Biology:METAP1
From HandWiki
Short description: Protein-coding gene in humans
 Generic protein structure example |
Methionine aminopeptidase 1 is an enzyme that in humans is encoded by the METAP1 gene.[1][2][3] This enzyme is a methionyl aminopeptidase which cleaves the N-terminal methionine from precursor proteins, with particular affinity for when the second amino acid is small and non-charged.[4] Also important for the normal functioning of the cell cycle.[4] This enzyme uses metal cations as a cofactor (making it a metalloprotein), but which one is used in the body remains debated.[4]
References
- ↑ "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res 2 (1): 37–43. Jul 1995. doi:10.1093/dnares/2.1.37. PMID 7788527.
- ↑ "Functional expression of human methionine aminopeptidase type 1 in Saccharomyces cerevisiae". Protein Pept Lett 9 (4): 295–303. Jul 2002. doi:10.2174/0929866023408607. PMID 12144506.
- ↑ "Entrez Gene: METAP1 methionyl aminopeptidase 1". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=23173.
- ↑ 4.0 4.1 4.2 "Methionine aminopeptidase 1". UniProt consortium. https://www.uniprot.org/uniprotkb/P53582/entry.
Further reading
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway.". J. Biol. Chem. 278 (52): 52953–63. 2004. doi:10.1074/jbc.M309770200. PMID 14532271.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. 2005. doi:10.1038/nbt1046. PMID 15592455.
- "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. 2005. doi:10.1038/nature03207. PMID 15635413. Bibcode: 2005Natur.433...77A.
- "Structural basis for the functional differences between type I and type II human methionine aminopeptidases.". Biochemistry 44 (45): 14741–9. 2006. doi:10.1021/bi051691k. PMID 16274222.
- "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. 2006. doi:10.1101/gr.4039406. PMID 16344560.
- "Methionine aminopeptidase 2 and cancer.". Biochim. Biophys. Acta 1765 (2): 148–54. 2006. doi:10.1016/j.bbcan.2005.11.001. PMID 16386852.
- "Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression.". Proc. Natl. Acad. Sci. U.S.A. 103 (48): 18148–53. 2007. doi:10.1073/pnas.0608389103. PMID 17114291.
- "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. 2007. doi:10.1038/msb4100134. PMID 17353931.
External links
- PDBe-KB provides an overview of all the structure information available in the PDB for Human Methionine aminopeptidase 1
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