Contents

Search


insulin receptor-related protein; IR-related receptor; contains: insulin receptor-related protein alpha chain & insulin receptor-related protein beta chain (INSRR, IRR)

Function: - probably binds an insulin related protein - has a tyrosine-protein kinase activity - phosphorylates insulin receptor substrates IRS-1 & IRS-2 Structure: - probable tetramer of 2 alpha & 2 beta chains linked by disulfide bonds - the alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain - belongs to the protein kinase superfamily, Tyr protein kinase family, insulin receptor subfamily - contains 4 fibronectin F3 modules - contains 1 protein kinase domain Compartment: membrane

General

glycoprotein tyrosine kinase receptor (RTK)

Properties

SIZE: entity length = 1297 aa MW = 144 kD COMPARTMENT: cellular membrane STATE: active state MOTIF: signal sequence {1-26} N-glycosylation site {N47} cysteine residue {C214} MODIFICATION: cysteine residue {C222} cysteine residue {C216} MODIFICATION: cysteine residue {C228} cysteine residue {C222} MODIFICATION: cysteine residue {C214} cysteine residue {C228} MODIFICATION: cysteine residue {C216} cysteine residue {C229} MODIFICATION: cysteine residue {C237} cysteine residue {C233} MODIFICATION: cysteine residue {C246} cysteine residue {C237} MODIFICATION: cysteine residue {C229} cysteine residue {C246} MODIFICATION: cysteine residue {C233} cysteine residue {C249} MODIFICATION: cysteine residue {C258} cysteine residue {C258} MODIFICATION: cysteine residue {C249} cysteine residue {C262} MODIFICATION: cysteine residue {C274} cysteine residue {C274} MODIFICATION: cysteine residue {C262} cysteine residue {C280} MODIFICATION: cysteine residue {C300} cysteine residue {C300} MODIFICATION: cysteine residue {C280} cysteine residue {C304} MODIFICATION: cysteine residue {C317} N-glycosylation site {N311} cysteine residue {C317} MODIFICATION: cysteine residue {C304} cysteine residue {C320} MODIFICATION: cysteine residue {C324} cysteine residue {C324} MODIFICATION: cysteine residue {C320} N-glycosylation site {N411} fibronectin type III domain or F3 module {484-594} MOTIF: N-glycosylation site {N492} N-glycosylation site {N528} fibronectin type III domain or F3 module {605-686} MOTIF: N-glycosylation site {N616} N-glycosylation site {N634} cysteine residue {C657} MODIFICATION: cysteine residue {C-INTERCHAIN} fibronectin type III domain or F3 module {724-805} MOTIF: N-glycosylation site {N756} fibronectin type III domain or F3 module {815-909} MOTIF: N-glycosylation site {N885} N-glycosylation site {N898} transmembrane domain {922-943} kinase domain SITE: 979-1254 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 985-993 ATP-binding site NAME: ATP-binding site SITE: 1013-1013 aspartate residue {D1115} Tyr phosphorylation site {Y1145}

Database Correlations

OMIM 147671 UniProt P14616 PFAM correlations Kegg hsa:3645 ENZYME 2.7.10.1

References

UniProt :accession P14616