NMT2

Human N-myristoyltransferase 2
Human N-myristoyltransferase isoform 2 (NMT2) (based on PDB: 4c2x)
Identifiers
Symbol	NMT2
Pfam	PF01233.14
InterPro	IPR022676
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

N-myristoyltransferase 2
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4C2X​
Identifiers
Symbol	NMT2
External IDs	OMIM: 603801 MGI: 1202298 HomoloGene: 101539 ChEMBL: 2849 GeneCards: NMT2 Gene
EC number	2.3.1.97
Gene ontology Molecular function • glycylpeptide N-tetradecanoyltransferase activity Cellular component • cytoplasm • Golgi apparatus • cytosol • plasma membrane • extrinsic component of membrane Biological process • phototransduction, visible light • viral process • rhodopsin mediated signaling pathway • N-terminal peptidyl-glycine N-myristoylation • virion assembly • viral protein processing • regulation of rhodopsin mediated signaling pathway • intracellular transport of virus Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9397	18108
Ensembl	ENSG00000152465	ENSMUSG00000026643
UniProt	O60551	O70311
RefSeq (mRNA)	NM_001308295	NM_001290368
RefSeq (protein)	NP_001295224	NP_001277297
Location (UCSC)	Chr 10: 15.1 – 15.17 Mb	Chr 2: 3.28 – 3.33 Mb
PubMed search

Glycylpeptide N-tetradecanoyltransferase 2 known also as N-myristoyltransferase, is an enzyme (EC: 2.3.1.97) that in humans is encoded by the NMT2 gene.^[1]

Function

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 496-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]

Interactions

NMT2 has been shown to interact with:

• caspase 3^[3]
• MARCKS^[4]

See also

N-myristoyltransferase 1

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. Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW (2014). "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells.". Nat Commun 5: 4919. doi:10.1038/ncomms5919. PMID 25255805.
3. Selvakumar P, Sharma RK (2007). "Role of calpain and caspase system in the regulation of N-myristoyltransferase in human colon cancer (Review).". Int J Mol Med 19 (5): 823–7. doi:10.3892/ijmm.19.5.823. PMID 17390089.
4. Selvakumar P, Lakshmikuttyamma A, Sharma RK (2009). "Biochemical characterization of bovine brain myristoyl-CoA:protein N-myristoyltransferase type 2.". J Biomed Biotechnol 2009: 907614. doi:10.1155/2009/907614. PMID 19746168.

Further reading

• 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.
• Wright MH, Clough B, Rackham MD, Rangachari K, Brannigan JA, Grainger M, Moss DK, Bottrill AR, Heal WP, Broncel M, Serwa RA, Brady D, Mann DJ, Leatherbarrow RJ, Tewari R, Wilkinson AJ, Holder AA, Tate EW (2014). "Validation of N-myristoyltransferase as an antimalarial drug target using an integrated chemical biology approach.". Nat Chem 6 (2): 112–21. doi:10.1038/nchem.1830. PMID 24451586.