HSPA9

Heat shock 70kDa protein 9 (mortalin)
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3N8E
Identifiers
Symbols	HSPA9; CSA; GRP-75; GRP75; HSPA9B; MOT; MOT2; MTHSP75; PBP74
External IDs	OMIM: 600548 MGI: 96245 HomoloGene: 39452 GeneCards: HSPA9 Gene
Gene Ontology Molecular function • protein binding • ATP binding • enzyme binding • unfolded protein binding Cellular component • nucleolus • cytoplasm • mitochondrion • cell surface • mitochondrial nucleoid Biological process • protein folding • protein export from nucleus • protein targeting to mitochondrion • negative regulation of apoptotic process • cellular protein metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3313	15526
Ensembl	ENSG00000113013	ENSMUSG00000024359
UniProt	P38646	P38647
RefSeq (mRNA)	NM_004134	NM_010481
RefSeq (protein)	NP_004125	NP_034611
Location (UCSC)	Chr 5: 137.89 – 137.91 Mb	Chr 18: 34.94 – 34.95 Mb
PubMed search	[1]	[2]

Stress-70 protein, mitochondrial is a protein that in humans is encoded by the HSPA9 gene.

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.

Interactions

HSPA9 has been shown to interact with FGF1 and P53.

Further reading

• Kaul SC, Taira K, Pereira-Smith OM, Wadhwa R (2003). "Mortalin: present and prospective". Exp. Gerontol. 37 (10–11): 1157–64. doi:10.1016/S0531-5565(02)00135-3. PMID 12470827. 
• Yaguchi T, Aida S, Kaul SC, Wadhwa R (2007). "Involvement of mortalin in cellular senescence from the perspective of its mitochondrial import, chaperone, and oxidative stress management functions". Ann. N. Y. Acad. Sci. 1100: 306–11. doi:10.1196/annals.1395.032. PMID 17460192. 
• Hochstrasser DF, Frutiger S, Paquet N, et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis 13 (12): 992–1001. doi:10.1002/elps.11501301201. PMID 1286669. 
• Kaul SC, Wadhwa R, Matsuda Y, et al. (1995). "Mouse and human chromosomal assignments of mortalin, a novel member of the murine hsp70 family of proteins". FEBS Lett. 361 (2–3): 269–72. doi:10.1016/0014-5793(95)00177-B. PMID 7698336. 
• Bhattacharyya T, Karnezis AN, Murphy SP, et al. (1995). "Cloning and subcellular localization of human mitochondrial hsp70". J. Biol. Chem. 270 (4): 1705–10. doi:10.1074/jbc.270.4.1705. PMID 7829505. 
• 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 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708. 
• Matoba R, Okubo K, Hori N, et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID 8076819. 
• 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Hughes GJ, Frutiger S, Paquet N, et al. (1994). "Human liver protein map: update 1993". Electrophoresis 14 (11): 1216–22. doi:10.1002/elps.11501401181. PMID 8313870. 
• Ji H, Reid GE, Moritz RL, et al. (1997). "A two-dimensional gel database of human colon carcinoma proteins". Electrophoresis 18 (3–4): 605–13. doi:10.1002/elps.1150180344. PMID 9150948. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Mizukoshi E, Suzuki M, Loupatov A, et al. (1999). "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". Biochem. J. 343 Pt 2 (2): 461–6. doi:10.1042/0264-6021:3430461. PMC 1220575. PMID 10510314. 
• O'Keeffe B, Fong Y, Chen D, et al. (2000). "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". J. Biol. Chem. 275 (1): 279–87. doi:10.1074/jbc.275.1.279. PMID 10617616. 
• Kaula SC, Reddelb RR, Sugiharac T, et al. (2000). "Inactivation of p53 and life span extension of human diploid fibroblasts by mot-2". FEBS Lett. 474 (2–3): 159–64. doi:10.1016/S0014-5793(00)01594-5. PMID 10838077. 
• Agostini I, Popov S, Li J, et al. (2000). "Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex". Exp. Cell Res. 259 (2): 398–403. doi:10.1006/excr.2000.4992. PMID 10964507. 
• Xie H, Hu Z, Chyna B, et al. (2001). "Human mortalin (HSPA9): a candidate for the myeloid leukemia tumor suppressor gene on 5q31". Leukemia 14 (12): 2128–34. doi:10.1038/sj.leu.2401935. PMID 11187902. 
• Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. 
• Carette J, Lehnert S, Chow TY (2002). "Implication of PBP74/mortalin/GRP75 in the radio-adaptive response". Int. J. Radiat. Biol. 78 (3): 183–90. doi:10.1080/09553000110097208. PMID 11869473. 
• Wadhwa R, Yaguchi T, Hasan MK, et al. (2002). "Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein". Exp. Cell Res. 274 (2): 246–53. doi:10.1006/excr.2002.5468. PMID 11900485. 

External links

• HSPA9 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)