HSPA9

Heat shock 70kDa protein 9 (mortalin), also known as HSPA9, is a human gene.cite web | title = Entrez Gene: HSPA9 heat shock 70kDa protein 9 (mortalin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3313| accessdate = ]

PBB_Summary
section_title =
summary_text = The product encoded by this gene belongs to the heat shock protein 70 family which contains both heat-inducible and constitutively expressed members. The latter are called heat-shock cognate proteins. This gene encodes a heat-shock cognate protein. This protein plays a role in the control of cell proliferation. It may also act as a chaperone.cite web | title = Entrez Gene: HSPA9 heat shock 70kDa protein 9 (mortalin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3313| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Kaul SC, Taira K, Pereira-Smith OM, Wadhwa R |title=Mortalin: present and prospective. |journal=Exp. Gerontol. |volume=37 |issue= 10-11 |pages= 1157–64 |year= 2003 |pmid= 12470827 |doi=
*cite journal | author=Yaguchi T, Aida S, Kaul SC, Wadhwa R |title=Involvement of mortalin in cellular senescence from the perspective of its mitochondrial import, chaperone, and oxidative stress management functions. |journal=Ann. N. Y. Acad. Sci. |volume=1100 |issue= |pages= 306–11 |year= 2007 |pmid= 17460192 |doi= 10.1196/annals.1395.032
*cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, "et al." |title=Human liver protein
journal=Electrophoresis |volume=13 |issue= 12 |pages= 992–1001 |year= 1993 |pmid= 1286669 |doi=
*cite journal | author=Domanico SZ, DeNagel DC, Dahlseid JN, "et al." |title=Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. |journal=Mol. Cell. Biol. |volume=13 |issue= 6 |pages= 3598–610 |year= 1993 |pmid= 7684501 |doi=
*cite journal | author=Kaul SC, Wadhwa R, Matsuda Y, "et al." |title=Mouse and human chromosomal assignments of mortalin, a novel member of the murine hsp70 family of proteins. |journal=FEBS Lett. |volume=361 |issue= 2-3 |pages= 269–72 |year= 1995 |pmid= 7698336 |doi=
*cite journal | author=Bhattacharyya T, Karnezis AN, Murphy SP, "et al." |title=Cloning and subcellular localization of human mitochondrial hsp70. |journal=J. Biol. Chem. |volume=270 |issue= 4 |pages= 1705–10 |year= 1995 |pmid= 7829505 |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=Matoba R, Okubo K, Hori N, "et al." |title=The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression. |journal=Gene |volume=146 |issue= 2 |pages= 199–207 |year= 1994 |pmid= 8076819 |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=Hughes GJ, Frutiger S, Paquet N, "et al." |title=Human liver protein
journal=Electrophoresis |volume=14 |issue= 11 |pages= 1216–22 |year= 1994 |pmid= 8313870 |doi=
*cite journal | author=Ji H, Reid GE, Moritz RL, "et al." |title=A two-dimensional gel database of human colon carcinoma proteins. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 605–13 |year= 1997 |pmid= 9150948 |doi= 10.1002/elps.1150180344
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Mizukoshi E, Suzuki M, Loupatov A, "et al." |title=Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin. |journal=Biochem. J. |volume=343 Pt 2 |issue= |pages= 461–6 |year= 1999 |pmid= 10510314 |doi=
*cite journal | author=O'Keeffe B, Fong Y, Chen D, "et al." |title=Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 279–87 |year= 2000 |pmid= 10617616 |doi=
*cite journal | author=Kaula SC, Reddelb RR, Sugiharac T, "et al." |title=Inactivation of p53 and life span extension of human diploid fibroblasts by mot-2. |journal=FEBS Lett. |volume=474 |issue= 2-3 |pages= 159–64 |year= 2000 |pmid= 10838077 |doi=
*cite journal | author=Agostini I, Popov S, Li J, "et al." |title=Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 398–403 |year= 2000 |pmid= 10964507 |doi= 10.1006/excr.2000.4992
*cite journal | author=Xie H, Hu Z, Chyna B, "et al." |title=Human mortalin (HSPA9): a candidate for the myeloid leukemia tumor suppressor gene on 5q31. |journal=Leukemia |volume=14 |issue= 12 |pages= 2128–34 |year= 2001 |pmid= 11187902 |doi=
*cite journal | author=Andersen JS, Lyon CE, Fox AH, "et al." |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1–11 |year= 2002 |pmid= 11790298 |doi=
*cite journal | author=Carette J, Lehnert S, Chow TY |title=Implication of PBP74/mortalin/GRP75 in the radio-adaptive response. |journal=Int. J. Radiat. Biol. |volume=78 |issue= 3 |pages= 183–90 |year= 2002 |pmid= 11869473 |doi= 10.1080/09553000110097208
*cite journal | author=Wadhwa R, Yaguchi T, Hasan MK, "et al." |title=Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein. |journal=Exp. Cell Res. |volume=274 |issue= 2 |pages= 246–53 |year= 2002 |pmid= 11900485 |doi= 10.1006/excr.2002.5468

External links

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