BNIP2

BCL2/adenovirus E1B 19kDa interacting protein 2
Identifiers
Symbols	BNIP2 ; BNIP-2; NIP2
External IDs	OMIM: 603292 MGI: 109327 HomoloGene: 3194 GeneCards: BNIP2 Gene
Gene ontology Molecular function • GTPase activator activity • calcium ion binding • protein binding • identical protein binding Cellular component • nuclear envelope • cytoplasm • cytosol • intracellular membrane-bounded organelle • perinuclear region of cytoplasm Biological process • apoptotic process • muscle cell differentiation • negative regulation of apoptotic process • positive regulation of GTPase activity • positive regulation of muscle cell differentiation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	663	12175
Ensembl	ENSG00000140299	ENSMUSG00000011958
UniProt	Q12982	O54940
RefSeq (mRNA)	NM_004330	NM_001008238
RefSeq (protein)	NP_004321	NP_001008239
Location (UCSC)	Chr 15: 59.66 – 59.69 Mb	Chr 9: 69.99 – 70.01 Mb
PubMed search

BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 is a protein that in humans is encoded by the BNIP2 gene.^[1][2]

Function

This gene is a member of the BCL2/adenovirus E1B 19 kd-interacting protein (BNIP) family. Though the specific function is unknown, it interacts with the E1B 19 kDa protein which is responsible for the protection of virally induced cell death, as well as E1B 19 kDa-like sequences of BCL-2, also an apoptotic protector.^[2]

Interactions

BNIP2 has been shown to interact with:

• ARHGAP1,^[3][4]
• Bcl-2,^[1][5] and
• CDC42.^[6][3][4]

References

1. Boyd JM, Malstrom S, Subramanian T, Venkatesh LK, Schaeper U, Elangovan B, D'Sa-Eipper C, Chinnadurai G (November 1994). "Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of cellular proteins". Cell 79 (2): 341–51. doi:10.1016/0092-8674(94)90202-X. PMID 7954800.
2. "Entrez Gene: BNIP2 BCL2/adenovirus E1B 19kDa interacting protein 2".
3. Low BC, Seow KT, Guy GR (December 2000). "The BNIP-2 and Cdc42GAP homology domain of BNIP-2 mediates its homophilic association and heterophilic interaction with Cdc42GAP". J. Biol. Chem. 275 (48): 37742–51. doi:10.1074/jbc.M004897200. PMID 10954711.
4. Low BC, Lim YP, Lim J, Wong ES, Guy GR (November 1999). "Tyrosine phosphorylation of the Bcl-2-associated protein BNIP-2 by fibroblast growth factor receptor-1 prevents its binding to Cdc42GAP and Cdc42". J. Biol. Chem. 274 (46): 33123–30. doi:10.1074/jbc.274.46.33123. PMID 10551883.
5. Qin W, Hu J, Guo M, Xu J, Li J, Yao G, Zhou X, Jiang H, Zhang P, Shen L, Wan D, Gu J (August 2003). "BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis". Biochem. Biophys. Res. Commun. 308 (2): 379–85. doi:10.1016/s0006-291x(03)01387-1. PMID 12901880.
6. Low BC, Seow KT, Guy GR (May 2000). "Evidence for a novel Cdc42GAP domain at the carboxyl terminus of BNIP-2". J. Biol. Chem. 275 (19): 14415–22. doi:10.1074/jbc.275.19.14415. PMID 10799524.

Further reading

• Belcredito S, Vegeto E, Brusadelli A; et al. (2002). "Estrogen neuroprotection: the involvement of the Bcl-2 binding protein BNIP2". Brain Res. Brain Res. Rev. 37 (1–3): 335–42. doi:10.1016/S0165-0173(01)00138-2. PMID 11744098.
• Ohi N, Tokunaga A, Tsunoda H; et al. (1999). "A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region". Cell Death Differ. 6 (4): 314–25. doi:10.1038/sj.cdd.4400493. PMID 10381623.
• Zhou YT, Soh UJ, Shang X; et al. (2002). "The BNIP-2 and Cdc42GAP homology/Sec14p-like domain of BNIP-Salpha is a novel apoptosis-inducing sequence". J. Biol. Chem. 277 (9): 7483–92. doi:10.1074/jbc.M109459200. PMID 11741952.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Shang X, Zhou YT, Low BC (2003). "Concerted regulation of cell dynamics by BNIP-2 and Cdc42GAP homology/Sec14p-like, proline-rich, and GTPase-activating protein domains of a novel Rho GTPase-activating protein, BPGAP1". J. Biol. Chem. 278 (46): 45903–14. doi:10.1074/jbc.M304514200. PMID 12944407.
• Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Zhou YT, Guy GR, Low BC (2005). "BNIP-2 induces cell elongation and membrane protrusions by interacting with Cdc42 via a unique Cdc42-binding motif within its BNIP-2 and Cdc42GAP homology domain". Exp. Cell Res. 303 (2): 263–74. doi:10.1016/j.yexcr.2004.08.044. PMID 15652341.
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.