- HSPA1A
Heat shock 70kDa protein 1A, also known as HSPA1A, is a human
gene .PBB_Summary
section_title =
summary_text = Thisintron less 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.cite web | title = Entrez Gene: HSPA1A heat shock 70kDa protein 1A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3303| accessdate = ]ee also
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Heat shock proteins
*Hsp70 References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Andersen JL, Planelles V |title=The role of Vpr in HIV-1 pathogenesis. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 43–51 |year= 2005 |pmid= 15638722 |doi=
*cite journal | author=Zhao RY, Elder RT |title=Viral infections and cell cycle G2/M regulation. |journal=Cell Res. |volume=15 |issue= 3 |pages= 143–9 |year= 2005 |pmid= 15780175 |doi= 10.1038/sj.cr.7290279
*cite journal | author=Zhao RY, Bukrinsky M, Elder RT |title=HIV-1 viral protein R (Vpr) & host cellular responses. |journal=Indian J. Med. Res. |volume=121 |issue= 4 |pages= 270–86 |year= 2005 |pmid= 15817944 |doi=
*cite journal | author=Muthumani K, Choo AY, Premkumar A, "et al." |title=Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism. |journal=Cell Death Differ. |volume=12 Suppl 1 |issue= |pages= 962–70 |year= 2006 |pmid= 15832179 |doi= 10.1038/sj.cdd.4401583
*cite journal | author=Grosz MD, Womack JE, Skow LC |title=Syntenic conservation of HSP70 genes in cattle and humans. |journal=Genomics |volume=14 |issue= 4 |pages= 863–8 |year= 1993 |pmid= 1478667 |doi=
*cite journal | author=Veldscholte J, Berrevoets CA, Brinkmann AO, "et al." |title=Anti-androgens and the mutated androgen receptor of LNCaP cells: differential effects on binding affinity, heat-shock protein interaction, and transcription activation. |journal=Biochemistry |volume=31 |issue= 8 |pages= 2393–9 |year= 1992 |pmid= 1540595 |doi=
*cite journal | author=Abravaya K, Myers MP, Murphy SP, Morimoto RI |title=The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. |journal=Genes Dev. |volume=6 |issue= 7 |pages= 1153–64 |year= 1992 |pmid= 1628823 |doi=
*cite journal | author=Milner CM, Campbell RD |title=Structure and expression of the three MHC-linked HSP70 genes. |journal=Immunogenetics |volume=32 |issue= 4 |pages= 242–51 |year= 1990 |pmid= 1700760 |doi=
*cite journal | author=Sargent CA, Dunham I, Trowsdale J, Campbell RD |title=Human major histocompatibility complex contains genes for the major heat shock protein HSP70. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 6 |pages= 1968–72 |year= 1989 |pmid= 2538825 |doi=
*cite journal | author=Wu B, Hunt C, Morimoto R |title=Structure and expression of the human gene encoding major heat shock protein HSP70. |journal=Mol. Cell. Biol. |volume=5 |issue= 2 |pages= 330–41 |year= 1985 |pmid= 2858050 |doi=
*cite journal | author=Goate AM, Cooper DN, Hall C, "et al." |title=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. |journal=Hum. Genet. |volume=75 |issue= 2 |pages= 123–8 |year= 1987 |pmid= 2880793 |doi=
*cite journal | author=Hickey E, Brandon SE, Sadis S, "et al." |title=Molecular cloning of sequences encoding the human heat-shock proteins and their expression during hyperthermia. |journal=Gene |volume=43 |issue= 1-2 |pages= 147–54 |year= 1986 |pmid= 3019832 |doi=
*cite journal | author=Harrison GS, Drabkin HA, Kao FT, "et al." |title=Chromosomal location of human genes encoding major heat-shock protein HSP70. |journal=Somat. Cell Mol. Genet. |volume=13 |issue= 2 |pages= 119–30 |year= 1987 |pmid= 3470951 |doi=
*cite journal | author=Drabent B, Genthe A, Benecke BJ |title=In vitro transcription of a human hsp 70 heat shock gene by extracts prepared from heat-shocked and non-heat-shocked human cells. |journal=Nucleic Acids Res. |volume=14 |issue= 22 |pages= 8933–48 |year= 1987 |pmid= 3786141 |doi=
*cite journal | author=Hunt C, Morimoto RI |title=Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 19 |pages= 6455–9 |year= 1985 |pmid= 3931075 |doi=
*cite journal | author=Liao J, Lowthert LA, Ghori N, Omary MB |title=The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner. |journal=J. Biol. Chem. |volume=270 |issue= 2 |pages= 915–22 |year= 1995 |pmid= 7529764 |doi=
*cite journal | author=Selkirk JK, Merrick BA, Stackhouse BL, He C |title=Multiple p53 protein isoforms and formation of oligomeric complexes with heat shock proteins Hsp70 and Hsp90 in the human mammary tumor, T47D, cell line. |journal=Appl. Theor. Electrophor. |volume=4 |issue= 1 |pages= 11–8 |year= 1995 |pmid= 7811761 |doi=
*cite journal | author=Furlini G, Vignoli M, Re MC, "et al." |title=Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein. |journal=J. Gen. Virol. |volume=75 ( Pt 1) |issue= |pages= 193–9 |year= 1994 |pmid= 7906708 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Prapapanich V, Chen S, Toran EJ, "et al." |title=Mutational analysis of the hsp70-interacting protein Hip. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6200–7 |year= 1996 |pmid= 8887650 |doi=External links
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