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Query author contributions in Reactome

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Details on Person UniProt:P01308 INS

Class:IdReferenceGeneProduct:57415
_chainChangeLogsignal peptide:1-24 added on Fri February 6 2015;peptide:25-54 added on Fri February 6 2015;propeptide:57-87 added on Fri February 6 2015;peptide:90-110 added on Fri February 6 2015
_displayNameUniProt:P01308 INS
_timestamp2026-02-20 21:40:34
chainsignal peptide:1-24
peptide:25-54
propeptide:57-87
peptide:90-110
checksumC2C3B23B85E520E5
commentFUNCTION 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.SUBUNIT Heterodimer of a B chain and an A chain linked by two disulfide bonds (PubMed:25423173).INTERACTION Expressed by pancreatic beta-cells (at protein level).DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.PHARMACEUTICAL 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.SIMILARITY Belongs to the insulin family.SEQUENCE CAUTION Protein of the 20th century - Issue 9 of April 2001ONLINE INFORMATION Insulin entry
descriptionrecommendedName: Insulin component recommendedName: Insulin B chain /component component recommendedName: Insulin A chain /component
geneNameINS
identifierP01308
isSequenceChangedFALSE
keyword3D-structure
Alternative splicing
Carbohydrate metabolism
Cleavage on pair of basic residues
Diabetes mellitus
Direct protein sequencing
Disease variant
Disulfide bond
Glucose metabolism
Hormone
Pharmaceutical
Proteomics identification
Reference proteome
Secreted
Signal
modified[InstanceEdit:9836292] Weiser, Joel, 2023-05-25
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
[InstanceEdit:9948485] Weiser, Joel, 2025-05-21
[InstanceEdit:9983091] Weiser, Joel, 2026-02-20
nameINS
referenceDatabase[ReferenceDatabase:2] UniProt
referenceGene[ReferenceDNASequence:8931794] ENSEMBL:ENSG00000254647 INS [Homo sapiens]
secondaryIdentifierINS_HUMAN
Q5EEX2
sequenceLength110
species[Species:48887] Homo sapiens
(isoformParent)[ReferenceIsoform:4341201] UniProt:F8WCM5-1 INS-IGF2 [Homo sapiens]
[ReferenceIsoform:8967023] UniProt:P01308-1 INS [Homo sapiens]
(referenceEntity)[EntityWithAccessionedSequence:74672] 4xHC-INS(90-110) [extracellular region] [Homo sapiens]
[EntityWithAccessionedSequence:74673] 2xHC-INS(25-54) [extracellular region] [Homo sapiens]
[EntityWithAccessionedSequence:141720] INS(90-110) [endosome lumen] [Homo sapiens]
[EntityWithAccessionedSequence:141723] INS(25-54) [endosome lumen] [Homo sapiens]
[EntityWithAccessionedSequence:264890] 6xHC-INS(25-110) [Golgi lumen] [Homo sapiens]
[EntityWithAccessionedSequence:264893] INS(25-110) [endoplasmic reticulum lumen] [Homo sapiens]
[EntityWithAccessionedSequence:264902] 2xHC-INS(25-54) [secretory granule lumen] [Homo sapiens]
[EntityWithAccessionedSequence:264959] INS(1-710) [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:264971] 4xHC-INS(90-110) [secretory granule lumen] [Homo sapiens]
[EntityWithAccessionedSequence:264984] 6xHC-INS(25-110) [secretory granule lumen] [Homo sapiens]
List all 27 refering instances
(referenceSequence)[IntraChainCrosslinkedResidue:264874] Intra-chain Crosslink via L-cystine (cross-link) at 109 and 43
[IntraChainCrosslinkedResidue:264928] Intra-chain Crosslink via L-cystine (cross-link) at 95 and 100
[IntraChainCrosslinkedResidue:264936] Intra-chain Crosslink via L-cystine (cross-link) at 96 and 31
[IntraChainCrosslinkedResidue:265017] Intra-chain Crosslink via L-cystine (cross-link) at 43 and 109
[IntraChainCrosslinkedResidue:265035] Intra-chain Crosslink via L-cystine (cross-link) at 100 and 95
[IntraChainCrosslinkedResidue:265094] Intra-chain Crosslink via L-cystine (cross-link) at 31 and 96
[ReplacedResidue:429344] L-lysine 53 replaced with L-proline
[ReplacedResidue:429361] L-proline 52 replaced with L-aspartic acid
[ReplacedResidue:429362] L-asparagine 110 replaced with glycine
[ReplacedResidue:429374] L-proline 52 replaced with L-lysine
List all 18 refering instances
(secondReferenceSequence)[InterChainCrosslinkedResidue:9023152] Inter-chain Crosslink via L-cystine (cross-link) at 43 and 109
[InterChainCrosslinkedResidue:9023170] Inter-chain Crosslink via L-cystine (cross-link) at 96 and 31
[InterChainCrosslinkedResidue:9023187] Inter-chain Crosslink via L-cystine (cross-link) at 31 and 96
[InterChainCrosslinkedResidue:9023205] Inter-chain Crosslink via L-cystine (cross-link) at 109 and 43
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No pathways have been reviewed or authored by UniProt:P01308 INS (57415)