HSPA9

HSPA9
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; OMA:HSPA9 - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3N8E, 4KBO
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.6.4.10 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 5 (human) Band 5q31.2 Start 138,553,756 bp End 138,575,675 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18 B1|18 18.8 cM Start 35,070,467 bp End 35,087,410 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal gland right adrenal cortex left adrenal gland left adrenal cortex epithelium of colon muscle of thigh ventricular zone Achilles tendon gastrocnemius muscle islet of Langerhans Top expressed in Ileal epithelium primitive streak Paneth cell endothelial cell of lymphatic vessel right kidney epiblast medullary collecting duct interventricular septum muscle of thigh adrenal gland More reference expression data BioGPS n/a
Gene ontology Molecular function nucleotide binding unfolded protein binding protein binding ATP binding ubiquitin protein ligase binding RNA binding ATPase activity heat shock protein binding protein folding chaperone activity misfolded protein binding enzyme binding Cellular component cytoplasm focal adhesion nucleolus mitochondrion mitochondrial nucleoid extracellular exosome 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 Unfolded Protein Response protein refolding regulation of erythrocyte differentiation chaperone cofactor-dependent protein refolding protein export from nucleus negative regulation of hematopoietic stem cell differentiation negative regulation of hemopoiesis 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: 138.55 – 138.58 Mb Chr 18: 35.07 – 35.09 Mb PubMed search
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.

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.

Interactions

HSPA9 has been shown to interact with FGF1 and P53.

Clinical relevance and genetic deficiency

In 2015, a group around Andrea Superti-Furga showed that biallelic variants in the HSPA9 gene may result in a combination of congenital malformations called the EVEN-PLUS syndrome. These genetic variants have been shown to interfere with normal HSPA9 function

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. 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 (1): 306–11. Bibcode:2007NYASA1100..306Y. 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. Bibcode:1995FEBSL.361..269K. 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 (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. Bibcode:2000FEBSL.474..159K. 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. Bibcode:2002CBio...12....1A. 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 U.S. 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