Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Bad
  • participates in the following biological processes:
    • activation of cysteine-type endopeptidase activity involved in apoptotic process ^[12]
    • ADP metabolic process ^[5]
    • apoptotic process ^[1]
    • ATP metabolic process ^[5]
    • cell proliferation ^[14]
    • cellular process regulating host cell cycle in response to virus ^[13]
    • cytokine-mediated signaling pathway ^{[14, 11]}
    • induction of apoptosis by extracellular signals ^[13]
    • positive regulation of apoptotic process ^[8]
    • positive regulation of glucokinase activity ^[5]
    • positive regulation of insulin secretion^[5]
    • positive regulation of insulin secretion involved in cellular response to glucose stimulus ^[5]
    • positive regulation of mitochondrial membrane potential ^[5]
    • positive regulation of type B pancreatic cell development ^[5]
    • regulation of apoptotic process ^[15]
    • type B pancreatic cell proliferation ^[5]
  • performs the following molecular functions:
    • cysteine-type endopeptidase activator activity involved in apoptotic process activity ^{[12, 11]}
  • is located in the following cellular components:
    • cytoplasm ^[9]
    • cytosol ^[11]
    • mitochondrion ^{[5, 10]}
  
  
• The gene product of gene X has been shown to bind to the gene products of Bcl2, Bcl2l1, Gck, Ywhab, Ywhaq, and Q07817-1 ^{[5, 8, 12, 2, 3, 4]}.
  In addition, researchers have inferred, based on physical interactions, that the gene product of Bad
  • performs the following molecular functions:
    • binding activity ^[4]
    • protein heterodimerization activity ^[15]
  
  
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Bad
  • participates in the following biological processes:
    • glucose homeostasis ^{[5, 6]}
    • regulation of apoptotic process ^{[16, 7]}
    • positive regulation of B cell differentiation ^[7]
    • positive regulation of T cell differentiation ^[7]
    • glucose catabolic process ^[5]
    • induction of apoptosis by extracellular signals ^[5]

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References
^[1] Ayllon V et al. The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad.
^[2] Certo M et al. Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members.
^[3] Chen L et al. Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function.
^[4] Chiang CW et al. Protein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosis.
^[5] Danial NN et al. BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis.
^[6] Danial NN et al. Dual role of proapoptotic BAD in insulin secretion and beta cell survival.
^[7] Datta SR et al. Survival factor-mediated BAD phosphorylation raises the mitochondrial threshold for apoptosis.
^[8] Deng H et al. Phosphorylation of Bcl-associated death protein (Bad) by erythropoietin-activated c-Jun N-terminal protein kinase 1 contributes to survival of erythropoietin-dependent cells.
^[9] Dominov JA et al. Pro- and anti-apoptotic members of the bcl-2 family in skeletal muscle: A distinct role for bcl-2 in later stages of myogenesis.
^[10] Pagliarini DJ et al. A mitochondrial protein compendium elucidates complex I disease biology.
^[11] Putcha GV et al. Intrinsic and extrinsic pathway signaling during neuronal apoptosis: lessons from the analysis of mutant mice.
^[12] Quoyer J et al. GLP-1 mediates antiapoptotic effect by phosphorylating Bad through a beta-arrestin 1-mediated ERK1/2 activation in pancreatic beta-cells.
^[13] Seo SY et al. BAD is a pro-survival factor prior to activation of its pro-apoptotic function.
^[14] Tzung SP et al. Expression of Bcl-2 family during liver regeneration and identification of Bcl-x as a delayed early response gene.
^[15] Yang E et al. Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death.
^[16] Yu C et al. JNK suppresses apoptosis via phosphorylation of the proapoptotic Bcl-2 family protein BAD.