5KY8
mouse POFUT1 in complex with O-glucosylated mouse Notch1 EGF12 mutant (D464G) and GDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001525 | biological_process | angiogenesis |
| A | 0001756 | biological_process | somitogenesis |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0006004 | biological_process | fucose metabolic process |
| A | 0006486 | biological_process | protein glycosylation |
| A | 0007219 | biological_process | Notch signaling pathway |
| A | 0007399 | biological_process | nervous system development |
| A | 0007507 | biological_process | heart development |
| A | 0008417 | molecular_function | fucosyltransferase activity |
| A | 0008593 | biological_process | regulation of Notch signaling pathway |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0036066 | biological_process | protein O-linked fucosylation |
| A | 0046922 | molecular_function | peptide-O-fucosyltransferase activity |
| 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. ClDqigeFqCiC |
| Chain | Residue | Details |
| B | CYS467-CYS478 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CiCmpGyeGVyC |
| Chain | Residue | Details |
| B | CYS476-CYS487 |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CiCmpGYegvy....C |
| Chain | Residue | Details |
| B | CYS476-CYS487 |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DvNECisnp..........Cqngat..ClDqigeFqC |
| Chain | Residue | Details |
| B | ASP452-CYS476 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9H488","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Interaction with DLL4","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Glc...) serine","evidences":[{"source":"PubMed","id":"21757702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28089369","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Fuc...) threonine","evidences":[{"source":"PubMed","id":"21757702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28089369","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
