METAP1 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). Required for normal progression through the cell cycle. Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.11.18; Protease
Chromosomal Location of Human Ortholog: 4q23
Cellular Component:  cytoplasm; cytosol
Molecular Function:  aminopeptidase activity; metal ion binding; metalloaminopeptidase activity; metalloexopeptidase activity
Biological Process:  N-terminal protein amino acid modification; peptidyl-methionine modification; protein initiator methionine removal; proteolysis; regulation of rhodopsin mediated signaling pathway; regulation of translation
Reference #:  P53582 (UniProtKB)
Alt. Names/Synonyms: AMPM1; DKFZp781C0419; KIAA0094; MAP 1; MAP11; MAP1A; MetAP 1; METAP1; MetAP1A; Methionine aminopeptidase 1; methionyl aminopeptidase 1; Peptidase M 1
Gene Symbols: METAP1
Molecular weight: 43,215 Da
Basal Isoelectric point: 6.75  Predict pI for various phosphorylation states
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METAP1

Protein Structure Not Found.


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