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Glycylpeptide N-tetradecanoyltransferase 2

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Human N-myristoyltransferase 2
Human N-myristoyltransferase isoform 2 (NMT2) (based on PDB: 4c2x)
Identifiers
SymbolNMT2
PfamPF01233.14
InterProIPR022676
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
NMT2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesNMT2, N-myristoyltransferase 2
External IDsOMIM: 603801; MGI: 1202298; HomoloGene: 101539; GeneCards: NMT2; OMA:NMT2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001308295
NM_004808

NM_001290368
NM_001290369
NM_001290370
NM_008708

RefSeq (protein)

NP_001295224
NP_004799

NP_001277297
NP_001277298
NP_001277299
NP_032734

Location (UCSC)Chr 10: 15.1 – 15.17 MbChr 2: 3.29 – 3.33 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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.[5]

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.[6]

Interactions

NMT2 has been shown to interact with:

See also

N-myristoyltransferase 1

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000152465Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026643Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  6. ^ 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.
  7. ^ 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.
  8. ^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

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.