ALPHASUITEATLASTM
INS · P01308Homo sapiens
PROTEIN OVERVIEW

INSInsulin

P01308Homo sapiensReviewed · UniProt

Hormone secreted by pancreatic islet beta cells, that is the principal anabolic regulator of glucose, lipid, and protein metabolism and the central controller of blood glucose homeostasis.

Sequence110 aa
Source mass11.98 kDa
Recorded PDB entries384
Isoforms listed2

UniProt locations Secreted

01

Function

Hormone secreted by pancreatic islet beta cells, that is the principal anabolic regulator of glucose, lipid, and protein metabolism and the central controller of blood glucose homeostasis [19]. Acts by binding to and activating the insulin receptor INSR, a receptor tyrosine kinase, triggering INSR autophosphorylation and recruitment/phosphorylation of insulin receptor substrate proteins IRS1 and IRS2, which activate the downstream PI3K/AKT and RAS/MAPK signaling cascades [33]. Through the PI3K/AKT pathway, stimulates glucose uptake into skeletal muscle and adipose tissue by promoting translocation of the glucose transporter GLUT4/SLC2A4 from intracellular storage vesicles to the plasma membrane [35].

In liver and muscle, promotes glycogen synthesis through AKT-mediated inhibitory phosphorylation of glycogen synthase kinase-3 (GSK3), thereby activating glycogen synthase [34]. In the liver, suppresses hepatic glucose production by inhibiting gluconeogenesis, in part through phosphorylation and exclusion of the FOXO1 transcription factor, which downregulates the gluconeogenic enzymes PEPCK and glucose-6-phosphatase [37]. In adipose tissue, promotes lipogenesis and potently suppresses lipolysis, reducing the flux of free fatty acids and glycerol to the liver and thereby further restraining hepatic gluconeogenesis [38]

Experimental evidence 6 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12754525"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15113941"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32291281"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "7763247"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "7983060"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9235985"
        }
      ],
      "value": "Hormone secreted by pancreatic islet beta cells, that is the principal anabolic regulator of glucose, lipid, and protein metabolism and the central controller of blood glucose homeostasis (PubMed:32291281). Acts by binding to and activating the insulin receptor INSR, a receptor tyrosine kinase, triggering INSR autophosphorylation and recruitment/phosphorylation of insulin receptor substrate proteins IRS1 and IRS2, which activate the downstream PI3K/AKT and RAS/MAPK signaling cascades (PubMed:7983060). Through the PI3K/AKT pathway, stimulates glucose uptake into skeletal muscle and adipose tissue by promoting translocation of the glucose transporter GLUT4/SLC2A4 from intracellular storage vesicles to the plasma membrane (PubMed:9235985). In liver and muscle, promotes glycogen synthesis through AKT-mediated inhibitory phosphorylation of glycogen synthase kinase-3 (GSK3), thereby activating glycogen synthase (PubMed:7763247). In the liver, suppresses hepatic glucose production by inhibiting gluconeogenesis, in part through phosphorylation and exclusion of the FOXO1 transcription factor, which downregulates the gluconeogenic enzymes PEPCK and glucose-6-phosphatase (PubMed:12754525). In adipose tissue, promotes lipogenesis and potently suppresses lipolysis, reducing the flux of free fatty acids and glycerol to the liver and thereby further restraining hepatic gluconeogenesis (PubMed:15113941)"
    }
  ],
  "commentType": "FUNCTION"
}

Pharmaceutical notes

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

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation
{
  "texts": [
    {
      "value": "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"
    }
  ],
  "commentType": "PHARMACEUTICAL"
}

GO functions & biological processes

negative regulation of gene expressionacts upstream ofUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0010629 · evidence & context
  • ECO:0000314 PMID:31501273 ↗ IDA · ARUK-UCL · 20210717
    qualifier: acts_upstream_of
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000540", "relation": "occurs_in"}, {"db": "RNAcentral", "id": "URS0000591950_9606", "relation": "has_input"}]}]
negative regulation of gene expressionacts upstream ofUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0010629 · evidence & context
  • ECO:0000314 PMID:31501273 ↗ IDA · ARUK-UCL · 20210717
    qualifier: acts_upstream_of
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000540", "relation": "occurs_in"}, {"db": "UniProtKB", "id": "P61978", "relation": "has_input"}]}]
protease bindingenablesUniProtKB:P01308
GO
GO:0002020 · evidence & context
  • ECO:0000353 PMID:20082125 ↗ IPI · UniProt · 20120713
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P14735"}]}]
insulin receptor bindingenablesUniProtKB:P01308
GO
GO:0005158 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250306
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN002606702"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2915"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "A5PJB2"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P01317"}]}]
  • ECO:0000314 PMID:7556975 ↗ IDA · UniProt · 20050722
    qualifier: enables
  • ECO:0000353 PMID:8452530 ↗ IPI · BHF-UCL · 20080528
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06213"}]}]
  • ECO:0000314 PMID:9667398 ↗ IDA · BHF-UCL · 20080602
    qualifier: enables
insulin-like growth factor receptor bindingenablesUniProtKB:P01308
GO
GO:0005159 · evidence & context
  • ECO:0000353 PMID:8452530 ↗ IPI · BHF-UCL · 20080528
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08069"}]}]
All recorded function and process assertions (68)
hormone activityenablesUniProtKB:P01308
GO
GO:0005179 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR004825"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR016179"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR022352"}]}]
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250306
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN002606702"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P01315"}]}]
  • ECO:0000303 PMID:14986111 ↗ NAS · UniProt · 20050722
    qualifier: enables
  • ECO:0000315 PMID:381941 ↗ IMP · BHF-UCL · 20080602
    qualifier: enables
  • ECO:0000305 PMID:9667398 ↗ IC · BHF-UCL · 20080602
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "GO", "id": "0005158"}]}]
protein bindingenablesUniProtKB:P01308
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:17051221 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P14735-1"}]}]
  • ECO:0000353 PMID:23302862 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06213-2"}]}]
  • ECO:0000353 PMID:29512653 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06213-2"}]}]
  • ECO:0000353 PMID:32296183 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "A8MQ03"}]}]
  • ECO:0000353 PMID:32296183 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P0DPK4"}]}]
  • ECO:0000353 PMID:32296183 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q07627"}]}]
  • ECO:0000353 PMID:32296183 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6UY14-3"}]}]
  • ECO:0000353 PMID:32296183 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8IUG1"}]}]
  • ECO:0000353 PMID:9388210 ↗ IPI · BHF-UCL · 20090923
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P17936"}]}]
  • ECO:0000353 PMID:9388210 ↗ IPI · BHF-UCL · 20090923
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16270"}]}]
  • ECO:0000353 PMID:9773776 ↗ IPI · UniProt · 20050722
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P98164"}]}]
identical protein bindingenablesUniProtKB:P01308
GO
GO:0042802 · evidence & context
  • ECO:0000353 PMID:17472440 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}]
  • ECO:0000353 PMID:20738396 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}]
  • ECO:0000353 PMID:22854022 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}]
  • ECO:0000353 PMID:23106816 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}]
  • ECO:0000353 PMID:23416304 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}]
  • ECO:0000353 PMID:23510797 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}]
receptor ligand activityenablesUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0048018 · evidence & context
  • ECO:0000314 PMID:29512653 ↗ IDA · MGI · 20220712
    qualifier: enables
    extensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06213", "relation": "has_input"}]}]
receptor ligand activityenablesUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0048018 · evidence & context
  • ECO:0000314 PMID:8702995 ↗ IDA · BHF-UCL · 20250305
    qualifier: enables
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0008286", "relation": "part_of"}]}]
positive regulation of cytokine productioninvolved inUniProtKB:P01308
GO
GO:0001819 · evidence & context
negative regulation of acute inflammatory responseinvolved inUniProtKB:P01308
GO
GO:0002674 · evidence & context
regulation of DNA-templated transcriptioninvolved inUniProtKB:P01308
GO
GO:0006355 · evidence & context
acute-phase responseinvolved inUniProtKB:P01308
GO
GO:0006953 · evidence & context
G protein-coupled receptor signaling pathwayinvolved inUniProtKB:P01308
GO
GO:0007186 · evidence & context
cell-cell signalinginvolved inUniProtKB:P01308
GO
GO:0007267 · evidence & context
  • ECO:0000305 PMID:7556975 ↗ IC · UniProt · 20050722
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "GO", "id": "0005158"}]}]
positive regulation of cell population proliferationinvolved inUniProtKB:P01308
GO
GO:0008284 · evidence & context
insulin receptor signaling pathwayinvolved inUniProtKB:P01308
GO
GO:0008286 · evidence & context
insulin receptor signaling pathwayinvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0008286 · evidence & context
  • ECO:0000316 PMID:19727662 ↗ IGI · ARUK-UCL · 20241029
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}]
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0002539", "relation": "occurs_in"}]}]
positive regulation of gene expressioninvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0010628 · evidence & context
  • ECO:0000316 PMID:25403480 ↗ IGI · BHF-UCL · 20160425
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "RNAcentral", "id": "URS00004AD914_9606"}, {"db": "RNAcentral", "id": "URS00004BCD9C_9606"}]}]
    extensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06213", "relation": "has_input"}, {"db": "CL", "id": "0000737", "relation": "occurs_in"}]}]
positive regulation of neuron projection developmentinvolved inUniProtKB:P01308
GO
GO:0010976 · evidence & context
positive regulation of cell growthinvolved inUniProtKB:P01308
GO
GO:0030307 · evidence & context
positive regulation of cell migrationinvolved inUniProtKB:P01308
GO
GO:0030335 · evidence & context
  • ECO:0000250 PMID:12138094 ↗ ISS · BHF-UCL · 20090430
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01315"}]}]
regulation of protein localizationinvolved inUniProtKB:P01308
GO
GO:0032880 · evidence & context
nitric oxide-cGMP-mediated signalinginvolved inUniProtKB:P01308
GO
GO:0038060 · evidence & context
wound healinginvolved inUniProtKB:P01308
GO
GO:0042060 · evidence & context
negative regulation of protein catabolic processinvolved inUniProtKB:P01308
GO
GO:0042177 · evidence & context
vasodilationinvolved inUniProtKB:P01308
GO
GO:0042311 · evidence & context
glucose homeostasisinvolved inUniProtKB:P01308
GO
GO:0042593 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20220922
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:96573"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000155764"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2915"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}]
  • ECO:0000315 PMID:381941 ↗ IMP · BHF-UCL · 20080602
    qualifier: involved_in
positive regulation of canonical NF-kappaB signal transductioninvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0043123 · evidence & context
  • ECO:0000314 PMID:19727662 ↗ IDA · BHF-UCL · 20241029
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0002539", "relation": "occurs_in"}, {"db": "GO", "id": "0008286", "relation": "part_of"}]}]
positive regulation of MAPK cascadeinvolved inUniProtKB:P01308
GO
GO:0043410 · evidence & context
positive regulation of MAPK cascadeinvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0043410 · evidence & context
  • ECO:0000314 PMID:20455999 ↗ IDA · BHF-UCL · 20141205
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0008286", "relation": "part_of"}]}]
positive regulation of cell differentiationinvolved inUniProtKB:P01308
GO
GO:0045597 · evidence & context
negative regulation of gluconeogenesisinvolved inUniProtKB:P01308
GO
GO:0045721 · evidence & context
positive regulation of glycogen biosynthetic processinvolved inUniProtKB:P01308
GO
GO:0045725 · evidence & context
negative regulation of glycogen catabolic processinvolved inUniProtKB:P01308
GO
GO:0045818 · evidence & context
  • ECO:0000315 PMID:381941 ↗ IMP · BHF-UCL · 20080602
    qualifier: involved_in
positive regulation of glycolysisinvolved inUniProtKB:P01308
GO
GO:0045821 · evidence & context
positive regulation of mitotic nuclear divisioninvolved inUniProtKB:P01308
GO
GO:0045840 · evidence & context
negative regulation of fatty acid metabolic processinvolved inUniProtKB:P01308
GO
GO:0045922 · evidence & context
positive regulation of D-glucose import across plasma membraneinvolved inUniProtKB:P01308
GO
GO:0046326 · evidence & context
positive regulation of D-glucose import across plasma membraneinvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0046326 · evidence & context
  • ECO:0000314 PMID:15792832 ↗ IDA · UniProt · 20180914
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0071731", "relation": "happens_during"}]}, {"connectedXrefs": [{"db": "GO", "id": "0032868", "relation": "happens_during"}]}]
positive regulation of insulin receptor signaling pathwayinvolved inUniProtKB:P01308
GO
GO:0046628 · evidence & context
alpha-beta T cell activationinvolved inUniProtKB:P01308
GO
GO:0046631 · evidence & context
positive regulation of lipid biosynthetic processinvolved inUniProtKB:P01308
GO
GO:0046889 · evidence & context
regulation of synaptic plasticityinvolved inUniProtKB:P01308
GO
GO:0048167 · evidence & context
regulation of protein secretioninvolved inUniProtKB:P01308
GO
GO:0050708 · evidence & context
negative regulation of protein secretioninvolved inUniProtKB:P01308
GO
GO:0050709 · evidence & context
positive regulation of protein secretioninvolved inUniProtKB:P01308
GO
GO:0050714 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20230602
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "PANTHER", "id": "PTN000155764"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "A5PJB2"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P01317"}]}]
cognitioninvolved inUniProtKB:P01308
GO
GO:0050890 · evidence & context
negative regulation of lipid catabolic processinvolved inUniProtKB:P01308
GO
GO:0050995 · evidence & context
positive regulation of nitric-oxide synthase activityinvolved inUniProtKB:P01308
GO
GO:0051000 · evidence & context
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transductioninvolved inUniProtKB:P01308
GO
GO:0051897 · evidence & context
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transductioninvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0051897 · evidence & context
  • ECO:0000314 PMID:25240198 ↗ IDA · ARUK-UCL · 20210709
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0008286", "relation": "part_of"}]}]
  • ECO:0000314 PMID:8702995 ↗ IDA · BHF-UCL · 20250305
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0008286", "relation": "part_of"}]}]
fatty acid homeostasisinvolved inUniProtKB:P01308
GO
GO:0055089 · evidence & context
relaxation of vascular associated smooth muscleinvolved inUniProtKB:P01308
GO
GO:0060087 · evidence & context
negative regulation of respiratory burst involved in inflammatory responseinvolved inUniProtKB:P01308
GO
GO:0060266 · evidence & context
positive regulation of respiratory burstinvolved inUniProtKB:P01308
GO
GO:0060267 · evidence & context
positive regulation of peptide hormone secretioninvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:0090277 · evidence & context
  • ECO:0000304 PMID:11387233 ↗ TAS · BHF-UCL · 20130111
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P41159", "relation": "has_input"}]}]
positive regulation of brown fat cell differentiationinvolved inUniProtKB:P01308
GO
GO:0090336 · evidence & context
positive regulation of protein localization to nucleusinvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:1900182 · evidence & context
  • ECO:0000314 PMID:20455999 ↗ IDA · BHF-UCL · 20141205
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0008286", "relation": "part_of"}]}]
positive regulation of long-term synaptic potentiationinvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:1900273 · evidence & context
  • ECO:0000304 PMID:19188609 ↗ TAS · ARUK-UCL · 20170524
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "UBERON", "id": "0002421", "relation": "occurs_in"}]}]
cellular response to oxygen-containing compoundinvolved inUniProtKB:P01308
GO
GO:1901701 · evidence & context
  • ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027483"}]}]
negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathwayinvolved inUniProtKB:P01308
GO
GO:1902176 · evidence & context
positive regulation of dendritic spine maintenanceinvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:1902952 · evidence & context
  • ECO:0000316 PMID:19188609 ↗ IGI · ARUK-UCL · 20170628
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ComplexPortal", "id": "CPX-1134"}]}]
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0002608", "relation": "occurs_in"}]}]
regulation of protein localization to plasma membraneinvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:1903076 · evidence & context
  • ECO:0000316 PMID:19188609 ↗ IGI · ARUK-UCL · 20170628
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ComplexPortal", "id": "CPX-1134"}]}]
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0002608", "relation": "occurs_in"}, {"db": "GO", "id": "0032590", "relation": "has_target_start_location"}, {"db": "UniProtKB", "id": "P06213", "relation": "has_input"}, {"db": "GO", "id": "0032809", "relation": "has_target_end_location"}]}]
negative regulation of reactive oxygen species biosynthetic processinvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:1903427 · evidence & context
  • ECO:0000316 PMID:19188609 ↗ IGI · ARUK-UCL · 20170628
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ComplexPortal", "id": "CPX-1134"}]}]
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0002608", "relation": "occurs_in"}, {"db": "GO", "id": "1990535", "relation": "part_of"}]}]
neuron projection maintenanceinvolved inUniProtKB:P01308 · Context-qualified assertion; see evidence
GO
GO:1990535 · evidence & context
  • ECO:0000316 PMID:19188609 ↗ IGI · ARUK-UCL · 20170628
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ComplexPortal", "id": "CPX-1134"}, {"db": "UniProtKB", "id": "P15127"}]}]
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0002608", "relation": "occurs_in"}]}]
negative regulation of feeding behaviorinvolved inUniProtKB:P01308
GO
GO:2000252 · evidence & context
02

Names & Taxonomy

Recommended name
Insulin
Gene
INS
Accession / entry
P01308 · INS_HUMAN
Species
Homo sapiens · NCBI 9606
Recorded aliases
Full taxonomy & recorded names

Eukaryota → Metazoa → Chordata → Craniata → Vertebrata → Euteleostomi → Mammalia → Eutheria → Euarchontoglires → Primates → Haplorrhini → Catarrhini → Hominidae → Homo

{
  "names": {
    "recommendedName": {
      "fullName": {
        "value": "Insulin"
      }
    },
    "contains": [
      {
        "recommendedName": {
          "fullName": {
            "value": "Insulin B chain"
          }
        }
      },
      {
        "recommendedName": {
          "fullName": {
            "value": "Insulin A chain"
          }
        }
      }
    ],
    "flag": "Precursor"
  },
  "genes": [
    {
      "geneName": {
        "value": "INS"
      }
    }
  ]
}
03

Subcellular Location

UniProt locations and GO cellular-component assertions. Relations and contexts remain distinct; “part of” is not automatically a residence claim.

SecretedReported location
UniProt
Experimental evidence 1 publication
Evidence & references
extracellular regionis active in
GO
Evidence & references
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260528
    qualifier: is_active_in
    withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:96572"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96573"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN002606702"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2915"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2916"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "A5PJB2"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P01308"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P01317"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P67970"}]}]
Golgi membranelocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-6809006 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-6809010 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-6809011 TAS · Reactome · 20231126
    qualifier: located_in
extracellular regionlocated in
GO
Curator inference 3 publications
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR004825"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR016179"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0243"}]}]
  • ECO:0000314 PMID:36309486 ↗ IDA · UniProt · 20251218
    qualifier: located_in
  • ECO:0000305 PMID:7556975 ↗ IC · UniProt · 20050722
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "GO", "id": "0005158"}]}]
  • ECO:0000314 PMID:9667398 ↗ IDA · BHF-UCL · 20080602
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-110011 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74707 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74711 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74712 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74715 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74716 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74718 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74740 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74742 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74743 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-976734 TAS · Reactome · 20200509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-977136 TAS · Reactome · 20200509
    qualifier: located_in
endoplasmic reticulum lumenlocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-264997 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-265010 TAS · Reactome · 20231126
    qualifier: located_in
Golgi lumenlocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-264976 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-265010 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-265153 TAS · Reactome · 20231126
    qualifier: located_in
transport vesiclelocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-6807877 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-6809003 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-6809006 TAS · Reactome · 20231126
    qualifier: located_in
endosome lumenlocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-74718 TAS · Reactome · 20130503
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74726 TAS · Reactome · 20130503
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-74730 TAS · Reactome · 20130503
    qualifier: located_in
All recorded location assertions (10)
endoplasmic reticulum-Golgi intermediate compartment membranelocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-6807875 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-6807877 TAS · Reactome · 20231126
    qualifier: located_in
secretory granule lumenlocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-265153 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-NUL-9023165 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-NUL-9023166 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-NUL-9023180 TAS · Reactome · 20231126
    qualifier: located_in
  • ECO:0000304 Reactome:R-NUL-9023186 TAS · Reactome · 20231126
    qualifier: located_in

Membrane topology 0

No annotation is recorded in this UniProt entry.

04

Disease & Variants

Source annotations; a recorded variant is not automatically a clinical classification.

Hyperproinsulinemia HPRI

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

Experimental evidence 7 publications
Evidence & references

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

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation
{
  "commentType": "DISEASE",
  "disease": {
    "diseaseId": "Hyperproinsulinemia",
    "diseaseAccession": "DI-01585",
    "acronym": "HPRI",
    "description": "An autosomal dominant condition characterized by elevated levels of serum proinsulin-like material.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "616214"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "1601997"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "2196279"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "3470784"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "4019786"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "6312455"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "6424111"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "8421693"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "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.

Experimental evidence 1 publication
Evidence & references

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

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation
{
  "commentType": "DISEASE",
  "disease": {
    "diseaseId": "Type 1 diabetes mellitus 2",
    "diseaseAccession": "DI-02788",
    "acronym": "T1D2",
    "description": "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.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "125852"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "18192540"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "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.

Experimental evidence 2 publications
Evidence & references

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

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation
{
  "commentType": "DISEASE",
  "disease": {
    "diseaseId": "Diabetes mellitus, permanent neonatal, 4",
    "diseaseAccession": "DI-05825",
    "acronym": "PNDM4",
    "description": "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.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "618858"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "17855560"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "18162506"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "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.

Experimental evidence 4 publications
Evidence & references

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

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation
{
  "commentType": "DISEASE",
  "disease": {
    "diseaseId": "Maturity-onset diabetes of the young 10",
    "diseaseAccession": "DI-02786",
    "acronym": "MODY10",
    "description": "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.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "613370"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "18162506"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "18192540"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "20226046"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "25423173"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The disease is caused by variants affecting the gene represented in this entry"
      }
    ]
  }
}

Natural variants 27

Scroll across the table for evidence and actions.

27 recorded rows

FeaturePositionDescriptionEvidenceInspect
R6CVAR_0637216in MODY10; dbSNP:rs121908278
R → C
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R6HVAR_0637226in MODY10; dbSNP:rs121908259
R → H
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
A24DVAR_06372324in PNDM4; dbSNP:rs80356663
A → D
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
H29DVAR_06372429in PNDM4; dbSNP:rs121908272
H → D
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 6TC2
G32RVAR_06372532in PNDM4; dbSNP:rs80356664
G → R
Experimental evidence 2 publications
Evidence & references
1/1 residues mapped to 6TC2
G32SVAR_06372632in PNDM4; dbSNP:rs80356664
G → S
Experimental evidence 2 publications
Evidence & references
1/1 residues mapped to 6TC2
H34DVAR_00397134in HPRI; Providence; dbSNP:rs121918101
H → D
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 6TC2
L35PVAR_06372735in PNDM4; dbSNP:rs121908273
L → P
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 6TC2
C43GVAR_06372843in PNDM4; dbSNP:rs80356666
C → G
Experimental evidence 2 publications
Evidence & references
1/1 residues mapped to 6TC2
R46QVAR_06372946in MODY10; reduces binding affinity to INSR; reduces biological activity; reduces folding properties; dbSNP:rs121908260
R → Q
Experimental evidence 3 publications
Evidence & references
1/1 residues mapped to 6TC2
G47VVAR_06373047in PNDM4; dbSNP:rs80356667
G → V
Experimental evidence 2 publications
Evidence & references
1/1 residues mapped to 6TC2
F48CVAR_06373148in PNDM4; dbSNP:rs80356668
F → C
Experimental evidence 2 publications
Evidence & references
1/1 residues mapped to 6TC2
F48SVAR_00397248in HPRI; Los-Angeles; dbSNP:rs80356668
F → S
Experimental evidence 3 publications
Evidence & references
1/1 residues mapped to 6TC2
F49LVAR_00397349in Chicago; dbSNP:rs148685531
F → L
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 6TC2
R55CVAR_06373255in T1D2; dbSNP:rs121908261
R → C
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
L68MVAR_06373368in dbSNP:rs121908279
L → M
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
G84RVAR_06373484in PNDM4; uncertain significance; dbSNP:rs121908274
G → R
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R89CVAR_06373589in PNDM4; dbSNP:rs80356669
R → C
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
R89HVAR_00397489in HPRI; impairs post-translational cleavage; dbSNP:rs28933985
R → H
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
R89LVAR_00397589in HPRI; Kyoto; dbSNP:rs28933985
R → L
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
G90CVAR_06373690in PNDM4; dbSNP:rs80356670
G → C
Experimental evidence 2 publications
Evidence & references
1/1 residues mapped to 6TC2
V92LVAR_00397692in Wakayama; dbSNP:rs121918102
V → L
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 6TC2
C96SVAR_06373796in PNDM4; dbSNP:rs80356671
C → S
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 6TC2
C96YVAR_06373896in PNDM4; dbSNP:rs80356671
C → Y
Experimental evidence 2 publications
Evidence & references
1/1 residues mapped to 6TC2
S101CVAR_063739101in PNDM4; dbSNP:rs121908276
S → C
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 6TC2
Y103CVAR_063740103in PNDM4; dbSNP:rs121908277
Y → C
Experimental evidence 1 publication
Evidence & references
1/1 residues mapped to 6TC2
Y108CVAR_063741108in PNDM4; dbSNP:rs80356672
Y → C
Experimental evidence 2 publications
Evidence & references
1/1 residues mapped to 6TC2

Laboratory mutagenesis 0

No annotation is recorded in this UniProt entry.

05

PTM/Processing

Processed by PCSK1 but not PCSK2

Experimental evidence 1 publication
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32291281"
        }
      ],
      "value": "Processed by PCSK1 but not PCSK2"
    }
  ],
  "commentType": "PTM"
}

Processed chains & precursor regions 4

Scroll across the table for evidence and actions.

4 recorded rows

FeaturePositionDescriptionEvidenceInspect
Signal1–24Signal
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
PeptidePRO_000001581925–54Insulin B chain
Evidence & references

No separate evidence record is supplied for this statement.

30/30 residues mapped to 6TC2
PropeptidePRO_000001582057–87C peptide
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure
PeptidePRO_000001582190–110Insulin A chain
Evidence & references

No separate evidence record is supplied for this statement.

21/21 residues mapped to 6TC2

Modifications 3

Scroll across the table for evidence and actions.

3 recorded rows

FeaturePositionDescriptionEvidenceInspect
Disulfide bond31, 96Interchain (between B and A chains)
Experimental evidence 3 publications
Evidence & references
2/2 residues mapped to 6TC2
Disulfide bond43, 109Interchain (between B and A chains)
Experimental evidence 3 publications
Evidence & references
2/2 residues mapped to 6TC2
Disulfide bond95, 100Disulfide bond
Experimental evidence 5 publications
Evidence & references
2/2 residues mapped to 6TC2
06

Expression

Expressed by pancreatic beta-cells (at protein level)

Experimental evidence 1 publication
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "36309486"
        }
      ],
      "value": "Expressed by pancreatic beta-cells (at protein level)"
    }
  ],
  "commentType": "TISSUE SPECIFICITY"
}
07

Interaction

Documented interaction partners

UniProt’s filtered IntAct records. Experiment counts describe reported experiments, not binding strength or independent publications. Separate products remain separate rows.

9 records
Partner / productSpeciesExperimentsEvidence & actions
ADAMTSL4Q6UY14-3With P01308Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P01308. Partner: Q6UY14-3. Reported experiment count: 3.

Open protein ↗
CYSRT1A8MQ03With P01308Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P01308. Partner: A8MQ03. Reported experiment count: 3.

Open protein ↗
IDEP14735-1With P01308Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P01308. Partner: P14735-1. Reported experiment count: 3.

Open protein ↗
INSP01308With P01308Homo sapiens19
IntAct evidence

Pair evidence in IntAct ↗

Source product: P01308. Partner: P01308. Reported experiment count: 19.

Open protein ↗
INSRP06213-2With P01308Homo sapiens6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P01308. Partner: P06213-2. Reported experiment count: 6.

Open protein ↗
KRTAP1-1Q07627With P01308Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P01308. Partner: Q07627. Reported experiment count: 3.

Open protein ↗
KRTAP1-3Q8IUG1With P01308Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P01308. Partner: Q8IUG1. Reported experiment count: 3.

Open protein ↗
NOTCH2NLCP0DPK4With P01308Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P01308. Partner: P0DPK4. Reported experiment count: 3.

Open protein ↗
HSPA8P11142With PRO_0000015820Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: PRO_0000015820. Partner: P11142. Reported experiment count: 2.

Open protein ↗

Complex membership & assembly descriptions

Co-membership does not by itself prove direct binding between every pair.

INS-INSR receptor-ligand complex CPX-26678 Complex Portal

Homo sapiens; 9606 · Heterohexamer

Evidence: physical interaction evidence

  • INS · P01308-PRO_0000015821 · minValue: 1, maxValue: 1
  • INS · P01308-PRO_0000015819 · minValue: 1, maxValue: 1
  • INSR, insulin receptor complex · CPX-26675 · minValue: 1, maxValue: 1

Glucose-regulating complex. Upon binding with high affinity to INS, INSR undergoes major conformational shift from an autoinhibited, inverted-U shape to an active T-shaped conformation. Conformational rearrangement brings the membrane-proximal regions and intracellular kinase domains into close proximity, enabling trans-autophosphorylation and signal initiation. Once activated, INSR triggers downstream signalling pathways, including the PI3K-AKT and MAPK cascades, that regulate glucose uptake, lipid metabolism, protein synthesis, cell growth, and survival, thus playing a critical role in maintaining metabolic and systemic homeostasis.

Source & references ↗
Insulin complex CPX-943 Complex Portal

Homo sapiens; 9606 · Heterodimer

Evidence: physical interaction evidence

  • INS · P01308-PRO_0000015821 · minValue: 1, maxValue: 1
  • INS · P01308-PRO_0000015819 · minValue: 1, maxValue: 1

Insulin is a protein hormone that regulates the metabolism of carbohydrates, fats and protein by promoting the absorption of glucose from the blood into liver, fat and skeletal muscle cells

Source & references ↗

UniProt subunit description

Heterodimer of a B chain and an A chain linked by two disulfide bonds [43]

Experimental evidence 1 publication
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "25423173"
        }
      ],
      "value": "Heterodimer of a B chain and an A chain linked by two disulfide bonds (PubMed:25423173)"
    }
  ],
  "commentType": "SUBUNIT"
}

Other association resources

Resource links only; their association networks and counts are not added to the partner table.

BioGRID · 109842 ↗IntAct · P01308 ↗STRING · 9606.ENSP00000380432 ↗
08

Structure

SELECTED EXPERIMENTAL STRUCTURE

6TC2 · Monoclinic human insulin in complex with p-coumaric acid

Method
X-ray diffraction
Resolution
1.36 Å
Assembly 1
Hetero 12-mer · A6B6
Symmetry
D3
Deposited / released
04/11/2019 / 11/11/2020
Entry version
1.2 · 24/01/2024
110aa · full canonical protein
110aa · deposited protein construct(s)
51canonical residues verified in coordinates

Verified residue selection uses chain(s) A, B, H. Deposited construct lengths are per protein entity, not the full precursor or a total across assembly copies.

51/51 residues mapped to 6TC2

Components & chains

Chain labels below are mmCIF identifiers used by the viewer. Assembly membership does not establish direct binding.

ComponentIdentity / lengthChainsInspect
InsulinProtein / polymer · Entity 1Homo sapiensP01308110 aaA, B, C, D, E, F, G, H, I, J, K, L
ZINC IONLigand / ion · Entity 2CCD ZN ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of ZN
ZN
ZNM, RAuthor: B, D
PHOSPHATE IONLigand / ion · Entity 3CCD PO4 ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of PO4
PO4
PO4N, U, WAuthor: B, H, L
4'-HYDROXYCINNAMIC ACIDLigand / ion · Entity 4CCD HC4 ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of HC4
HC4
HC4O, Q, S, T, VAuthor: C, D, G, H, K
THIOCYANATE IONLigand / ion · Entity 5CCD SCN ↗
Chemical diagram · RCSB PDB
RCSB chemical diagram of SCN
SCN
SCNPAuthor: D

Chemical diagrams are recorded RCSB component depictions. Glycan names and source identifiers retain the recorded linkage information.

Structure validation

Recorded PDBe metrics describe model geometry. Percentiles compare with the archive; they are not probabilities of correctness. Missing metrics are not zero.

Clashscore4.68

Serious atomic overlaps per 1,000 atoms; lower is better.

Archive percentile: 59.0
Ramachandran outliers0.0%

Backbone conformations outside preferred regions; lower is better.

Archive percentile: 100.0
Side-chain outliers0.0%

Unusual side-chain conformations; lower is better.

Archive percentile: 100.0
Full validation report ↗

Publication

Insulin polymorphism induced by two polyphenols: new crystal forms and advances in macromolecular powder diffraction.

Paper date: 13/10/2020 · Read publication ↗

Structure references are from the dated source record. Opening another structure follows your existing Atlas account permissions.

Available structures 385

Scroll across the table for evidence and actions.

385 recorded rows

RecordEvidence typeMethodResolutionOpen
6TC2experimentalX-ray1.36 AOpen in Atlas ↗
7STHexperimentalEM3.50 AOpen in Atlas ↗
6B3QexperimentalEM3.70 AOpen in Atlas ↗
6B70experimentalEM3.70 AOpen in Atlas ↗
6BFCexperimentalEM3.70 AOpen in Atlas ↗
8EZ0experimentalEM3.70 AOpen in Atlas ↗
7STKexperimentalEM4.00 AOpen in Atlas ↗
8YYSexperimentalEM4.14 AOpen in Atlas ↗
7STJexperimentalEM4.40 AOpen in Atlas ↗
8EYXexperimentalEM4.50 AOpen in Atlas ↗
6JK8experimentalEM4.70 AOpen in Atlas ↗
7STIexperimentalEM4.90 AOpen in Atlas ↗
8EYYexperimentalEM4.90 AOpen in Atlas ↗
9DNNexperimentalEM6.10 AOpen in Atlas ↗
7JP3experimentalX-ray1.95 AOpen in Atlas ↗
7KD6experimentalX-ray2.60 AOpen in Atlas ↗
5WDMexperimentalX-ray2.80 AOpen in Atlas ↗
8PJCexperimentalX-ray2.14 AOpen in Atlas ↗
7BW8experimentalEM3.80 AOpen in Atlas ↗
7BW7experimentalEM4.10 AOpen in Atlas ↗
7BWAexperimentalEM4.90 AOpen in Atlas ↗
1EFEexperimentalNMR-Open in Atlas ↗
1SJUexperimentalNMR-Open in Atlas ↗
2KQPexperimentalNMR-Open in Atlas ↗
6U46experimentalNMR-Open in Atlas ↗
8PJHexperimentalX-ray1.50 AOpen in Atlas ↗
3W7YexperimentalX-ray0.92 AOpen in Atlas ↗
5E7WexperimentalX-ray0.95 AOpen in Atlas ↗
5HQIexperimentalX-ray0.97 AOpen in Atlas ↗
1MSOexperimentalX-ray1.00 AOpen in Atlas ↗
4FKAexperimentalX-ray1.08 AOpen in Atlas ↗
3TT8experimentalX-ray1.12 AOpen in Atlas ↗
3W7ZexperimentalX-ray1.15 AOpen in Atlas ↗
5UOZexperimentalX-ray1.17 AOpen in Atlas ↗
5USPexperimentalX-ray1.17 AOpen in Atlas ↗
5URTexperimentalX-ray1.18 AOpen in Atlas ↗
1G7AexperimentalX-ray1.20 AOpen in Atlas ↗
5UU2experimentalX-ray1.22 AOpen in Atlas ↗
7RKDexperimentalX-ray1.25 AOpen in Atlas ↗
6GV0experimentalX-ray1.26 AOpen in Atlas ↗
5HRQexperimentalX-ray1.28 AOpen in Atlas ↗
1G7BexperimentalX-ray1.30 AOpen in Atlas ↗
3BXQexperimentalX-ray1.30 AOpen in Atlas ↗
5USVexperimentalX-ray1.30 AOpen in Atlas ↗
9R4EexperimentalX-ray1.30 AOpen in Atlas ↗
5UQAexperimentalX-ray1.31 AOpen in Atlas ↗
5HPRexperimentalX-ray1.33 AOpen in Atlas ↗
4AJXexperimentalX-ray1.20 AOpen in Atlas ↗
7QGFexperimentalX-ray1.20 AOpen in Atlas ↗
3EXXexperimentalX-ray1.35 AOpen in Atlas ↗
5ENAexperimentalX-ray1.35 AOpen in Atlas ↗
5UDPexperimentalX-ray1.35 AOpen in Atlas ↗
6S34experimentalX-ray1.35 AOpen in Atlas ↗
2OMHexperimentalX-ray1.36 AOpen in Atlas ↗
8PI4experimentalX-ray1.25 AOpen in Atlas ↗
1BENexperimentalX-ray1.40 AOpen in Atlas ↗
3W80experimentalX-ray1.40 AOpen in Atlas ↗
4CY7experimentalX-ray1.40 AOpen in Atlas ↗
4NIBexperimentalX-ray1.40 AOpen in Atlas ↗
7Z5LexperimentalX-ray1.40 AOpen in Atlas ↗
9R4CexperimentalX-ray1.41 AOpen in Atlas ↗
9R4AexperimentalX-ray1.45 AOpen in Atlas ↗
4EY1experimentalX-ray1.47 AOpen in Atlas ↗
4EY9experimentalX-ray1.47 AOpen in Atlas ↗
4EYDexperimentalX-ray1.47 AOpen in Atlas ↗
3FQ9experimentalX-ray1.35 AOpen in Atlas ↗
1ZEHexperimentalX-ray1.50 AOpen in Atlas ↗
2WRXexperimentalX-ray1.50 AOpen in Atlas ↗
2WS6experimentalX-ray1.50 AOpen in Atlas ↗
4CXLexperimentalX-ray1.50 AOpen in Atlas ↗
4P65experimentalX-ray1.50 AOpen in Atlas ↗
4XC4experimentalX-ray1.50 AOpen in Atlas ↗
5EN9experimentalX-ray1.50 AOpen in Atlas ↗
9R4BexperimentalX-ray1.50 AOpen in Atlas ↗
2OMGexperimentalX-ray1.52 AOpen in Atlas ↗
4EYNexperimentalX-ray1.53 AOpen in Atlas ↗
7NHUexperimentalX-ray1.40 AOpen in Atlas ↗
8IPZexperimentalX-ray1.40 AOpen in Atlas ↗
4EXXexperimentalX-ray1.55 AOpen in Atlas ↗
5T7RexperimentalX-ray1.55 AOpen in Atlas ↗
4EYPexperimentalX-ray1.59 AOpen in Atlas ↗
4F1BexperimentalX-ray1.59 AOpen in Atlas ↗
4UNEexperimentalX-ray1.59 AOpen in Atlas ↗
1TRZexperimentalX-ray1.60 AOpen in Atlas ↗
1ZEGexperimentalX-ray1.60 AOpen in Atlas ↗
2WS1experimentalX-ray1.60 AOpen in Atlas ↗
3ZU1experimentalX-ray1.60 AOpen in Atlas ↗
4IUZexperimentalX-ray1.60 AOpen in Atlas ↗
6NWVexperimentalX-ray1.60 AOpen in Atlas ↗
6TYHexperimentalX-ray1.60 AOpen in Atlas ↗
1GUJexperimentalX-ray1.62 AOpen in Atlas ↗
4F1DexperimentalX-ray1.64 AOpen in Atlas ↗
4F1GexperimentalX-ray1.64 AOpen in Atlas ↗
4F4TexperimentalX-ray1.64 AOpen in Atlas ↗
4F4VexperimentalX-ray1.64 AOpen in Atlas ↗
4F51experimentalX-ray1.64 AOpen in Atlas ↗
9R49experimentalX-ray1.64 AOpen in Atlas ↗
2C8RexperimentalX-ray1.50 AOpen in Atlas ↗
6S4JexperimentalX-ray1.50 AOpen in Atlas ↗
9R48experimentalX-ray1.65 AOpen in Atlas ↗
6S4IexperimentalX-ray1.51 AOpen in Atlas ↗
4EX1experimentalX-ray1.66 AOpen in Atlas ↗
4F0OexperimentalX-ray1.67 AOpen in Atlas ↗
4F0NexperimentalX-ray1.68 AOpen in Atlas ↗
4F1FexperimentalX-ray1.68 AOpen in Atlas ↗
4F8FexperimentalX-ray1.68 AOpen in Atlas ↗
9M4XexperimentalX-ray1.40 AOpen in Atlas ↗
9M4YexperimentalX-ray1.40 AOpen in Atlas ↗
9M50experimentalX-ray1.40 AOpen in Atlas ↗
2OLYexperimentalX-ray1.70 AOpen in Atlas ↗
2OLZexperimentalX-ray1.70 AOpen in Atlas ↗
3ZI3experimentalX-ray1.70 AOpen in Atlas ↗
4CXNexperimentalX-ray1.70 AOpen in Atlas ↗
4F1CexperimentalX-ray1.70 AOpen in Atlas ↗
5BOQexperimentalX-ray1.70 AOpen in Atlas ↗
5CNYexperimentalX-ray1.70 AOpen in Atlas ↗
5CO2experimentalX-ray1.70 AOpen in Atlas ↗
7S4YexperimentalX-ray1.71 AOpen in Atlas ↗
6O17experimentalX-ray1.58 AOpen in Atlas ↗
4RXWexperimentalX-ray1.73 AOpen in Atlas ↗
1UZ9experimentalX-ray1.60 AOpen in Atlas ↗
3E7YexperimentalX-ray1.60 AOpen in Atlas ↗
3I3ZexperimentalX-ray1.60 AOpen in Atlas ↗
9CIVexperimentalX-ray1.60 AOpen in Atlas ↗
8OKYexperimentalX-ray1.17 AOpen in Atlas ↗
5BTSexperimentalX-ray1.77 AOpen in Atlas ↗
1EV3experimentalX-ray1.78 AOpen in Atlas ↗
4GBCexperimentalX-ray1.78 AOpen in Atlas ↗
8HSKexperimentalX-ray1.64 AOpen in Atlas ↗
4EWZexperimentalX-ray1.79 AOpen in Atlas ↗
9M4ZexperimentalX-ray1.50 AOpen in Atlas ↗
1RWEexperimentalX-ray1.80 AOpen in Atlas ↗
2VJZexperimentalX-ray1.80 AOpen in Atlas ↗
4F1AexperimentalX-ray1.80 AOpen in Atlas ↗
5CO6experimentalX-ray1.80 AOpen in Atlas ↗
6P4ZexperimentalX-ray1.80 AOpen in Atlas ↗
7Z5QexperimentalX-ray1.80 AOpen in Atlas ↗
8WU0experimentalX-ray1.95 AOpen in Atlas ↗
8PI5experimentalX-ray1.66 AOpen in Atlas ↗
4UNGexperimentalX-ray1.81 AOpen in Atlas ↗
6H3MexperimentalX-ray1.82 AOpen in Atlas ↗
5BQQexperimentalX-ray1.54 AOpen in Atlas ↗
9IBBexperimentalX-ray1.84 AOpen in Atlas ↗
3E7ZexperimentalX-ray1.70 AOpen in Atlas ↗
8HGZexperimentalX-ray1.70 AOpen in Atlas ↗
3INCexperimentalX-ray1.85 AOpen in Atlas ↗
2QIUexperimentalX-ray2.00 AOpen in Atlas ↗
2R36experimentalX-ray2.00 AOpen in Atlas ↗
4EX0experimentalX-ray1.86 AOpen in Atlas ↗
4GBNexperimentalX-ray1.87 AOpen in Atlas ↗
5MT9experimentalX-ray1.88 AOpen in Atlas ↗
1EV6experimentalX-ray1.90 AOpen in Atlas ↗
1EVRexperimentalX-ray1.90 AOpen in Atlas ↗
1TYLexperimentalX-ray1.90 AOpen in Atlas ↗
1TYMexperimentalX-ray1.90 AOpen in Atlas ↗
3ILGexperimentalX-ray1.90 AOpen in Atlas ↗
3KQ6experimentalX-ray1.90 AOpen in Atlas ↗
3ZQRexperimentalX-ray1.90 AOpen in Atlas ↗
5BPOexperimentalX-ray1.90 AOpen in Atlas ↗
5CO9experimentalX-ray1.92 AOpen in Atlas ↗
2R35experimentalX-ray2.08 AOpen in Atlas ↗
1XDAexperimentalX-ray1.80 AOpen in Atlas ↗
4AJZexperimentalX-ray1.80 AOpen in Atlas ↗
1OS3experimentalX-ray1.95 AOpen in Atlas ↗
4IYDexperimentalX-ray1.66 AOpen in Atlas ↗
2OM1experimentalX-ray1.97 AOpen in Atlas ↗
3ZS2experimentalX-ray1.97 AOpen in Atlas ↗
5UU4experimentalX-ray1.97 AOpen in Atlas ↗
5VIZexperimentalX-ray1.70 AOpen in Atlas ↗
3I40experimentalX-ray1.85 AOpen in Atlas ↗
1J73experimentalX-ray2.00 AOpen in Atlas ↗
1Q4VexperimentalX-ray2.00 AOpen in Atlas ↗
1QIZexperimentalX-ray2.00 AOpen in Atlas ↗
1ZNJexperimentalX-ray2.00 AOpen in Atlas ↗
3P2XexperimentalX-ray2.00 AOpen in Atlas ↗
3V19experimentalX-ray2.00 AOpen in Atlas ↗
4FG3experimentalX-ray2.00 AOpen in Atlas ↗
5MT3experimentalX-ray2.02 AOpen in Atlas ↗
2OM0experimentalX-ray2.05 AOpen in Atlas ↗
3Q6EexperimentalX-ray2.05 AOpen in Atlas ↗
8GSGexperimentalX-ray2.05 AOpen in Atlas ↗
9M51experimentalX-ray1.76 AOpen in Atlas ↗
5USSexperimentalX-ray2.06 AOpen in Atlas ↗
1W8PexperimentalX-ray2.08 AOpen in Atlas ↗
4IYFexperimentalX-ray1.80 AOpen in Atlas ↗
2C8QexperimentalX-ray1.95 AOpen in Atlas ↗
2WS0experimentalX-ray2.10 AOpen in Atlas ↗
2R34experimentalX-ray2.25 AOpen in Atlas ↗
3U4NexperimentalX-ray1.98 AOpen in Atlas ↗
8RRPexperimentalX-ray2.00 AOpen in Atlas ↗
2WRUexperimentalX-ray1.57 AOpen in Atlas ↗
4AKJexperimentalX-ray2.01 AOpen in Atlas ↗
25HFexperimentalX-ray2.20 AOpen in Atlas ↗
2VK0experimentalX-ray2.20 AOpen in Atlas ↗
3IR0experimentalX-ray2.20 AOpen in Atlas ↗
3V1GexperimentalX-ray2.20 AOpen in Atlas ↗
4EWXexperimentalX-ray2.20 AOpen in Atlas ↗
5HPUexperimentalX-ray2.20 AOpen in Atlas ↗
5MAMexperimentalX-ray2.20 AOpen in Atlas ↗
6GNQexperimentalX-ray2.20 AOpen in Atlas ↗
6Z7YexperimentalX-ray2.20 AOpen in Atlas ↗
6VERexperimentalX-ray1.05 AOpen in Atlas ↗
2OMIexperimentalX-ray2.24 AOpen in Atlas ↗
9UTJexperimentalX-ray1.95 AOpen in Atlas ↗
1OS4experimentalX-ray2.25 AOpen in Atlas ↗
5UU3experimentalX-ray2.25 AOpen in Atlas ↗
6CK2experimentalX-ray2.25 AOpen in Atlas ↗
4EFXexperimentalX-ray1.98 AOpen in Atlas ↗
8PI6experimentalX-ray2.14 AOpen in Atlas ↗
7QACexperimentalX-ray2.29 AOpen in Atlas ↗
1LPHexperimentalX-ray2.30 AOpen in Atlas ↗
1QIYexperimentalX-ray2.30 AOpen in Atlas ↗
1XW7experimentalX-ray2.30 AOpen in Atlas ↗
3P33experimentalX-ray2.30 AOpen in Atlas ↗
3ROVexperimentalX-ray2.30 AOpen in Atlas ↗
4EWWexperimentalX-ray2.30 AOpen in Atlas ↗
5EMSexperimentalX-ray2.30 AOpen in Atlas ↗
8ONIexperimentalX-ray2.30 AOpen in Atlas ↗
1HTVexperimentalX-ray1.90 AOpen in Atlas ↗
8ONPexperimentalX-ray1.77 AOpen in Atlas ↗
1QJ0experimentalX-ray2.40 AOpen in Atlas ↗
4GBKexperimentalX-ray2.40 AOpen in Atlas ↗
5URUexperimentalX-ray2.41 AOpen in Atlas ↗
6Z7WexperimentalX-ray2.42 AOpen in Atlas ↗
4AK0experimentalX-ray2.28 AOpen in Atlas ↗
9LVCexperimentalX-ray2.30 AOpen in Atlas ↗
8ONRexperimentalX-ray1.88 AOpen in Atlas ↗
2WS4experimentalX-ray1.90 AOpen in Atlas ↗
1B9EexperimentalX-ray2.50 AOpen in Atlas ↗
1JCAexperimentalX-ray2.50 AOpen in Atlas ↗
3JSDexperimentalX-ray2.50 AOpen in Atlas ↗
4GBIexperimentalX-ray2.50 AOpen in Atlas ↗
4GBLexperimentalX-ray2.50 AOpen in Atlas ↗
8Z4BexperimentalX-ray2.50 AOpen in Atlas ↗
9UTKexperimentalX-ray2.38 AOpen in Atlas ↗
2CEUexperimentalX-ray1.80 AOpen in Atlas ↗
9QLDexperimentalX-ray2.55 AOpen in Atlas ↗
6VETexperimentalX-ray1.46 AOpen in Atlas ↗
2W44experimentalX-ray2.00 AOpen in Atlas ↗
2WRVexperimentalX-ray2.15 AOpen in Atlas ↗
4UNHexperimentalX-ray2.75 AOpen in Atlas ↗
2WC0experimentalX-ray2.80 AOpen in Atlas ↗
9LVXexperimentalX-ray2.70 AOpen in Atlas ↗
6VEPexperimentalX-ray2.90 AOpen in Atlas ↗
8HSFexperimentalX-ray2.90 AOpen in Atlas ↗
2WRWexperimentalX-ray2.41 AOpen in Atlas ↗
25HLexperimentalX-ray2.85 AOpen in Atlas ↗
9LVDexperimentalX-ray2.85 AOpen in Atlas ↗
9LVYexperimentalX-ray2.85 AOpen in Atlas ↗
7RZIexperimentalEM3.00 AOpen in Atlas ↗
7U6EexperimentalEM3.00 AOpen in Atlas ↗
6VESexperimentalX-ray1.85 AOpen in Atlas ↗
9LVEexperimentalX-ray2.88 AOpen in Atlas ↗
1FUBexperimentalX-ray3.09 AOpen in Atlas ↗
7SL7experimentalEM3.10 AOpen in Atlas ↗
2WS7experimentalX-ray2.59 AOpen in Atlas ↗
6HN5experimentalEM3.20 AOpen in Atlas ↗
8SBDexperimentalEM3.20 AOpen in Atlas ↗
1FU2experimentalX-ray3.24 AOpen in Atlas ↗
7RZEexperimentalEM3.30 AOpen in Atlas ↗
7RZFexperimentalEM3.40 AOpen in Atlas ↗
7SL1experimentalEM3.40 AOpen in Atlas ↗
7SL3experimentalEM3.40 AOpen in Atlas ↗
8ONKexperimentalX-ray3.40 AOpen in Atlas ↗
4OGAexperimentalX-ray3.50 AOpen in Atlas ↗
7SL2experimentalEM3.60 AOpen in Atlas ↗
7V3PexperimentalEM3.60 AOpen in Atlas ↗
7SL6experimentalEM3.70 AOpen in Atlas ↗
5MWQexperimentalNMR-Open in Atlas ↗
2LGBexperimentalNMR-Open in Atlas ↗
2LWZexperimentalNMR-Open in Atlas ↗
5MHDexperimentalNMR-Open in Atlas ↗
6K59experimentalNMR-Open in Atlas ↗
3W11experimentalX-ray3.90 AOpen in Atlas ↗
6SOFexperimentalEM4.30 AOpen in Atlas ↗
7MD4experimentalEM4.50 AOpen in Atlas ↗
7QIDexperimentalEM5.00 AOpen in Atlas ↗
7SL4experimentalEM5.00 AOpen in Atlas ↗
7MD5experimentalEM5.20 AOpen in Atlas ↗
7PG2experimentalEM6.70 AOpen in Atlas ↗
7PG3experimentalEM7.30 AOpen in Atlas ↗
7PG0experimentalEM7.60 AOpen in Atlas ↗
7PG4experimentalEM9.10 AOpen in Atlas ↗
6JR3experimentalEM14.50 AOpen in Atlas ↗
1AI0experimentalNMR-Open in Atlas ↗
1AIYexperimentalNMR-Open in Atlas ↗
1HIQexperimentalNMR-Open in Atlas ↗
1HITexperimentalNMR-Open in Atlas ↗
1HLSexperimentalNMR-Open in Atlas ↗
1JCOexperimentalNMR-Open in Atlas ↗
1K3MexperimentalNMR-Open in Atlas ↗
1KMFexperimentalNMR-Open in Atlas ↗
1LKQexperimentalNMR-Open in Atlas ↗
1MHIexperimentalNMR-Open in Atlas ↗
1MHJexperimentalNMR-Open in Atlas ↗
1SF1experimentalNMR-Open in Atlas ↗
1T1KexperimentalNMR-Open in Atlas ↗
1T1PexperimentalNMR-Open in Atlas ↗
1T1QexperimentalNMR-Open in Atlas ↗
1VKTexperimentalNMR-Open in Atlas ↗
1XGLexperimentalNMR-Open in Atlas ↗
2AIYexperimentalNMR-Open in Atlas ↗
2H67experimentalNMR-Open in Atlas ↗
2HH4experimentalNMR-Open in Atlas ↗
2HHOexperimentalNMR-Open in Atlas ↗
2HIUexperimentalNMR-Open in Atlas ↗
2JMNexperimentalNMR-Open in Atlas ↗
2JUMexperimentalNMR-Open in Atlas ↗
2JUUexperimentalNMR-Open in Atlas ↗
2JUVexperimentalNMR-Open in Atlas ↗
2JV1experimentalNMR-Open in Atlas ↗
2JZQexperimentalNMR-Open in Atlas ↗
2K91experimentalNMR-Open in Atlas ↗
2K9RexperimentalNMR-Open in Atlas ↗
2KJJexperimentalNMR-Open in Atlas ↗
2KJUexperimentalNMR-Open in Atlas ↗
2KQQexperimentalNMR-Open in Atlas ↗
2KXKexperimentalNMR-Open in Atlas ↗
2L1YexperimentalNMR-Open in Atlas ↗
2L1ZexperimentalNMR-Open in Atlas ↗
2M1DexperimentalNMR-Open in Atlas ↗
2M1EexperimentalNMR-Open in Atlas ↗
2M2MexperimentalNMR-Open in Atlas ↗
2M2NexperimentalNMR-Open in Atlas ↗
2M2OexperimentalNMR-Open in Atlas ↗
2M2PexperimentalNMR-Open in Atlas ↗
2MLIexperimentalNMR-Open in Atlas ↗
2MPGexperimentalNMR-Open in Atlas ↗
2MPIexperimentalNMR-Open in Atlas ↗
2MVCexperimentalNMR-Open in Atlas ↗
2MVDexperimentalNMR-Open in Atlas ↗
2N2VexperimentalNMR-Open in Atlas ↗
2N2WexperimentalNMR-Open in Atlas ↗
2N2XexperimentalNMR-Open in Atlas ↗
2RN5experimentalNMR-Open in Atlas ↗
3AIYexperimentalNMR-Open in Atlas ↗
4AIYexperimentalNMR-Open in Atlas ↗
5AIYexperimentalNMR-Open in Atlas ↗
5WBTexperimentalNMR-Open in Atlas ↗
6X4XexperimentalNMR-Open in Atlas ↗
8RVTexperimentalNMR-Open in Atlas ↗
1A7FexperimentalNMR-Open in Atlas ↗
1IOGexperimentalNMR-Open in Atlas ↗
1IOHexperimentalNMR-Open in Atlas ↗
1SJTexperimentalNMR-Open in Atlas ↗
1HUIexperimentalNMR-Open in Atlas ↗
2WBYexperimentalX-ray2.60 AOpen in Atlas ↗
7MQOexperimentalEM3.40 AOpen in Atlas ↗
3W12experimentalX-ray4.30 AOpen in Atlas ↗
3W13experimentalX-ray4.30 AOpen in Atlas ↗
1HISexperimentalNMR-Open in Atlas ↗
7MQRexperimentalEM4.10 AOpen in Atlas ↗
7MQSexperimentalEM4.40 AOpen in Atlas ↗
2G56experimentalX-ray2.20 AOpen in Atlas ↗
2G54experimentalX-ray2.25 AOpen in Atlas ↗
9PUWexperimentalEM3.64 AOpen in Atlas ↗
1T0CexperimentalNMR-Open in Atlas ↗
9PVOexperimentalEM3.89 AOpen in Atlas ↗
3HYDexperimentalX-ray1.00 AOpen in Atlas ↗
4Y19experimentalX-ray2.50 AOpen in Atlas ↗
3UTQexperimentalX-ray1.67 AOpen in Atlas ↗
5C0DexperimentalX-ray1.68 AOpen in Atlas ↗
5CJOexperimentalX-ray3.29 AOpen in Atlas ↗
8VCXexperimentalX-ray2.59 AOpen in Atlas ↗
8VDDexperimentalX-ray2.60 AOpen in Atlas ↗
1JK8experimentalX-ray2.40 AOpen in Atlas ↗
4Z77experimentalX-ray1.85 AOpen in Atlas ↗
7YQ3experimentalEM3.60 AOpen in Atlas ↗
4Z76experimentalX-ray1.88 AOpen in Atlas ↗
4Z78experimentalX-ray2.30 AOpen in Atlas ↗
7YQ4experimentalEM3.95 AOpen in Atlas ↗
8GUYexperimentalEM4.18 AOpen in Atlas ↗
7YQ5experimentalEM4.27 AOpen in Atlas ↗
6CE9experimentalEM4.30 AOpen in Atlas ↗
6CEBexperimentalEM4.70 AOpen in Atlas ↗
6CE7experimentalEM7.40 AOpen in Atlas ↗
4WDIexperimentalX-ray2.31 AOpen in Atlas ↗
5WOBexperimentalX-ray3.95 AOpen in Atlas ↗
2OMQexperimentalX-ray2.00 AOpen in Atlas ↗
3UTTexperimentalX-ray2.60 AOpen in Atlas ↗
7NMGexperimentalX-ray2.48 AOpen in Atlas ↗
3UTSexperimentalX-ray2.71 AOpen in Atlas ↗
5HYJexperimentalX-ray3.06 AOpen in Atlas ↗
4Y1AexperimentalX-ray4.00 AOpen in Atlas ↗
AF-P01308-F1predictedAlphaFoldNot applicableOpen in Atlas ↗
09

Family & Domains

Belongs to the insulin family

Curator inference
Evidence & references
  • ECO:0000305
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000305"
        }
      ],
      "value": "Belongs to the insulin family"
    }
  ],
  "commentType": "SIMILARITY"
}

Domain architecture

Canonical sequence1110 aa
Coverage
Domains & repeats
Variants
Processing

Canonical coordinates. Overlapping marks share a lane; individual records and evidence are in the tables below. Gaps in coverage are not selectable in 3D. Use the track links and tables for keyboard inspection.

Atlas domains, motifs & repeats 1

Scroll across the table for evidence and actions.

1 recorded rows

AnnotationPositionSource & interpretationInspect
Insulin-likeIPR01617928–109INTERPROdomain

This entry represents a disulphide-rich α-helical domain found in insulin, as well as in related proteins, such as insulin-like growth factor, relaxin and bombyxin. Insulin is found in many animals, and is involved in the regulation of normal glucose homeostasis.

Full source description

This entry represents a disulphide-rich α-helical domain found in insulin, as well as in related proteins, such as insulin-like growth factor, relaxin and bombyxin. Insulin is found in many animals, and is involved in the regulation of normal glucose homeostasis. It also has other specific physiological effects, such as increasing the permeability of cells to monosaccharides, amino acids and fatty acids, and accelerating glycolysis and glycogen synthesis in the liver. Insulin exerts its effects by interaction with a cell-surface receptor, which may also result in the promotion of cell growth. The insulin/IGF/relaxin superfamily is an ancient family of functionally diverse proteins. The 3D structures of a number of family members have been determined. The fold comprises two polypeptide chains (A and B) linked by two disulphide bonds: all share a conserved arrangement of four cysteines in their A chain, the first of which is linked by a disulfide bond to the third, while the second and fourth are linked by interchain disulfide bonds to cysteines in the B chain. This family includes: Insulin and insulin-like proteins Relaxin and prorelaxin Insect prothoracicotropic hormone (bombyxin) Insulin-like growth factors (IGF1 and IGF2) Mammalian Leydig cell-specific insulin-like peptide (gene INSL3) Invertebrates insulin-related peptides (IRPs)

Source entry ↗		47/82 residues mapped to 6TC2

UniProt domains, repeats & motifs 0

No annotation is recorded in this UniProt entry.

Functional sites 0

No annotation is recorded in this UniProt entry.

Sequence regions 0

No annotation is recorded in this UniProt entry.

10

Sequence & Isoforms

Sequence & isoforms

UniProt’s canonical sequence is its selected representative. It is not necessarily the dominant isoform in every tissue.

UniProt’s canonical sequence · P01308-1110 aa11,981 Da · source sequence mass

Full precursor sequence, including processing regions. The mass describes this unmodified source sequence, not every mature or modified product.

MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN

Source isoform notes & selection

Alternative splicing

Complete source annotation
{
  "commentType": "ALTERNATIVE PRODUCTS",
  "events": [
    "Alternative splicing"
  ],
  "isoforms": [
    {
      "name": {
        "value": "1"
      },
      "isoformIds": [
        "P01308-1"
      ],
      "isoformSequenceStatus": "Displayed"
    },
    {
      "name": {
        "value": "2"
      },
      "synonyms": [
        {
          "value": "INS-IGF2"
        }
      ],
      "isoformIds": [
        "F8WCM5-1"
      ],
      "isoformSequenceStatus": "External"
    }
  ]
}
  • P01308-1 · 1 · Displayed
    Complete source annotation
    {
  "name": {
    "value": "1"
  },
  "isoformIds": [
    "P01308-1"
  ],
  "isoformSequenceStatus": "Displayed"
}
  • F8WCM5-1 · 2 · External · INS-IGF2
    Complete source annotation
    {
  "name": {
    "value": "2"
  },
  "synonyms": [
    {
      "value": "INS-IGF2"
    }
  ],
  "isoformIds": [
    "F8WCM5-1"
  ],
  "isoformSequenceStatus": "External"
}

Isoform sequence differences 0

No annotation is recorded in this UniProt entry.

Sequence conflicts & cautions 0

No annotation is recorded in this UniProt entry.

Erroneous gene model prediction

Source sequence: AAA59179.1

Curator inference
Evidence & references
  • ECO:0000305

Recorded secondary structure 14

Scroll across the table for evidence and actions.

14 recorded rows

FeaturePositionDescriptionEvidenceInspect
Helix25–27Helix
Evidence & references
  • ECO:0007829 PDB:8HSK
3/3 residues mapped to 6TC2
Helix28–31Helix
Evidence & references
  • ECO:0007829 PDB:1AIY
4/4 residues mapped to 6TC2
Helix33–43Helix
Evidence & references
  • ECO:0007829 PDB:3W7Y
11/11 residues mapped to 6TC2
Helix44–46Helix
Evidence & references
  • ECO:0007829 PDB:3W7Y
3/3 residues mapped to 6TC2
Beta strand48–50Beta strand
Evidence & references
  • ECO:0007829 PDB:3W7Y
3/3 residues mapped to 6TC2
Beta strand56–58Beta strand
Evidence & references
  • ECO:0007829 PDB:1EFE
No verified residues in this structure
Turn59–66Turn
Evidence & references
  • ECO:0007829 PDB:1T0C
No verified residues in this structure
Helix72–75Helix
Evidence & references
  • ECO:0007829 PDB:8VCX
No verified residues in this structure
Helix79–81Helix
Evidence & references
  • ECO:0007829 PDB:1T0C
No verified residues in this structure
Helix83–87Helix
Evidence & references
  • ECO:0007829 PDB:4Y19
No verified residues in this structure
Helix91–97Helix
Evidence & references
  • ECO:0007829 PDB:3W7Y
7/7 residues mapped to 6TC2
Beta strand98–101Beta strand
Evidence & references
  • ECO:0007829 PDB:4EFX
4/4 residues mapped to 6TC2
Helix102–106Helix
Evidence & references
  • ECO:0007829 PDB:3W7Y
5/5 residues mapped to 6TC2
Turn107–109Turn
Evidence & references
  • ECO:0007829 PDB:1HIQ
3/3 residues mapped to 6TC2
12

Homologs

OMA orthologs

Evolutionary relationships assigned by OMA, kept separate from sequence clusters. “1:1” describes an orthology relationship, not percentage identity.

Recorded preview of up to 12 orthologs; not an exhaustive list. Entries without a verified UniProt mapping open their OMA record.

XP_032894479.1Amblyraja radiata1:1OMA record ↗
A0A401SFM9Chiloscyllium punctatum1:1OMA record ↗
A0A4W3I9K0Callorhinchus milii1:1OMA record ↗
XP_035288546.1Anguilla anguilla1:nOMA record ↗
XP_035288548.1Anguilla anguilla1:nOMA record ↗
XP_035288545.1Anguilla anguilla1:nOMA record ↗
A0A9D3RJ02Anguilla anguilla1:nOMA record ↗
A0A672SA64Sinocyclocheilus grahami1:nOMA record ↗
A0A672JV68Sinocyclocheilus grahami1:nOMA record ↗
INS_DANREDanio rerio1:nOMA record ↗
INS_DANREDanio rerio1:nOMA record ↗
Q2QAJ9Danio rerio1:nOMA record ↗
13

Sources & References

Scientific descriptions and evidence come from the named sources. Atlas assembles the presentation and verifies residue mappings; it does not independently curate these claims.

UniProt ↗QuickGO ↗InterPro ↗PDB / PDBe ↗Complex Portal ↗UniRef ↗OMA ↗
Source dates & provenance

Recorded 2026-11-10. Source dates and identifiers are retained below.

Publications in this UniProt entry

1 · Sequence of the human insulin gene.

1980 · Nature

PubMed 6243748 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]

Bell G.I., Pictet R.L., Rutter W.J., Cordell B., Tischer E., Goodman H.M.

2 · Genetic variation in the human insulin gene.

1980 · Science

PubMed 6248962 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]

Ullrich A., Dull T.J., Gray A., Brosius J., Sures I.

3 · Nucleotide sequence of a cDNA clone encoding human preproinsulin.

1979 · Nature

PubMed 503234 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]

Bell G.I., Swain W.F., Pictet R.L., Cordell B., Goodman H.M., Rutter W.J.

4 · Nucleotide sequence of human preproinsulin complementary DNA.

1980 · Science

PubMed 6927840 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]

Sures I., Goeddel D.V., Gray A., Ullrich A.

All source publications (43)
5 · Susceptibility to insulin dependent diabetes mellitus maps to a 4.1 kb segment of DNA spanning the insulin gene and associated VNTR.

1993 · Nat. Genet.

PubMed 8358440 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]

Lucassen A.M., Julier C., Beressi J.-P., Boitard C., Froguel P., Lathrop M., Bell J.I.

6 · Insulinomas and expression of an insulin splice variant.

2004 · Lancet

PubMed 15070567 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA]

Minn A.H., Kayton M., Lorang D., Hoffmann S.C., Harlan D.M., Libutti S.K., Shalev A.

7 · Global haplotype diversity in the human insulin gene region.

2003 · Genome Res.

PubMed 12952878 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]

Stead J.D.H., Hurles M.E., Jeffreys A.J.

· Cloning of human full-length CDSs in BD Creator(TM) system donor vector.

OCT-2004 ·

Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]

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.

· Reference

JUL-2005 ·

Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.

10 · The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

2004 · Genome Res.

PubMed 15489334 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]

· Description of a novel RFLP diallelic polymorphism (-127 BsgI C/G) within the 5' region of insulin gene.

JUL-1998 ·

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59

Fajardy I.I., Weill J.J., Stuckens C.C., Danze P.M.P.

12 · Amino-acid sequence of human insulin.

1960 · Nature

PubMed 14426955 ↗
Scope & authors

PROTEIN SEQUENCE OF 25-54 AND 90-110

Nicol D.S.H.W., Smith L.F.

13 · Studies on human proinsulin. Isolation and amino acid sequence of the human pancreatic C-peptide.

1971 · J. Biol. Chem.

PubMed 5101771 ↗
Scope & authors

PROTEIN SEQUENCE OF 57-87

Oyer P.E., Cho S., Peterson J.D., Steiner D.F.

14 · The amino acid sequence of the C-peptide of human proinsulin.

1971 · Eur. J. Biochem.

PubMed 5560404 ↗
Scope & authors

PROTEIN SEQUENCE OF 57-87

Ko A., Smyth D.G., Markussen J., Sundby F.

15 · Total synthesis of human insulin under directed formation of the disulfide bonds.

1974 · Helv. Chim. Acta

PubMed 4443293 ↗
Scope & authors

SYNTHESIS

Sieber P., Kamber B., Hartmann A., Joehl A., Riniker B., Rittel W.

16 · Studies on polypeptides, IV. The synthesis of C-peptide of human proinsulin.

1973 · Hoppe-Seyler's Z. Physiol. Chem.

PubMed 4803504 ↗
Scope & authors

SYNTHESIS OF 57-87

Naithani V.K.

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.

1973 · Chem. Ber.

PubMed 4698555 ↗
Scope & authors

SYNTHESIS OF 65-69 AND 70-73

Geiger R., Volk A.

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.

1973 · Chem. Ber.

PubMed 4698553 ↗
Scope & authors

SYNTHESIS OF 84-87

Geiger R., Jaeger G., Keonig W., Treuth G.

19 · Revisiting Proinsulin Processing: Evidence That Human beta-Cells Process Proinsulin With Prohormone Convertase (PC) 1/3 but Not PC2.

2020 · Diabetes

PubMed 32291281 ↗
Scope & authors

PROCESSING

Ramzy A., Asadi A., Kieffer T.J.

20 · Desmoglein-2 is important for islet function and beta-cell survival.

2022 · Cell Death Dis.

PubMed 36309486 ↗
Scope & authors

SUBCELLULAR LOCATION; TISSUE SPECIFICITY

Myo Min K.K., Rojas-Canales D., Penko D., DeNichilo M., Cockshell M.P., Ffrench C.B., Thompson E.J., Asplund O., Drogemuller C.J., Prasad R.B., Groop L., Grey S.T., Thomas H.E., Loudovaris T., Kay T.W., Mahoney M.G., Jessup C.F., Coates P.T., Bonder C.S.

21 · Studies on mutant human insulin genes: identification and sequence analysis of a gene encoding [SerB24]insulin.

1983 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 6312455 ↗
Scope & authors

VARIANT HPRI SER-48

Haneda M., Chan S.J., Kwok S.C.M., Rubenstein A.H., Steiner D.F.

22 · Identification of a mutant human insulin predicted to contain a serine-for-phenylalanine substitution.

1983 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 6424111 ↗
Scope & authors

VARIANT HPRI SER-48; VARIANT LEU-49

Shoelson S., Fickova M., Haneda M., Nahum A., Musso G., Kaiser E.T., Rubenstein A.H., Tager H.

23 · A mutation in the B chain coding region is associated with impaired proinsulin conversion in a family with hyperproinsulinemia.

1987 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 3470784 ↗
Scope & authors

VARIANT HPRI ASP-34

Chan S.J., Seino S., Gruppuso P.A., Schwartz R., Steiner D.F.

24 · Structurally abnormal insulin in a diabetic patient. Characterization of the mutant insulin A3 (Val-->Leu) isolated from the pancreas.

1986 · J. Clin. Invest.

PubMed 3537011 ↗
Scope & authors

VARIANT WAKAYAMA LEU-92

Sakura H., Iwamoto Y., Sakamoto Y., Kuzuya T., Hirata H.

25 · 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.

1990 · J. Clin. Endocrinol. Metab.

PubMed 2196279 ↗
Scope & authors

VARIANT HPRI HIS-89

Barbetti F., Raben N., Kadowaki T., Cama A., Accili D., Gabbay K.H., Merenich J.A., Taylor S.I., Roth J.

26 · Posttranslational cleavage of proinsulin is blocked by a point mutation in familial hyperproinsulinemia.

1985 · J. Clin. Invest.

PubMed 4019786 ↗
Scope & authors

VARIANT HPRI HIS-89

Shibasaki Y., Kawakami T., Kanazawa Y., Akanuma Y., Takaku F.

27 · A novel point mutation in the human insulin gene giving rise to hyperproinsulinemia (proinsulin Kyoto).

1992 · J. Clin. Invest.

PubMed 1601997 ↗
Scope & authors

VARIANT HPRI LEU-89

Yano H., Kitano N., Morimoto M., Polonsky K.S., Imura H., Seino Y.

28 · Toward the solution structure of human insulin: sequential 2D 1H NMR assignment of a des-pentapeptide analogue and comparison with crystal structure.

1990 · Biochemistry

PubMed 2271664 ↗
Scope & authors

STRUCTURE BY NMR

Hua Q.-X., Weiss M.A.

29 · Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition.

1991 · Biochemistry

PubMed 2036420 ↗
Scope & authors

STRUCTURE BY NMR

Hua Q.-X., Weiss M.A.

30 · Two-dimensional NMR studies of Des-(B26-B30)-insulin: sequence-specific resonance assignments and effects of solvent composition.

1991 · Biochim. Biophys. Acta

PubMed 1646635 ↗
Scope & authors

STRUCTURE BY NMR

Hua Q.-X., Weiss M.A.

31 · 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.

1992 · J. Mol. Biol.

PubMed 1433291 ↗
Scope & authors

STRUCTURE BY NMR OF 90-110 AND 25-54; DISULFIDE BONDS

Joergensen A.M.M., Kristensen S.M., Led J.J., Balschmidt P.

32 · Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus.

1993 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 8421693 ↗
Scope & authors

STRUCTURE BY NMR OF 90-110 AND 25-54 OF VARIANT HPRI SER-48; DISULFIDE BONDS

Hua Q.-X., Shoelson S.E., Inouye K., Weiss M.A.

33 · Insulin-induced activation of phosphatidyl inositol 3-kinase. Demonstration that the p85 subunit binds directly to the COOH terminus of the insulin receptor in intact cells.

1994 · J. Biol. Chem.

PubMed 7983060 ↗
Scope & authors

FUNCTION

Levy-Toledano R., Taouis M., Blaettler D.H., Gorden P., Taylor S.I.

34 · Inhibition of glycogen synthase kinase-3 by insulin in cultured human skeletal muscle myoblasts.

1995 · Biochem. Biophys. Res. Commun.

PubMed 7763247 ↗
Scope & authors

FUNCTION

Borthwick A.C., Wells A.M., Rochford J.J., Hurel S.J., Turnbull D.M., Yeaman S.J.

35 · Solution structures of the R6 human insulin hexamer.

1997 · Biochemistry

PubMed 9235985 ↗
Scope & authors

STRUCTURE BY NMR OF 90-110 AND 25-54; DISULFIDE BONDS

Chang X., Joergensen A.M., Bardrum P., Led J.J.

36 · Exercise and insulin cause GLUT-4 translocation in human skeletal muscle.

1999 · Am. J. Physiol.

PubMed 10516134 ↗
Scope & authors

FUNCTION

Thorell A., Hirshman M.F., Nygren J., Jorfeldt L., Wojtaszewski J.F., Dufresne S.D., Horton E.S., Ljungqvist O., Goodyear L.J.

37 · Insulin-regulated hepatic gluconeogenesis through FOXO1-PGC-1alpha interaction.

2003 · Nature

PubMed 12754525 ↗
Scope & authors

FUNCTION

Puigserver P., Rhee J., Donovan J., Walkey C.J., Yoon J.C., Oriente F., Kitamura Y., Altomonte J., Dong H., Accili D., Spiegelman B.M.

38 · The human fatty acid synthase gene and de novo lipogenesis are coordinately regulated in human adipose tissue.

2004 · J. Nutr.

PubMed 15113941 ↗
Scope & authors

FUNCTION

Wang Y., Jones Voy B., Urs S., Kim S., Soltani-Bejnood M., Quigley N., Heo Y.R., Standridge M., Andersen B., Dhar M., Joshi R., Wortman P., Taylor J.W., Chun J., Leuze M., Claycombe K., Saxton A.M., Moustaid-Moussa N.

39 · Insulin gene mutations as a cause of permanent neonatal diabetes.

2007 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 17855560 ↗
Scope & authors

VARIANTS PNDM4 ASP-24; ARG-32; SER-32; GLY-43; VAL-47; CYS-48; CYS-89; CYS-90; TYR-96 AND CYS-108

Stoy J., Edghill E.L., Flanagan S.E., Ye H., Paz V.P., Pluzhnikov A., Below J.E., Hayes M.G., Cox N.J., Lipkind G.M., Lipton R.B., Greeley S.A., Patch A.M., Ellard S., Steiner D.F., Hattersley A.T., Philipson L.H., Bell G.I.

40 · 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.

2008 · Diabetes

PubMed 18162506 ↗
Scope & authors

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

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.

41 · Mutations in the insulin gene can cause MODY and autoantibody-negative type 1 diabetes.

2008 · Diabetes

PubMed 18192540 ↗
Scope & authors

VARIANT MODY10 GLN-46; VARIANT T1D2 CYS-55

Molven A., Ringdal M., Nordbo A.M., Raeder H., Stoy J., Lipkind G.M., Steiner D.F., Philipson L.H., Bergmann I., Aarskog D., Undlien D.E., Joner G., Sovik O., Bell G.I., Njolstad P.R.

42 · Further evidence that mutations in INS can be a rare cause of Maturity-Onset Diabetes of the Young (MODY).

2010 · BMC Med. Genet.

PubMed 20226046 ↗
Scope & authors

VARIANTS MODY10 HIS-6 AND GLN-46

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.

43 · Structural and functional study of the GlnB22-insulin mutant responsible for maturity-onset diabetes of the young.

2014 · PLoS ONE

PubMed 25423173 ↗
Scope & authors

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

Krizkova K., Veverka V., Maletinska L., Hexnerova R., Brzozowski A.M., Jiracek J., Zakova L.

Protein Spotlight ↗

Wikipedia ↗

Annotation coverage audit

Every recorded UniProt comment and feature has a destination in this page. GO, Atlas annotations and interaction rows retain their separate source counts.

64 source comments and features accounted for.

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Source recordTypeSection
FUNCTION:0FUNCTIONfunction
SUBUNIT:0SUBUNITinteractions
INTERACTION:0INTERACTIONinteractions
SUBCELLULAR LOCATION:0SUBCELLULAR LOCATIONlocation
ALTERNATIVE PRODUCTS:0ALTERNATIVE PRODUCTSsequence
TISSUE SPECIFICITY:0TISSUE SPECIFICITYexpression
PTM:0PTMprocessing
DISEASE:0DISEASEdisease
DISEASE:1DISEASEdisease
DISEASE:2DISEASEdisease
DISEASE:3DISEASEdisease
PHARMACEUTICAL:0PHARMACEUTICALfunction
SIMILARITY:0SIMILARITYdomains
SEQUENCE CAUTION:0SEQUENCE CAUTIONsequence
WEB RESOURCE:0WEB RESOURCEsources
WEB RESOURCE:1WEB RESOURCEsources
feature-0Signalprocessing
feature-1Peptideprocessing
feature-2Propeptideprocessing
feature-3Peptideprocessing
feature-4Disulfide bondprocessing
feature-5Disulfide bondprocessing
feature-6Disulfide bondprocessing
feature-7Natural variantdisease
feature-8Natural variantdisease
feature-9Natural variantdisease
feature-10Natural variantdisease
feature-11Natural variantdisease
feature-12Natural variantdisease
feature-13Natural variantdisease
feature-14Natural variantdisease
feature-15Natural variantdisease
feature-16Natural variantdisease
feature-17Natural variantdisease
feature-18Natural variantdisease
feature-19Natural variantdisease
feature-20Natural variantdisease
feature-21Natural variantdisease
feature-22Natural variantdisease
feature-23Natural variantdisease
feature-24Natural variantdisease
feature-25Natural variantdisease
feature-26Natural variantdisease
feature-27Natural variantdisease
feature-28Natural variantdisease
feature-29Natural variantdisease
feature-30Natural variantdisease
feature-31Natural variantdisease
feature-32Natural variantdisease
feature-33Natural variantdisease
feature-34Helixsequence
feature-35Helixsequence
feature-36Helixsequence
feature-37Helixsequence
feature-38Beta strandsequence
feature-39Beta strandsequence
feature-40Turnsequence
feature-41Helixsequence
feature-42Helixsequence
feature-43Helixsequence
feature-44Helixsequence
feature-45Beta strandsequence
feature-46Helixsequence
feature-47Turnsequence