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GeneQ18036007· pop 5· linked from 159 articles

METAP2

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Also known as MAP2, MNPEP, p67, p67eIF2, methionyl aminopeptidase 2

Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the METAP2 gene.

Gene data

METAP2
Name
methionyl aminopeptidase 2
Type
protein-coding
Position
95,473,520–95,515,935 (+)
Aliases
MAP2, MNPEP, p67eIF2
Ensembl
ENSG00000111142
RefSeq RNA
NM_001317182.2, NM_001317183.2, NM_001330246.2, NM_006838.4, NR_133673.2
RefSeq protein
NP_001304111.1, NP_001304112.1, NP_001317175.1, NP_006829.1

The protein encoded by this gene is a member of the methionyl aminopeptidase family. The encoded protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amino-terminal methionine residue from nascent proteins. Increased expression of this gene is associated with various forms of cancer, and the anti-cancer drugs fumagillin and ovalicin inhibit the protein by irreversibly binding to its active site. Inhibitors of this gene have also been shown to be effective for the treatment of obesity. A pseudogene of this gene is located on chromosome 2. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2015].

Gene Ontology

Pathways

Visual phototransductionThe phototransduction cascadeInactivation, recovery and regulation of the phototransduction cascadeSensory Perception

via MyGene.info

Gene · Ensembl

methionyl aminopeptidase 2

Symbol
METAP2
Biotype
Protein coding
Organism
Homo sapiens
Location
12:95,473,520-95,515,935
Strand
Forward (+)
Assembly
GRCh38
View on Ensembl →

via Ensembl · EMBL-EBI

~8 min read

Encyclopedic overview

9 sections
Contents
  • Structure
  • Active site
  • Dimetal center
  • Mechanism
  • Function
  • Clinical significance
  • Interactions
  • References
  • Further reading

Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the METAP2 gene.

Methionine aminopeptidase 2, a member of the dimetallohydrolase family, is a cytosolic metalloenzyme that catalyzes the hydrolytic removal of N-terminal methionine residues from nascent proteins. peptide-methionine \rightleftharpoons peptide + methionine

Excerpted from Wikipedia’s “METAP2” article, available under the CC BY-SA 4.0 licence.

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via Wikidata sitelinks · CC0