N-myristoyltransferase 1: Difference between revisions

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{{Infobox_gene}}
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'''Glycylpeptide N-tetradecanoyltransferase 1''' also known as '''myristoyl-CoA:protein N-myristoyltransferase 1''' ('''NMT-1''') is an [[enzyme]] that in humans is encoded by the ''NMT1'' [[gene]].<ref name="pmid1570339">{{cite journal |vauthors=Duronio RJ, Reed SI, Gordon JI | title = Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae | journal = Proc Natl Acad Sci U S A | volume = 89 | issue = 9 | pages = 4129–33 |date=May 1992 | pmid = 1570339 | pmc = 525646 | doi =10.1073/pnas.89.9.4129  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NMT1 N-myristoyltransferase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4836| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==References==
{{GNF_Protein_box
{{reflist}}
| image = PBB_Protein_NMT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1rxt.
| PDB = {{PDB2|1rxt}}
| Name = N-myristoyltransferase 1
| HGNCid = 7857
| Symbol = NMT1
| AltSymbols =; NMT
| OMIM = 160993
| ECnumber = 
| Homologene = 69027
| MGIid = 102579
| GeneAtlas_image1 = PBB_GE_NMT1_201157_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NMT1_201158_at_tn.png
| GeneAtlas_image3 = PBB_GE_NMT1_201159_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 = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0006498 |text = N-terminal protein lipidation}} {{GNF_GO|id=GO:0006499 |text = N-terminal protein myristoylation}} {{GNF_GO|id=GO:0009249 |text = protein lipoylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4836
    | Hs_Ensembl = ENSG00000136448
    | Hs_RefseqProtein = NP_066565
    | Hs_RefseqmRNA = NM_021079
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 40494206
    | Hs_GenLoc_end = 40541903
    | Hs_Uniprot = P30419
    | Mm_EntrezGene = 18107
    | Mm_Ensembl = ENSMUSG00000020936
    | Mm_RefseqmRNA = XM_906274
    | Mm_RefseqProtein = XP_911367
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 102844436
    | Mm_GenLoc_end = 102885002
    | Mm_Uniprot = Q3UJC3
  }}
}}
'''N-myristoyltransferase 1''', also known as '''NMT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NMT1 N-myristoyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4836| accessdate = }}</ref>
 
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{{PBB_Summary
| section_title =
| summary_text =
}}


==References==
{{reflist|2}}
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal   |vauthors=Rajala RV, Datla RS, Moyana TN, etal |title=N-myristoyltransferase. |journal=Mol. Cell. Biochem. |volume=204 |issue= 1–2 |pages= 135–55 |year= 2000 |pmid= 10718634 |doi=10.1023/A:1007012622030 }}
| citations =
*{{cite journal  |vauthors=Geyer M, Fackler OT, Peterlin BM |title=Structure--function relationships in HIV-1 Nef |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580–5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 | pmc=1083955 }}
*{{cite journal | author=Rajala RV, Datla RS, Moyana TN, ''et al.'' |title=N-myristoyltransferase. |journal=Mol. Cell. Biochem. |volume=204 |issue= 1-2 |pages= 135-55 |year= 2000 |pmid= 10718634 |doi=  }}
*{{cite journal  |vauthors=Wice BM, Gordon JI |title=A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin |journal=J. Cell Biol. |volume=116 |issue= 2 |pages= 405–22 |year= 1992 |pmid= 1530946 |doi=10.1083/jcb.116.2.405  | pmc=2289284 }}
*{{cite journal  | author=Geyer M, Fackler OT, Peterlin BM |title=Structure--function relationships in HIV-1 Nef. |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580-5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 }}
*{{cite journal  |vauthors=Mumby SM, Heukeroth RO, Gordon JI, Gilman AG |title=G-protein alpha-subunit expression, myristoylation, and membrane association in COS cells |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 728–32 |year= 1990 |pmid= 2153964 |doi=10.1073/pnas.87.2.728  | pmc=53339  }}
*{{cite journal  | author=Wice BM, Gordon JI |title=A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexin. |journal=J. Cell Biol. |volume=116 |issue= 2 |pages= 405-22 |year= 1992 |pmid= 1530946 |doi=  }}
*{{cite journal   |vauthors=Pal R, Reitz MS, Tschachler E, etal |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=10.1089/aid.1990.6.721 }}
*{{cite journal  | author=Duronio RJ, Reed SI, Gordon JI |title=Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 9 |pages= 4129-33 |year= 1992 |pmid= 1570339 |doi= }}
*{{cite journal  |vauthors=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=10.1073/pnas.87.2.523  | pmc=53297  }}
*{{cite journal | author=Mumby SM, Heukeroth RO, Gordon JI, Gilman AG |title=G-protein alpha-subunit expression, myristoylation, and membrane association in COS cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 728-32 |year= 1990 |pmid= 2153964 |doi=  }}
*{{cite journal  |vauthors=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=10.1016/0006-291X(89)92722-8 }}
*{{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  |vauthors=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=10.1111/j.1432-1033.1989.tb14833.x }}
*{{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  |vauthors=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=10.1073/pnas.86.15.5781  | pmc=297714  }}
*{{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   |vauthors=Schultz AM, Henderson LE, Oroszlan S, etal |title=Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein |journal=Science |volume=227 |issue= 4685 |pages= 427–9 |year= 1985 |pmid= 3917576 |doi=10.1126/science.3917576 }}
*{{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  |vauthors=Liu J, Sessa WC |title=Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 11691–4 |year= 1994 |pmid= 7512951 |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  |vauthors=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= | pmc=237085 }}
*{{cite journal  | author=Schultz AM, Henderson LE, Oroszlan S, ''et al.'' |title=Amino terminal myristylation of the protein kinase p60src, a retroviral transforming protein. |journal=Science |volume=227 |issue= 4685 |pages= 427-9 |year= 1985 |pmid= 3917576 |doi=  }}
*{{cite journal   |vauthors=Sigal CT, Zhou W, Buser CA, etal |title=Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 25 |pages= 12253–7 |year= 1995 |pmid= 7527558 |doi=10.1073/pnas.91.25.12253  | pmc=45415  }}
*{{cite journal  | author=Liu J, Sessa WC |title=Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 11691-4 |year= 1994 |pmid= 7512951 |doi=  }}
*{{cite journal  |vauthors=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= | pmc=236733 }}
*{{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  |vauthors=Kobayashi M, Takamatsu K, Saitoh S, Noguchi T |title=Myristoylation of hippocalcin is linked to its calcium-dependent membrane association properties |journal=J. Biol. Chem. |volume=268 |issue= 25 |pages= 18898–904 |year= 1993 |pmid= 8360179 |doi=  }}
*{{cite journal  | author=Sigal CT, Zhou W, Buser CA, ''et al.'' |title=Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 25 |pages= 12253-7 |year= 1995 |pmid= 7527558 |doi=  }}
*{{cite journal   |vauthors=Morikawa Y, Hinata S, Tomoda H, etal |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=10.1074/jbc.271.5.2868 }}
*{{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   |vauthors=Andersson B, Wentland MA, Ricafrente JY, etal |title=A "double adaptor" method for improved shotgun library construction |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Kobayashi M, Takamatsu K, Saitoh S, Noguchi T |title=Myristoylation of hippocalcin is linked to its calcium-dependent membrane association properties. |journal=J. Biol. Chem. |volume=268 |issue= 25 |pages= 18898-904 |year= 1993 |pmid= 8360179 |doi=  }}
*{{cite journal  |vauthors=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= | pmc=190946  }}
*{{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   |vauthors=Yu W, Andersson B, Worley KC, etal |title=Large-scale concatenation cDNA sequencing |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=  10.1101/gr.7.4.353| pmc=139146 }}
*{{cite journal  | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{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=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==See also==
{{WikiDoc Sources}}
* [[Myristoylation]]
* [[NMT2|N-myristoyltransferase 2]]
 
{{PDB Gallery|geneid=4836}}
{{Acyltransferases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
 
[[Category:EC 2.3.1]]
[[Category:Human proteins]]
 
 
{{gene-17-stub}}

Latest revision as of 11:32, 1 August 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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

Glycylpeptide N-tetradecanoyltransferase 1 also known as myristoyl-CoA:protein N-myristoyltransferase 1 (NMT-1) is an enzyme that in humans is encoded by the NMT1 gene.[1][2]

References

  1. ↑ Duronio RJ, Reed SI, Gordon JI (May 1992). "Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae". Proc Natl Acad Sci U S A. 89 (9): 4129–33. doi:10.1073/pnas.89.9.4129. PMC 525646. PMID 1570339.
  2. ↑ "Entrez Gene: NMT1 N-myristoyltransferase 1".

Further reading

See also


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