METAP1

Methionyl aminopeptidase 1

PDB rendering based on 2b3h.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2B3H, 2B3K, 2B3L, 2G6P, 2GZ5, 2NQ6, 2NQ7, 4FLI, 4FLJ, 4FLK, 4FLL, 4HXX, 4IKR, 4IKS, 4IKT, 4IKU, 4IU6, 4U1B, 4U69, 4U6C, 4U6E, 4U6J, 4U6W, 4U6Z, 4U70, 4U71, 4U73, 4U75, 4U76

Identifiers

Symbols

METAP1 ; MAP1A; MetAP1A

External IDs

OMIM: 610151 HomoloGene: 6488 IUPHAR: 1572 ChEMBL: 2474 GeneCards: METAP1 Gene

EC number

3.4.11.18

Gene ontology
Molecular function	• aminopeptidase activity • metalloexopeptidase activity • metal ion binding • metalloaminopeptidase activity
Cellular component	• nucleus • cytoplasm • cytosol • cytosolic ribosome
Biological process	• regulation of translation • proteolysis • phototransduction, visible light • rhodopsin mediated signaling pathway • peptidyl-methionine modification • regulation of rhodopsin mediated signaling pathway • N-terminal protein amino acid modification • protein initiator methionine removal • platelet aggregation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
138.46 – 138.49 Mb

PubMed search

Methionine aminopeptidase 1 is an enzyme that in humans is encoded by the METAP1 gene.^[1]^[2]^[3]

References

↑ Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H; et al. (Jul 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. doi:10.1093/dnares/2.1.37. PMID 7788527.
↑ Dummitt B, Fei Y, Chang YH (Jul 2002). "Functional expression of human methionine aminopeptidase type 1 in Saccharomyces cerevisiae". Protein Pept Lett 9 (4): 295–303. doi:10.2174/0929866023408607. PMID 12144506.
↑ "Entrez Gene: METAP1 methionyl aminopeptidase 1".

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. PMC 139241. 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. PMC 528928. 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. PMC 1356129. 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. PMC 1838721. 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 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

PDB gallery

2b3h: Crystal structure of Human Methionine Aminopeptidase Type I with a third cobalt in the active site

2b3k: Crystal structure of Human Methionine Aminopeptidase Type I in the holo form

2b3l: Crystal structure of type I human methionine aminopeptidase in the apo form

2g6p: Crystal structure of truncated (delta 1-89) human methionine aminopeptidase Type 1 in complex with Pyridyl pyrimidine derivative

2gz5: Human Type 1 methionine aminopeptidase in complex with ovalicin at 1.1 Ang

2nq6: Crystal structure of human methionine aminopeptidase type 1 in complex with 3-tert-Butoxycarbonylaminopyridine-2-carboxylic acid thiazole-2-ylamide

2nq7: Crystal structure of type 1 human methionine aminopeptidase in complex with 3-(2,2-Dimethylpropionylamino)pyridine-2-carboxylic acid thiazole-2-ylamide

Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase

3.4.11	Aminopeptidase Alanine Arginyl Aspartyl Cystinyl Leucyl Glutamyl Methionyl 1 2 O

3.4.13	Dipeptidase 1 2 3

3.4.14	Dipeptidyl peptidase Cathepsin C Dipeptidyl peptidase-4 Tripeptidyl peptidase Tripeptidyl peptidase I Tripeptidyl peptidase II

3.4.15	Angiotensin-converting enzyme

3.4.16	Serine type carboxypeptidases: Cathepsin A DD-transpeptidase

3.4.17	Metalloexopeptidases Carboxypeptidase A A2 B C E Glutamate II

Other/ungrouped	Metalloexopeptidase

3.4.21-25: Endopeptidase

Other/ungrouped: Amyloid precursor protein secretase

3.4.99: Unknown

Staphylokinase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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METAP1

References

Further reading