Bad Gene Summary [Rat]
Enables 14-3-3 protein binding activity; protein kinase B binding activity; and protein phosphatase 2B binding activity. Involved in several processes, including cellular response to chromate; positive regulation of granulosa cell apoptotic process; and response to anesthetic. Located in cytosol and mitochondrion. Used to study several diseases, including Parkinsonism; diabetic neuropathy; gastric ulcer; impotence; and middle cerebral artery infarction. Biomarker of several diseases, including artery disease (multiple); brain ischemia; obesity; traumatic brain injury; and type 2 diabetes mellitus. Human ortholog(s) of this gene implicated in endometrial cancer; lung non-small cell carcinoma; and pancreatic cancer. Orthologous to human BAD (BCL2 associated agonist of cell death). [provided by Alliance of Genome Resources, Jul 2025]
Details
| Type | Protein Coding |
| Official Symbol | Bad |
| Official Name | BCL2-associated agonist of cell death [Source:RGD Symbol;Acc:620103] |
| Ensembl ID | ENSRNOG00000021147 |
| Bio databases IDs | |
| Aliases | BCL2-associated agonist of cell death |
| Synonyms | Bad v1, Bad v2, BBC2, BCL2-associated agonist of cell death, BCL2L8 |
| Species | Rat, Rattus norvegicus |
| Orthologies |
Protein Domains
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in rat Bad often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- 14-3-3 binding domain
- phospholipid binding
- lipid binding domain
- lipid binding
- protein kinase binding
- protein phosphatase binding
- alpha helix
- enzyme regulator activity
- caspase activator
- protein binding
- cleavage site
- protease activator
- Pro-apoptotic Bcl-2 protein, BAD
- phosphorylation site
- PEST domain
- BH3 binding domain
- protein phosphatase 2B binding
- Bcl-2 homology 1 domain
- Bcl-2 homology 2 domain
- Bcl-2 homology 3 domain
- serine phosphorylation site
- Pka phosphorylation site
Pathways
Biological processes and signaling networks where the Bad gene in rat plays a role, providing insight into its function and relevance in health or disease.
- 14-3-3-mediated Signaling
- Acute Myeloid Leukemia Signaling
- Angiopoietin Signaling
- Apoptosis Signaling
- Autophagy
- Ceramide Signaling
- DNA damage-induced 14-3-3σ Signaling
- Docosahexaenoic Acid (DHA) Signaling
- Endocannabinoid Cancer Inhibition Pathway
- Endometrial Cancer Signaling
- ErbB2-ErbB3 Signaling
- HER-2 Signaling in Breast Cancer
- IGF-1 Signaling
- IL-3 Signaling
- IL-7 Signaling Pathway
- Melanoma Signaling
- Molecular Mechanisms of Cancer
- Neuregulin Signaling
- Non-Small Cell Lung Cancer Signaling
- Prostate Cancer Signaling
- Protein Kinase A Signaling
- UVB-Induced MAPK Signaling
- VEGF Signaling
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- neoplasia
- seizures
- breast cancer
- hematological neoplasia
- cancer
- epithelial cancer
- amyotrophic lateral sclerosis
- HER2 negative hormone receptor negative breast cancer
- diabetes mellitus
- organismal death
role in cell
- activation in
- phosphorylation in
- proliferation
- cell death
- apoptosis
- quantity
- differentiation
- survival
- binding in
- cytotoxic reaction
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Cytoplasm
- nuclear fraction
- endoplasmic reticulum fraction
- membrane fraction
- mitochondrial fraction
- pH resistant lipid raft fraction
- Mitochondria
- cytosol
- mitochondrial membrane
- mitochondrial outer membrane
- cytosolic fraction
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Bad gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- extrinsic apoptotic signaling pathway
- pore complex assembly
- intrinsic apoptotic signaling pathway
- positive regulation of proteolysis
- extrinsic apoptotic signaling pathway in absence of ligand
- induction of apoptosis via death domain receptors
- glucose catabolic process
- positive regulation of mitochondrial membrane potential
- activation of cysteine-type endopeptidase activity
- cellular response to lipid
- type B pancreatic cell proliferation
- cytokine-mediated signaling pathway
- apoptotic process
- positive regulation of type B pancreatic cell development
- cellular response to hypoxia
- positive regulation of insulin secretion
- activation of cysteine-type endopeptidase activity involved in apoptotic process
- positive regulation of insulin secretion involved in cellular response to glucose stimulus
- positive regulation of epithelial cell proliferation
- cellular response to nicotine
- positive regulation of glucokinase activity
- positive regulation of release of cytochrome c from mitochondria
- DNA damage response, signal transduction resulting in induction of apoptosis
- regulation of mitochondrial membrane permeability
- positive regulation of B cell differentiation
- positive regulation of cysteine-type endopeptidase activity involved in apoptotic process
- ADP metabolic process
- positive regulation of autophagy
- cellular response to mechanical stimulus
- positive regulation of T cell differentiation
- ATP metabolic process
- glucose homeostasis
- positive regulation of apoptotic process
- release of cytochrome c from mitochondria
Cellular Component
Where in the cell the gene product is active
- mitochondrion
- BAD-BCL-2 complex
- cytosol
- mitochondrial outer membrane
Molecular Function
What the gene product does at the molecular level
- protein kinase binding
- protein binding
- protein phosphatase binding
- lipid binding
- phospholipid binding
- cysteine-type endopeptidase activator activity involved in apoptotic process