Methionine aminopeptidase 2
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N- terminal Met-Val and Met-Thr sequences in vivo.
Database | Links |
---|---|
UniProt | P50579 |
PDB | 1B59, 1B6A, 1BN5, 1BOA, 1KQ0, 1KQ9, 1QZY, 1R58, 1R5G, 1R5H, 1YW7, 1YW8, 1YW9, 2ADU, 2EA2, 2EA4, 2GA2, 2OAZ |
BioGrid | 116184 |
BindingDB | P50579 |
DrugBank | DB00134 |
Guide to PHARMACOLOGY | 1573 |
PharmGKB | PA30765 |
KEGG | hsa:10988 |
BioCyc | Not available |
Entrez Gene (GeneID) | 10988 |
Metric | Mean Value | Standard Deviation |
---|---|---|
AUC | 0.979 | 0.0015 |
Accuracy | 0.9616 | 0.0033 |
Sensitivity | 0.9743 | 0.0045 |
Specificity | 0.9484 | 0.0041 |
BEDROC | 0.9942 | 0.0123 |
MCC Threshold | 0.4 | N/A |
MCC | 0.9304 | N/A |
F-score Threshold | 0.4 | N/A |
F-score | 0.9661 | N/A |