METAP2 - Methionine aminopeptidase 2 - human protein (Function)
 
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METAP2 »  Methionine aminopeptidase 2   [ EC 3.4.11.18 ]  (MAP 2)
 
Protein also known as:  Initiation factor 2-associated 67 kDa glycoprotein (p67).
Gene name:  METAP2
Entry whose protein(s) existence is based on evidence at protein level
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GENE REF ISO

Function

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Overview 
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.  
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  • CuratedUniProtKB
Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.  
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  • CuratedUniProtKB
GO molecular function 
Aminopeptidase activitydefinition[GO:0004177]  
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  • IDAUniProtKB
Metal ion bindingdefinition[GO:0046872]  
  • IEAUniProtKB Annot
Metalloaminopeptidase activitydefinition[GO:0070006]  
  • IEAUniProtKB Annot
Metalloexopeptidase activitydefinition[GO:0008235]  
1
  • IDAUniProtKB
GO biological process 
N-terminal protein amino acid modificationdefinition[GO:0031365]  
1
  • IDAHGNC
Peptidyl-methionine modificationdefinition[GO:0018206]  
1
  • IDAHGNC
Protein initiator methionine removaldefinition[GO:0070084]  
  • IEAUniProtKB Annot
Protein processingdefinition[GO:0016485]  
1
  • IDAHGNC
Proteolysisdefinition[GO:0006508]  
  • IEAUniProtKB KW
Enzymatic activity 
This protein acts as an enzyme. It is known to catalyze the following reaction
EC 3.4.11.18: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.  
1
  • CuratedUniProtKB
It requires the following cofactor
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site (By similarity). Also manganese has been proposed to be the physiological cofactor for human METAP2.  
3
  • CuratedUniProtKB
 
More information is available from:
Pathways 
According to Reactome, this protein belongs to the following pathways:
Disease  REACT_116125  
Signal Transduction  REACT_111102  
 

Keywords

Molecular function 
Aminopeptidase  definition   [KW-0031]
Hydrolase  definition   [KW-0378]
Protease  definition   [KW-0645]
Technical term 
Reference proteome  definition   [KW-1185]
 

Further external links

Other
GeneWiki: METAP2
GenomeRNAi: 10988
PRO: PR:P50579
Chemistry
GuidetoPHARMACOLOGY: 1573