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8VJC

Cryo-EM structure of short form insulin receptor (IR-A) with three IGF2 bound, asymmetric conformation.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
A0016020cellular_componentmembrane
A0043548molecular_functionphosphatidylinositol 3-kinase binding
A0043560molecular_functioninsulin receptor substrate binding
A0046777biological_processprotein autophosphorylation
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
B0016020cellular_componentmembrane
B0043548molecular_functionphosphatidylinositol 3-kinase binding
B0043560molecular_functioninsulin receptor substrate binding
B0046777biological_processprotein autophosphorylation
C0005179molecular_functionhormone activity
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0008083molecular_functiongrowth factor activity
D0005179molecular_functionhormone activity
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0008083molecular_functiongrowth factor activity
E0005179molecular_functionhormone activity
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0008083molecular_functiongrowth factor activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnardiikgeaetr.....VAVK
ChainResidueDetails
ALEU990-LYS1018

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
ChainResidueDetails
APHE1116-VAL1128

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR
ChainResidueDetails
AASP1144-ARG1152

site_idPS00262
Number of Residues15
DetailsINSULIN Insulin family signature. CCFRsCDlalLetyC
ChainResidueDetails
CCYS46-CYS60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsRegion: {"description":"Insulin-binding"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Insulin-binding","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16894147","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23302862","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2983222","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16894147","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23302862","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16894147","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23302862","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16894147","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16894147","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1472036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues5
DetailsSite: {"description":"Important for interaction with integrin","evidences":[{"source":"PubMed","id":"28873464","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues40
DetailsRegion: {"description":"A"}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 246
ChainResidueDetails

site_idMCSA2
Number of Residues
DetailsM-CSA 246
ChainResidueDetails

238895

PDB entries from 2025-07-16

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