METAP1

From Wikipedia, the free encyclopedia

Methionyl aminopeptidase 1

PDB rendering based on 2b3h.

Available structures: 2b3h, 2b3k, 2b3l, 2g6p, 2gz5, 2nq6, 2nq7

Identifiers

Symbol(s)

METAP1; DKFZp781C0419; KIAA0094

External IDs

OMIM: 610151

Gene ontology
Molecular Function:	• methionyl aminopeptidase activity • serine-type endopeptidase inhibitor activity • peptidase activity • metal ion binding • cobalt ion binding
Cellular Component:	• cytoplasm
Biological Process:	• regulation of translation • proteolysis • peptidyl-methionine modification • N-terminal protein amino acid modification

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

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Refseq

NM_015143 (mRNA)
NP_055958 (protein)

n/a (mRNA)
n/a (protein)

Location

Chr 4: 100.14 - 100.2 Mb

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Pubmed search

[1]

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Methionyl aminopeptidase 1, also known as METAP1, is a human gene.^[1]

[edit] References

^ Entrez Gene: METAP1 methionyl aminopeptidase 1.

[edit] Further reading

Nagase T, Miyajima N, Tanaka A, et al. (1995). "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. PMID 7788527.
Dummitt B, Fei Y, Chang YH (2002). "Functional expression of human methionine aminopeptidase type 1 in Saccharomyces cerevisiae.". Protein Pept. Lett. 9 (4): 295-303. PMID 12144506.
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.
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.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94-101. doi:10.1038/nbt1046. PMID 15592455.
Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77-83. doi:10.1038/nature03207. PMID 15635413.
Addlagatta A, Hu X, Liu JO, Matthews BW (2006). "Structural basis for the functional differences between type I and type II human methionine aminopeptidases.". Biochemistry 44 (45): 14741-9. doi:10.1021/bi051691k. PMID 16274222.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55-65. doi:10.1101/gr.4039406. PMID 16344560.
Selvakumar P, Lakshmikuttyamma A, Dimmock JR, Sharma RK (2006). "Methionine aminopeptidase 2 and cancer.". Biochim. Biophys. Acta 1765 (2): 148-54. doi:10.1016/j.bbcan.2005.11.001. PMID 16386852.
Hu X, Addlagatta A, Lu J, et al. (2007). "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. doi:10.1073/pnas.0608389103. PMID 17114291.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.