HSPA1A

From Wikipedia, the free encyclopedia

Heat shock 70kDa protein 1A

PDB rendering based on 1hjo.

Available structures: 1hjo, 1s3x, 1xqs

Identifiers

Symbol(s)

HSPA1A; HSP70-1; HSP72; HSPA1; HSPA1B; HSPA1A; HSP70-2

External IDs

OMIM: 140550 MGI: 99517 HomoloGene: 74294

Gene ontology
Molecular Function:	• nucleotide binding • ATP binding • unfolded protein binding
Cellular Component:	• nucleus • cytoplasm • mitochondrion • endoplasmic reticulum
Biological Process:	• protein folding • response to unfolded protein • mRNA catabolic process • anti-apoptosis

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_005345 (mRNA)
NP_005336 (protein)

XM_001002795 (mRNA)
XP_001002795 (protein)

Location

n/a

Chr 17: 34.57 - 34.57 Mb

Pubmed search

[1]

[2]

Heat shock 70kDa protein 1A, also known as HSPA1A, is a human gene.

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]

[edit] See also

[edit] References

^ Entrez Gene: HSPA1A heat shock 70kDa protein 1A.

[edit] Further reading

Andersen JL, Planelles V (2005). "The role of Vpr in HIV-1 pathogenesis.". Curr. HIV Res. 3 (1): 43–51. PMID 15638722.
Zhao RY, Elder RT (2005). "Viral infections and cell cycle G2/M regulation.". Cell Res. 15 (3): 143–9. doi:10.1038/sj.cr.7290279. PMID 15780175.
Zhao RY, Bukrinsky M, Elder RT (2005). "HIV-1 viral protein R (Vpr) & host cellular responses.". Indian J. Med. Res. 121 (4): 270–86. PMID 15817944.
Muthumani K, Choo AY, Premkumar A, et al. (2006). "Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism.". Cell Death Differ. 12 Suppl 1: 962–70. doi:10.1038/sj.cdd.4401583. PMID 15832179.
Grosz MD, Womack JE, Skow LC (1993). "Syntenic conservation of HSP70 genes in cattle and humans.". Genomics 14 (4): 863–8. PMID 1478667.
Veldscholte J, Berrevoets CA, Brinkmann AO, et al. (1992). "Anti-androgens and the mutated androgen receptor of LNCaP cells: differential effects on binding affinity, heat-shock protein interaction, and transcription activation.". Biochemistry 31 (8): 2393–9. PMID 1540595.
Abravaya K, Myers MP, Murphy SP, Morimoto RI (1992). "The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression.". Genes Dev. 6 (7): 1153–64. PMID 1628823.
Milner CM, Campbell RD (1990). "Structure and expression of the three MHC-linked HSP70 genes.". Immunogenetics 32 (4): 242–51. PMID 1700760.
Sargent CA, Dunham I, Trowsdale J, Campbell RD (1989). "Human major histocompatibility complex contains genes for the major heat shock protein HSP70.". Proc. Natl. Acad. Sci. U.S.A. 86 (6): 1968–72. PMID 2538825.
Wu B, Hunt C, Morimoto R (1985). "Structure and expression of the human gene encoding major heat shock protein HSP70.". Mol. Cell. Biol. 5 (2): 330–41. PMID 2858050.
Goate AM, Cooper DN, Hall C, et al. (1987). "Localization of a human heat-shock HSP 70 gene sequence to chromosome 6 and detection of two other loci by somatic-cell hybrid and restriction fragment length polymorphism analysis.". Hum. Genet. 75 (2): 123–8. PMID 2880793.
Hickey E, Brandon SE, Sadis S, et al. (1986). "Molecular cloning of sequences encoding the human heat-shock proteins and their expression during hyperthermia.". Gene 43 (1-2): 147–54. PMID 3019832.
Harrison GS, Drabkin HA, Kao FT, et al. (1987). "Chromosomal location of human genes encoding major heat-shock protein HSP70.". Somat. Cell Mol. Genet. 13 (2): 119–30. PMID 3470951.
Drabent B, Genthe A, Benecke BJ (1987). "In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells.". Nucleic Acids Res. 14 (22): 8933–48. PMID 3786141.
Hunt C, Morimoto RI (1985). "Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70.". Proc. Natl. Acad. Sci. U.S.A. 82 (19): 6455–9. PMID 3931075.
Liao J, Lowthert LA, Ghori N, Omary MB (1995). "The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner.". J. Biol. Chem. 270 (2): 915–22. PMID 7529764.
Selkirk JK, Merrick BA, Stackhouse BL, He C (1995). "Multiple p53 protein isoforms and formation of oligomeric complexes with heat shock proteins Hsp70 and Hsp90 in the human mammary tumor, T47D, cell line.". Appl. Theor. Electrophor. 4 (1): 11–8. PMID 7811761.
Furlini G, Vignoli M, Re MC, et al. (1994). "Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein.". J. Gen. Virol. 75 ( Pt 1): 193–9. PMID 7906708.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Prapapanich V, Chen S, Toran EJ, et al. (1996). "Mutational analysis of the hsp70-interacting protein Hip.". Mol. Cell. Biol. 16 (11): 6200–7. PMID 8887650.