Mouse Anti-BNIP3 Recombinant Antibody (CBYY-0707) (CBMAB-0710-YY)

BCL2 interacting protein 3

This gene is encodes a mitochondrial protein that contains a BH3 domain and acts as a pro-apoptotic factor. The encoded protein interacts with anti-apoptotic proteins, including the E1B 19 kDa protein and Bcl2. This gene is silenced in tumors by DNA methylation.

BCL2 Interacting Protein 3; BCL2/Adenovirus E1B 19kDa Interacting Protein 3; NIP3; BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 3;

Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway.

Apoptotic process Source: MGI
Autophagic cell death Source: Ensembl
Autophagy of mitochondrion Source: ParkinsonsUK-UCL
Brown fat cell differentiation Source: Ensembl
Cardiac muscle cell apoptotic process Source: Ensembl
Cell death Source: UniProtKB
Cellular response to cobalt ion Source: BHF-UCL
Cellular response to hydrogen peroxide Source: Ensembl
Cellular response to hypoxia Source: BHF-UCL
Cellular response to mechanical stimulus Source: UniProtKB
Cerebral cortex development Source: Ensembl
Defense response to virus Source: UniProtKB
Granzyme-mediated programmed cell death signaling pathway Source: GO_Central
Intrinsic apoptotic signaling pathway in response to hypoxia Source: BHF-UCL
Mitochondrial fragmentation involved in apoptotic process Source: BHF-UCL
Mitochondrial outer membrane permeabilization Source: UniProtKB
Mitochondrial protein catabolic process Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of cell death Source: MGI
Negative regulation of membrane potential Source: UniProtKB
Negative regulation of mitochondrial fusion Source: BHF-UCL
Negative regulation of mitochondrial membrane permeability involved in apoptotic process Source: Ensembl
Negative regulation of mitochondrial membrane potential Source: Ensembl
Negative regulation of reactive oxygen species metabolic process Source: Ensembl
Neuron apoptotic process Source: UniProtKB
Oligodendrocyte differentiation Source: Ensembl
Positive regulation of apoptotic process Source: UniProtKB
Positive regulation of autophagy Source: UniProtKB
Positive regulation of autophagy of mitochondrion Source: Ensembl
Positive regulation of cardiac muscle cell apoptotic process Source: Ensembl
Positive regulation of macroautophagy Source: MGI
Positive regulation of mitochondrial calcium ion concentration Source: Ensembl
Positive regulation of mitochondrial fission Source: BHF-UCL
Positive regulation of necrotic cell death Source: Ensembl
Positive regulation of programmed cell death Source: UniProtKB
Positive regulation of protein-containing complex disassembly Source: BHF-UCL
Positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
Reactive oxygen species metabolic process Source: UniProtKB
Regulation of aerobic respiration Source: Ensembl
Regulation of mitochondrial membrane permeability Source: UniProtKB
Regulation of programmed cell death Source: GO_Central
Response to axon injury Source: Ensembl
Response to bacterium Source: Ensembl
Response to hyperoxia Source: Ensembl
Response to hypoxia Source: UniProtKB
Response to oxygen-glucose deprivation Source: Ensembl
Toxin transport Source: Ensembl
Viral process Source: UniProtKB-KW

Mitochondrion; Mitochondrion outer membrane. Coexpression with the EIB 19-kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the mitochondrion outer membrane.

Helical: 229-249 aa