Protein Domain : IPR001426

Type:  Conserved_site Name:  Tyrosine-protein kinase, receptor class V, conserved site
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 [].A number of growth factors stimulate mitogenesis by interacting with a familyof cell surface receptors which possess an intrinsic, ligand-sensitive,protein tyrosine kinase activity []. These receptor tyrosine kinases (RTK)all share the same topology: an extracellular ligand-binding domain, a singletransmembrane region and a cytoplasmic kinase domain and have beenclassified into at least five groups on the basis of sequence similarities.The extracellular domain of class V RTK's has 16 conserved cysteine residues that are probably involved indisulphide bonds; this region is followed by two copies of a fibronectin typeIII domain. The ligands for these receptors are proteins known as ephrins. The EPHA subtype receptors bind to GPI-anchored ephrins while the EPHB subtypereceptors bind to type-I membrane ephrins. Short Name:  Tyr_kinase_rcpt_V_CS

0 Child Features

0 Contains

2 Cross Referencess

Identifier
PS00790
PS00791

4 Found Ins

DB identifier Type Name
IPR008979 Domain Galactose-binding domain-like
IPR020766 Family Receptor-like tyrosine-protein kinase kin-15/kin-16
IPR001090 Domain Ephrin receptor ligand binding domain
IPR016257 Family Ephrin receptor type-A /type-B

5 GO Annotations

GO Term Gene Name Organism
GO:0005003 IPR001426
GO:0005524 IPR001426
GO:0006468 IPR001426
GO:0007169 IPR001426
GO:0016021 IPR001426

0 Parent Features

0 Proteins

9 Publications

First Author Title Year Journal Volume Pages PubMed ID
            3291115
            12368087
            12471243
            15078142
            15320712
            3052279
            19275641
            16700535
            15845350