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UniProtKB - P01308 (INS_HUMAN)

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Protein

Insulin

Gene

INS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • hormone activity Source: BHF-UCL
  • identical protein binding Source: IntAct
  • insulin-like growth factor receptor binding Source: BHF-UCL
  • insulin receptor binding Source: UniProtKB
  • protease binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • activation of protein kinase B activity Source: BHF-UCL
  • acute-phase response Source: BHF-UCL
  • alpha-beta T cell activation Source: UniProtKB
  • cell-cell signaling Source: UniProtKB
  • cellular protein metabolic process Source: Reactome
  • cognition Source: ARUK-UCL
  • ER to Golgi vesicle-mediated transport Source: Reactome
  • fatty acid homeostasis Source: BHF-UCL
  • glucose homeostasis Source: BHF-UCL
  • glucose metabolic process Source: UniProtKB-KW
  • glucose transport Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: BHF-UCL
  • insulin receptor signaling pathway Source: BHF-UCL
  • MAPK cascade Source: BHF-UCL
  • negative regulation of acute inflammatory response Source: BHF-UCL
  • negative regulation of blood vessel diameter Source: UniProtKB
  • negative regulation of fatty acid metabolic process Source: BHF-UCL
  • negative regulation of feeding behavior Source: DFLAT
  • negative regulation of gluconeogenesis Source: BHF-UCL
  • negative regulation of glycogen catabolic process Source: BHF-UCL
  • negative regulation of lipid catabolic process Source: AgBase
  • negative regulation of NAD(P)H oxidase activity Source: BHF-UCL
  • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of protein catabolic process Source: UniProtKB
  • negative regulation of protein oligomerization Source: UniProtKB
  • negative regulation of protein secretion Source: BHF-UCL
  • negative regulation of proteolysis Source: BHF-UCL
  • negative regulation of reactive oxygen species biosynthetic process Source: ARUK-UCL
  • negative regulation of respiratory burst involved in inflammatory response Source: BHF-UCL
  • neuron projection maintenance Source: ARUK-UCL
  • positive regulation of blood vessel diameter Source: UniProtKB
  • positive regulation of brown fat cell differentiation Source: BHF-UCL
  • positive regulation of cell differentiation Source: BHF-UCL
  • positive regulation of cell growth Source: BHF-UCL
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of cellular protein metabolic process Source: BHF-UCL
  • positive regulation of cytokine secretion Source: UniProtKB
  • positive regulation of dendritic spine maintenance Source: ARUK-UCL
  • positive regulation of DNA replication Source: BHF-UCL
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of glucose import Source: BHF-UCL
  • positive regulation of glycogen biosynthetic process Source: BHF-UCL
  • positive regulation of glycolytic process Source: BHF-UCL
  • positive regulation of insulin receptor signaling pathway Source: BHF-UCL
  • positive regulation of lipid biosynthetic process Source: BHF-UCL
  • positive regulation of long-term synaptic potentiation Source: ARUK-UCL
  • positive regulation of MAPK cascade Source: BHF-UCL
  • positive regulation of mitotic nuclear division Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  • positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  • positive regulation of nitric-oxide synthase activity Source: UniProtKB
  • positive regulation of peptide hormone secretion Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  • positive regulation of protein autophosphorylation Source: BHF-UCL
  • positive regulation of protein kinase B signaling Source: BHF-UCL
  • positive regulation of protein localization to nucleus Source: BHF-UCL
  • positive regulation of respiratory burst Source: BHF-UCL
  • regulation of cellular amino acid metabolic process Source: BHF-UCL
  • regulation of protein localization Source: BHF-UCL
  • regulation of protein localization to plasma membrane Source: ARUK-UCL
  • regulation of protein secretion Source: UniProtKB
  • regulation of synaptic plasticity Source: ARUK-UCL
  • regulation of transcription, DNA-templated Source: BHF-UCL
  • regulation of transmembrane transporter activity Source: BHF-UCL
  • wound healing Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHormone
Biological processCarbohydrate metabolism, Glucose metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16190.
ReactomeiR-HSA-210745. Regulation of gene expression in beta cells.
R-HSA-264876. Insulin processing.
R-HSA-422085. Synthesis, secretion, and deacylation of Ghrelin.
R-HSA-422356. Regulation of insulin secretion.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-74713. IRS activation.
R-HSA-74749. Signal attenuation.
R-HSA-74751. Insulin receptor signalling cascade.
R-HSA-74752. Signaling by Insulin receptor.
R-HSA-77387. Insulin receptor recycling.
R-HSA-977225. Amyloid fiber formation.
SignaLinkiP01308.
SIGNORiP01308.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin
Cleaved into the following 2 chains:
Insulin B chain
Insulin A chain
Gene namesi
Name:INS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000254647.6.
HGNCiHGNC:6081. INS.
MIMi176730. gene.
neXtProtiNX_P01308.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Hyperproinsulinemia (HPRI)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:616214
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00397134H → D in HPRI; Providence. 1 PublicationCorresponds to variant dbSNP:rs121918101Ensembl.1
Natural variantiVAR_00397489R → H in HPRI; impairs post-translational cleavage. 2 PublicationsCorresponds to variant dbSNP:rs28933985Ensembl.1
Natural variantiVAR_00397589R → L in HPRI; Kyoto. 1 PublicationCorresponds to variant dbSNP:rs28933985Ensembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06373255R → C in IDDM2. 1 PublicationCorresponds to variant dbSNP:rs121908261Ensembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06372324A → D in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356663Ensembl.1
Natural variantiVAR_06372429H → D in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908272Ensembl.1
Natural variantiVAR_06372532G → R in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356664Ensembl.1
Natural variantiVAR_06372632G → S in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356664Ensembl.1
Natural variantiVAR_06372735L → P in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908273Ensembl.1
Natural variantiVAR_06372843C → G in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356666Ensembl.1
Natural variantiVAR_06373047G → V in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356667Ensembl.1
Natural variantiVAR_06373148F → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356668Ensembl.1
Natural variantiVAR_06373484G → R in PNDM; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs121908274Ensembl.1
Natural variantiVAR_06373589R → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356669Ensembl.1
Natural variantiVAR_06373690G → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356670Ensembl.1
Natural variantiVAR_06373796C → S in PNDM. 1 PublicationCorresponds to variant dbSNP:rs80356671Ensembl.1
Natural variantiVAR_06373896C → Y in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356671Ensembl.1
Natural variantiVAR_063739101S → C in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908276Ensembl.1
Natural variantiVAR_063740103Y → C in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908277Ensembl.1
Natural variantiVAR_063741108Y → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356672Ensembl.1
Maturity-onset diabetes of the young 10 (MODY10)4 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_0637216R → C in MODY10. 1 PublicationCorresponds to variant dbSNP:rs121908278Ensembl.1
Natural variantiVAR_0637226R → H in MODY10. 1 PublicationCorresponds to variant dbSNP:rs121908259Ensembl.1
Natural variantiVAR_06372946R → Q in MODY10; reduces binding affinity to INSR; reduces biological activity; reduces folding properties. 3 PublicationsCorresponds to variant dbSNP:rs121908260Ensembl.1

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

DisGeNETi3630.
GeneReviewsiINS.
MalaCardsiINS.
MIMi125852. phenotype.
606176. phenotype.
613370. phenotype.
616214. phenotype.
OpenTargetsiENSG00000254647.
Orphaneti552. MODY.
99885. Permanent neonatal diabetes mellitus.
PharmGKBiPA201.

Protein family/group databases

Allergomei2121. Hom s Insulin.

Chemistry databases

ChEMBLiCHEMBL5881.
DrugBankiDB01776. M-Cresol.
DB08231. MYRISTIC ACID.

Polymorphism and mutation databases

BioMutaiINS.
DMDMi124617.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
PeptideiPRO_000001581925 – 54Insulin B chainAdd BLAST30
PropeptideiPRO_000001582057 – 87C peptideAdd BLAST31
PeptideiPRO_000001582190 – 110Insulin A chainAdd BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 96Interchain (between B and A chains)Combined sources3 Publications
Disulfide bondi43 ↔ 109Interchain (between B and A chains)Combined sources3 Publications
Disulfide bondi95 ↔ 100Combined sources5 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbiP01308.
PeptideAtlasiP01308.
PRIDEiP01308.

PTM databases

CarbonylDBiP01308.
iPTMnetiP01308.
PhosphoSitePlusiP01308.

Miscellaneous databases

PMAP-CutDBiP01308.

Expressioni

Gene expression databases

BgeeiENSG00000254647.
ExpressionAtlasiP01308. baseline and differential.
GenevisibleiP01308. HS.

Organism-specific databases

HPAiCAB000048.
CAB012098.
CAB053843.
HPA004932.

Interactioni

Subunit structurei

Heterodimer of a B chain and an A chain linked by two disulfide bonds (PubMed:25423173).1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • hormone activity Source: BHF-UCL
  • identical protein binding Source: IntAct
  • insulin-like growth factor receptor binding Source: BHF-UCL
  • insulin receptor binding Source: UniProtKB
  • protease binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi109842. 13 interactors.
DIPiDIP-6024N.
IntActiP01308. 14 interactors.
MINTiP01308.
STRINGi9606.ENSP00000250971.

Structurei

Secondary structure

1110
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 29Combined sources4
Helixi33 – 43Combined sources11
Helixi44 – 46Combined sources3
Beta strandi48 – 50Combined sources3
Beta strandi56 – 58Combined sources3
Turni59 – 66Combined sources8
Beta strandi74 – 76Combined sources3
Helixi79 – 81Combined sources3
Turni84 – 86Combined sources3
Helixi91 – 97Combined sources7
Beta strandi98 – 101Combined sources4
Helixi102 – 106Combined sources5
Turni107 – 109Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2N2VNMR-A90-110[»]
B25-54[»]
2N2WNMR-A90-110[»]
B25-54[»]
2N2XNMR-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[»]
4Q5ZX-ray3.93a/b/c/d/e/f/g/h90-109[»]
x25-43[»]
4RXWX-ray1.73A/C90-110[»]
B/D25-54[»]
4UNEX-ray1.59A/C90-110[»]
B/D25-54[»]
4UNGX-ray1.81A/C90-110[»]
B/D25-54[»]
4UNHX-ray2.75A90-110[»]
B25-54[»]
4WDIX-ray2.31C/F39-47[»]
4XC4X-ray1.50A/C90-110[»]
B/D25-54[»]
4Y19X-ray2.50C75-90[»]
4Y1AX-ray4.00C75-90[»]
4Z76X-ray1.88C/F39-46[»]
4Z77X-ray1.85C/F39-47[»]
4Z78X-ray2.30C/F/I39-48[»]
5AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
5BOQX-ray1.70A/C/E/G90-110[»]
B/D/F/H25-54[»]
5BPOX-ray1.90A/C90-110[»]
B/D25-54[»]
5BQQX-ray1.54A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-50[»]
5BTSX-ray1.77A90-110[»]
B25-54[»]
5C0DX-ray1.68C15-24[»]
5CJOX-ray3.29a90-109[»]
5CNYX-ray1.70A/C90-110[»]
B/D25-54[»]
5CO2X-ray1.70A/C90-110[»]
B/D25-54[»]
5CO6X-ray1.80A/C90-110[»]
B/D25-54[»]
5CO9X-ray1.92A/C90-110[»]
B/D25-54[»]
5E7WX-ray0.95A/C90-110[»]
B/D25-54[»]
5EMSX-ray2.30A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-52[»]
5EN9X-ray1.50A90-110[»]
B25-54[»]
5ENAX-ray1.35A90-110[»]
B25-54[»]
5HPRX-ray1.33A90-110[»]
B25-54[»]
5HPUX-ray2.20A/C90-110[»]
B/D25-54[»]
5HQIX-ray0.97A90-110[»]
B25-54[»]
5HRQX-ray1.28A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
5HYJX-ray3.06C/H15-24[»]
5MAMX-ray2.200/2/4/A/C/E/G/I/K/M/O/Q/S/U/W/Y90-110[»]
1/3/5/B/D/F/H/J/L/N/P/R/T/V/X/Z25-54[»]
5MHDNMR-A90-110[»]
B25-55[»]
5MT3X-ray2.02A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e90-110[»]
B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f25-54[»]
5MT9X-ray1.88A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e90-110[»]
B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f25-54[»]
5MWQNMR-A90-110[»]
B25-56[»]
5T7RX-ray1.55A/C90-110[»]
B/D25-54[»]
5UDPX-ray1.35A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
5UOZX-ray1.17A90-110[»]
B25-54[»]
5URTX-ray1.18A90-110[»]
B25-54[»]
5VIZX-ray1.70A90-109[»]
B25-53[»]
5WBTNMR-A25-54[»]
A90-110[»]
5WDMX-ray2.80A/B/C/D/E/F25-110[»]
6B3Qelectron microscopy3.70a/b1-110[»]
6B70electron microscopy3.70a/c1-110[»]
6BFCelectron microscopy3.70a/b1-110[»]
ProteinModelPortaliP01308.
SMRiP01308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01308.

Family & Domainsi

Sequence similaritiesi

Belongs to the insulin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J0XC. Eukaryota.
ENOG4111VJB. LUCA.
GeneTreeiENSGT00390000015440.
HOGENOMiHOG000261669.
HOVERGENiHBG006137.
InParanoidiP01308.
KOiK04526.
OMAiPQHLCGS.
OrthoDBiEOG091G0H56.
PhylomeDBiP01308.
TreeFamiTF332820.

Family and domain databases

InterProiView protein in InterPro
IPR004825. Insulin.
IPR016179. Insulin-like.
IPR036438. Insulin-like_sf.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
PfamiView protein in Pfam
PF00049. Insulin. 1 hit.
PRINTSiPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTiView protein in SMART
SM00078. IlGF. 1 hit.
SUPFAMiSSF56994. SSF56994. 1 hit.
PROSITEiView protein in PROSITE
PS00262. INSULIN. 1 hit.

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 21, 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 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0637216R → C in MODY10. 1 PublicationCorresponds to variant dbSNP:rs121908278Ensembl.1
Natural variantiVAR_0637226R → H in MODY10. 1 PublicationCorresponds to variant dbSNP:rs121908259Ensembl.1
Natural variantiVAR_06372324A → D in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356663Ensembl.1
Natural variantiVAR_06372429H → D in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908272Ensembl.1
Natural variantiVAR_06372532G → R in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356664Ensembl.1
Natural variantiVAR_06372632G → S in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356664Ensembl.1
Natural variantiVAR_00397134H → D in HPRI; Providence. 1 PublicationCorresponds to variant dbSNP:rs121918101Ensembl.1
Natural variantiVAR_06372735L → P in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908273Ensembl.1
Natural variantiVAR_06372843C → G in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356666Ensembl.1
Natural variantiVAR_06372946R → Q in MODY10; reduces binding affinity to INSR; reduces biological activity; reduces folding properties. 3 PublicationsCorresponds to variant dbSNP:rs121908260Ensembl.1
Natural variantiVAR_06373047G → V in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356667Ensembl.1
Natural variantiVAR_06373148F → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356668Ensembl.1
Natural variantiVAR_00397248F → S Associated with diabetes mellitus type-II; Los-Angeles. 3 PublicationsCorresponds to variant dbSNP:rs80356668Ensembl.1
Natural variantiVAR_00397349F → L in Chicago. 1 PublicationCorresponds to variant dbSNP:rs148685531Ensembl.1
Natural variantiVAR_06373255R → C in IDDM2. 1 PublicationCorresponds to variant dbSNP:rs121908261Ensembl.1
Natural variantiVAR_06373368L → M1 PublicationCorresponds to variant dbSNP:rs121908279Ensembl.1
Natural variantiVAR_06373484G → R in PNDM; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs121908274Ensembl.1
Natural variantiVAR_06373589R → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356669Ensembl.1
Natural variantiVAR_00397489R → H in HPRI; impairs post-translational cleavage. 2 PublicationsCorresponds to variant dbSNP:rs28933985Ensembl.1
Natural variantiVAR_00397589R → L in HPRI; Kyoto. 1 PublicationCorresponds to variant dbSNP:rs28933985Ensembl.1
Natural variantiVAR_06373690G → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356670Ensembl.1
Natural variantiVAR_00397692V → L in Wakayama. 1 PublicationCorresponds to variant dbSNP:rs121918102Ensembl.1
Natural variantiVAR_06373796C → S in PNDM. 1 PublicationCorresponds to variant dbSNP:rs80356671Ensembl.1
Natural variantiVAR_06373896C → Y in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356671Ensembl.1
Natural variantiVAR_063739101S → C in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908276Ensembl.1
Natural variantiVAR_063740103Y → C in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908277Ensembl.1
Natural variantiVAR_063741108Y → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356672Ensembl.1

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.3. human. [P01308-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi