NMT2

Human N-myristoyltransferase 2
Human N-myristoyltransferase isoform 2 (NMT2) (based on PDB: 4c2x)
Identifiers
Symbol NMT2
Pfam PF01233.14
InterPro IPR022676
NMT2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesNMT2, N-myristoyltransferase 2
External IDsMGI: 1202298 HomoloGene: 101539 GeneCards: NMT2
Gene location (Human)
Chr.Chromosome 10 (human)[1]
Band10p13Start15,102,584 bp[1]
End15,168,693 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
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
NP_004799

NP_001277297
NP_001277298
NP_001277299
NP_032734

Location (UCSC)Chr 10: 15.1 – 15.17 MbChr 2: 3.28 – 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

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000152465 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026643 - Ensembl, May 2017
  3. "Human PubMed Reference:".
  4. "Mouse PubMed Reference:".
  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.
  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. PMC 4200515. 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. PMC 2737134. 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. PMC 4739506. PMID 24451586.


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