Biology:HSPA9
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Mitochondrial 70kDa heat shock protein (mtHsp70), also known as mortalin, is a protein that in humans is encoded by the HSPA9 gene.[1][2]
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.[2]
Interactions
HSPA9 has been shown to interact with FGF1[3] and P53.[4]
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.[5][6] These genetic variants have been shown to interfere with normal HSPA9 function [7]
References
- ↑ "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. Jun 1993. doi:10.1128/mcb.13.6.3598. PMID 7684501.
- ↑ 2.0 2.1 "Entrez Gene: HSPA9 heat shock 70kDa protein 9 (mortalin)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3313.
- ↑ "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". Biochem. J. 343 (2): 461–6. Oct 1999. doi:10.1042/0264-6021:3430461. PMID 10510314.
- ↑ "Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein". Exp. Cell Res. 274 (2): 246–53. Apr 2002. doi:10.1006/excr.2002.5468. PMID 11900485.
- ↑ "Mutations in the heat-shock protein A9 (HSPA9) gene cause the EVEN-PLUS syndrome of congenital malformations and skeletal dysplasia". Scientific Reports 5: 17154. November 2015. doi:10.1038/srep17154. PMID 26598328. Bibcode: 2015NatSR...517154R.
- ↑ "MIM 616854: Even Plus Syndrome". OMIM. https://omim.org/entry/616854.
- ↑ "Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin". The Journal of Physical Chemistry B 123 (16): 3383–3396. April 2019. doi:10.1021/acs.jpcb.9b00071. PMID 30933555.
Further reading
- "Mortalin: present and prospective". Exp. Gerontol. 37 (10–11): 1157–64. 2003. doi:10.1016/S0531-5565(02)00135-3. PMID 12470827.
- "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. 2007. doi:10.1196/annals.1395.032. PMID 17460192. Bibcode: 2007NYASA1100..306Y.
- "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis 13 (12): 992–1001. 1993. doi:10.1002/elps.11501301201. PMID 1286669.
- "Mouse and human chromosomal assignments of mortalin, a novel member of the murine hsp70 family of proteins". FEBS Lett. 361 (2–3): 269–72. 1995. doi:10.1016/0014-5793(95)00177-B. PMID 7698336.
- "Cloning and subcellular localization of human mitochondrial hsp70". J. Biol. Chem. 270 (4): 1705–10. 1995. doi:10.1074/jbc.270.4.1705. PMID 7829505.
- "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. 1994. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
- "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene 146 (2): 199–207. 1994. doi:10.1016/0378-1119(94)90293-3. PMID 8076819.
- "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- "Human liver protein map: update 1993". Electrophoresis 14 (11): 1216–22. 1994. doi:10.1002/elps.11501401181. PMID 8313870.
- "A two-dimensional gel database of human colon carcinoma proteins". Electrophoresis 18 (3–4): 605–13. 1997. doi:10.1002/elps.1150180344. PMID 9150948.
- "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". Biochem. J. 343 (2): 461–6. 1999. doi:10.1042/0264-6021:3430461. PMID 10510314.
- "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. 2000. doi:10.1074/jbc.275.1.279. PMID 10617616.
- "Inactivation of p53 and life span extension of human diploid fibroblasts by mot-2". FEBS Lett. 474 (2–3): 159–64. 2000. doi:10.1016/S0014-5793(00)01594-5. PMID 10838077.
- "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. 2000. doi:10.1006/excr.2000.4992. PMID 10964507.
- "Human mortalin (HSPA9): a candidate for the myeloid leukemia tumor suppressor gene on 5q31". Leukemia 14 (12): 2128–34. 2001. doi:10.1038/sj.leu.2401935. PMID 11187902.
- "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. 2002. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- "Implication of PBP74/mortalin/GRP75 in the radio-adaptive response". Int. J. Radiat. Biol. 78 (3): 183–90. 2002. doi:10.1080/09553000110097208. PMID 11869473.
- "Hsp70 family member, mot-2/mthsp70/GRP75, binds to the cytoplasmic sequestration domain of the p53 protein". Exp. Cell Res. 274 (2): 246–53. 2002. 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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