Gene Ontology annotation through association of InterPro records with GO terms

Gene Ontology annotation by the MGI curatorial staff, curated orthology

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

Annotation inferences using phylogenetic trees

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs

Combined Automated Annotation using Multiple IEA Methods

Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria.

Proapoptotic Nix activates the JNK pathway by interacting with POSH and mediates death in a Parkinson disease model.

Nix is a selective autophagy receptor for mitochondrial clearance.

Nix, a receptor protein for mitophagy in mammals.

Cellular adaptation to anthrax lethal toxin-induced mitochondrial cholesterol enrichment, hyperpolarization, and reactive oxygen species generation through downregulating MLN64 in macrophages.

Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins.

NIX is required for programmed mitochondrial clearance during reticulocyte maturation.

Essential role for Nix in autophagic maturation of erythroid cells.

Unrestrained erythroblast development in Nix-/- mice reveals a mechanism for apoptotic modulation of erythropoiesis.

A short linear motif in BNIP3L (NIX) mediates mitochondrial clearance in reticulocytes.

Programmed mitophagy is essential for the glycolytic switch during cell differentiation.

Dimerization of mitophagy receptor BNIP3L/NIX is essential for recruitment of autophagic machinery.

Dual autonomous mitochondrial cell death pathways are activated by Nix/BNip3L and induce cardiomyopathy.

A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region.

BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3.

Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains.

Mieap, a p53-inducible protein, controls mitochondrial quality by repairing or eliminating unhealthy mitochondria.

UniProt entry Q9Z2F7 (BNIP3L_MOUSE)