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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Pfam box
{{PBB_Controls
| Symbol = NMT2
| update_page = yes
| Name =  Human N-myristoyltransferase 2
| require_manual_inspection = no
| image = 4c2x_Human_N-myristoyltransferase_isoform_2_NMT2.png
| update_protein_box = yes
| width = 310px
| update_summary = yes
| caption = Human N-myristoyltransferase isoform 2 (NMT2) (based on PDB: 4c2x)
| update_citations = yes
| Pfam= PF01233.14
| InterPro= IPR022676
| SMART=
| SCOP =
| TCDB =
| OPM family=
| OPM protein=
}}
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{Infobox_gene}}
{{GNF_Protein_box
'''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]].<ref name="pmid9506952">{{cite journal | vauthors = Giang DK, Cravatt BF | title = A second mammalian N-myristoyltransferase | journal = J Biol Chem | volume = 273 | issue = 12 | pages = 6595–8 | date = Apr 1998 | pmid = 9506952 | pmc =  | doi = 10.1074/jbc.273.12.6595 }}</ref>
| image =
 
| image_source = 
== Function ==
| PDB =
 
| Name = N-myristoyltransferase 2
N-myristoyltransferase (NMT) catalyzes the reaction of N-terminal [[myristoylation]] of many [[signaling protein]]s. 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.<ref>{{cite journal | vauthors = Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW | title = Global profiling of co- and post-translationally N-myristoylated proteomes in human cells. | journal = Nat Commun | volume = 5 | issue = | pages = 4919 | year = 2014 | pmid = 25255805 | doi = 10.1038/ncomms5919 | pmc=4200515}}</ref>
| HGNCid = 7858
 
| Symbol = NMT2
==Interactions==
| AltSymbols =;
NMT2 has been shown to [[Protein-protein interaction|interact]] with:
| OMIM = 603801
* [[caspase 3]]<ref>{{cite journal | vauthors = Selvakumar P, Sharma RK | title = Role of calpain and caspase system in the regulation of N-myristoyltransferase in human colon cancer (Review). | journal = Int J Mol Med | volume = 19 | issue = 5 | pages = 823–7 | year = 2007 | pmid = 17390089 | doi = 10.3892/ijmm.19.5.823}}</ref>
| ECnumber =
* [[MARCKS]]<ref>{{cite journal | vauthors = Selvakumar P, Lakshmikuttyamma A, Sharma RK | title = Biochemical characterization of bovine brain myristoyl-CoA:protein N-myristoyltransferase type 2. | journal = J Biomed Biotechnol | volume = 2009 | issue =  | pages = 907614 | year = 2009 | pmid = 19746168 | doi = 10.1155/2009/907614 | pmc=2737134}}</ref>
| Homologene = 68416
| MGIid = 1202298
  | GeneAtlas_image1 = PBB_GE_NMT2_205005_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NMT2_205006_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0004379 |text = glycylpeptide N-tetradecanoyltransferase activity}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =  
| Process = {{GNF_GO|id=GO:0006499 |text = N-terminal protein myristoylation}} {{GNF_GO|id=GO:0009249 |text = protein lipoylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 9397
    | Hs_Ensembl = ENSG00000152465
    | Hs_RefseqProtein = NP_004799
    | Hs_RefseqmRNA = NM_004808
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 15189909
    | Hs_GenLoc_end = 15250698
    | Hs_Uniprot = O60551
    | Mm_EntrezGene = 18108
    | Mm_Ensembl = ENSMUSG00000026643
    | Mm_RefseqmRNA = NM_008708
    | Mm_RefseqProtein = NP_032734
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 3201484
    | Mm_GenLoc_end = 3256020
    | Mm_Uniprot = Q3THR4
  }}
}}
'''N-myristoyltransferase 2''', also known as '''NMT2''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==See also==
{{PBB_Summary
* [[N-myristoyltransferase 1]]
| section_title =  
| summary_text = 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 predicted 498-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.<ref name="entrez">{{cite web | title = Entrez Gene: NMT2 N-myristoyltransferase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9397| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}


==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal | vauthors = Kolluri SK, Balduf C, Hofmann M, Göttlicher M | title = Novel target genes of the Ah (dioxin) receptor: transcriptional induction of N-myristoyltransferase 2 | journal = Cancer Res. | volume = 61 | issue = 23 | pages = 8534–9 | year = 2002 | pmid = 11731439 | doi =  }}
| citations =
* {{cite journal | vauthors = 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 | title = Validation of N-myristoyltransferase as an antimalarial drug target using an integrated chemical biology approach. | url=http://eprints.whiterose.ac.uk/121536/ | journal = Nat Chem | volume = 6 | issue = 2 | pages = 112–21 | year = 2014 | pmid = 24451586 | doi = 10.1038/nchem.1830 | pmc=4739506}}
*{{cite journal  | author=Pal R, Reitz MS, Tschachler E, ''et al.'' |title=Myristoylation of gag proteins of HIV-1 plays an important role in virus assembly. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 6 |pages= 721-30 |year= 1990 |pmid= 2194551 |doi=  }}
*{{cite journal  | author=Bryant M, Ratner L |title=Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 523-7 |year= 1990 |pmid= 2405382 |doi=  }}
*{{cite journal  | author=Tashiro A, Shoji S, Kubota Y |title=Antimyristoylation of the gag proteins in the human immunodeficiency virus-infected cells with N-myristoyl glycinal diethylacetal resulted in inhibition of virus production. |journal=Biochem. Biophys. Res. Commun. |volume=165 |issue= 3 |pages= 1145-54 |year= 1990 |pmid= 2692561 |doi=  }}
*{{cite journal  | author=Goddard C, Aquino A, Glazer RI, Felsted RL |title=Chemical characterization of p17gag from human immunodeficiency virus as an N-terminally myristoylated protein. |journal=Eur. J. Biochem. |volume=182 |issue= 2 |pages= 323-6 |year= 1989 |pmid= 2737204 |doi=  }}
*{{cite journal  | author=Göttlinger HG, Sodroski JG, Haseltine WA |title=Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 15 |pages= 5781-5 |year= 1989 |pmid= 2788277 |doi=  }}
*{{cite journal | author=Lee PP, Linial ML |title=Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal. |journal=J. Virol. |volume=68 |issue= 10 |pages= 6644-54 |year= 1994 |pmid= 7521919 |doi=  }}
*{{cite journal  | author=Zhou W, Parent LJ, Wills JW, Resh MD |title=Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. |journal=J. Virol. |volume=68 |issue= 4 |pages= 2556-69 |year= 1994 |pmid= 8139035 |doi=  }}
*{{cite journal  | author=Morikawa Y, Hinata S, Tomoda H, ''et al.'' |title=Complete inhibition of human immunodeficiency virus Gag myristoylation is necessary for inhibition of particle budding. |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2868-73 |year= 1996 |pmid= 8576268 |doi=  }}
*{{cite journal  | author=Zhou W, Resh MD |title=Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. |journal=J. Virol. |volume=70 |issue= 12 |pages= 8540-8 |year= 1997 |pmid= 8970978 |doi=  }}
*{{cite journal  | author=Spearman P, Horton R, Ratner L, Kuli-Zade I |title=Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism. |journal=J. Virol. |volume=71 |issue= 9 |pages= 6582-92 |year= 1997 |pmid= 9261380 |doi=  }}
*{{cite journal  | author=Furuishi K, Matsuoka H, Takama M, ''et al.'' |title=Blockage of N-myristoylation of HIV-1 gag induces the production of impotent progeny virus. |journal=Biochem. Biophys. Res. Commun. |volume=237 |issue= 3 |pages= 504-11 |year= 1997 |pmid= 9299393 |doi= 10.1006/bbrc.1997.7178 }}
*{{cite journal  | author=Giang DK, Cravatt BF |title=A second mammalian N-myristoyltransferase. |journal=J. Biol. Chem. |volume=273 |issue= 12 |pages= 6595-8 |year= 1998 |pmid= 9506952 |doi=  }}
*{{cite journal  | author=Hermida-Matsumoto L, Resh MD |title=Human immunodeficiency virus type 1 protease triggers a myristoyl switch that modulates membrane binding of Pr55(gag) and p17MA. |journal=J. Virol. |volume=73 |issue= 3 |pages= 1902-8 |year= 1999 |pmid= 9971769 |doi=  }}
*{{cite journal  | author=Paillart JC, Göttlinger HG |title=Opposing effects of human immunodeficiency virus type 1 matrix mutations support a myristyl switch model of gag membrane targeting. |journal=J. Virol. |volume=73 |issue= 4 |pages= 2604-12 |year= 1999 |pmid= 10074105 |doi=  }}
*{{cite journal  | author=Ono A, Freed EO |title=Binding of human immunodeficiency virus type 1 Gag to membrane: role of the matrix amino terminus. |journal=J. Virol. |volume=73 |issue= 5 |pages= 4136-44 |year= 1999 |pmid= 10196310 |doi=  }}
*{{cite journal  | author=Shiraishi T, Misumi S, Takama M, ''et al.'' |title=Myristoylation of human immunodeficiency virus type 1 gag protein is required for efficient env protein transportation to the surface of cells. |journal=Biochem. Biophys. Res. Commun. |volume=282 |issue= 5 |pages= 1201-5 |year= 2001 |pmid= 11302743 |doi= 10.1006/bbrc.2001.4696 }}
*{{cite journal  | author=Kolluri SK, Balduf C, Hofmann M, Göttlicher M |title=Novel target genes of the Ah (dioxin) receptor: transcriptional induction of N-myristoyltransferase 2. |journal=Cancer Res. |volume=61 |issue= 23 |pages= 8534-9 |year= 2002 |pmid= 11731439 |doi=  }}
*{{cite journal | author=Lindwasser OW, Resh MD |title=Myristoylation as a target for inhibiting HIV assembly: unsaturated fatty acids block viral budding. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 20 |pages= 13037-42 |year= 2002 |pmid= 12244217 |doi= 10.1073/pnas.212409999 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Bouamr F, Scarlata S, Carter C |title=Role of myristylation in HIV-1 Gag assembly. |journal=Biochemistry |volume=42 |issue= 21 |pages= 6408-17 |year= 2003 |pmid= 12767222 |doi= 10.1021/bi020692z }}
}}
{{refend}}
{{refend}}


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Latest revision as of 12:59, 4 October 2017

Human N-myristoyltransferase 2
File:4c2x Human N-myristoyltransferase isoform 2 NMT2.png
Human N-myristoyltransferase isoform 2 (NMT2) (based on PDB: 4c2x)
Identifiers
SymbolNMT2
PfamPF01233.14
InterProIPR022676
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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:

See also

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. PMC 4200515. 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. PMC 2737134. PMID 19746168.

Further reading


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