Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
B | 0005509 | molecular_function | calcium ion binding |
C | 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. CkDdinsYeCwC |
Chain | Residue | Details |
B | CYS62-CYS73 | |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CwCpfGfeGKnC |
Chain | Residue | Details |
B | CYS71-CYS82 | |
site_id | PS01186 |
Number of Residues | 12 |
Details | EGF_2 EGF-like domain signature 2. CwCpfGFegkn....C |
Chain | Residue | Details |
B | CYS71-CYS82 | |
site_id | PS01187 |
Number of Residues | 25 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC |
Chain | Residue | Details |
B | ASP47-CYS71 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | ASP47 | |
A | ASP65 | |
C | ASP47 | |
C | GLY48 | |
C | GLN50 | |
C | ASP64 | |
C | ASP65 | |
B | GLY48 | |
B | GLN50 | |
B | ASP64 | |
B | ASP65 | |
A | ASP47 | |
A | GLY48 | |
A | GLN50 | |
A | ASP64 | |
Chain | Residue | Details |
B | ASP64 | |
A | ASP64 | |
C | ASP64 | |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000269|Ref.28 |
Chain | Residue | Details |
B | SER68 | |
A | SER68 | |
C | SER68 | |
Chain | Residue | Details |
B | SER53 | |
A | SER53 | |
C | SER53 | |
Chain | Residue | Details |
B | SER61 | |
A | SER61 | |
C | SER61 | |