HSPA9

HSPA9
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3N8E, 4KBO
Identifiers
Aliases	HSPA9, CSA, GRP-75, GRP75, HEL-S-124m, HSPA9B, MOT, MOT2, MTHSP75, PBP74, CRP40, EVPLS, SAAN, SIDBA4, heat shock protein family A (Hsp70) member 9
External IDs	OMIM: 600548 MGI: 96245 HomoloGene: 39452 GeneCards: HSPA9
Gene location (Human)
Chr.	Chromosome 5 (human)[1]
End	138,575,416 bp[1]
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)[2]
End	34,954,357 bp[2]
Gene ontology
Molecular function	• nucleotide binding; • unfolded protein binding; • GO:0001948 protein binding; • ATP binding; • ubiquitin protein ligase binding; • RNA binding; • ATPase activity; • heat shock protein binding; • protein binding involved in protein folding; • misfolded protein binding; • enzyme binding;
Cellular component	• cytoplasm; • focal adhesion; • nucleolus; • mitochondrion; • mitochondrial nucleoid; • extracellular exosome; • cell nucleus; • extracellular matrix; • mitochondrial matrix;
Biological process	• negative regulation of apoptotic process; • protein folding; • negative regulation of erythrocyte differentiation; • erythrocyte differentiation; • interleukin-12-mediated signaling pathway; • response to unfolded protein; • iron-sulfur cluster assembly; • cellular response to heat; • cellular response to unfolded protein; • protein refolding; • regulation of erythrocyte differentiation; • chaperone mediated protein folding requiring cofactor; • protein export from nucleus; • negative regulation of hematopoietic stem cell differentiation; • negative regulation of hemopoiesis;
	Sources:Amigo / QuickGO
Orthologs
	3313
	15526
	ENSG00000113013
	ENSMUSG00000024359
	P38646
	P38647
	NM_004134
	NM_010481
	NP_004125
	NP_034611
	Wikidata
View/Edit Human	View/Edit Mouse

Mitochondrial 70kDa heat shock protein (mtHsp70), also known as mortalin, is a protein that in humans is encoded by the HSPA9 gene.[5][6]

Function

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.[6]

Interactions

HSPA9 has been shown to interact with FGF1[7] and P53.[8]

References

GRCh38: Ensembl release 89: ENSG00000113013 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000024359 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Domanico SZ, DeNagel DC, Dahlseid JN, Green JM, Pierce SK (Jun 1993). "Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family". Mol Cell Biol. 13 (6): 3598–610. doi:10.1128/mcb.13.6.3598. PMC 359829. PMID 7684501.
"Entrez Gene: HSPA9 heat shock 70kDa protein 9 (mortalin)".
Mizukoshi E, Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T (Oct 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.
Wadhwa R, Yaguchi T, Hasan MK, Mitsui Y, Reddel RR, Kaul SC (Apr 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.

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. S2CID 44450296.
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. S2CID 43848246.
Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R (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. S2CID 23518983.
Kaul SC, Wadhwa R, Matsuda Y, Hensler PJ, Pereira-Smith OM, Komatsu Y, Mitsui Y (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. S2CID 36957259.
Bhattacharyya T, Karnezis AN, Murphy SP, Hoang T, Freeman BC, Phillips B, Morimoto RI (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, Gibellini D, Ramazzotti E, Zauli G, La Placa M (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, Fukushima A, Matsubara K (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, Pasquali C, Sanchez JC, Tissot JD, Bairoch A, Appel RD, Hochstrasser DF (1994). "Human liver protein map: update 1993". Electrophoresis. 14 (11): 1216–22. doi:10.1002/elps.11501401181. PMID 8313870. S2CID 33424554.
Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ (1997). "A two-dimensional gel database of human colon carcinoma proteins". Electrophoresis. 18 (3–4): 605–13. doi:10.1002/elps.1150180344. PMID 9150948. S2CID 25454450.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (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, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T (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, Zhou S, Zhou Q (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, Mitsuia Y, Wadhwac R (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. S2CID 85853656.
Agostini I, Popov S, Li J, Dubrovsky L, Hao T, Bukrinsky M (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, Horrigan SK, Westbrook CA (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, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
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. S2CID 536461.
Wadhwa R, Yaguchi T, Hasan MK, Mitsui Y, Reddel RR, Kaul SC (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)
PDBe-KB provides an overview of all the structure information available in the PDB for Human Stress-70 protein, mitochondrial

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000113013 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000024359 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7684501-5] Domanico SZ, DeNagel DC, Dahlseid JN, Green JM, Pierce SK (Jun 1993). "Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family". Mol Cell Biol. 13 (6): 3598–610. doi:10.1128/mcb.13.6.3598. PMC 359829. PMID 7684501.

[entrez-6] "Entrez Gene: HSPA9 heat shock 70kDa protein 9 (mortalin)".

[pmid10510314-7] Mizukoshi E, Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul SC, Wadhwa R, Imamura T (Oct 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.

[pmid11900485-8] Wadhwa R, Yaguchi T, Hasan MK, Mitsui Y, Reddel RR, Kaul SC (Apr 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.

HSPA9

Function

Interactions

References

Further reading

External links