Contents

Search


Ephrin type-A receptor 2; tyrosine-protein kinase receptor ECK; epithelial cell kinase (EPHA2, ECK, myk2, sek2)

Function: - receptor for members of the ephrin-A family - binds to ephrin-A1, -A3, -A4 & -A5 - interacts with SLA (putative) - interacts with INPPL1/SHIP2 Structure: - belongs to the protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily - contains 2 fibronectin F3 modules - contains 1 protein kinase domain - contains 1 SAM (sterile alpha motif) domain Compartment: membrane Expression: - highly expressed in tissues containing many epithelial cells, i.e. skin, intestine, lung, & ovary

General

ephA receptor

Properties

SIZE: entity length = 976 aa MW = 108 kD COMPARTMENT: cellular membrane STATE: active state MOTIF: signal sequence {1-24} N-glycosylation site {N99} cysteine-rich region {188-325} fibronectin type III domain or F3 module {328-429} MOTIF: N-glycosylation site {N407} fibronectin type III domain or F3 module {435-526} MOTIF: N-glycosylation site {N435} transmembrane domain {535-558} Ser phosphorylation site {S570} Tyr phosphorylation site {Y575} Ser phosphorylation site {S579} Tyr phosphorylation site {Y588} Tyr phosphorylation site {Y594} kinase domain SITE: 613-875 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 619-627 Tyr phosphorylation site {Y628} ATP-binding site NAME: ATP-binding site SITE: 646-646 Thr phosphorylation site {T647} aspartate residue {D739} Tyr phosphorylation site {Y772} Ser phosphorylation site {S892} Ser phosphorylation site {S897} Thr phosphorylation site {T898} Ser phosphorylation site {S899} Ser phosphorylation site {S901} sterile alpha motif NAME: sterile alpha motif SITE: 904-968 MOTIF: Tyr phosphorylation site {Y921} Tyr phosphorylation site {Y930} PDZ recognition motif NAME: PDZ recognition motif SITE: 974-976 FOR-BINDING-VIA: PDZ domain

Database Correlations

OMIM 176946 MORBIDMAP 176946 UniProt P29317 PFAM correlations Entrez Gene 1969 Kegg hsa:1969 ENZYME 2.7.10.1

References

  1. Eph Nomenclature Committee. Cell 90:403-4 1997
  2. UniProt :accession P29317