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. CvNtpgsYiCdC |
Chain | Residue | Details |
A | CYS1502-CYS1513 | |
A | CYS1622-CYS1633 | |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CrCptGYylnedtrvC |
Chain | Residue | Details |
A | CYS1631-CYS1646 | |
site_id | PS01187 |
Number of Residues | 25 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DvNECldptt.........Cisgn...CvNtpgsYiC |
Chain | Residue | Details |
A | ASP1487-CYS1511 | |
A | ASP1606-CYS1631 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | Domain: {"description":"EGF-like 26; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 41 |
Details | Domain: {"description":"EGF-like 27; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"O-linked (Glc) serine","evidences":[{"source":"PubMed","id":"34411563","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |