Protein Domain : IPR016246

Type:  Family Name:  Tyrosine-protein kinase, insulin-like receptor
Description:  Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].Tyrosine-protein kinases can transfer a phosphate group from ATP to a tyrosine residue in a protein. These enzymes can be divided into two main groups []:Receptor tyrosine kinases (RTK), which are transmembrane proteins involved in signal transduction; they play key roles in growth, differentiation, metabolism, adhesion, motility, death and oncogenesis []. RTKs are composed of 3 domains: an extracellular domain (binds ligand), a transmembrane (TM) domain, and an intracellular catalytic domain (phosphorylates substrate). The TM domain plays an important role in the dimerisation process necessary for signal transduction []. Cytoplasmic / non-receptor tyrosine kinases, which act as regulatory proteins, playing key roles in cell differentiation, motility, proliferation, and survival. For example, the Src-family of protein-tyrosine kinases [].This entry represents the insulin receptor, as well as related insulin-like receptors. The insulin receptor binds insulin and has a tyrosine-protein kinase activity, and mediates the metabolic functions of insulin. Binding to insulin stimulates the association of the receptor with downstream mediators, including IRS1 and phosphatidylinositol 3'-kinase (PI3K). The insulin receptor can activate PI3K either directly by binding to the p85 regulatory subunit, or indirectly via IRS1. When the insulin receptor is present in a hybrid receptor with IGF1R (insulin growth factor receptor), it binds IGF1 (insulin growth factor 1) [, , ]. Short Name:  Tyr_kinase_insulin-like_rcpt

1 Child Features

DB identifier Type Name
IPR028792 Family Insulin receptor-related protein

12 Contains

DB identifier Type Name
IPR000719 Domain Protein kinase domain
IPR011009 Domain Protein kinase-like domain
IPR020635 Domain Tyrosine-protein kinase, catalytic domain
IPR001245 Domain Serine-threonine/tyrosine-protein kinase catalytic domain
IPR009030 Domain Insulin-like growth factor binding protein, N-terminal
IPR003961 Domain Fibronectin type III
IPR000494 Domain Receptor L-domain
IPR006212 Repeat Furin-like repeat
IPR017441 Binding_site Protein kinase, ATP binding site
IPR008266 Active_site Tyrosine-protein kinase, active site
IPR006211 Domain Furin-like cysteine-rich domain
IPR002011 Conserved_site Tyrosine-protein kinase, receptor class II, conserved site

1 Cross References


0 Found In

8 GO Annotations

GO Term Gene Name Organism
GO:0004714 IPR016246
GO:0005524 IPR016246
GO:0043548 IPR016246
GO:0043560 IPR016246
GO:0006468 IPR016246
GO:0007169 IPR016246
GO:0046777 IPR016246
GO:0016021 IPR016246

0 Parent Features

0 Proteins

11 Publications

First Author Title Year Journal Volume Pages PubMed ID