NMT1 N-myristoyltransferase 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: NMT1provided by HGNC
Official Full Name: N-myristoyltransferase 1provided by HGNC
Primary source: HGNC:HGNC:7857
See related: Ensembl:ENSG00000136448 MIM:160993; AllianceGenome:HGNC:7857
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: NMT; HsNMT1
Summary: Myristate, a rare 14-carbon saturated fatty acid, is cotranslationally attached by an amide linkage to the N-terminal glycine residue of cellular and viral proteins with diverse functions. N-myristoyltransferase (NMT; EC 2.3.1.97) catalyzes the transfer of myristate from CoA to proteins. N-myristoylation appears to be irreversible and is required for full expression of the biologic activities of several N-myristoylated proteins, including the alpha subunit of the signal-transducing guanine nucleotide-binding protein (G protein) GO (GNAO1; MIM 139311) (Duronio et al., 1992 [PubMed 1570339]).[supplied by OMIM, Nov 2008]
Expression: Ubiquitous expression in brain (RPKM 21.5), thyroid (RPKM 17.0) and 25 other tissues See more
Orthologs: mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 17q21.31

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	17	NC_000017.11 (45061317..45109016)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	17	NC_060941.1 (45915189..45962892)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	17	NC_000017.10 (43138685..43186384)

Chromosome 17 - NC_000017.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

SPI1 Mediates N-Myristoyltransferase 1 to Advance Gastric Cancer Progression via PI3K/AKT/mTOR Pathway.
Title: SPI1 Mediates N-Myristoyltransferase 1 to Advance Gastric Cancer Progression via PI3K/AKT/mTOR Pathway.
N-mytistoyltransferase 1 and 2 are potential tumor suppressors and novel targets of miR-182 in human non-small cell lung carcinomas.
Title: N-mytistoyltransferase 1 and 2 are potential tumor suppressors and novel targets of miR-182 in human non-small cell lung carcinomas.
N-myristoyltransferase-1 deficiency blocks myristoylation of LAMTOR1 and inhibits bladder cancer progression.
Title: N-myristoyltransferase-1 deficiency blocks myristoylation of LAMTOR1 and inhibits bladder cancer progression.
mTOR, a downstream target of PKB/Akt, regulates NMT1 in ER positive breast cancer cells (MCF7 cells). NMT1 increased with rapamycin treatment over the period of time with a concomitant decrease in mTOR phosphorylation.
Title: Investigation of Novel Regulation of N-myristoyltransferase by Mammalian Target of Rapamycin in Breast Cancer Cells.
inhibition of NMT1 caused degraded proteins increase and ER stress, which cross-talked with mitochondria to produce more ROS. And both of oxidative stress and ER stress could activate JNK pathway, leading to autophagy which abrogated breast cancer progression especially triple-negative breast cancer (TNBC).
Title: NMT1 inhibition modulates breast cancer progression through stress-triggered JNK pathway.
Data showed that rheumatoid arthritis (RA) T cells had a defect in type I N-myristoyltransferase (NMT1) function, which prevented AMP-activated protein kinase (AMPK) activation.
Title: N-myristoyltransferase deficiency impairs activation of kinase AMPK and promotes synovial tissue inflammation.
Genetic and pharmacologic evidence that inhibiting the N-myristoyltransferase NMT1 suppresses cell-cycle progression, proliferation, and malignant growth of prostate cancer cells.
Title: Blocking Myristoylation of Src Inhibits Its Kinase Activity and Suppresses Prostate Cancer Progression.
These observations point at a previously unrecognized contribution of calnexin to the retention of NMT1 at the ER membrane.
Title: N-Myristoyltransferase 1 interacts with calnexin at the endoplasmic reticulum.
findings suggest that both NMT1 and hnRNP A2/B1 take part in the regulation of HIV-1 RNA expression through their mutual opposite effects on the viral RNA expression in HIV-1-producing cells
Title: N-Myristoyltransferase 1 enhances human immunodeficiency virus replication through regulation of viral RNA expression level.
we propose a model of the Nef:NMT complex in which only the myristoyl moiety holds the two proteins together in complex and speculate that perhaps NMT chaperones Nef to the membrane and thereby protects the myristic acid group from the cytosol
Title: Effects of HIV-1 Nef on human N-myristoyltransferase 1.

Submit: New GeneRIF Correction See all GeneRIFs (18)

Phenotypes

Go to the top of the page Help

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

Go to the top of the page Help

Replication interactions

Interaction	Pubs
Knockdown of N-myristoyltransferase 1 (NMT1) by siRNA inhibits HIV-1 replication in HeLa-derived TZM-bl cells	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Nef	nef	HIV-1 Nef is identified to have a physical interaction with N-myristoyltransferase 1 (NMT1) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	PubMed
	nef	The N-terminal glycine of HIV-1 Nef is myristoylated by N-myristoyltransferase	PubMed
	nef	p65 N-myristoyltransferase isoform 1 coimmunoprecipitates with HIV-1 Nef in experiments using antibodies to Nef, and this interaction requires an intact myristoylation signal in Nef	PubMed
matrix	gag	NMR studies of membrane binding-defective V7R and L8A HIV-1 Matrix mutants reveal minor structural changes that appear to be responsible for stabilizing the myristate-sequestered (myr(s)) species and inhibiting exposure	PubMed
	gag	HIV-1 Matrix is myristoylated on its N-terminal glycine residue by N-myristoyltransferase, a chemical modification important for membrane targeting of Gag/Matrix, for facilitating Matrix multimerization, and for virus particle formation and budding	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Markers

WI-13574 (e-PCR)
- UniSTS:74772

RH70326 (e-PCR)
- UniSTS:46123

NMT1_8508 (e-PCR)
- UniSTS:467801

STS-M86707 (e-PCR)
- UniSTS:26977

MARC_16857-16858:1015861084:3 (e-PCR)
- UniSTS:268139

D17S1494E (e-PCR)
- UniSTS:151699

RH66609 (e-PCR)
- UniSTS:26300

SHGC-34291 (e-PCR)
- UniSTS:3300

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables glycylpeptide N-tetradecanoyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables glycylpeptide N-tetradecanoyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables glycylpeptide N-tetradecanoyltransferase activity	TAS Traceable Author Statement more info
enables myristoyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables myristoyltransferase activity	TAS Traceable Author Statement more info
enables peptidyl-lysine N6-myristoyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in N-terminal peptidyl-glycine N-myristoylation	IDA Inferred from Direct Assay more info	PubMed
involved_in cellular ketone metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in in utero embryonic development	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of establishment of protein localization to mitochondrion	TAS Traceable Author Statement more info
involved_in protein localization to membrane	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein localization to membrane	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of opsin-mediated signaling pathway	TAS Traceable Author Statement more info

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	TAS Traceable Author Statement more info
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: glycylpeptide N-tetradecanoyltransferase 1

Names: alternative, short form NMT-S; long form, NMT-L; myristoyl-CoA:protein N-myristoyltransferase 1; protein-lysine myristoyltransferase NMT1; type I N-myristoyltransferase

NP_066565.1

EC 2.3.1.97

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.