Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNylggYyCsC |
Chain | Residue | Details |
A | CYS137-CYS148 | |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CsCrvGYilhqnkhtC |
Chain | Residue | Details |
A | CYS146-CYS161 | |
site_id | PS01187 |
Number of Residues | 28 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DvDECrtslgdsvp.....Cdhy....ChNylggYyC |
Chain | Residue | Details |
A | ASP119-CYS146 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU48 | |
A | ASP56 | |
A | ASP101 | |
A | SER103 | |
A | ASN104 | |
A | GLY143 | |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP119 | |
A | VAL120 | |
A | TYR140 | |
Chain | Residue | Details |
A | ASN139 | |
Chain | Residue | Details |
A | ASN84 | |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN266 | |