSPA1A ; HEL-S-103; HSP70-1; HSP70-1A; HSP70I; HSP72; HSPA1
External IDs OMIM140550 MGI99517 HomoloGene74294 ChEMBL: 5460 GeneCards: HSPA1A Gene
Orthologs
Species Human Mouse
Entrez 3303 193740
Ensembl ENSG00000204388 ENSMUSG00000091971
UniProt P08107 Q61696
RefSeq (mRNA) NM_005345 NM_010479
RefSeq (protein) NP_005336 NP_034609
Location (UCSC) Chr 6:
31.78 – 31.79 Mb
Chr 17:
34.97 – 34.97 Mb
PubMed search [1] [2]

Heat shock 70 kDa protein 1 is a protein that in humans is encoded by the HSPA1A gene.

Function[edit]

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. 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.[1]

Interactions[edit]

HSPA1A has been shown to interact with:

See also[edit]


References[edit]

  1. ^ "Entrez Gene: HSPA1A heat shock 70kDa protein 1A". 
  2. ^ Ruchalski K, Mao H, Singh SK, Wang Y, Mosser DD, Li F et al. (December 2003). "HSP72 inhibits apoptosis-inducing factor release in ATP-depleted renal epithelial cells". Am. J. Physiol., Cell Physiol. 285 (6): C1483–93. doi:10.1152/ajpcell.00049.2003. PMID 12930708. 
  3. ^ Ravagnan L, Gurbuxani S, Susin SA, Maisse C, Daugas E, Zamzami N et al. (September 2001). "Heat-shock protein 70 antagonizes apoptosis-inducing factor". Nat. Cell Biol. 3 (9): 839–43. doi:10.1038/ncb0901-839. PMID 11533664. 
  4. ^ Park HS, Cho SG, Kim CK, Hwang HS, Noh KT, Kim MS et al. (November 2002). "Heat shock protein hsp72 is a negative regulator of apoptosis signal-regulating kinase 1". Mol. Cell. Biol. 22 (22): 7721–30. PMC 134722. PMID 12391142. 
  5. ^ Doong H, Price J, Kim YS, Gasbarre C, Probst J, Liotta LA et al. (September 2000). "CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70". Oncogene 19 (38): 4385–95. doi:10.1038/sj.onc.1203797. PMID 10980614. 
  6. ^ Antoku K, Maser RS, Scully WJ, Delach SM, Johnson DE (September 2001). "Isolation of Bcl-2 binding proteins that exhibit homology with BAG-1 and suppressor of death domains protein". Biochem. Biophys. Res. Commun. 286 (5): 1003–10. doi:10.1006/bbrc.2001.5512. PMID 11527400. 
  7. ^ Pang Q, Christianson TA, Keeble W, Koretsky T, Bagby GC (December 2002). "The anti-apoptotic function of Hsp70 in the interferon-inducible double-stranded RNA-dependent protein kinase-mediated death signaling pathway requires the Fanconi anemia protein, FANCC". J. Biol. Chem. 277 (51): 49638–43. doi:10.1074/jbc.M209386200. PMID 12397061. 
  8. ^ Reuter TY, Medhurst AL, Waisfisz Q, Zhi Y, Herterich S, Hoehn H et al. (October 2003). "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport". Exp. Cell Res. 289 (2): 211–21. PMID 14499622. 
  9. ^ a b c Imai Y, Soda M, Hatakeyama S, Akagi T, Hashikawa T, Nakayama KI et al. (July 2002). "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity". Mol. Cell 10 (1): 55–67. PMID 12150907. 
  10. ^ Shi Y, Mosser DD, Morimoto RI (March 1998). "Molecular chaperones as HSF1-specific transcriptional repressors". Genes Dev. 12 (5): 654–66. PMC 316571. PMID 9499401. 
  11. ^ Zhou X, Tron VA, Li G, Trotter MJ (August 1998). "Heat shock transcription factor-1 regulates heat shock protein-72 expression in human keratinocytes exposed to ultraviolet B light". J. Invest. Dermatol. 111 (2): 194–8. doi:10.1046/j.1523-1747.1998.00266.x. PMID 9699716. 
  12. ^ Nakamura T, Hinagata J, Tanaka T, Imanishi T, Wada Y, Kodama T et al. (January 2002). "HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors". Biochem. Biophys. Res. Commun. 290 (2): 858–64. doi:10.1006/bbrc.2001.6271. PMID 11785981. 
  13. ^ Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY et al. (June 1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions". Mol. Cell. Biol. 19 (6): 4535–45. PMC 104411. PMID 10330192. 

Further reading[edit]

External links[edit]