Detail Information of Protein

Basic Information:

Symbol Hspa9
Synonyms Grp75; Hsp74; Hspa9a
Protein Name Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (p66 MOT)
Species Mouse
Entrez ID 15526
Uniprot ID P38647
Membrane Contact Site ER-MT; MT-ER
Location (from literature) MT
Cell line/Tissue Mouse livers; MEFs; Mouse testes; Mouse brains and retinas; RGCs; HRECs; C57BL6 mice
Experimental Method Low throughput experimental methods
Protein Sequence
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Complex Information:

Complex ID Subunit of complex Subcellular location Species More
CMCS00107 Itpr3; Hspa9; Vdac1; Park7 ER-MT; MT-ER Mouse more
CMCS00161 Tgm2; Vdac1; Itpr1; Hspa9 ER-MT; MT-ER Mouse more
CMCS00175 Vdac1; Itpr1; Hspa9 ER-MT; MT-ER Mouse more
CMCS00266 Itpr3; Hspa9; Vdac1; Pdk4 ER-MT; MT-ER Mouse more

Expression Overview of Hspa9:

Homology Information of Hspa9:

Uniprot ID P38647
EggNOG KOG0102
HOGENOM CLU_005965_2_1_1
OrthoDB 143at2759
TreeFam TF105046
GeneTree ENSGT00920000149123

References:

Pubmed ID 30590033
DOI 10.1016/j.celrep.2018.11.094
Description GRP75 localizes in Mitochondrion-associated membranes (MAMs) and acts as a bridging molecule between the two organelles by assembling the IP3R-GRP75-VDAC complex, which is involved in the transport of Ca2+from the endoplasmic reticulum (ER) to Mitochondrion.
Description of experimental evidence The protein was validated by western blot analysis, Co-IP and PLA in mouse livers and MEFs.
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Pubmed ID 29785746
DOI 10.1002/pmic.201700478
Description By Andromeda search engine against the decoy UniProt-mouse database and Swiss-Prot human database, which yielded 2,808 proteins from mouse testes (mT),2,478 proteins from mouse brain (mB) and 2,155 proteins from human testes (hT).
Description of experimental evidence The protein was validated by TEM and LC -MS/MS analyses in mouse testes.
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Pubmed ID 28522876
DOI 10.1038/s41598-017-02213-1
Description Using this method, 1313 non-redundant proteins were identified in the MAM.
Description of experimental evidence The protein was validated by proteomic analysis, long gradient nano-reverse-phase liquid chromatography, mass spectrometry and bioinformatics analysis in RGCs, HRECs, mouse brains and retinas.
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Pubmed ID 27272971
DOI 10.1038/srep27351
Description In this work we describe for the first time the protein composition of highly purified hepatic MAM fractions and demonstrate that CAV1 is a MAM-resident protein.
Description of experimental evidence The protein was validated by stable isobaric labeling and LC-MS/MS in mouse livers.
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Pubmed ID 31767755
DOI 10.1073/pnas.1906565116
Description DJ-1 regulates the integrity and function of ER-mitochondria association through interaction with IP3R3-GRP75-VDAC1.
Description of experimental evidence The protein was validated by western blotting, electron microscopy, co-immunoprecipitation assays, PLA, Blue-Native and SDS-PAGE 2D separation in C57BL6 mice, and suggests that impaired ER-mitochondria association could contribute to the pathogenesis of PD.
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Pubmed ID 24947355
DOI 10.2337/db13-1751
Description Mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs) are functional domains between both organelles involved in Ca2+ exchange, through the voltage-dependent anion channel (VDAC)-1/glucose-regulated protein 75 (Grp75)/inositol 1,4,5-triphosphate receptor (IP3R)-1 complex, and regulating energy metabolism.
Description of experimental evidence The protein was validated by immunofluorescence, duolink II in situ PLA and western blot in mouse livers, which regulates energy metabolism.
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Pubmed ID 30523025
DOI 10.2337/db18-0363
Description Here, we demonstrate that PDK4 interacts with and stabilizes the IP3R1-GRP75-VDAC1 complex at the MAM interface.
Description of experimental evidence The protein was validated by in situ proximity ligation assay, immunofluorescence analysis, coimmunoprecipitation, transmission electron microscopy and immunoblotting in C2C12 myoblasts, which augments ER–Mitochondria contact to dampen skeletal muscle insulin signaling during obesity.
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Contact zhy1001@alu.uestc.edu.cn or yangzhang@cdutcm.edu.cn
© Department of Bioinformatics