Glycylpeptide N-tetradecanoyltransferase 1

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Protein names

Recommended name:
    Glycylpeptide N-tetradecanoyltransferase 1
    EC=2.3.1.97
Alternative name(s):
    Peptide N-myristoyltransferase 1
    Myristoyl-CoA:protein N-myristoyltransferase 1
      Short name=NMT 1
      Short name=Type I N-myristoyltransferase

Gene names

Name:	NMT1
Synonyms:	NMT

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Sequence length	496 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

Function	Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins.
Catalytic activity	Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.
Subcellular location	Cytoplasm.
Tissue specificity	Heart, gut, kidney, liver and placenta.
Sequence similarities	Belongs to the NMT family.

Hide | Top

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	N-terminal protein myristoylation Non-traceable author statement. Source: UniProtKB protein lipoylation Ref.2 Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	glycylpeptide N-tetradecanoyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Hide | Top

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 496

496

Glycylpeptide N-tetradecanoyltransferase 1

PRO_0000064221

Compositional bias

55 – 67

13

Poly-Lys

Modified residue

31

1

Phosphoserine By similarity

Modified residue

47

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Alternative sequence

1 – 80

80

Missing in isoform Short.

VSP_003570

Natural variant

61

1

Q → K: dbSNP rs3087878.

VAR_050286

Mutagenesis

492

1

G → D or K: Reduced activity. Ref.6

1

.

496

Helix Strand Turn

Details...

Hide | Top

Sequence		Length	Mass (Da)
Isoform Long [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 7661140D3837BE7A Show »	FASTA	496	56,806
10 20 30 40 50 60 MADESETAVK PPAPPLPQMM EGNGNGHEHC SDCENEEDNS YNRGGLSPAN DTGAKKKKKK 70 80 90 100 110 120 QKKKKEKGSE TDSAQDQPVK MNSLPAERIQ EIQKAIELFS VGQGPAKTME EASKRSYQFW 130 140 150 160 170 180 DTQPVPKLGE VVNTHGPVEP DKDNIRQEPY TLPQGFTWDA LDLGDRGVLK ELYTLLNENY 190 200 210 220 230 240 VEDDDNMFRF DYSPEFLLWA LRPPGWLPQW HCGVRVVSSR KLVGFISAIP ANIHIYDTEK 250 260 270 280 290 300 KMVEINFLCV HKKLRSKRVA PVLIREITRR VHLEGIFQAV YTAGVVLPKP VGTCRYWHRS 310 320 330 340 350 360 LNPRKLIEVK FSHLSRNMTM QRTMKLYRLP ETPKTAGLRP METKDIPVVH QLLTRYLKQF 370 380 390 400 410 420 HLTPVMSQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF YTLPSTIMNH PTHKSLKAAY 430 440 450 460 470 480 SFYNVHTQTP LLDLMSDALV LAKMKGFDVF NALDLMENKT FLEKLKFGIG DGNLQYYLYN 490 WKCPSMGAEK VGLVLQ « Hide
Isoform Short. Checksum: CF08D233B6DD9383 Show »	FASTA	416	48,141
10 20 30 40 50 60 MNSLPAERIQ EIQKAIELFS VGQGPAKTME EASKRSYQFW DTQPVPKLGE VVNTHGPVEP 70 80 90 100 110 120 DKDNIRQEPY TLPQGFTWDA LDLGDRGVLK ELYTLLNENY VEDDDNMFRF DYSPEFLLWA 130 140 150 160 170 180 LRPPGWLPQW HCGVRVVSSR KLVGFISAIP ANIHIYDTEK KMVEINFLCV HKKLRSKRVA 190 200 210 220 230 240 PVLIREITRR VHLEGIFQAV YTAGVVLPKP VGTCRYWHRS LNPRKLIEVK FSHLSRNMTM 250 260 270 280 290 300 QRTMKLYRLP ETPKTAGLRP METKDIPVVH QLLTRYLKQF HLTPVMSQEE VEHWFYPQEN 310 320 330 340 350 360 IIDTFVVENA NGEVTDFLSF YTLPSTIMNH PTHKSLKAAY SFYNVHTQTP LLDLMSDALV 370 380 390 400 410 LAKMKGFDVF NALDLMENKT FLEKLKFGIG DGNLQYYLYN WKCPSMGAEK VGLVLQ « Hide

Hide | Top

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction." Glover C.J., Hartman K.D., Felsted R.L. J. Biol. Chem. 272:28680-28689(1997) [PubMed: 9353336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A second mammalian N-myristoyltransferase." Giang D.K., Cravatt B.F. J. Biol. Chem. 273:6595-6598(1998) [PubMed: 9506952] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT). Tissue: Muscle and Skin.
[6]	"Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae." Duronio R.J., Reed S.I., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 89:4129-4133(1992) [PubMed: 1570339] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-496, MUTAGENESIS OF GLY-492.
[7]	"Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme." Mcilhinney R.A.J., Young K., Egerton M., Camble R., White A., Soloviev M. Biochem. J. 333:491-495(1998) [PubMed: 9677304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-89.
[8]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Hide | Top

AF043324 mRNA. Translation: AAC09294.1. Different initiation.
AF020500 mRNA. Translation: AAB95316.1.
AK291936 mRNA. Translation: BAF84625.1.
CH471178 Genomic DNA. Translation: EAW51554.1.
BC006538 mRNA. Translation: AAH06538.1.
BC006569 mRNA. Translation: AAH06569.1.
BC007258 mRNA. Translation: AAH07258.2.
BC008312 mRNA. Translation: AAH08312.2.
M86707 mRNA. No translation available.
Y17208 mRNA. Translation: CAA76685.1.
Y17209 mRNA. Translation: CAA76686.1.

IPI

IPI00218830.
IPI00329692.

PIR

JC1343.

RefSeq

NP_066565.1.

UniGene

Hs.532790

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RXT	X-ray	3.00	A/B/C/D	1-496	[»]
3IU1	X-ray	1.42	A/B	115-496	[»]
3IU2	X-ray	1.73	A/B	115-496	[»]
3IWE	X-ray	1.79	A/B	115-496	[»]
3JTK	X-ray	1.61	A/B	115-496	[»]

ModBase

Search...

STRING

P30419.

PhosphoSite

P30419.

PRIDE

P30419.

Ensembl

ENST00000258960; ENSP00000258960; ENSG00000136448; Homo sapiens. [Genome view]

GeneID

4836.

KEGG

hsa:4836.

UCSC

uc002ihz.1. human.

CTD

4836.

GeneCards

GC17P040494.

H-InvDB

HIX0013891.

HGNC

HGNC:7857. NMT1.

HPA

HPA022949.
HPA022963.

MIM

160993. gene.

PharmGKB

PA27443.

GenAtlas

Search...

HOVERGEN

P30419.

OMA

YRLPETP.

BRENDA

2.3.1.97. 247.

Reactome

REACT_578. Apoptosis.

ArrayExpress

P30419.

Bgee

P30419.

CleanEx

HS_NMT1.

Genevestigator

P30419.

GermOnline

ENSG00000136448. Homo sapiens.

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000903. Myristoyl_trans.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 2 hits.

PANTHER

PTHR11377. Myristoyl_trans. 1 hit.

Pfam

PF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]

PIRSF

PIRSF015892. N-myristl_transf. 1 hit.

PROSITE

PS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

NextBio

18634.

SOURCE

Search...

Hide | Top

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P30419-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P30419-2)

The sequence of this isoform differs from the canonical sequence as follows:
1-80: Missing.

Entry name

NMT1_HUMAN

Accession

Primary (citable) accession number: P30419
Secondary accession number(s): A8K7C1, Q9UE09

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 11, 2001
Last modified:	November 3, 2009
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Hide | Top