Alternative titles; symbols
HGNC Approved Gene Symbol: BNIP1
Cytogenetic location: 5q35.1 Genomic coordinates (GRCh38) : 5:173,144,531-173,164,387 (from NCBI)
Using a yeast 2-hybrid system to identify proteins that interact with discrete domains of the E1B 19-kD protein, which is involved in suppression of cell death, Boyd et al. (1994) cloned human B-cell cDNAs encoding NIP1, NIP2 (603292), and NIP3 (603293). The deduced NIP1 protein has 228 amino acids and contains a putative membrane-spanning hydrophobic domain. Although the authors found no significant sequence homology between NIP1 and other proteins, they identified a 59- to 83-amino acid region of NIP1 that shows 29% to 36% identity to a conserved region within the catalytic domain of 3 mammalian 3-prime-5-prime-cyclic nucleotide phosphodiesterases. Boyd et al. (1994) localized NIP1 to the nuclear envelope region and to other cytoplasmic structures.
Adenovirus E1B 19-kD protein protects against cell death induced by viral infection and certain external stimuli. Using yeast 2-hybrid analysis, Boyd et al. (1994) showed that NIP1, NIP2, and NIP3 interacted with the adenovirus E1B 19-kD protein and with human BCL2 (151430), which can functionally substitute for the 19-kD protein during adenovirus infection. The interactions occurred at bipartite sequence motifs common to both the E1B 19-kD and BCL2 proteins.
Tang et al. (2011) showed that overexpression of RNF185 (620096) induced autophagosome formation and mitochondrial autophagy in HeLa cells. Immunoprecipitation analysis revealed that RNF185 interacted with the mitochondrial proteins BNIP1 and ATG5 (604261) in 293T cells. Interaction of RNF185 with BNIP1 required the transmembrane domains of RNF185 and the coiled-coiled domain of BNIP1. RNF185 colocalized with BNIP1 at mitochondria and polyubiquitinated BNIP1 via lys63 (K63) linkage to enable its interaction with autophagy receptor p62 (SQSTM1; 601530).
Wang et al. (2013) found that induction of the E3 ubiquitin ligase RNF186 (617163) contributed to endoplasmic reticulum (ER) stress-associated signaling and apoptosis in a caspase (e.g., CASP9; 602234)-dependent manner. Cotransfection and immunoprecipitation analyses in HeLa cells showed that RNF186, through it transmembrane domains, interacted with BNIP1. Overexpression of RNF186 promoted BNIP1 ubiquitination and transfer of BNIP1 to mitochondria. Wang et al. (2013) concluded that BNIP1 functions as a downstream modulator of RNF186 to direct ER stress-associated apoptotic signaling.
Gross (2012) mapped the BNIP1 gene to chromosome 5q35.1 based on an alignment of the BNIP1 sequence (GenBank AF083956) with the genomic sequence (GRCh37).
Boyd, J. M., Malstrom, S., Subramanian, T., Venkatesh, L. K., Schaeper, U., Elangovan, B., D'Sa-Eipper, C., Chinnadurai, G. Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins. Cell 79: 341-351, 1994. Note: Erratum: Cell 79: 1121 only, 1994. [PubMed: 7954800] [Full Text: https://doi.org/10.1016/0092-8674(94)90202-x]
Gross, M. B. Personal Communication. Baltimore, Md. 6/29/2012.
Tang, F., Wang, B., Li, N., Wu, Y., Jia, J., Suo, T., Chen, Q., Liu, Y. J., Tang, J. RNF185, a novel mitochondrial ubiquitin E3 ligase, regulates autophagy through interaction with BNIP1. PLoS One 6: e24367, 2011. [PubMed: 21931693] [Full Text: https://doi.org/10.1371/journal.pone.0024367]
Wang, P., Wu, Y., Li, Y., Zheng, J., Tang, J. A novel RING finger E3 ligase RNF186 regulates ER stress-mediated apoptosis through interaction with BNip1. Cell. Signal. 25: 2320-2333, 2013. [PubMed: 23896122] [Full Text: https://doi.org/10.1016/j.cellsig.2013.07.016]