The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Hspa9  -  heat shock protein 9

Mus musculus

Synonyms: 74kDa, 75 kDa glucose-regulated protein, C3H-specific antigen, CSA, Csa, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Hspa9


High impact information on Hspa9


Biological context of Hspa9


Anatomical context of Hspa9

  • After coupled transcription-translation the precursor of PBP74 is imported into isolated yeast mitochondria, where it becomes processed to the mature protein [1].
  • Here we report the mortalin immunostaining observations on 21 human cell lines [7].
  • Differential subcellular distribution of mortalin in mortal and immortal mouse and human fibroblasts [8].
  • Four patterns of mortalin immunostaining were observed: granular-juxtanuclear cap, granular-gradient from nuclear to cell membrane, granular-juxtanuclear arch, and fibrous-perinuclear [7].
  • The mRNA for GRP75, a mitochondrial chaperone, HSC70, a cytoplasmic chaperone, protein disulfide isomerase, an endoplasmic reticulum chaperone, and C/EBPalpha, a transcription factor, was not regulated [9].

Associations of Hspa9 with chemical compounds

  • It was also cloned as glucose regulated protein, GRP75 and peptidebinding protein, PBP74 [5].
  • Western blot analysis indicates that one out of these two residues, arginine at residue 578 in the PBP74/CSA sequence of C3H mouse, contributes to the immunogenicity of CSA [10].
  • These six oxidation-sensitive proteins were identified by mass spectrometry as glial fibrillary acidic protein, creatine kinase BB, disulfide isomerase, chaperonin subunit 5, dihydropyrimidase-related protein 2, and mortalin [11].
  • Conversely, when phosphorylated mortalin was treated with tyrosine phosphatase, its interaction with FGF-1 was abrogated [12].
  • Interestingly, mortalin was preferentially tyrosine phosphorylated at the same time, and when its normally weak phosphorylation in early G1 phase was augmented by treating the cells with vanadate, a strong interaction between mortalin and FGF-1 was established [12].

Physical interactions of Hspa9


Regulatory relationships of Hspa9


Other interactions of Hspa9

  • Western analyses of transient and stable clones revealed that upregulation of p21WAF1 in stable NIH 3T3/mot-2 cells may be mediated by cyclin D1 and cdk-2 [14].
  • Our results show that mortalin and HisRS genes, which map closely to the Egr1 locus, have conserved the 129/Sv haplotype despite numerous back-crossing of the null mice progeny with C57Bl/6J animals [15].
  • Finally, we report the identification of new isoforms of HisRS and mortalin (mot-3) encoded by the 129/Sv haplotype [15].

Analytical, diagnostic and therapeutic context of Hspa9

  • By confocal immunofluorescence microscopy PBP74 is detected in mitochondria, colocalizing with the mitochondrial 60-kDa heat shock protein [1].
  • Cell fractionation studies demonstrated PBP74 in purified mitochondria in a protease-protected location [1].
  • To determine the genetic relation between the pancytosolic (uniformly distributed in cytoplasm-p66mot-1) and the perinuclear (p66mot-2) mortalin proteins found in normal and immortal mouse cells, respectively, we initiated the present study using PCR cloning, sequencing, and single nucleotide primer extension analyses [16].
  • In the present study, we report mot-2 cDNA cloning from RS-4 cells--an immortal clone from CD1-ICR mouse embryonic fibroblasts--and the chromosomal assignments of mortalin related genes to mouse chromosomes 18 and X by fluorescence in situ hybridization [17].
  • We describe here the use of quantum dots in mortalin imaging of normal and cancer cells [18].


  1. PBP74, a new member of the mammalian 70-kDa heat shock protein family, is a mitochondrial protein. Dahlseid, J.N., Lill, R., Green, J.M., Xu, X., Qiu, Y., Pierce, S.K. Mol. Biol. Cell (1994) [Pubmed]
  2. Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. Domanico, S.Z., DeNagel, D.C., Dahlseid, J.N., Green, J.M., Pierce, S.K. Mol. Cell. Biol. (1993) [Pubmed]
  3. Inactivation of tumor suppressor p53 by mot-2, a hsp70 family member. Wadhwa, R., Takano, S., Robert, M., Yoshida, A., Nomura, H., Reddel, R.R., Mitsui, Y., Kaul, S.C. J. Biol. Chem. (1998) [Pubmed]
  4. Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis. Merrick, B.A., Patterson, R.M., Witcher, L.L., He, C., Selkirk, J.K. Electrophoresis (1994) [Pubmed]
  5. Mortalin: a potential candidate for biotechnology and biomedicine. Wadhwa, R., Taira, K., Kaul, S.C. Histol. Histopathol. (2002) [Pubmed]
  6. Induction of cellular senescence by transfection of cytosolic mortalin cDNA in NIH 3T3 cells. Wadhwa, R., Kaul, S.C., Sugimoto, Y., Mitsui, Y. J. Biol. Chem. (1993) [Pubmed]
  7. Correlation between complementation group for immortality and the cellular distribution of mortalin. Wadhwa, R., Pereira-Smith, O.M., Reddel, R.R., Sugimoto, Y., Mitsui, Y., Kaul, S.C. Exp. Cell Res. (1995) [Pubmed]
  8. Differential subcellular distribution of mortalin in mortal and immortal mouse and human fibroblasts. Wadhwa, R., Kaul, S.C., Mitsui, Y., Sugimoto, Y. Exp. Cell Res. (1993) [Pubmed]
  9. Dietary energy tissue-specifically regulates endoplasmic reticulum chaperone gene expression in the liver of mice. Dhahbi, J.M., Mote, P.L., Tillman, J.B., Walford, R.L., Spindler, S.R. J. Nutr. (1997) [Pubmed]
  10. Antigenic protein specific for C3H strain mouse is a mitochondrial stress-70 protein. Michikawa, Y., Baba, T., Arai, Y., Sakakura, T., Tanaka, M., Kusakabe, M. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  11. Proteomic identification of specific oxidized proteins in ApoE-knockout mice: relevance to Alzheimer's disease. Choi, J., Forster, M.J., McDonald, S.R., Weintraub, S.T., Carroll, C.A., Gracy, R.W. Free Radic. Biol. Med. (2004) [Pubmed]
  12. Cell-cycle dependent tyrosine phosphorylation on mortalin regulates its interaction with fibroblast growth factor-1. Mizukoshi, E., Suzuki, M., Misono, T., Loupatov, A., Munekata, E., Kaul, S.C., Wadhwa, R., Imamura, T. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  13. An N-terminal region of mot-2 binds to p53 in vitro. Kaul, S.C., Reddel, R.R., Mitsui, Y., Wadhwa, R. Neoplasia (2001) [Pubmed]
  14. p53-independent upregulation of p21WAF1 in NIH 3T3 cells malignantly transformed by mot-2. Takano, S., Wadhwa, R., Mitsui, Y., Kaul, S.C. Cell Res. (2001) [Pubmed]
  15. New mortalin and histidyl tRNA synthetase isoforms point out a pitfall in proteomic analysis of Egr1 genetically modified mice. Chardonnet, S., Decottignies, P., Amar, L., Le Caer, J.P., Davis, S., Laroche, S., Le Mar??chal, P. Proteomics (2007) [Pubmed]
  16. Genetic differences between the pancytosolic and perinuclear forms of murine mortalin. Wadhwa, R., Akiyama, S., Sugihara, T., Reddel, R.R., Mitsui, Y., Kaul, S.C. Exp. Cell Res. (1996) [Pubmed]
  17. Mouse and human chromosomal assignments of mortalin, a novel member of the murine hsp70 family of proteins. Kaul, S.C., Wadhwa, R., Matsuda, Y., Hensler, P.J., Pereira-Smith, O.M., Komatsu, Y., Mitsui, Y. FEBS Lett. (1995) [Pubmed]
  18. Mortalin imaging in normal and cancer cells with quantum dot immuno-conjugates. Kaul, Z., Yaguchi, T., Kaul, S.C., Hirano, T., Wadhwa, R., Taira, K. Cell Res. (2003) [Pubmed]
WikiGenes - Universities