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Protein

Insulin

Gene

INS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. hormone activity Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. insulin-like growth factor receptor binding Source: BHF-UCL
  4. insulin receptor binding Source: UniProtKB
  5. protease binding Source: UniProtKB

GO - Biological processi

  1. activation of protein kinase B activity Source: BHF-UCL
  2. acute-phase response Source: BHF-UCL
  3. alpha-beta T cell activation Source: UniProtKB
  4. cell-cell signaling Source: UniProtKB
  5. cellular protein metabolic process Source: Reactome
  6. endocrine pancreas development Source: Reactome
  7. energy reserve metabolic process Source: Reactome
  8. fatty acid homeostasis Source: BHF-UCL
  9. glucose homeostasis Source: BHF-UCL
  10. glucose metabolic process Source: UniProtKB-KW
  11. glucose transport Source: UniProtKB
  12. G-protein coupled receptor signaling pathway Source: BHF-UCL
  13. insulin receptor signaling pathway Source: BHF-UCL
  14. MAPK cascade Source: BHF-UCL
  15. negative regulation of acute inflammatory response Source: BHF-UCL
  16. negative regulation of fatty acid metabolic process Source: BHF-UCL
  17. negative regulation of feeding behavior Source: DFLAT
  18. negative regulation of gluconeogenesis Source: BHF-UCL
  19. negative regulation of glycogen catabolic process Source: BHF-UCL
  20. negative regulation of lipid catabolic process Source: AgBase
  21. negative regulation of NAD(P)H oxidase activity Source: BHF-UCL
  22. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  23. negative regulation of protein catabolic process Source: UniProtKB
  24. negative regulation of protein oligomerization Source: UniProtKB
  25. negative regulation of protein secretion Source: BHF-UCL
  26. negative regulation of proteolysis Source: BHF-UCL
  27. negative regulation of respiratory burst involved in inflammatory response Source: BHF-UCL
  28. negative regulation of vasodilation Source: UniProtKB
  29. positive regulation of brown fat cell differentiation Source: BHF-UCL
  30. positive regulation of cell differentiation Source: BHF-UCL
  31. positive regulation of cell growth Source: BHF-UCL
  32. positive regulation of cell migration Source: BHF-UCL
  33. positive regulation of cell proliferation Source: BHF-UCL
  34. positive regulation of cellular protein metabolic process Source: BHF-UCL
  35. positive regulation of cytokine secretion Source: UniProtKB
  36. positive regulation of DNA replication Source: BHF-UCL
  37. positive regulation of glucose import Source: BHF-UCL
  38. positive regulation of glycogen biosynthetic process Source: BHF-UCL
  39. positive regulation of glycolytic process Source: BHF-UCL
  40. positive regulation of insulin receptor signaling pathway Source: BHF-UCL
  41. positive regulation of lipid biosynthetic process Source: BHF-UCL
  42. positive regulation of MAPK cascade Source: BHF-UCL
  43. positive regulation of mitotic nuclear division Source: UniProtKB
  44. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  45. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  46. positive regulation of nitric-oxide synthase activity Source: UniProtKB
  47. positive regulation of peptide hormone secretion Source: BHF-UCL
  48. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  49. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  50. positive regulation of protein autophosphorylation Source: BHF-UCL
  51. positive regulation of protein kinase B signaling Source: BHF-UCL
  52. positive regulation of protein localization to nucleus Source: BHF-UCL
  53. positive regulation of respiratory burst Source: BHF-UCL
  54. positive regulation of vasodilation Source: UniProtKB
  55. regulation of cellular amino acid metabolic process Source: BHF-UCL
  56. regulation of insulin secretion Source: Reactome
  57. regulation of protein localization Source: BHF-UCL
  58. regulation of protein secretion Source: UniProtKB
  59. regulation of transcription, DNA-templated Source: BHF-UCL
  60. regulation of transmembrane transporter activity Source: BHF-UCL
  61. small molecule metabolic process Source: Reactome
  62. wound healing Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16190.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_13819. Regulation of gene expression in beta cells.
REACT_15550. Insulin processing.
REACT_1661. SHC activation.
REACT_18325. Regulation of insulin secretion.
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
REACT_498. Signaling by Insulin receptor.
REACT_508. Signal attenuation.
REACT_570. IRS activation.
SignaLinkiP01308.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin
Cleaved into the following 2 chains:
Gene namesi
Name:INS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:6081. INS.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. endosome lumen Source: Reactome
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: BHF-UCL
  5. Golgi lumen Source: Reactome
  6. secretory granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Hyperproinsulinemia, familial (FHPRI)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant condition characterized by elevated levels of serum proinsulin-like material.

See also OMIM:176730
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341H → D in FHPRI; Providence. 1 Publication
VAR_003971
Natural varianti89 – 891R → H in FHPRI; impairs posttranslational cleavage. 2 Publications
Corresponds to variant rs28933985 [ dbSNP | Ensembl ].
VAR_003974
Natural varianti89 – 891R → L in FHPRI; Kyoto. 1 Publication
VAR_003975
Diabetes mellitus, insulin-dependent, 2 (IDDM2)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:125852
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551R → C in IDDM2. 1 Publication
Corresponds to variant rs121908261 [ dbSNP | Ensembl ].
VAR_063732
Diabetes mellitus, permanent neonatal (PNDM)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare form of diabetes distinct from childhood-onset autoimmune diabetes mellitus type 1. It is characterized by insulin-requiring hyperglycemia that is diagnosed within the first months of life. Permanent neonatal diabetes requires lifelong therapy.

See also OMIM:606176
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241A → D in PNDM. 2 Publications
Corresponds to variant rs80356663 [ dbSNP | Ensembl ].
VAR_063723
Natural varianti29 – 291H → D in PNDM. 1 Publication
Corresponds to variant rs121908272 [ dbSNP | Ensembl ].
VAR_063724
Natural varianti32 – 321G → R in PNDM. 2 Publications
Corresponds to variant rs80356664 [ dbSNP | Ensembl ].
VAR_063725
Natural varianti32 – 321G → S in PNDM. 2 Publications
Corresponds to variant rs80356664 [ dbSNP | Ensembl ].
VAR_063726
Natural varianti35 – 351L → P in PNDM. 1 Publication
Corresponds to variant rs121908273 [ dbSNP | Ensembl ].
VAR_063727
Natural varianti43 – 431C → G in PNDM. 2 Publications
Corresponds to variant rs80356666 [ dbSNP | Ensembl ].
VAR_063728
Natural varianti47 – 471G → V in PNDM. 2 Publications
Corresponds to variant rs80356667 [ dbSNP | Ensembl ].
VAR_063730
Natural varianti48 – 481F → C in PNDM. 2 Publications
Corresponds to variant rs80356668 [ dbSNP | Ensembl ].
VAR_063731
Natural varianti84 – 841G → R in PNDM; uncertain pathological significance. 1 Publication
Corresponds to variant rs121908274 [ dbSNP | Ensembl ].
VAR_063734
Natural varianti89 – 891R → C in PNDM. 2 Publications
Corresponds to variant rs80356669 [ dbSNP | Ensembl ].
VAR_063735
Natural varianti90 – 901G → C in PNDM. 2 Publications
Corresponds to variant rs80356670 [ dbSNP | Ensembl ].
VAR_063736
Natural varianti96 – 961C → S in PNDM. 1 Publication
Corresponds to variant rs80356671 [ dbSNP | Ensembl ].
VAR_063737
Natural varianti96 – 961C → Y in PNDM. 2 Publications
Corresponds to variant rs80356671 [ dbSNP | Ensembl ].
VAR_063738
Natural varianti101 – 1011S → C in PNDM. 1 Publication
Corresponds to variant rs121908276 [ dbSNP | Ensembl ].
VAR_063739
Natural varianti103 – 1031Y → C in PNDM. 1 Publication
Corresponds to variant rs121908277 [ dbSNP | Ensembl ].
VAR_063740
Natural varianti108 – 1081Y → C in PNDM. 2 Publications
Corresponds to variant rs80356672 [ dbSNP | Ensembl ].
VAR_063741
Maturity-onset diabetes of the young 10 (MODY10)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613370
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61R → C in MODY10. 1 Publication
Corresponds to variant rs121908278 [ dbSNP | Ensembl ].
VAR_063721
Natural varianti6 – 61R → H in MODY10. 1 Publication
Corresponds to variant rs121908259 [ dbSNP | Ensembl ].
VAR_063722
Natural varianti46 – 461R → Q in MODY10. 2 Publications
Corresponds to variant rs121908260 [ dbSNP | Ensembl ].
VAR_063729

Pharmaceutical usei

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.

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

MIMi125852. phenotype.
176730. gene+phenotype.
606176. phenotype.
613370. phenotype.
Orphaneti552. MODY.
99885. Permanent neonatal diabetes mellitus.
PharmGKBiPA201.

Protein family/group databases

Allergomei2121. Hom s Insulin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Peptidei25 – 5430Insulin B chainPRO_0000015819Add
BLAST
Propeptidei57 – 8731C peptidePRO_0000015820Add
BLAST
Peptidei90 – 11021Insulin A chainPRO_0000015821Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 96Interchain (between B and A chains)
Disulfide bondi43 ↔ 109Interchain (between B and A chains)
Disulfide bondi95 ↔ 1001 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiP01308.
PeptideAtlasiP01308.
PRIDEiP01308.

PTM databases

PhosphoSiteiP01308.

Miscellaneous databases

PMAP-CutDBP01308.

Expressioni

Gene expression databases

BgeeiP01308.
ExpressionAtlasiP01308. baseline.
GenevestigatoriP01308.

Organism-specific databases

HPAiCAB000048.
CAB012098.
CAB053843.
HPA004932.

Interactioni

Subunit structurei

Heterodimer of a B chain and an A chain linked by two disulfide bonds.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself16EBI-7090529,EBI-7090529

Protein-protein interaction databases

BioGridi109842. 12 interactions.
DIPiDIP-6024N.
IntActiP01308. 3 interactions.
MINTiMINT-106847.
STRINGi9606.ENSP00000348986.

Structurei

Secondary structure

1
110
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 294Combined sources
Helixi33 – 4311Combined sources
Helixi44 – 463Combined sources
Beta strandi48 – 503Combined sources
Turni59 – 668Combined sources
Beta strandi74 – 763Combined sources
Helixi79 – 813Combined sources
Turni84 – 863Combined sources
Helixi91 – 977Combined sources
Beta strandi98 – 1014Combined sources
Helixi102 – 1065Combined sources
Turni107 – 1093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7FNMR-A90-110[»]
B25-53[»]
1AI0NMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1B9EX-ray2.50A/C90-110[»]
B/D25-54[»]
1BENX-ray1.40A/C90-110[»]
B/D25-54[»]
1EFENMR-A25-54[»]
A90-110[»]
1EV3X-ray1.78A/C90-110[»]
B/D25-54[»]
1EV6X-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1EVRX-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1FU2X-ray3.24A/C/E/G90-110[»]
B/D/F/H25-54[»]
1FUBX-ray3.09A/C90-110[»]
B/D25-54[»]
1G7AX-ray1.20A/C/E/G90-110[»]
B/D/F/H25-54[»]
1G7BX-ray1.30A/C/E/G90-110[»]
B/D/F/H25-54[»]
1GUJX-ray1.62A/C90-110[»]
B/D25-54[»]
1HIQNMR-A90-110[»]
B25-54[»]
1HISNMR-A90-110[»]
B25-49[»]
1HITNMR-A90-110[»]
B25-54[»]
1HLSNMR-A90-110[»]
B25-54[»]
1HTVX-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-51[»]
1HUINMR-A90-110[»]
B26-53[»]
1IOGNMR-A90-110[»]
B25-53[»]
1IOHNMR-A90-110[»]
B25-53[»]
1J73X-ray2.00A/C90-110[»]
B/D25-54[»]
1JCAX-ray2.50A/C90-110[»]
B/D25-54[»]
1JCONMR-A90-110[»]
B25-54[»]
1JK8X-ray2.40C35-47[»]
1K3MNMR-A90-110[»]
B25-54[»]
1KMFNMR-A90-110[»]
B25-54[»]
1LKQNMR-A90-110[»]
B25-54[»]
1LPHX-ray2.30A/C90-110[»]
B/D25-54[»]
1MHINMR-A90-110[»]
B25-54[»]
1MHJNMR-A90-110[»]
B25-54[»]
1MSOX-ray1.00A/C90-110[»]
B/D25-54[»]
1OS3X-ray1.95A/C90-110[»]
B/D25-54[»]
1OS4X-ray2.25A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1Q4VX-ray2.00A/C90-110[»]
B/D25-54[»]
1QIYX-ray2.30A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1QIZX-ray2.00A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1QJ0X-ray2.40A/C90-110[»]
B/D25-54[»]
1RWEX-ray1.80A/C90-110[»]
B/D25-54[»]
1SF1NMR-A90-110[»]
B25-54[»]
1SJTNMR-A90-110[»]
B25-51[»]
1SJUNMR-A25-110[»]
1T0CNMR-A57-87[»]
1T1KNMR-A90-110[»]
B25-54[»]
1T1PNMR-A90-110[»]
B25-54[»]
1T1QNMR-A90-110[»]
B25-54[»]
1TRZX-ray1.60A/C90-110[»]
B/D25-54[»]
1TYLX-ray1.90A/C90-110[»]
B/D25-54[»]
1TYMX-ray1.90A/C90-110[»]
B/D25-54[»]
1UZ9X-ray1.60A90-110[»]
B25-53[»]
1VKTNMR-A90-110[»]
B25-54[»]
1W8PX-ray2.08A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1XDAX-ray1.80A/C/E/G90-110[»]
B/D/F/H25-53[»]
1XGLNMR-A90-110[»]
B25-54[»]
1XW7X-ray2.30A/C90-110[»]
B/D25-54[»]
1ZEGX-ray1.60A/C90-110[»]
B/D25-54[»]
1ZEHX-ray1.50A/C90-110[»]
B/D25-54[»]
1ZNJX-ray2.00A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2C8QX-ray1.95A90-110[»]
B25-53[»]
2C8RX-ray1.50A90-110[»]
B25-53[»]
2CEUX-ray1.80A/C90-110[»]
B/D25-49[»]
2G54X-ray2.25C/D25-54[»]
2G56X-ray2.20C/D25-54[»]
2H67NMR-A90-110[»]
B25-54[»]
2HH4NMR-A90-110[»]
B25-54[»]
2HHONMR-A90-110[»]
B25-54[»]
2HIUNMR-A90-110[»]
B25-54[»]
2JMNNMR-A90-110[»]
B25-54[»]
2JUMNMR-A90-110[»]
B25-54[»]
2JUUNMR-A90-110[»]
B25-54[»]
2JUVNMR-A90-110[»]
B25-54[»]
2JV1NMR-A90-110[»]
B25-54[»]
2JZQNMR-A25-54[»]
A90-110[»]
2K91NMR-A90-110[»]
B25-54[»]
2K9RNMR-A90-110[»]
B25-54[»]
2KJJNMR-A90-110[»]
B25-54[»]
2KJUNMR-A90-110[»]
B25-54[»]
2KQPNMR-A25-110[»]
2KQQNMR-A90-110[»]
B25-54[»]
2KXKNMR-A90-110[»]
B25-54[»]
2L1YNMR-A90-110[»]
B25-54[»]
2L1ZNMR-A90-110[»]
B25-54[»]
2LGBNMR-A90-110[»]
B25-55[»]
2LWZNMR-A25-54[»]
A89-110[»]
2M1DNMR-A90-110[»]
B25-54[»]
2M1ENMR-A90-110[»]
B25-54[»]
2M2MNMR-A90-110[»]
B25-54[»]
2M2NNMR-A90-110[»]
B25-54[»]
2M2ONMR-A90-110[»]
B25-54[»]
2M2PNMR-A90-110[»]
B25-54[»]
2MLINMR-A90-110[»]
B25-54[»]
2MPGNMR-A90-110[»]
B25-54[»]
2MPINMR-A90-110[»]
B25-54[»]
2MVCNMR-A90-110[»]
B25-54[»]
2MVDNMR-A90-110[»]
B25-54[»]
2OLYX-ray1.70A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2OLZX-ray1.70A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2OM0X-ray2.051/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k90-110[»]
2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l25-54[»]
2OM1X-ray1.971/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k90-110[»]
2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l25-54[»]
2OMGX-ray1.52A/C/E90-110[»]
B/D/F25-54[»]
2OMHX-ray1.36A/C/E90-110[»]
B/D/F25-54[»]
2OMIX-ray2.24A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2OMQX-ray2.00A/B/C/D36-41[»]
2QIUX-ray2.00A/C89-110[»]
B/D25-54[»]
2R34X-ray2.25A/C89-110[»]
B/D25-54[»]
2R35X-ray2.08A/C89-110[»]
B/D25-54[»]
2R36X-ray2.00A/C89-110[»]
B/D25-54[»]
2RN5NMR-A90-110[»]
B25-54[»]
2VJZX-ray1.80A/C90-110[»]
B/D25-54[»]
2VK0X-ray2.20A/C90-110[»]
B/D25-54[»]
2W44X-ray2.00A/C/E94-110[»]
B/D/F25-53[»]
2WBYX-ray2.60C/E90-109[»]
D/F25-43[»]
2WC0X-ray2.80C/E90-110[»]
D/F25-54[»]
2WRUX-ray1.57A90-110[»]
B25-50[»]
2WRVX-ray2.15A90-110[»]
B25-50[»]
2WRWX-ray2.41A90-110[»]
B25-50[»]
2WRXX-ray1.50A/C90-110[»]
B/D25-54[»]
2WS0X-ray2.10A90-110[»]
B25-54[»]
2WS1X-ray1.60A90-110[»]
B25-54[»]
2WS4X-ray1.90A90-110[»]
B25-50[»]
2WS6X-ray1.50A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2WS7X-ray2.59A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-50[»]
3AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3BXQX-ray1.30A/C90-110[»]
B/D25-54[»]
3E7YX-ray1.60A/C90-110[»]
B/D25-53[»]
3E7ZX-ray1.70A/C90-110[»]
B/D25-53[»]
3EXXX-ray1.35A/C90-110[»]
B/D25-54[»]
3FQ9X-ray1.35A/C91-110[»]
B/D25-54[»]
3HYDX-ray1.00A35-41[»]
3I3ZX-ray1.60A90-110[»]
B25-54[»]
3I40X-ray1.85A90-110[»]
B25-54[»]
3ILGX-ray1.90A/C90-110[»]
B/D25-54[»]
3INCX-ray1.85A/C90-110[»]
B/D25-54[»]
3IR0X-ray2.20A/C/E/G/I/K/M/O/R/T/V/X90-110[»]
B/D/F/H/J/L/N/P/S/U/W/Y25-54[»]
3JSDX-ray2.50A/C90-110[»]
B/D25-54[»]
3KQ6X-ray1.90A/C90-110[»]
B/D25-54[»]
3P2XX-ray2.00A/C90-110[»]
B/D25-54[»]
3P33X-ray2.30A/C/E/G90-110[»]
B/D/F/H25-54[»]
3Q6EX-ray2.05A/C90-110[»]
B/D25-54[»]
3ROVX-ray2.30A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3TT8X-ray1.12A/C90-110[»]
B/D25-54[»]
3U4NX-ray1.98A90-110[»]
B25-53[»]
3UTQX-ray1.67C15-24[»]
3UTSX-ray2.71C/H15-24[»]
3UTTX-ray2.60C/H15-24[»]
3V19X-ray2.00A/C90-110[»]
B/D25-54[»]
3V1GX-ray2.20A/C90-110[»]
B/D25-54[»]
3W11X-ray3.90A90-110[»]
B25-54[»]
3W12X-ray4.30A90-110[»]
B25-50[»]
3W13X-ray4.30A90-110[»]
B25-50[»]
3W7YX-ray0.92A/C90-110[»]
B/D25-54[»]
3W7ZX-ray1.15A/C90-110[»]
B/D25-54[»]
3W80X-ray1.40A/C/E/G90-110[»]
B/D/F/H25-54[»]
3ZI3X-ray1.70A90-110[»]
B25-54[»]
3ZQRX-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3ZS2X-ray1.97A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3ZU1X-ray1.60A/C90-110[»]
B/D25-54[»]
4AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
4AJXX-ray1.20A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-53[»]
4AJZX-ray1.80A/C90-110[»]
B/D25-53[»]
4AK0X-ray2.28A90-110[»]
B25-53[»]
4AKJX-ray2.01A/C90-110[»]
B/D25-53[»]
4CXLX-ray1.50A90-110[»]
B25-54[»]
4CXNX-ray1.70A90-110[»]
B25-54[»]
4CY7X-ray1.40A/C90-110[»]
B/D25-54[»]
4EFXX-ray1.98A/C90-110[»]
B/D25-52[»]
4EWWX-ray2.30A/C90-110[»]
B/D25-54[»]
4EWXX-ray2.20A/C90-110[»]
B/D25-54[»]
4EWZX-ray1.79A/C90-110[»]
B/D25-54[»]
4EX0X-ray1.86A/C90-110[»]
B/D25-54[»]
4EX1X-ray1.66A/C90-110[»]
B/D25-54[»]
4EXXX-ray1.55A/C90-110[»]
B/D25-54[»]
4EY1X-ray1.47A/C90-110[»]
B/D25-54[»]
4EY9X-ray1.47A/C90-110[»]
B/D25-54[»]
4EYDX-ray1.47A/C90-110[»]
B/D25-54[»]
4EYNX-ray1.53A/C90-110[»]
B/D25-54[»]
4EYPX-ray1.59A/C90-110[»]
B/D25-54[»]
4F0NX-ray1.68A/C90-110[»]
B/D25-54[»]
4F0OX-ray1.67A/C90-110[»]
B/D25-54[»]
4F1AX-ray1.80A/C90-110[»]
B/D25-54[»]
4F1BX-ray1.59A/C90-110[»]
B/D25-54[»]
4F1CX-ray1.70A/C90-110[»]
B/D25-54[»]
4F1DX-ray1.64A/C90-110[»]
B/D25-54[»]
4F1FX-ray1.68A/C90-110[»]
B/D25-54[»]
4F1GX-ray1.64A/C90-110[»]
B/D25-54[»]
4F4TX-ray1.64A/C90-110[»]
B/D25-54[»]
4F4VX-ray1.64A/C90-110[»]
B/D25-54[»]
4F51X-ray1.64A/C90-110[»]
B/D25-54[»]
4F8FX-ray1.68A/C90-110[»]
B/D25-54[»]
4FG3X-ray2.00A/C90-110[»]
B/D25-54[»]
4FKAX-ray1.08A/C90-110[»]
B/D25-54[»]
4GBCX-ray1.78A/C90-110[»]
B/D25-54[»]
4GBIX-ray2.50A/C90-110[»]
B/D25-54[»]
4GBKX-ray2.40A/C90-110[»]
B/D25-54[»]
4GBLX-ray2.50A/C90-110[»]
B/D25-54[»]
4GBNX-ray1.87A/C90-110[»]
B/D25-54[»]
4IUZX-ray1.60A90-110[»]
B25-54[»]
4IYDX-ray1.66A90-109[»]
B25-53[»]
4IYFX-ray1.80A90-109[»]
B25-53[»]
4NIBX-ray1.40A90-110[»]
B25-54[»]
4OGAX-ray3.50A90-110[»]
B25-54[»]
4P65X-ray1.50A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
4UNEX-ray1.59A/C90-110[»]
B/D25-54[»]
4UNGX-ray1.81A/C90-110[»]
B/D25-54[»]
4UNHX-ray2.75A90-110[»]
B25-54[»]
4XC4X-ray1.50A/C90-110[»]
B/D25-53[»]
5AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
ProteinModelPortaliP01308.
SMRiP01308. Positions 25-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01308.

Family & Domainsi

Sequence similaritiesi

Belongs to the insulin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45999.
GeneTreeiENSGT00390000015440.
HOGENOMiHOG000261669.
HOVERGENiHBG006137.
InParanoidiP01308.
KOiK04526.
OMAiVEQCCHN.
PhylomeDBiP01308.
TreeFamiTF332820.

Family and domain databases

Gene3Di1.10.100.10. 2 hits.
InterProiIPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamiPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSiPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTiSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMiSSF56994. SSF56994. 1 hit.
PROSITEiPS00262. INSULIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P01308-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY
60 70 80 90 100
TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC
110
SLYQLENYCN
Length:110
Mass (Da):11,981
Last modified:July 20, 1986 - v1
Checksum:iC2C3B23B85E520E5
GO
Isoform 2 (identifier: F8WCM5-1) [UniParc]FASTAAdd to basket

Also known as: INS-IGF2

The sequence of this isoform can be found in the external entry F8WCM5.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Based on a readthrough transcript which may produce an INS-IGF2 fusion protein.

Length:200
Mass (Da):21,537
GO

Sequence cautioni

The sequence AAA59179.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61R → C in MODY10. 1 Publication
Corresponds to variant rs121908278 [ dbSNP | Ensembl ].
VAR_063721
Natural varianti6 – 61R → H in MODY10. 1 Publication
Corresponds to variant rs121908259 [ dbSNP | Ensembl ].
VAR_063722
Natural varianti24 – 241A → D in PNDM. 2 Publications
Corresponds to variant rs80356663 [ dbSNP | Ensembl ].
VAR_063723
Natural varianti29 – 291H → D in PNDM. 1 Publication
Corresponds to variant rs121908272 [ dbSNP | Ensembl ].
VAR_063724
Natural varianti32 – 321G → R in PNDM. 2 Publications
Corresponds to variant rs80356664 [ dbSNP | Ensembl ].
VAR_063725
Natural varianti32 – 321G → S in PNDM. 2 Publications
Corresponds to variant rs80356664 [ dbSNP | Ensembl ].
VAR_063726
Natural varianti34 – 341H → D in FHPRI; Providence. 1 Publication
VAR_003971
Natural varianti35 – 351L → P in PNDM. 1 Publication
Corresponds to variant rs121908273 [ dbSNP | Ensembl ].
VAR_063727
Natural varianti43 – 431C → G in PNDM. 2 Publications
Corresponds to variant rs80356666 [ dbSNP | Ensembl ].
VAR_063728
Natural varianti46 – 461R → Q in MODY10. 2 Publications
Corresponds to variant rs121908260 [ dbSNP | Ensembl ].
VAR_063729
Natural varianti47 – 471G → V in PNDM. 2 Publications
Corresponds to variant rs80356667 [ dbSNP | Ensembl ].
VAR_063730
Natural varianti48 – 481F → C in PNDM. 2 Publications
Corresponds to variant rs80356668 [ dbSNP | Ensembl ].
VAR_063731
Natural varianti48 – 481F → S Associated with diabetes mellitus type-II; Los-Angeles. 3 Publications
VAR_003972
Natural varianti49 – 491F → L in Chicago. 1 Publication
VAR_003973
Natural varianti55 – 551R → C in IDDM2. 1 Publication
Corresponds to variant rs121908261 [ dbSNP | Ensembl ].
VAR_063732
Natural varianti68 – 681L → M.1 Publication
Corresponds to variant rs121908279 [ dbSNP | Ensembl ].
VAR_063733
Natural varianti84 – 841G → R in PNDM; uncertain pathological significance. 1 Publication
Corresponds to variant rs121908274 [ dbSNP | Ensembl ].
VAR_063734
Natural varianti89 – 891R → C in PNDM. 2 Publications
Corresponds to variant rs80356669 [ dbSNP | Ensembl ].
VAR_063735
Natural varianti89 – 891R → H in FHPRI; impairs posttranslational cleavage. 2 Publications
Corresponds to variant rs28933985 [ dbSNP | Ensembl ].
VAR_003974
Natural varianti89 – 891R → L in FHPRI; Kyoto. 1 Publication
VAR_003975
Natural varianti90 – 901G → C in PNDM. 2 Publications
Corresponds to variant rs80356670 [ dbSNP | Ensembl ].
VAR_063736
Natural varianti92 – 921V → L in Wakayama. 1 Publication
VAR_003976
Natural varianti96 – 961C → S in PNDM. 1 Publication
Corresponds to variant rs80356671 [ dbSNP | Ensembl ].
VAR_063737
Natural varianti96 – 961C → Y in PNDM. 2 Publications
Corresponds to variant rs80356671 [ dbSNP | Ensembl ].
VAR_063738
Natural varianti101 – 1011S → C in PNDM. 1 Publication
Corresponds to variant rs121908276 [ dbSNP | Ensembl ].
VAR_063739
Natural varianti103 – 1031Y → C in PNDM. 1 Publication
Corresponds to variant rs121908277 [ dbSNP | Ensembl ].
VAR_063740
Natural varianti108 – 1081Y → C in PNDM. 2 Publications
Corresponds to variant rs80356672 [ dbSNP | Ensembl ].
VAR_063741

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00565 Genomic DNA. Translation: CAA23828.1.
M10039 Genomic DNA. Translation: AAA59173.1.
J00265 Genomic DNA. Translation: AAA59172.1.
X70508 mRNA. Translation: CAA49913.1.
L15440 Genomic DNA. Translation: AAA59179.1. Sequence problems.
AY899304 mRNA. Translation: AAW83741.1.
AY138590 Genomic DNA. Translation: AAN39451.1.
BT006808 mRNA. Translation: AAP35454.1.
CH471158 Genomic DNA. Translation: EAX02488.1.
BC005255 mRNA. Translation: AAH05255.1.
AJ009655 Genomic DNA. Translation: CAA08766.1.
CCDSiCCDS7729.1. [P01308-1]
PIRiA93222. IPHU.
RefSeqiNP_000198.1. NM_000207.2. [P01308-1]
NP_001172026.1. NM_001185097.1. [P01308-1]
NP_001172027.1. NM_001185098.1. [P01308-1]
NP_001278826.1. NM_001291897.1. [P01308-1]
UniGeneiHs.272259.

Genome annotation databases

EnsembliENST00000250971; ENSP00000250971; ENSG00000254647. [P01308-1]
ENST00000381330; ENSP00000370731; ENSG00000254647. [P01308-1]
ENST00000397262; ENSP00000380432; ENSG00000254647. [P01308-1]
GeneIDi3630.
KEGGihsa:3630.
UCSCiuc001lvn.2. human. [P01308-1]

Polymorphism databases

DMDMi124617.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Insulin at Eli Lilly

Clinical information on Eli Lilly insulin products

Protein Spotlight

Protein of the 20th century - Issue 9 of April 2001

Wikipedia

Insulin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00565 Genomic DNA. Translation: CAA23828.1.
M10039 Genomic DNA. Translation: AAA59173.1.
J00265 Genomic DNA. Translation: AAA59172.1.
X70508 mRNA. Translation: CAA49913.1.
L15440 Genomic DNA. Translation: AAA59179.1. Sequence problems.
AY899304 mRNA. Translation: AAW83741.1.
AY138590 Genomic DNA. Translation: AAN39451.1.
BT006808 mRNA. Translation: AAP35454.1.
CH471158 Genomic DNA. Translation: EAX02488.1.
BC005255 mRNA. Translation: AAH05255.1.
AJ009655 Genomic DNA. Translation: CAA08766.1.
CCDSiCCDS7729.1. [P01308-1]
PIRiA93222. IPHU.
RefSeqiNP_000198.1. NM_000207.2. [P01308-1]
NP_001172026.1. NM_001185097.1. [P01308-1]
NP_001172027.1. NM_001185098.1. [P01308-1]
NP_001278826.1. NM_001291897.1. [P01308-1]
UniGeneiHs.272259.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7FNMR-A90-110[»]
B25-53[»]
1AI0NMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1B9EX-ray2.50A/C90-110[»]
B/D25-54[»]
1BENX-ray1.40A/C90-110[»]
B/D25-54[»]
1EFENMR-A25-54[»]
A90-110[»]
1EV3X-ray1.78A/C90-110[»]
B/D25-54[»]
1EV6X-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1EVRX-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1FU2X-ray3.24A/C/E/G90-110[»]
B/D/F/H25-54[»]
1FUBX-ray3.09A/C90-110[»]
B/D25-54[»]
1G7AX-ray1.20A/C/E/G90-110[»]
B/D/F/H25-54[»]
1G7BX-ray1.30A/C/E/G90-110[»]
B/D/F/H25-54[»]
1GUJX-ray1.62A/C90-110[»]
B/D25-54[»]
1HIQNMR-A90-110[»]
B25-54[»]
1HISNMR-A90-110[»]
B25-49[»]
1HITNMR-A90-110[»]
B25-54[»]
1HLSNMR-A90-110[»]
B25-54[»]
1HTVX-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-51[»]
1HUINMR-A90-110[»]
B26-53[»]
1IOGNMR-A90-110[»]
B25-53[»]
1IOHNMR-A90-110[»]
B25-53[»]
1J73X-ray2.00A/C90-110[»]
B/D25-54[»]
1JCAX-ray2.50A/C90-110[»]
B/D25-54[»]
1JCONMR-A90-110[»]
B25-54[»]
1JK8X-ray2.40C35-47[»]
1K3MNMR-A90-110[»]
B25-54[»]
1KMFNMR-A90-110[»]
B25-54[»]
1LKQNMR-A90-110[»]
B25-54[»]
1LPHX-ray2.30A/C90-110[»]
B/D25-54[»]
1MHINMR-A90-110[»]
B25-54[»]
1MHJNMR-A90-110[»]
B25-54[»]
1MSOX-ray1.00A/C90-110[»]
B/D25-54[»]
1OS3X-ray1.95A/C90-110[»]
B/D25-54[»]
1OS4X-ray2.25A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1Q4VX-ray2.00A/C90-110[»]
B/D25-54[»]
1QIYX-ray2.30A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1QIZX-ray2.00A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1QJ0X-ray2.40A/C90-110[»]
B/D25-54[»]
1RWEX-ray1.80A/C90-110[»]
B/D25-54[»]
1SF1NMR-A90-110[»]
B25-54[»]
1SJTNMR-A90-110[»]
B25-51[»]
1SJUNMR-A25-110[»]
1T0CNMR-A57-87[»]
1T1KNMR-A90-110[»]
B25-54[»]
1T1PNMR-A90-110[»]
B25-54[»]
1T1QNMR-A90-110[»]
B25-54[»]
1TRZX-ray1.60A/C90-110[»]
B/D25-54[»]
1TYLX-ray1.90A/C90-110[»]
B/D25-54[»]
1TYMX-ray1.90A/C90-110[»]
B/D25-54[»]
1UZ9X-ray1.60A90-110[»]
B25-53[»]
1VKTNMR-A90-110[»]
B25-54[»]
1W8PX-ray2.08A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1XDAX-ray1.80A/C/E/G90-110[»]
B/D/F/H25-53[»]
1XGLNMR-A90-110[»]
B25-54[»]
1XW7X-ray2.30A/C90-110[»]
B/D25-54[»]
1ZEGX-ray1.60A/C90-110[»]
B/D25-54[»]
1ZEHX-ray1.50A/C90-110[»]
B/D25-54[»]
1ZNJX-ray2.00A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2C8QX-ray1.95A90-110[»]
B25-53[»]
2C8RX-ray1.50A90-110[»]
B25-53[»]
2CEUX-ray1.80A/C90-110[»]
B/D25-49[»]
2G54X-ray2.25C/D25-54[»]
2G56X-ray2.20C/D25-54[»]
2H67NMR-A90-110[»]
B25-54[»]
2HH4NMR-A90-110[»]
B25-54[»]
2HHONMR-A90-110[»]
B25-54[»]
2HIUNMR-A90-110[»]
B25-54[»]
2JMNNMR-A90-110[»]
B25-54[»]
2JUMNMR-A90-110[»]
B25-54[»]
2JUUNMR-A90-110[»]
B25-54[»]
2JUVNMR-A90-110[»]
B25-54[»]
2JV1NMR-A90-110[»]
B25-54[»]
2JZQNMR-A25-54[»]
A90-110[»]
2K91NMR-A90-110[»]
B25-54[»]
2K9RNMR-A90-110[»]
B25-54[»]
2KJJNMR-A90-110[»]
B25-54[»]
2KJUNMR-A90-110[»]
B25-54[»]
2KQPNMR-A25-110[»]
2KQQNMR-A90-110[»]
B25-54[»]
2KXKNMR-A90-110[»]
B25-54[»]
2L1YNMR-A90-110[»]
B25-54[»]
2L1ZNMR-A90-110[»]
B25-54[»]
2LGBNMR-A90-110[»]
B25-55[»]
2LWZNMR-A25-54[»]
A89-110[»]
2M1DNMR-A90-110[»]
B25-54[»]
2M1ENMR-A90-110[»]
B25-54[»]
2M2MNMR-A90-110[»]
B25-54[»]
2M2NNMR-A90-110[»]
B25-54[»]
2M2ONMR-A90-110[»]
B25-54[»]
2M2PNMR-A90-110[»]
B25-54[»]
2MLINMR-A90-110[»]
B25-54[»]
2MPGNMR-A90-110[»]
B25-54[»]
2MPINMR-A90-110[»]
B25-54[»]
2MVCNMR-A90-110[»]
B25-54[»]
2MVDNMR-A90-110[»]
B25-54[»]
2OLYX-ray1.70A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2OLZX-ray1.70A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2OM0X-ray2.051/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k90-110[»]
2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l25-54[»]
2OM1X-ray1.971/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k90-110[»]
2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l25-54[»]
2OMGX-ray1.52A/C/E90-110[»]
B/D/F25-54[»]
2OMHX-ray1.36A/C/E90-110[»]
B/D/F25-54[»]
2OMIX-ray2.24A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2OMQX-ray2.00A/B/C/D36-41[»]
2QIUX-ray2.00A/C89-110[»]
B/D25-54[»]
2R34X-ray2.25A/C89-110[»]
B/D25-54[»]
2R35X-ray2.08A/C89-110[»]
B/D25-54[»]
2R36X-ray2.00A/C89-110[»]
B/D25-54[»]
2RN5NMR-A90-110[»]
B25-54[»]
2VJZX-ray1.80A/C90-110[»]
B/D25-54[»]
2VK0X-ray2.20A/C90-110[»]
B/D25-54[»]
2W44X-ray2.00A/C/E94-110[»]
B/D/F25-53[»]
2WBYX-ray2.60C/E90-109[»]
D/F25-43[»]
2WC0X-ray2.80C/E90-110[»]
D/F25-54[»]
2WRUX-ray1.57A90-110[»]
B25-50[»]
2WRVX-ray2.15A90-110[»]
B25-50[»]
2WRWX-ray2.41A90-110[»]
B25-50[»]
2WRXX-ray1.50A/C90-110[»]
B/D25-54[»]
2WS0X-ray2.10A90-110[»]
B25-54[»]
2WS1X-ray1.60A90-110[»]
B25-54[»]
2WS4X-ray1.90A90-110[»]
B25-50[»]
2WS6X-ray1.50A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2WS7X-ray2.59A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-50[»]
3AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3BXQX-ray1.30A/C90-110[»]
B/D25-54[»]
3E7YX-ray1.60A/C90-110[»]
B/D25-53[»]
3E7ZX-ray1.70A/C90-110[»]
B/D25-53[»]
3EXXX-ray1.35A/C90-110[»]
B/D25-54[»]
3FQ9X-ray1.35A/C91-110[»]
B/D25-54[»]
3HYDX-ray1.00A35-41[»]
3I3ZX-ray1.60A90-110[»]
B25-54[»]
3I40X-ray1.85A90-110[»]
B25-54[»]
3ILGX-ray1.90A/C90-110[»]
B/D25-54[»]
3INCX-ray1.85A/C90-110[»]
B/D25-54[»]
3IR0X-ray2.20A/C/E/G/I/K/M/O/R/T/V/X90-110[»]
B/D/F/H/J/L/N/P/S/U/W/Y25-54[»]
3JSDX-ray2.50A/C90-110[»]
B/D25-54[»]
3KQ6X-ray1.90A/C90-110[»]
B/D25-54[»]
3P2XX-ray2.00A/C90-110[»]
B/D25-54[»]
3P33X-ray2.30A/C/E/G90-110[»]
B/D/F/H25-54[»]
3Q6EX-ray2.05A/C90-110[»]
B/D25-54[»]
3ROVX-ray2.30A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3TT8X-ray1.12A/C90-110[»]
B/D25-54[»]
3U4NX-ray1.98A90-110[»]
B25-53[»]
3UTQX-ray1.67C15-24[»]
3UTSX-ray2.71C/H15-24[»]
3UTTX-ray2.60C/H15-24[»]
3V19X-ray2.00A/C90-110[»]
B/D25-54[»]
3V1GX-ray2.20A/C90-110[»]
B/D25-54[»]
3W11X-ray3.90A90-110[»]
B25-54[»]
3W12X-ray4.30A90-110[»]
B25-50[»]
3W13X-ray4.30A90-110[»]
B25-50[»]
3W7YX-ray0.92A/C90-110[»]
B/D25-54[»]
3W7ZX-ray1.15A/C90-110[»]
B/D25-54[»]
3W80X-ray1.40A/C/E/G90-110[»]
B/D/F/H25-54[»]
3ZI3X-ray1.70A90-110[»]
B25-54[»]
3ZQRX-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3ZS2X-ray1.97A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3ZU1X-ray1.60A/C90-110[»]
B/D25-54[»]
4AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
4AJXX-ray1.20A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-53[»]
4AJZX-ray1.80A/C90-110[»]
B/D25-53[»]
4AK0X-ray2.28A90-110[»]
B25-53[»]
4AKJX-ray2.01A/C90-110[»]
B/D25-53[»]
4CXLX-ray1.50A90-110[»]
B25-54[»]
4CXNX-ray1.70A90-110[»]
B25-54[»]
4CY7X-ray1.40A/C90-110[»]
B/D25-54[»]
4EFXX-ray1.98A/C90-110[»]
B/D25-52[»]
4EWWX-ray2.30A/C90-110[»]
B/D25-54[»]
4EWXX-ray2.20A/C90-110[»]
B/D25-54[»]
4EWZX-ray1.79A/C90-110[»]
B/D25-54[»]
4EX0X-ray1.86A/C90-110[»]
B/D25-54[»]
4EX1X-ray1.66A/C90-110[»]
B/D25-54[»]
4EXXX-ray1.55A/C90-110[»]
B/D25-54[»]
4EY1X-ray1.47A/C90-110[»]
B/D25-54[»]
4EY9X-ray1.47A/C90-110[»]
B/D25-54[»]
4EYDX-ray1.47A/C90-110[»]
B/D25-54[»]
4EYNX-ray1.53A/C90-110[»]
B/D25-54[»]
4EYPX-ray1.59A/C90-110[»]
B/D25-54[»]
4F0NX-ray1.68A/C90-110[»]
B/D25-54[»]
4F0OX-ray1.67A/C90-110[»]
B/D25-54[»]
4F1AX-ray1.80A/C90-110[»]
B/D25-54[»]
4F1BX-ray1.59A/C90-110[»]
B/D25-54[»]
4F1CX-ray1.70A/C90-110[»]
B/D25-54[»]
4F1DX-ray1.64A/C90-110[»]
B/D25-54[»]
4F1FX-ray1.68A/C90-110[»]
B/D25-54[»]
4F1GX-ray1.64A/C90-110[»]
B/D25-54[»]
4F4TX-ray1.64A/C90-110[»]
B/D25-54[»]
4F4VX-ray1.64A/C90-110[»]
B/D25-54[»]
4F51X-ray1.64A/C90-110[»]
B/D25-54[»]
4F8FX-ray1.68A/C90-110[»]
B/D25-54[»]
4FG3X-ray2.00A/C90-110[»]
B/D25-54[»]
4FKAX-ray1.08A/C90-110[»]
B/D25-54[»]
4GBCX-ray1.78A/C90-110[»]
B/D25-54[»]
4GBIX-ray2.50A/C90-110[»]
B/D25-54[»]
4GBKX-ray2.40A/C90-110[»]
B/D25-54[»]
4GBLX-ray2.50A/C90-110[»]
B/D25-54[»]
4GBNX-ray1.87A/C90-110[»]
B/D25-54[»]
4IUZX-ray1.60A90-110[»]
B25-54[»]
4IYDX-ray1.66A90-109[»]
B25-53[»]
4IYFX-ray1.80A90-109[»]
B25-53[»]
4NIBX-ray1.40A90-110[»]
B25-54[»]
4OGAX-ray3.50A90-110[»]
B25-54[»]
4P65X-ray1.50A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
4UNEX-ray1.59A/C90-110[»]
B/D25-54[»]
4UNGX-ray1.81A/C90-110[»]
B/D25-54[»]
4UNHX-ray2.75A90-110[»]
B25-54[»]
4XC4X-ray1.50A/C90-110[»]
B/D25-53[»]
5AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
ProteinModelPortaliP01308.
SMRiP01308. Positions 25-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109842. 12 interactions.
DIPiDIP-6024N.
IntActiP01308. 3 interactions.
MINTiMINT-106847.
STRINGi9606.ENSP00000348986.

Chemistry

ChEMBLiCHEMBL5881.

Protein family/group databases

Allergomei2121. Hom s Insulin.

PTM databases

PhosphoSiteiP01308.

Polymorphism databases

DMDMi124617.

Proteomic databases

PaxDbiP01308.
PeptideAtlasiP01308.
PRIDEiP01308.

Protocols and materials databases

DNASUi3630.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000250971; ENSP00000250971; ENSG00000254647. [P01308-1]
ENST00000381330; ENSP00000370731; ENSG00000254647. [P01308-1]
ENST00000397262; ENSP00000380432; ENSG00000254647. [P01308-1]
GeneIDi3630.
KEGGihsa:3630.
UCSCiuc001lvn.2. human. [P01308-1]

Organism-specific databases

CTDi3630.
GeneCardsiGC11M002181.
GeneReviewsiINS.
HGNCiHGNC:6081. INS.
HPAiCAB000048.
CAB012098.
CAB053843.
HPA004932.
MIMi125852. phenotype.
176730. gene+phenotype.
606176. phenotype.
613370. phenotype.
neXtProtiNX_P01308.
Orphaneti552. MODY.
99885. Permanent neonatal diabetes mellitus.
PharmGKBiPA201.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45999.
GeneTreeiENSGT00390000015440.
HOGENOMiHOG000261669.
HOVERGENiHBG006137.
InParanoidiP01308.
KOiK04526.
OMAiVEQCCHN.
PhylomeDBiP01308.
TreeFamiTF332820.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16190.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_13819. Regulation of gene expression in beta cells.
REACT_15550. Insulin processing.
REACT_1661. SHC activation.
REACT_18325. Regulation of insulin secretion.
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
REACT_498. Signaling by Insulin receptor.
REACT_508. Signal attenuation.
REACT_570. IRS activation.
SignaLinkiP01308.

Miscellaneous databases

EvolutionaryTraceiP01308.
GeneWikiiInsulin.
GenomeRNAii3630.
NextBioi14203.
PMAP-CutDBP01308.
PROiP01308.
SOURCEiSearch...

Gene expression databases

BgeeiP01308.
ExpressionAtlasiP01308. baseline.
GenevestigatoriP01308.

Family and domain databases

Gene3Di1.10.100.10. 2 hits.
InterProiIPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamiPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSiPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTiSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMiSSF56994. SSF56994. 1 hit.
PROSITEiPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genetic variation in the human insulin gene."
    Ullrich A., Dull T.J., Gray A., Brosius J., Sures I.
    Science 209:612-615(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequence of a cDNA clone encoding human preproinsulin."
    Bell G.I., Swain W.F., Pictet R.L., Cordell B., Goodman H.M., Rutter W.J.
    Nature 282:525-527(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Nucleotide sequence of human preproinsulin complementary DNA."
    Sures I., Goeddel D.V., Gray A., Ullrich A.
    Science 208:57-59(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Susceptibility to insulin dependent diabetes mellitus maps to a 4.1 kb segment of DNA spanning the insulin gene and associated VNTR."
    Lucassen A.M., Julier C., Beressi J.-P., Boitard C., Froguel P., Lathrop M., Bell J.I.
    Nat. Genet. 4:305-310(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. "Global haplotype diversity in the human insulin gene region."
    Stead J.D.H., Hurles M.E., Jeffreys A.J.
    Genome Res. 13:2101-2111(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  11. "Description of a novel RFLP diallelic polymorphism (-127 BsgI C/G) within the 5' region of insulin gene."
    Fajardy I.I., Weill J.J., Stuckens C.C., Danze P.M.P.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
    Tissue: Blood.
  12. "Amino-acid sequence of human insulin."
    Nicol D.S.H.W., Smith L.F.
    Nature 187:483-485(1959) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-54 AND 90-110.
  13. "Studies on human proinsulin. Isolation and amino acid sequence of the human pancreatic C-peptide."
    Oyer P.E., Cho S., Peterson J.D., Steiner D.F.
    J. Biol. Chem. 246:1375-1386(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-87.
  14. "The amino acid sequence of the C-peptide of human proinsulin."
    Ko A., Smyth D.G., Markussen J., Sundby F.
    Eur. J. Biochem. 20:190-199(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-87.
  15. "Total synthesis of human insulin under directed formation of the disulfide bonds."
    Sieber P., Kamber B., Hartmann A., Joehl A., Riniker B., Rittel W.
    Helv. Chim. Acta 57:2617-2621(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS.
  16. "Studies on polypeptides, IV. The synthesis of C-peptide of human proinsulin."
    Naithani V.K.
    Hoppe-Seyler's Z. Physiol. Chem. 354:659-672(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 57-87.
  17. "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."
    Geiger R., Volk A.
    Chem. Ber. 106:199-205(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 65-69 AND 70-73.
  18. "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."
    Geiger R., Jaeger G., Keonig W., Treuth G.
    Chem. Ber. 106:188-192(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 84-87.
  19. "Studies on mutant human insulin genes: identification and sequence analysis of a gene encoding [SerB24]insulin."
    Haneda M., Chan S.J., Kwok S.C.M., Rubenstein A.H., Steiner D.F.
    Proc. Natl. Acad. Sci. U.S.A. 80:6366-6370(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LOS ANGELES SER-48.
  20. "Identification of a mutant human insulin predicted to contain a serine-for-phenylalanine substitution."
    Shoelson S., Fickova M., Haneda M., Nahum A., Musso G., Kaiser E.T., Rubenstein A.H., Tager H.
    Proc. Natl. Acad. Sci. U.S.A. 80:7390-7394(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LOS ANGELES SER-48 AND CHICAGO LEU-49.
  21. "A mutation in the B chain coding region is associated with impaired proinsulin conversion in a family with hyperproinsulinemia."
    Chan S.J., Seino S., Gruppuso P.A., Schwartz R., Steiner D.F.
    Proc. Natl. Acad. Sci. U.S.A. 84:2194-2197(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FHPRI ASP-34.
  22. "Structurally abnormal insulin in a diabetic patient. Characterization of the mutant insulin A3 (Val-->Leu) isolated from the pancreas."
    Sakura H., Iwamoto Y., Sakamoto Y., Kuzuya T., Hirata H.
    J. Clin. Invest. 78:1666-1672(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT WAKAYAMA LEU-92.
  23. "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."
    Barbetti F., Raben N., Kadowaki T., Cama A., Accili D., Gabbay K.H., Merenich J.A., Taylor S.I., Roth J.
    J. Clin. Endocrinol. Metab. 71:164-169(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FHPRI HIS-89.
  24. "Posttranslational cleavage of proinsulin is blocked by a point mutation in familial hyperproinsulinemia."
    Shibasaki Y., Kawakami T., Kanazawa Y., Akanuma Y., Takaku F.
    J. Clin. Invest. 76:378-380(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FHPRI HIS-89.
  25. "A novel point mutation in the human insulin gene giving rise to hyperproinsulinemia (proinsulin Kyoto)."
    Yano H., Kitano N., Morimoto M., Polonsky K.S., Imura H., Seino Y.
    J. Clin. Invest. 89:1902-1907(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FHPRI LEU-89.
  26. "Toward the solution structure of human insulin: sequential 2D 1H NMR assignment of a des-pentapeptide analogue and comparison with crystal structure."
    Hua Q.-X., Weiss M.A.
    Biochemistry 29:10545-10555(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  27. "Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition."
    Hua Q.-X., Weiss M.A.
    Biochemistry 30:5505-5515(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  28. "Two-dimensional NMR studies of Des-(B26-B30)-insulin: sequence-specific resonance assignments and effects of solvent composition."
    Hua Q.-X., Weiss M.A.
    Biochim. Biophys. Acta 1078:101-110(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  29. "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."
    Joergensen A.M.M., Kristensen S.M., Led J.J., Balschmidt P.
    J. Mol. Biol. 227:1146-1163(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  30. "Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus."
    Hua Q.-X., Shoelson S.E., Inouye K., Weiss M.A.
    Proc. Natl. Acad. Sci. U.S.A. 90:582-586(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF VARIANT LOS-ANGELES SER-48.
  31. "Solution structures of the R6 human insulin hexamer."
    Chang X., Joergensen A.M., Bardrum P., Led J.J.
    Biochemistry 36:9409-9422(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  32. Cited for: VARIANTS PNDM ASP-24; ARG-32; SER-32; GLY-43; VAL-47; CYS-48; CYS-89; CYS-90; TYR-96 AND CYS-108.
  33. "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."
    Edghill E.L., Flanagan S.E., Patch A.M., Boustred C., Parrish A., Shields B., Shepherd M.H., Hussain K., Kapoor R.R., Malecki M., MacDonald M.J., Stoy J., Steiner D.F., Philipson L.H., Bell G.I., Hattersley A.T., Ellard S.
    Diabetes 57:1034-1042(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PNDM 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.
  34. Cited for: VARIANT MODY10 GLN-46, VARIANT IDDM2 CYS-55.
  35. "Further evidence that mutations in INS can be a rare cause of Maturity-Onset Diabetes of the Young (MODY)."
    Boesgaard T.W., Pruhova S., Andersson E.A., Cinek O., Obermannova B., Lauenborg J., Damm P., Bergholdt R., Pociot F., Pisinger C., Barbetti F., Lebl J., Pedersen O., Hansen T.
    BMC Med. Genet. 11:42-42(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MODY10 HIS-6 AND GLN-46.

Entry informationi

Entry nameiINS_HUMAN
AccessioniPrimary (citable) accession number: P01308
Secondary accession number(s): Q5EEX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: July 20, 1986
Last modified: March 31, 2015
This is version 202 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.