Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 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. CvNtpgsFmCiC |
Chain | Residue | Details |
B | CYS457-CYS468 | |
B | CYS572-CYS583 | |
B | CYS619-CYS630 | |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CaCpqGftGPsC |
Chain | Residue | Details |
B | CYS541-CYS552 | |
site_id | PS01186 |
Number of Residues | 15 |
Details | EGF_2 EGF-like domain signature 2. CiCktGYiriddys.C |
Chain | Residue | Details |
B | CYS466-CYS480 | |
B | CYS508-CYS521 | |
B | CYS541-CYS552 | |
site_id | PS01187 |
Number of Residues | 27 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECaegrhy........Crentm..CvNtpgsFmC |
Chain | Residue | Details |
B | ASP440-CYS466 | |
B | ASP555-CYS581 | |
B | ASP602-CYS628 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | ASP440 | |
B | ASN574 | |
B | LEU575 | |
B | TRP578 | |
B | ASP602 | |
B | ILE603 | |
B | GLU605 | |
B | ASN621 | |
B | LEU622 | |
B | GLY625 | |
B | ILE441 | |
B | GLU443 | |
B | ASN459 | |
B | THR460 | |
B | SER463 | |
B | ASP555 | |
B | ILE556 | |
B | GLU558 | |
Chain | Residue | Details |
B | ASN517 | |
Chain | Residue | Details |
B | THR548 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN615 | |
B | ASN635 | |