Glycylpeptide N-tetradecanoyltransferase 2

From Wikipedia the free encyclopedia

Human N-myristoyltransferase 2
Human N-myristoyltransferase isoform 2 (NMT2) (based on PDB: 4c2x)
Identifiers
SymbolNMT2
PfamPF01233
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
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[edit]

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[edit]

NMT2 has been shown to interact with:

See also[edit]

References[edit]

  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.
  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. Bibcode:2014NatCo...5.4919T. 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[edit]

External links[edit]

  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Glycylpeptide N-tetradecanoyltransferase 2 (NMT2)