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

NMT2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4C2X
Identifiers
Aliases	NMT2
External IDs	MGI: 1202298 HomoloGene: 101539 GeneCards: NMT2
Gene ontology Molecular function • transferase activity • transferase activity, transferring acyl groups • glycylpeptide N-tetradecanoyltransferase activity Cellular component • cytoplasm • cytosol • plasma membrane • Golgi apparatus • membrane • extrinsic component of membrane Biological process • regulation of rhodopsin mediated signaling pathway • intracellular transport of virus • N-terminal protein myristoylation • N-terminal peptidyl-glycine N-myristoylation 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_004808	NM_001290368 NM_001290369 NM_001290370 NM_008708
RefSeq (protein)	NP_001295224.1 NP_004799.1	NP_032734.1
Location (UCSC)	Chr 10: 15.1 – 15.17 Mb	Chr 2: 3.28 – 3.33 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

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.^[3]

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.^[4]

Interactions

NMT2 has been shown to interact with:

• caspase 3^[5]
• MARCKS^[6]

See also

N-myristoyltransferase 1

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. 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.
4. 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.
5. 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.
6. 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.