| D007328 |
Insulin |
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1). |
Iletin,Insulin A Chain,Insulin B Chain,Insulin, Regular,Novolin,Sodium Insulin,Soluble Insulin,Chain, Insulin B,Insulin, Sodium,Insulin, Soluble,Regular Insulin |
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| D007333 |
Insulin Resistance |
Diminished effectiveness of INSULIN in lowering blood sugar levels: requiring the use of 200 units or more of insulin per day to prevent HYPERGLYCEMIA or KETOSIS. |
Insulin Sensitivity,Resistance, Insulin,Sensitivity, Insulin |
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| D008969 |
Molecular Sequence Data |
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. |
Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular |
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| D010750 |
Phosphoproteins |
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Phosphoprotein |
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| D003924 |
Diabetes Mellitus, Type 2 |
A subclass of DIABETES MELLITUS that is not INSULIN-responsive or dependent (NIDDM). It is characterized initially by INSULIN RESISTANCE and HYPERINSULINEMIA; and eventually by GLUCOSE INTOLERANCE; HYPERGLYCEMIA; and overt diabetes. Type II diabetes mellitus is no longer considered a disease exclusively found in adults. Patients seldom develop KETOSIS but often exhibit OBESITY. |
Diabetes Mellitus, Adult-Onset,Diabetes Mellitus, Ketosis-Resistant,Diabetes Mellitus, Maturity-Onset,Diabetes Mellitus, Non-Insulin-Dependent,Diabetes Mellitus, Slow-Onset,Diabetes Mellitus, Stable,MODY,Maturity-Onset Diabetes Mellitus,NIDDM,Diabetes Mellitus, Non Insulin Dependent,Diabetes Mellitus, Noninsulin Dependent,Diabetes Mellitus, Noninsulin-Dependent,Diabetes Mellitus, Type II,Maturity-Onset Diabetes,Noninsulin-Dependent Diabetes Mellitus,Type 2 Diabetes,Type 2 Diabetes Mellitus,Adult-Onset Diabetes Mellitus,Diabetes Mellitus, Adult Onset,Diabetes Mellitus, Ketosis Resistant,Diabetes Mellitus, Maturity Onset,Diabetes Mellitus, Slow Onset,Diabetes, Maturity-Onset,Diabetes, Type 2,Ketosis-Resistant Diabetes Mellitus,Maturity Onset Diabetes,Maturity Onset Diabetes Mellitus,Non-Insulin-Dependent Diabetes Mellitus,Noninsulin Dependent Diabetes Mellitus,Slow-Onset Diabetes Mellitus,Stable Diabetes Mellitus |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D000595 |
Amino Acid Sequence |
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. |
Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein |
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| D000818 |
Animals |
Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. |
Animal,Metazoa,Animalia |
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| D016283 |
Proto-Oncogene Proteins p21(ras) |
Cellular proteins encoded by the H-ras, K-ras and N-ras genes. The proteins have GTPase activity and are involved in signal transduction as monomeric GTP-binding proteins. Elevated levels of p21 c-ras have been associated with neoplasia. This enzyme was formerly listed as EC 3.6.1.47. |
Proto-Oncogene Proteins c-ras,c-Ha-ras p21,c-Ki-ras p21,p21(N-ras),p21(c-Ha-ras),p21(c-Ki-ras),p21(c-ras),p21(ras),ras Proto-Oncogene Protein p21,Proto-Oncogene Protein p21(c-Ha-ras),Proto-Oncogene Protein p21(c-Ki-ras),Proto-Oncogene Protein p21(c-N-ras),Proto-Oncogene Protein p21(ras),Proto-Oncogene Protein ras,c-ras Proteins,p21 c-H-ras,p21 c-Ha-ras,p21 c-K-ras,p21 c-Ki-ras,p21 c-ras,ras Proto-Oncogene Product p21,Proteins c-ras, Proto-Oncogene,Proto Oncogene Protein ras,Proto Oncogene Proteins c ras,c Ha ras p21,c Ki ras p21,c ras Proteins,c-H-ras, p21,c-Ha-ras, p21,c-K-ras, p21,c-Ki-ras, p21,c-ras, Proto-Oncogene Proteins,c-ras, p21,p21 c H ras,p21 c Ha ras,p21 c K ras,p21 c Ki ras,p21 c ras,p21, c-Ha-ras,p21, c-Ki-ras,ras Proto Oncogene Product p21,ras Proto Oncogene Protein p21,ras, Proto-Oncogene Protein |
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| D055504 |
Insulin Receptor Substrate Proteins |
A structurally-related group of signaling proteins that are phosphorylated by the INSULIN RECEPTOR PROTEIN-TYROSINE KINASE. The proteins share an N-terminal PLECKSTRIN HOMOLOGY DOMAIN, a phosphotyrosine-binding domain that interacts with the phosphorylated INSULIN RECEPTOR, and a C-terminal TYROSINE-rich domain. Upon tyrosine phosphorylation, insulin receptor substrate proteins interact with specific SH2 DOMAIN containing proteins that are involved in insulin receptor signaling. |
IRS Signaling Adaptor Proteins,Insulin Receptor Substrate-1,Insulin Receptor Substrate-1 Protein,Insulin Receptor Substrate-2,Insulin Receptor Substrate-2 Protein,Insulin Receptor Substrate-3,Insulin Receptor Substrate-3 Protein,Insulin Receptor Substrate-4,Insulin Receptor Substrate-4 Protein,Insulin Receptor Substrate 1,Insulin Receptor Substrate 1 Protein,Insulin Receptor Substrate 2,Insulin Receptor Substrate 2 Protein,Insulin Receptor Substrate 3,Insulin Receptor Substrate 3 Protein,Insulin Receptor Substrate 4,Insulin Receptor Substrate 4 Protein |
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