The Function of INS
Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Protein names
Recommended name:
Insulin [Cleaved into: Insulin B chain; Insulin A chain]- RS28933985 (INS) ??
- RS689 (INS) ??
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Top Gene-Substance Interactions
INS Interacts with These Diseases
| Disease | Score |
Substances That Increase INS
| Substances | Interaction | Organism | Category |
Substances That Decrease INS
| Substances | Interaction | Organism | Category |
Advanced Summary
permanent neonatal diabetes mellitus At least 10 mutations in the INS gene have been identified in people with permanent neonatal diabetes mellitus. Individuals with this condition often have a low birth weight and develop increased blood sugar (hyperglycemia) within the first 6 months of life. INS gene mutations that cause permanent neonatal diabetes mellitus change single protein building blocks (amino acids) in the protein sequence. These mutations are believed to disrupt the cleavage of the proinsulin chain or the binding of the A and B chains to form insulin, leading to impaired blood sugar control. type 1 diabetes Genetics Home Reference provides information about type 1 diabetes. other disorders Mutations in the INS gene can also cause other disorders involving insulin production and blood sugar control. Some individuals with INS gene mutations have increased levels of proinsulin in their blood (hyperproinsulinemia) and may also have impaired blood sugar control. INS gene mutations are also associated with a disorder called maturity-onset diabetes of the young (MODY). This term refers to hereditary forms of relatively mild diabetes mellitus caused by changes in single genes.
The INS gene provides instructions for producing the hormone insulin, which is necessary for the control of glucose levels in the blood. Glucose is a simple sugar and the primary energy source for most cells in the body. Insulin is produced in a precursor form called proinsulin, which consists of a single chain of protein building blocks (amino acids). The proinsulin chain is cut (cleaved) to form individual pieces called the A and B chains, which are joined together by connections called disulfide bonds to form insulin .
Conditions with Increased Gene Activity
| Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
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Conditions with Decreased Gene Activity
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Technical
The following transcription factors affect gene expression:
Gene Pathways:
- mTOR signaling pathway
- Regulation of autophagy
- Prostate cancer
- Progesterone-mediated oocyte maturation
- Aldosterone-regulated sodium reabsorption
- Regulation of actin cytoskeleton
- Oocyte meiosis
- Type I diabetes mellitus
- Type II diabetes mellitus
- Metabolism
- Disease
- Insulin signaling pathway
- Maturity onset diabetes of the young
- Metabolism of proteins
- Signal Transduction
Molecular Function:
- Protease Binding
- Insulin Receptor Binding
- Insulin-Like Growth Factor Receptor Binding
- Hormone Activity
- Identical Protein Binding
Biological Processes:
- Mapk Cascade
- Negative Regulation Of Acute Inflammatory Response
- Glucose Metabolic Process
- Regulation Of Transcription, Dna-Templated
- Regulation Of Cellular Amino Acid Metabolic Process
- Er To Golgi Vesicle-Mediated Transport
- Acute-Phase Response
- G-Protein Coupled Receptor Signaling Pathway
- Cell-Cell Signaling
- Positive Regulation Of Cell Proliferation
- Insulin Receptor Signaling Pathway
- Positive Regulation Of Gene Expression
- Positive Regulation Of Phosphatidylinositol 3-Kinase Signaling
- Glucose Transport
- Regulation Of Transmembrane Transporter Activity
- Positive Regulation Of Cell Growth
- Positive Regulation Of Cell Migration
- Positive Regulation Of Protein Autophosphorylation
- Activation Of Protein Kinase B Activity
- Positive Regulation Of Cellular Protein Metabolic Process
- Negative Regulation Of Protein Oligomerization
- Regulation Of Protein Localization
- Negative Regulation Of Nad(P)H Oxidase Activity
- Wound Healing
- Negative Regulation Of Protein Catabolic Process
- Glucose Homeostasis
- Positive Regulation Of Mapk Cascade
- Cellular Protein Metabolic Process
- Positive Regulation Of Nitric Oxide Biosynthetic Process
- Positive Regulation Of Cell Differentiation
- Negative Regulation Of Gluconeogenesis
- Positive Regulation Of Glycogen Biosynthetic Process
- Positive Regulation Of Dna Replication
- Negative Regulation Of Glycogen Catabolic Process
- Positive Regulation Of Glycolytic Process
- Positive Regulation Of Mitotic Nuclear Division
- Negative Regulation Of Proteolysis
- Negative Regulation Of Vasodilation
- Positive Regulation Of Vasodilation
- Negative Regulation Of Fatty Acid Metabolic Process
- Positive Regulation Of Glucose Import
- Positive Regulation Of Insulin Receptor Signaling Pathway
- Alpha-Beta T Cell Activation
- Positive Regulation Of Lipid Biosynthetic Process
- Regulation Of Protein Secretion
- Negative Regulation Of Protein Secretion
- Positive Regulation Of Cytokine Secretion
- Positive Regulation Of Peptidyl-Tyrosine Phosphorylation
- Negative Regulation Of Lipid Catabolic Process
- Positive Regulation Of Nitric-Oxide Synthase Activity
- Positive Regulation Of Nf-Kappab Transcription Factor Activity
- Positive Regulation Of Protein Kinase B Signaling
- Fatty Acid Homeostasis
- Negative Regulation Of Respiratory Burst Involved In Inflammatory Response
- Positive Regulation Of Respiratory Burst
- Positive Regulation Of Peptide Hormone Secretion
- Positive Regulation Of Brown Fat Cell Differentiation
- Positive Regulation Of Protein Localization To Nucleus
- Negative Regulation Of Oxidative Stress-Induced Intrinsic Apoptotic Signaling Pathway
- Negative Regulation Of Feeding Behavior