NMT2

N-myristoyltransferase 2
Identifiers
Symbols	NMT2;
External IDs	OMIM: 603801 MGI: 1202298 HomoloGene: 101539 GeneCards: NMT2 Gene
EC number	2.3.1.97
Gene Ontology Molecular function • catalytic activity • glycylpeptide N-tetradecanoyltransferase activity • acyltransferase activity • transferase activity Cellular component • cytoplasm • Golgi apparatus • plasma membrane Biological process • N-terminal protein myristoylation • protein lipoylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9397	18108
Ensembl	ENSG00000152465	ENSMUSG00000026643
UniProt	O60551	Q3THR4
RefSeq (mRNA)	NM_004808	NM_008708.1
RefSeq (protein)	NP_004799	NP_032734.1
Location (UCSC)	Chr 10: 15.14 – 15.21 Mb	Chr 2: 3.2 – 3.25 Mb
PubMed search	[1]	[2]

Glycylpeptide N-tetradecanoyltransferase 2 is an enzyme that in humans is encoded by the NMT2 gene.^[1]

N-myristoyltransferase (NMT) catalyzes the reaction of N-terminal myristoylation of many signaling proteins. It transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. Biochemical evidence indicates the presence of several distinct NMTs, varying in apparent molecular weight and /or subcellular distribution. The predicted 498-amino acid of human NMT2 protein shares 77% and 96% sequence identity with human NMT1 and mouse Nmt2 comprise two distinct families of N-myristoyltransferases.^[2]

References

1. ^ Giang DK, Cravatt BF (Apr 1998). "A second mammalian N-myristoyltransferase". J Biol Chem 273 (12): 6595–8. doi:10.1074/jbc.273.12.6595. PMID 9506952. 
2. ^ "Entrez Gene: NMT2 N-myristoyltransferase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9397. 

Further reading

• Pal R, Reitz MS, Tschachler E et al. (1990). "Myristoylation of gag proteins of HIV-1 plays an important role in virus assembly". AIDS Res. Hum. Retroviruses 6 (6): 721–30. doi:10.1089/aid.1990.6.721. PMID 2194551. 
• Bryant M, Ratner L (1990). "Myristoylation-dependent replication and assembly of human immunodeficiency virus 1". Proc. Natl. Acad. Sci. U.S.A. 87 (2): 523–7. doi:10.1073/pnas.87.2.523. PMC 53297. PMID 2405382. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=53297. 
• Tashiro A, Shoji S, Kubota Y (1990). "Antimyristoylation of the gag proteins in the human immunodeficiency virus-infected cells with N-myristoyl glycinal diethylacetal resulted in inhibition of virus production". Biochem. Biophys. Res. Commun. 165 (3): 1145–54. doi:10.1016/0006-291X(89)92722-8. PMID 2692561. 
• Goddard C, Aquino A, Glazer RI, Felsted RL (1989). "Chemical characterization of p17gag from human immunodeficiency virus as an N-terminally myristoylated protein". Eur. J. Biochem. 182 (2): 323–6. doi:10.1111/j.1432-1033.1989.tb14833.x. PMID 2737204. 
• Göttlinger HG, Sodroski JG, Haseltine WA (1989). "Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 86 (15): 5781–5. doi:10.1073/pnas.86.15.5781. PMC 297714. PMID 2788277. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=297714. 
• Lee PP, Linial ML (1994). "Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal". J. Virol. 68 (10): 6644–54. PMC 237085. PMID 7521919. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=237085. 
• Zhou W, Parent LJ, Wills JW, Resh MD (1994). "Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids". J. Virol. 68 (4): 2556–69. PMC 236733. PMID 8139035. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=236733. 
• Morikawa Y, Hinata S, Tomoda H et al. (1996). "Complete inhibition of human immunodeficiency virus Gag myristoylation is necessary for inhibition of particle budding". J. Biol. Chem. 271 (5): 2868–73. doi:10.1074/jbc.271.5.2868. PMID 8576268. 
• Zhou W, Resh MD (1997). "Differential membrane binding of the human immunodeficiency virus type 1 matrix protein". J. Virol. 70 (12): 8540–8. PMC 190946. PMID 8970978. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=190946. 
• Spearman P, Horton R, Ratner L, Kuli-Zade I (1997). "Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism". J. Virol. 71 (9): 6582–92. PMC 191936. PMID 9261380. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=191936. 
• Furuishi K, Matsuoka H, Takama M et al. (1997). "Blockage of N-myristoylation of HIV-1 gag induces the production of impotent progeny virus". Biochem. Biophys. Res. Commun. 237 (3): 504–11. doi:10.1006/bbrc.1997.7178. PMID 9299393. 
• Hermida-Matsumoto L, Resh MD (1999). "Human immunodeficiency virus type 1 protease triggers a myristoyl switch that modulates membrane binding of Pr55(gag) and p17MA". J. Virol. 73 (3): 1902–8. PMC 104431. PMID 9971769. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=104431. 
• Paillart JC, Göttlinger HG (1999). "Opposing effects of human immunodeficiency virus type 1 matrix mutations support a myristyl switch model of gag membrane targeting". J. Virol. 73 (4): 2604–12. PMC 104015. PMID 10074105. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=104015. 
• Ono A, Freed EO (1999). "Binding of human immunodeficiency virus type 1 Gag to membrane: role of the matrix amino terminus". J. Virol. 73 (5): 4136–44. PMC 104193. PMID 10196310. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=104193. 
• Shiraishi T, Misumi S, Takama M et al. (2001). "Myristoylation of human immunodeficiency virus type 1 gag protein is required for efficient env protein transportation to the surface of cells". Biochem. Biophys. Res. Commun. 282 (5): 1201–5. doi:10.1006/bbrc.2001.4696. PMID 11302743. 
• Kolluri SK, Balduf C, Hofmann M, Göttlicher M (2002). "Novel target genes of the Ah (dioxin) receptor: transcriptional induction of N-myristoyltransferase 2". Cancer Res. 61 (23): 8534–9. PMID 11731439. 
• Lindwasser OW, Resh MD (2002). "Myristoylation as a target for inhibiting HIV assembly: unsaturated fatty acids block viral budding". Proc. Natl. Acad. Sci. U.S.A. 99 (20): 13037–42. doi:10.1073/pnas.212409999. PMC 130582. PMID 12244217. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=130582. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Bouamr F, Scarlata S, Carter C (2003). "Role of myristylation in HIV-1 Gag assembly". Biochemistry 42 (21): 6408–17. doi:10.1021/bi020692z. PMID 12767222.