Protein Domain : IPR011641

Type:  Domain Name:  Tyrosine-protein kinase ephrin type A/B receptor-like
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 various ephrin type A and B receptors, which have tyrosine kinase activity. Short Name:  Tyr-kin_ephrin_A/B_rcpt-like

0 Child Features

0 Contains

1 Cross References

Identifier
PF07699

2 Found Ins

DB identifier Type Name
IPR009030 Domain Insulin-like growth factor binding protein, N-terminal
IPR016257 Family Ephrin receptor type-A /type-B

0 GO Annotation

0 Ontology Annotations

0 Parent Features

32 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
47747 I0YX10 PAC:27388743 Coccomyxa subellipsoidea C-169 1337  
71069 C1N4C1 PAC:27339826 Micromonas pusilla CCMP1545 3898  
53165 PAC:27342419 Micromonas pusilla CCMP1545 593  
169231 PAC:27346232 Micromonas pusilla CCMP1545 2242  
155662 PAC:27341424 Micromonas pusilla CCMP1545 217  
57780 C1MSQ5 PAC:27341411 Micromonas pusilla CCMP1545 1516  
58389 PAC:27341290 Micromonas pusilla CCMP1545 1345  
170439 PAC:27348058 Micromonas pusilla CCMP1545 306  
61687 C1FHY3 PAC:27397583 Micromonas sp RCC299 3770  
109052 C1FHB4 PAC:27397353 Micromonas sp RCC299 329  
68421 C1FGM9 PAC:27403298 Micromonas sp RCC299 248  
55832 C1DYT6 PAC:27396142 Micromonas sp RCC299 2297  
59639 C1E983 PAC:27401931 Micromonas sp RCC299 1724  
10107 A4RRT8 PAC:27417892 Ostreococcus lucimarinus 331  
10106 PAC:27415507 Ostreococcus lucimarinus 279  
32006 A4RYF1 PAC:27418529 Ostreococcus lucimarinus 366  
93102 A4S0Z6 PAC:27419381 Ostreococcus lucimarinus 1360  
Cre01.g044350.t1.1 A0A2K3E7M6 PAC:30789607 Chlamydomonas reinhardtii 1558  
Cre10.g421050.t1.1 A0A2K3D966 PAC:30790932 Chlamydomonas reinhardtii 1459  
Cre12.g488351.t1.1 A0A2K3D288 PAC:30792775 Chlamydomonas reinhardtii 604  
Cre14.g630700.t2.1 A0A2K3CYP3 PAC:30776586 Chlamydomonas reinhardtii 950  
Cre14.g630700.t1.2 A0A2K3CYP3 PAC:30776585 Chlamydomonas reinhardtii 950  
Cre16.g650600.t1.2 A8J9H7 PAC:30777876 Chlamydomonas reinhardtii 1987  
Cre04.g215900.t1.1 A0A2K3DTN7 PAC:30791612 Chlamydomonas reinhardtii 952  
Cre04.g215700.t1.2 A0A2K3DTR6 PAC:30791087 Chlamydomonas reinhardtii 880  
Cre06.g309900.t1.2 A0A2K3DRK8 PAC:30779116 Chlamydomonas reinhardtii 928  
Dusal.0025s00015.1.p PAC:33200681 Dunaliella salina 934  
Cz11g14050.t1 PAC:38237650 Chromochloris zofingiensis 850  
Cz19g10200.t1 PAC:38241889 Chromochloris zofingiensis 379  
Bobra.0352s0001.1.p PAC:40706925 Botryococcus braunii 1499  

8 Publications

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