SUBCELLULAR LOCALIZATION
| intracellular
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| intracellular,cytoplasm,organelle,mitochondria,outer
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| intracellular,cytoplasm,organelle,membrane
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| intracellular,cytoplasm,organelle,endoplasmic reticulum
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| intracellular,nucleus,nucleoplasm
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| intracellular,nuclear envelope
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text
| coexpression with the E1B/19 kda protein results in a shift in BNIP3 localization pattern to the nuclear envelope |
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is localized to the nucleus in the majority of glioblastoma multiforme (GBM) tumors and fails to induce cell death ![](pubmed.jpg) |
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localized to both mitochondria and the endoplasmic reticulum (ER)![](pubmed.jpg) |
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localizes to the outer mitochondrial membrane, where it functions in mitophagy and mitochondrial dynamics ![](pubmed.jpg) |
basic FUNCTION
| apoptosis inducing protein, even in the presence of BCL2 |
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playing a role in hypoxia-induced cell death in epithelial cells that could be circumvented by growth factor signaling |
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mediates mitochondrial dysfunction through activation of BAX or BAK1 which is independent of mitochondrial permeability transition pore opening ![](pubmed.jpg) |
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might play a role in gastric carcinoma development ![](pubmed.jpg) |
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implicated in the pathogenesis of cancer and heart disease ![](pubmed.jpg) |
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involved in the induction of autophagy and required for mitophagy (specialized autophagy that targets mitochondria) , and is clearly a survival mechanism that promotes tumor progression ![](pubmed.jpg) |
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in tumor cells, BNIP3 is regulated by hypoxia and deregulation is associated with tumor growth ![](pubmed.jpg) |
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transcriptional repression function causing reduced apoptosis-inducing factor expression and increased resistance to apoptosis in GBM tumors ![](pubmed.jpg) |
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mediates permeabilization of mitochondria and release of cytochrome c via a novel mechanism ![](pubmed.jpg) |
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BNIP3 and PDK1 are involved in two important pathways, cell death and glycolytic, playing critical roles in these pathways in cardiomyocytes after severe hypoxia ![](pubmed.jpg) |
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might have a dual function in the myocardium, where it regulates both mitochondrial turnover via autophagy and cell death and that these are two separate processes activated by BNIP3 ![](pubmed.jpg) |
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contributes to cell death through activation of the mitochondrial pathway of apoptosis ![](pubmed.jpg) |
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caused an increase in mitochondrial protease activity, suggesting that BNIP3 might promote degradation of proteins in the mitochondria ![](pubmed.jpg) |
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BNIP3-mediated impairment of mitochondrial respiration induces mitochondrial turnover by activating mitochondrial autophagy ![](pubmed.jpg) |
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key regulator of cell death/autophagy and can act as an effector of a necrosis-like, atypical death program ![](pubmed.jpg) |
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regulates the apoptotic balance as an autophagy receptor that induces removal of both mitochondria and ER ![](pubmed.jpg) |
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role in limiting mitochondrial mass and maintaining mitochondrial integrity in the liver that has consequences for lipid metabolism and disease ![](pubmed.jpg) |
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BNIP3 and AIFM1 cooperate to induce apoptosis and cavitation during epithelial morphogenesis ![](pubmed.jpg) |
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could play a protective role in tumor cells under hypoxia ![](pubmed.jpg) |
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BNIP3 regulates mitophagy during hypoxia, whereas BNIP3L is required for mitophagy during development of the erythroid lineage ![](pubmed.jpg) |
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temporally regulated role for BNIP3 and BNIP3L in the generation of robust NK cell memory ![](pubmed.jpg) |