Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
B | 0005509 | molecular_function | calcium ion binding |
B | 0007154 | biological_process | cell communication |
B | 0007219 | biological_process | Notch signaling pathway |
B | 0007275 | biological_process | multicellular organism development |
B | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CrCqyGwqGLyC |
Chain | Residue | Details |
A | CYS359-CYS370 | |
A | CYS321-CYS332 | |
B | CYS251-CYS262 | |
B | CYS282-CYS293 | |
B | CYS322-CYS333 | |
A | CYS398-CYS409 | |
A | CYS438-CYS449 | |
A | CYS476-CYS487 | |
site_id | PS01186 |
Number of Residues | 15 |
Details | EGF_2 EGF-like domain signature 2. CrCqyGWqglycdk.C |
Chain | Residue | Details |
A | CYS398-CYS409 | |
A | CYS321-CYS332 | |
B | CYS251-CYS265 | |
B | CYS322-CYS333 | |
A | CYS438-CYS449 | |
A | CYS476-CYS487 | |
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNshggYnCvC |
Chain | Residue | Details |
A | CYS312-CYS323 | |
A | CYS350-CYS361 | |
A | CYS429-CYS440 | |
A | CYS467-CYS478 | |
site_id | PS01187 |
Number of Residues | 27 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DvDECqlmpna........Cqnggt..ChNshggYnC |
Chain | Residue | Details |
A | ASP295-CYS321 | |
A | ASN335-CYS359 | |
A | ASP412-CYS438 | |
A | ASP452-CYS476 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASP452 | |
A | VAL453 | |
A | GLU455 | |
A | ASP469 | |
A | GLN470 | |
B | ASN143 | |
B | ASN217 | |
Chain | Residue | Details |
A | ASP469 | |
Chain | Residue | Details |
A | THR311 | |
A | THR349 | |
Chain | Residue | Details |
A | SER341 | |
A | SER378 | |
Chain | Residue | Details |
A | SER435 | |
Chain | Residue | Details |
A | SER458 | |
Chain | Residue | Details |
A | THR466 | |