HSP75
Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA. Belongs to the heat shock protein 90 family. Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung, placenta and bladder. Expression is highly reduced in bladder cancer and renal cell carcinoma specimens compared to healthy tissues, but it is increased in other type of tumors. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
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Protein type: Chaperone; Heat shock protein |
Chromosomal Location of mouse Ortholog: 16 A1|16 2.38 cM |
Cellular Component:
cell periphery; membrane; mitochondrial inner membrane; mitochondrial intermembrane space; mitochondrial matrix; mitochondrion; nucleoplasm
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Molecular Function:
ATP binding; ATP hydrolysis activity; ATP-dependent protein folding chaperone; nucleotide binding; protein kinase binding; unfolded protein binding
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Biological Process:
negative regulation of cellular respiration; negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; protein folding; translational attenuation
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Reference #:
Q9CQN1
(UniProtKB)
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Alt. Names/Synonyms: 2410002K23Rik; Heat shock protein 75 kDa, mitochondrial; HSP; HSP 75; Hsp75; OTTMUSP00000021685; TNF receptor-associated protein 1; TNFR-associated protein 1; TRAP-1; Trap1; Tumor necrosis factor type 1 receptor-associated protein
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Gene Symbols: Trap1
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Molecular weight:
80,209 Da
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Basal Isoelectric point:
6.25
Predict pI for various phosphorylation states
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