Functional Information from GO Data
| Chain | GOid | namespace | contents |
| E | 0005179 | molecular_function | hormone activity |
| E | 0005576 | cellular_component | extracellular region |
| F | 0005179 | molecular_function | hormone activity |
| F | 0005576 | cellular_component | extracellular region |
Functional Information from PROSITE/UniProt
| site_id | PS00262 |
| Number of Residues | 15 |
| Details | INSULIN Insulin family signature. CCTSiCSlyqLenyC |
| Chain | Residue | Details |
| E | CYS6-CYS20 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 186 |
| Details | Domain: {"description":"Fibronectin type-III 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9690478","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Peptide: {"description":"Insulin A chain","featureId":"PRO_0000015821"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 29 |
| Details | Peptide: {"description":"Insulin B chain","featureId":"PRO_0000015819"} |