Sequence of the human insulin gene.

P01308 Q5EEX2 INS_HUMAN Insulin Insulin B chain Insulin A chain INS Homo sapiens Human Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Haplorrhini Catarrhini Hominidae Homo Sequence of the human insulin gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Genetic variation in the human insulin gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Nucleotide sequence of a cDNA clone encoding human preproinsulin. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Nucleotide sequence of human preproinsulin complementary DNA. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Susceptibility to insulin dependent diabetes mellitus maps to a 4.1 kb segment of DNA spanning the insulin gene and associated VNTR. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Insulinomas and expression of an insulin splice variant. NUCLEOTIDE SEQUENCE [MRNA] Global haplotype diversity in the human insulin gene region. NUCLEOTIDE SEQUENCE [GENOMIC DNA] Cloning of human full-length CDSs in BD Creator(TM) system donor vector. NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Pancreas Description of a novel RFLP diallelic polymorphism (-127 BsgI C/G) within the 5' region of insulin gene. NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59 Blood Amino-acid sequence of human insulin. PROTEIN SEQUENCE OF 25-54 AND 90-110 Studies on human proinsulin. Isolation and amino acid sequence of the human pancreatic C-peptide. PROTEIN SEQUENCE OF 57-87 The amino acid sequence of the C-peptide of human proinsulin. PROTEIN SEQUENCE OF 57-87 Total synthesis of human insulin under directed formation of the disulfide bonds. SYNTHESIS Studies on polypeptides, IV. The synthesis of C-peptide of human proinsulin. SYNTHESIS OF 57-87 Synthesis of peptides with the properties of human proinsulin C peptides (hC peptide). 3. Synthesis of the sequences 14-17 and 9-13 of human proinsulin C peptides. SYNTHESIS OF 65-69 AND 70-73 Synthesis of peptides with the properties of human proinsulin C peptides (hC peptide). I. Scheme for the synthesis and preparation of the sequence 28-31 of human proinsulin C peptide. SYNTHESIS OF 84-87 Studies on mutant human insulin genes: identification and sequence analysis of a gene encoding [SerB24]insulin. VARIANT HPRI SER-48 Identification of a mutant human insulin predicted to contain a serine-for-phenylalanine substitution. VARIANT HPRI SER-48 VARIANT LEU-49 A mutation in the B chain coding region is associated with impaired proinsulin conversion in a family with hyperproinsulinemia. VARIANT HPRI ASP-34 Structurally abnormal insulin in a diabetic patient. Characterization of the mutant insulin A3 (Val-->Leu) isolated from the pancreas. VARIANT WAKAYAMA LEU-92 Two unrelated patients with familial hyperproinsulinemia due to a mutation substituting histidine for arginine at position 65 in the proinsulin molecule: identification of the mutation by direct sequencing of genomic deoxyribonucleic acid amplified by polymerase chain reaction. VARIANT HPRI HIS-89 Posttranslational cleavage of proinsulin is blocked by a point mutation in familial hyperproinsulinemia. VARIANT HPRI HIS-89 A novel point mutation in the human insulin gene giving rise to hyperproinsulinemia (proinsulin Kyoto). VARIANT HPRI LEU-89 Toward the solution structure of human insulin: sequential 2D 1H NMR assignment of a des-pentapeptide analogue and comparison with crystal structure. STRUCTURE BY NMR Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition. STRUCTURE BY NMR Two-dimensional NMR studies of Des-(B26-B30)-insulin: sequence-specific resonance assignments and effects of solvent composition. STRUCTURE BY NMR Three-dimensional solution structure of an insulin dimer. A study of the B9(Asp) mutant of human insulin using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. STRUCTURE BY NMR OF 90-110 AND 25-54 DISULFIDE BONDS Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus. STRUCTURE BY NMR OF 90-110 AND 25-54 OF VARIANT HPRI SER-48 DISULFIDE BONDS Solution structures of the R6 human insulin hexamer. STRUCTURE BY NMR OF 90-110 AND 25-54 DISULFIDE BONDS Insulin gene mutations as a cause of permanent neonatal diabetes. VARIANTS PNDM4 ASP-24; ARG-32; SER-32; GLY-43; VAL-47; CYS-48; CYS-89; CYS-90; TYR-96 AND CYS-108 Insulin mutation screening in 1,044 patients with diabetes: mutations in the INS gene are a common cause of neonatal diabetes but a rare cause of diabetes diagnosed in childhood or adulthood. VARIANTS PNDM4 ASP-24; ASP-29; ARG-32; SER-32; PRO-35; GLY-43; VAL-47; CYS-48; ARG-84; CYS-89; CYS-90; SER-96; TYR-96; CYS-101; CYS-103 AND CYS-108 VARIANT MODY10 CYS-6 VARIANT MET-68 Mutations in the insulin gene can cause MODY and autoantibody-negative type 1 diabetes. VARIANT MODY10 GLN-46 VARIANT T1D2 CYS-55 Further evidence that mutations in INS can be a rare cause of Maturity-Onset Diabetes of the Young (MODY). VARIANTS MODY10 HIS-6 AND GLN-46 Structural and functional study of the GlnB22-insulin mutant responsible for maturity-onset diabetes of the young. VARIANT MODY10 GLN-46 CHARACTERIZATION OF VARIANT MODY10 GLN-46 STRUCTURE BY NMR OF 90-110 AND 25-54 DISULFIDE BONDS OF VARIANT MODY10 GLN-46 SUBUNIT 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. Heterodimer of a B chain and an A chain linked by two disulfide bonds (PubMed:25423173). P01308 Q6UY14-3 ADAMTSL4 false 3 P01308 A8MQ03 CYSRT1 false 3 P01308 P14735-1 IDE false 3 P01308 P01308 INS false 19 P01308 P06213-2 INSR false 6 P01308 Q07627 KRTAP1-1 false 3 P01308 Q8IUG1 KRTAP1-3 false 3 P01308 P0DPK4 NOTCH2NLC false 3 PRO_0000015820 P11142 HSPA8 false 2 Secreted P01308-1 1 F8WCM5-1 2 INS-IGF2 Hyperproinsulinemia HPRI An autosomal dominant condition characterized by elevated levels of serum proinsulin-like material. The disease is caused by variants affecting the gene represented in this entry. Type 1 diabetes mellitus 2 T1D2 A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. The disease is caused by variants affecting the gene represented in this entry. Diabetes mellitus, permanent neonatal, 4 PNDM4 A form of permanent neonatal diabetes mellitus, a type of diabetes characterized by onset of persistent hyperglycemia within the first six months of life. Initial clinical manifestations include intrauterine growth retardation, hyperglycemia, glycosuria, osmotic polyuria, severe dehydration, and failure to thrive. PNDM4 transmission pattern is consistent with autosomal dominant or autosomal recessive inheritance. The disease is caused by variants affecting the gene represented in this entry. Maturity-onset diabetes of the young 10 MODY10 A form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease. The disease is caused by variants affecting the gene represented in this entry. Available under the names Humulin or Humalog (Eli Lilly) and Novolin (Novo Nordisk). Used in the treatment of diabetes. Humalog is an insulin analog with 52-Lys-Pro-53 instead of 52-Pro-Lys-53. Belongs to the insulin family. Clinical information on Eli Lilly insulin products Protein of the 20th century - Issue 9 of April 2001 Insulin entry Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License