Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005003 | molecular_function | ephrin receptor activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
A | 0016020 | cellular_component | membrane |
B | 0005003 | molecular_function | ephrin receptor activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
B | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
B | 0016020 | cellular_component | membrane |
C | 0016020 | cellular_component | membrane |
D | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
site_id | PS00790 |
Number of Residues | 21 |
Details | RECEPTOR_TYR_KIN_V_1 Receptor tyrosine kinase class V signature 1. FqDvGACIALVSVRVfykKCP |
Chain | Residue | Details |
A | PHE185-PRO205 | |
site_id | PS00791 |
Number of Residues | 21 |
Details | RECEPTOR_TYR_KIN_V_2 Receptor tyrosine kinase class V signature 2. CgaDGEWlv.PIGnClCnaGHE |
Chain | Residue | Details |
A | CYS247-GLU267 | |
site_id | PS01299 |
Number of Residues | 28 |
Details | EPHRIN_RBD_1 Ephrin receptor-binding (ephrin RBD) domain signature. RFTiKFQeYSPnlwGhEFrshhdYYiiA |
Chain | Residue | Details |
C | ARG112-ALA139 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 358 |
Details | Domain: {"description":"Eph LBD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00883","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 222 |
Details | Domain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |