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Methionyl aminopeptidase 2

PDB rendering based on 1b59.
Available structures
1b59, 1b6a, 1bn5, 1boa, 1kq0, 1kq9, 1qzy, 1r58, 1r5g, 1r5h, 1yw7, 1yw8, 1yw9, 2adu, 2ga2
Identifiers
Symbols METAP2; p67; MNPEP; p67eIF2
External IDs OMIM601870 MGI1929701 HomoloGene4981 GeneCards: METAP2 Gene
EC number 3.4.11.-
RNA expression pattern
PBB GE METAP2 209861 s at tn.png
PBB GE METAP2 213899 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 10988 56307
Ensembl ENSG00000111142 n/a
UniProt P50579 n/a
RefSeq (mRNA) NM_006838 NM_019648
RefSeq (protein) NP_006829 NP_062622
Location (UCSC) Chr 12:
94.39 - 94.43 Mb
n/a
PubMed search [1] [2]

Methionine aminopeptidase 2 is an enzyme that in humans is encoded by the METAP2 gene.[1][2]

This gene is a member of the methionyl aminopeptidase family and encodes a protein that binds 2 cobalt or manganese ions. This 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 protein. 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. A pseudogene of this gene is located on chromosome 2.[3]

Interactions

METAP2 has been shown to interact with Protein kinase R.[4]

References

  1. ^ Arfin SM, Kendall RL, Hall L, Weaver LH, Stewart AE, Matthews BW, Bradshaw RA (Sep 1995). "Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes". Proc Natl Acad Sci U S A 92 (17): 7714–8. PMID 7644482.  
  2. ^ Li X, Chang YH (Nov 1996). "Evidence that the human homologue of a rat initiation factor-2 associated protein (p67) is a methionine aminopeptidase". Biochem Biophys Res Commun 227 (1): 152–9. doi:10.1006/bbrc.1996.1482. PMID 8858118.  
  3. ^ "Entrez Gene: METAP2 methionyl aminopeptidase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10988.  
  4. ^ Gil, J; Esteban M, Roth D (Dec. 2000). "In vivo regulation of the dsRNA-dependent protein kinase PKR by the cellular glycoprotein p67". Biochemistry (UNITED STATES) 39 (51): 16016–25. ISSN 0006-2960. PMID 11123929.  

Further reading

  • Prigmore E, Ahmed S, Best A, et al. (1995). "A 68-kDa kinase and NADPH oxidase component p67phox are targets for Cdc42Hs and Rac1 in neutrophils.". J. Biol. Chem. 270 (18): 10717–22. doi:10.1074/jbc.270.18.10717. PMID 7738010.  
  • Li X, Chang YH (1995). "Molecular cloning of a human complementary DNA encoding an initiation factor 2-associated protein (p67).". Biochim. Biophys. Acta 1260 (3): 333–6. PMID 7873610.  
  • Ray MK, Chakraborty A, Datta B, et al. (1993). "Characteristics of the eukaryotic initiation factor 2 associated 67-kDa polypeptide.". Biochemistry 32 (19): 5151–9. doi:10.1021/bi00070a026. PMID 8098621.  
  • Sin N, Meng L, Wang MQ, et al. (1997). "The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2.". Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6099–103. doi:10.1073/pnas.94.12.6099. PMID 9177176.  
  • Liu S, Widom J, Kemp CW, et al. (1998). "Structure of human methionine aminopeptidase-2 complexed with fumagillin.". Science 282 (5392): 1324–7. doi:10.1126/science.282.5392.1324. PMID 9812898.  
  • Griffith EC, Su Z, Niwayama S, et al. (1999). "Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2.". Proc. Natl. Acad. Sci. U.S.A. 95 (26): 15183–8. doi:10.1073/pnas.95.26.15183. PMID 9860943.  
  • Datta B, Datta R, Mukherjee S, Zhang Z (1999). "Increased phosphorylation of eukaryotic initiation factor 2alpha at the G2/M boundary in human osteosarcoma cells correlates with deglycosylation of p67 and a decreased rate of protein synthesis.". Exp. Cell Res. 250 (1): 223–30. doi:10.1006/excr.1999.4508. PMID 10388536.  
  • Gil J, Esteban M, Roth D (2001). "In vivo regulation of the dsRNA-dependent protein kinase PKR by the cellular glycoprotein p67.". Biochemistry 39 (51): 16016–25. doi:10.1021/bi001754t. PMID 11123929.  
  • Catalano A, Romano M, Robuffo I, et al. (2001). "Methionine aminopeptidase-2 regulates human mesothelioma cell survival: role of Bcl-2 expression and telomerase activity.". Am. J. Pathol. 159 (2): 721–31. PMID 11485930.  
  • Endo H, Takenaga K, Kanno T, et al. (2002). "Methionine aminopeptidase 2 is a new target for the metastasis-associated protein, S100A4.". J. Biol. Chem. 277 (29): 26396–402. doi:10.1074/jbc.M202244200. PMID 11994292.  
  • Kanno T, Endo H, Takeuchi K, et al. (2002). "High expression of methionine aminopeptidase type 2 in germinal center B cells and their neoplastic counterparts.". Lab. Invest. 82 (7): 893–901. PMID 12118091.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.  
  • Datta R, Tammali R, Datta B (2003). "Negative regulation of the protection of eIF2alpha phosphorylation activity by a unique acidic domain present at the N-terminus of p67.". Exp. Cell Res. 283 (2): 237–46. doi:10.1016/S0014-4827(02)00042-3. PMID 12581743.  
  • Wang J, Sheppard GS, Lou P, et al. (2003). "Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese.". Biochemistry 42 (17): 5035–42. doi:10.1021/bi020670c. PMID 12718546.  
  • Serero A, Giglione C, Sardini A, et al. (2004). "An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway.". J. Biol. Chem. 278 (52): 52953–63. doi:10.1074/jbc.M309770200. PMID 14532271.  
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.  
  • Selvakumar P, Lakshmikuttyamma A, Kanthan R, et al. (2004). "High expression of methionine aminopeptidase 2 in human colorectal adenocarcinomas.". Clin. Cancer Res. 10 (8): 2771–5. doi:10.1158/1078-0432.CCR-03-0218. PMID 15102683.  
  • Kim S, LaMontagne K, Sabio M, et al. (2004). "Depletion of methionine aminopeptidase 2 does not alter cell response to fumagillin or bengamides.". Cancer Res. 64 (9): 2984–7. doi:10.1158/0008-5472.CAN-04-0019. PMID 15126329.  
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