Literature summary for 2.7.10.1 extracted from

Singla, N.; Erdjument-Bromage, H.; Himanen, J.; Muir, T.; Nikolov, D.
A semisynthetic Eph receptor tyrosine kinase provides insight into ligand-induced kinase activation (2011), Chem. Biol., 18, 361-371.

Search for more literature for 2.7.10.1

Application

Application	Comment	Organism
synthesis	methodology for generating milligram amounts of functional Eph tyrosine kinase receptor using the protein engineering approach of expressed protein ligation. Stimulation with ligand induces efficient autophosphorylation of the semisynthetic Eph construct. The in vitro phosphorylation of key Eph tyrosine residues upon ligand-induced activation follows a precise and unique order of phosphorylation of the Eph tyrosines in the kinase activation process	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P54764	EPHA4	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	Eph receptor tyrosine kinases are activated upon ephrin binding via a sequential and ordered autophosphorylation process where residue YJM2 is phosphorylated first, followed by YJM1, and, finally by Yact. The Eph kinase activity most closely correlates with the phosphorylation status of the juxtamembrane region and not that of the activation loop. Eph kinase activity is primarily correlated with phosphorylation of residue YJM2 and not of the adjacent YJM1	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Eph receptor tyrosine kinase	-	Homo sapiens
EPHA4	-	Homo sapiens
ephrin type-A receptor 4	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	Eph receptor tyrosine kinases are activated upon ephrin binding via a sequential and ordered autophosphorylation process where residue YJM2 is phosphorylated first, followed by YJM1, and, finally by Yact. The Eph kinase activity most closely correlates with the phosphorylation status of the juxtamembrane region and not that of the activation loop. Eph kinase activity is primarily correlated with phosphorylation of residue YJM2 and not of the adjacent YJM1	Homo sapiens

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Release 2023.1 (January 2023)