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; GeneCards: HSPA9
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3N8E, 4KBO
Enzyme activity
Gene location (Human)
Chr.	Chromosome 5 (human)
End	138,575,675 bp
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)
End	35,087,410 bp
RNA expression pattern
	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
	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
Databases	NCBI: entry; OMA: entry
	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.

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

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000113013 – Ensembl, May 2017
1 2 3 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.
1 2 "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 (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.
↑ Royer-Bertrand B, Castillo-Taucher S, Moreno-Salinas R, Cho TJ, Chae JH, Choi M, et al. (November 2015). "Mutations in the heat-shock protein A9 (HSPA9) gene cause the EVEN-PLUS syndrome of congenital malformations and skeletal dysplasia". Scientific Reports. 5 17154. Bibcode:2015NatSR...517154R. doi:10.1038/srep17154. PMC 4657157. PMID 26598328.
↑ "MIM 616854: Even Plus Syndrome". OMIM.
↑ Moseng MA, Nix JC, Page RC (April 2019). "Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin". The Journal of Physical Chemistry B. 123 (16): 3383–3396. doi:10.1021/acs.jpcb.9b00071. PMC 6483861. PMID 30933555.

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

This protein-related article is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000113013 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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] 1 2 "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 (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.

[pmid26598328-9] Royer-Bertrand B, Castillo-Taucher S, Moreno-Salinas R, Cho TJ, Chae JH, Choi M, et al. (November 2015). "Mutations in the heat-shock protein A9 (HSPA9) gene cause the EVEN-PLUS syndrome of congenital malformations and skeletal dysplasia". Scientific Reports. 5 17154. Bibcode:2015NatSR...517154R. doi:10.1038/srep17154. PMC 4657157. PMID 26598328.

[10] "MIM 616854: Even Plus Syndrome". OMIM.

[pmid30933555-11] Moseng MA, Nix JC, Page RC (April 2019). "Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin". The Journal of Physical Chemistry B. 123 (16): 3383–3396. doi:10.1021/acs.jpcb.9b00071. PMC 6483861. PMID 30933555.