2CRI
Solution structure of the MSP domain of mouse VAMP-associated proteinA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 117 |
| Details | Domain: {"description":"MSP","evidences":[{"source":"PROSITE-ProRule","id":"PRU00132","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Region: {"description":"phosphorylated FFAT motif binding","evidences":[{"source":"UniProtKB","id":"Q9P0L0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in binding the phosphorylated serine of the phospho-FFAT motif","evidences":[{"source":"UniProtKB","id":"Q9P0L0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"Q9P0L0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9P0L0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
