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Protein

Glycylpeptide N-tetradecanoyltransferase 1

Gene

NMT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins.3 Publications

Catalytic activityi

Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciZFISH:HS06161-MONOMER.
BRENDAi2.3.1.97. 2681.
ReactomeiR-HSA-162599. Late Phase of HIV Life Cycle.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-75108. Activation, myristolyation of BID and translocation to mitochondria.
SIGNORiP30419.

Chemistry databases

SwissLipidsiSLP:000001287.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycylpeptide N-tetradecanoyltransferase 1 (EC:2.3.1.973 Publications)
Alternative name(s):
Myristoyl-CoA:protein N-myristoyltransferase 1
Short name:
NMT 1
Short name:
Type I N-myristoyltransferase
Peptide N-myristoyltransferase 1
Gene namesi
Name:NMT1
Synonyms:NMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7857. NMT1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • cell junction Source: HPA
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extrinsic component of membrane Source: UniProtKB
  • mitochondrion Source: GOC
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi492G → D or K: Reduced activity. 1 Publication1

Organism-specific databases

DisGeNETi4836.
OpenTargetsiENSG00000136448.
PharmGKBiPA31661.

Chemistry databases

ChEMBLiCHEMBL2593.

Polymorphism and mutation databases

BioMutaiNMT1.
DMDMi12231020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000642211 – 496Glycylpeptide N-tetradecanoyltransferase 1Add BLAST496

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31PhosphoserineBy similarity1
Modified residuei47PhosphoserineCombined sources1
Modified residuei83PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP30419.
MaxQBiP30419.
PaxDbiP30419.
PeptideAtlasiP30419.
PRIDEiP30419.
TopDownProteomicsiP30419-2. [P30419-2]

PTM databases

iPTMnetiP30419.
PhosphoSitePlusiP30419.
SwissPalmiP30419.

Expressioni

Tissue specificityi

Heart, gut, kidney, liver and placenta.

Gene expression databases

BgeeiENSG00000136448.
CleanExiHS_NMT1.
ExpressionAtlasiP30419. baseline and differential.
GenevisibleiP30419. HS.

Organism-specific databases

HPAiHPA022949.
HPA022963.

Interactioni

Protein-protein interaction databases

BioGridi110899. 81 interactors.
IntActiP30419. 20 interactors.
MINTiMINT-5004170.
STRINGi9606.ENSP00000258960.

Chemistry databases

BindingDBiP30419.

Structurei

Secondary structure

1496
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi120 – 122Combined sources3
Beta strandi123 – 125Combined sources3
Beta strandi156 – 160Combined sources5
Helixi166 – 179Combined sources14
Beta strandi188 – 190Combined sources3
Helixi194 – 201Combined sources8
Helixi208 – 210Combined sources3
Beta strandi211 – 216Combined sources6
Turni217 – 219Combined sources3
Beta strandi222 – 235Combined sources14
Beta strandi238 – 250Combined sources13
Helixi252 – 254Combined sources3
Helixi259 – 272Combined sources14
Turni273 – 275Combined sources3
Beta strandi279 – 285Combined sources7
Beta strandi291 – 302Combined sources12
Helixi303 – 308Combined sources6
Helixi320 – 327Combined sources8
Beta strandi338 – 340Combined sources3
Helixi343 – 345Combined sources3
Helixi346 – 356Combined sources11
Helixi357 – 359Combined sources3
Beta strandi360 – 365Combined sources6
Helixi368 – 375Combined sources8
Turni379 – 381Combined sources3
Beta strandi382 – 388Combined sources7
Beta strandi390 – 392Combined sources3
Beta strandi394 – 402Combined sources9
Beta strandi405 – 407Combined sources3
Beta strandi418 – 421Combined sources4
Beta strandi427 – 429Combined sources3
Helixi431 – 444Combined sources14
Beta strandi448 – 454Combined sources7
Helixi458 – 460Combined sources3
Turni461 – 466Combined sources6
Beta strandi468 – 480Combined sources13
Helixi488 – 490Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RXTX-ray3.00A/B/C/D1-496[»]
3IU1X-ray1.42A/B115-496[»]
3IU2X-ray1.73A/B115-496[»]
3IWEX-ray1.79A/B115-496[»]
3JTKX-ray1.61A/B115-496[»]
4C2YX-ray1.64A/B109-496[»]
4C2ZX-ray2.08A/B109-496[»]
ProteinModelPortaliP30419.
SMRiP30419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30419.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni118 – 120Myristoyl-CoA binding2 Publications3
Regioni248 – 250Myristoyl-CoA binding2 Publications3
Regioni256 – 260Myristoyl-CoA binding2 Publications5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi55 – 67Poly-LysAdd BLAST13

Sequence similaritiesi

Belongs to the NMT family.Curated

Phylogenomic databases

eggNOGiKOG2779. Eukaryota.
COG5092. LUCA.
GeneTreeiENSGT00390000017837.
HOGENOMiHOG000189123.
HOVERGENiHBG003404.
InParanoidiP30419.
KOiK00671.
OMAiEMCTEVY.
OrthoDBiEOG091G06JB.
PhylomeDBiP30419.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
PANTHERiPTHR11377. PTHR11377. 1 hit.
PfamiPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P30419-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MADESETAVK PPAPPLPQMM EGNGNGHEHC SDCENEEDNS YNRGGLSPAN
60 70 80 90 100
DTGAKKKKKK QKKKKEKGSE TDSAQDQPVK MNSLPAERIQ EIQKAIELFS
110 120 130 140 150
VGQGPAKTME EASKRSYQFW DTQPVPKLGE VVNTHGPVEP DKDNIRQEPY
160 170 180 190 200
TLPQGFTWDA LDLGDRGVLK ELYTLLNENY VEDDDNMFRF DYSPEFLLWA
210 220 230 240 250
LRPPGWLPQW HCGVRVVSSR KLVGFISAIP ANIHIYDTEK KMVEINFLCV
260 270 280 290 300
HKKLRSKRVA PVLIREITRR VHLEGIFQAV YTAGVVLPKP VGTCRYWHRS
310 320 330 340 350
LNPRKLIEVK FSHLSRNMTM QRTMKLYRLP ETPKTAGLRP METKDIPVVH
360 370 380 390 400
QLLTRYLKQF HLTPVMSQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF
410 420 430 440 450
YTLPSTIMNH PTHKSLKAAY SFYNVHTQTP LLDLMSDALV LAKMKGFDVF
460 470 480 490
NALDLMENKT FLEKLKFGIG DGNLQYYLYN WKCPSMGAEK VGLVLQ
Length:496
Mass (Da):56,806
Last modified:January 11, 2001 - v2
Checksum:i7661140D3837BE7A
GO
Isoform Short (identifier: P30419-2) [UniParc]FASTAAdd to basket

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

Show »
Length:416
Mass (Da):48,141
Checksum:iCF08D233B6DD9383
GO

Sequence cautioni

The sequence AAC09294 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05028661Q → K.Corresponds to variant rs3087878dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0035701 – 80Missing in isoform Short. 1 PublicationAdd BLAST80

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11494.1. [P30419-1]
PIRiJC1343.
RefSeqiNP_066565.1. NM_021079.4. [P30419-1]
UniGeneiHs.532790.

Genome annotation databases

EnsembliENST00000258960; ENSP00000258960; ENSG00000136448. [P30419-1]
ENST00000592782; ENSP00000468424; ENSG00000136448. [P30419-1]
GeneIDi4836.
KEGGihsa:4836.
UCSCiuc002ihz.4. human. [P30419-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11494.1. [P30419-1]
PIRiJC1343.
RefSeqiNP_066565.1. NM_021079.4. [P30419-1]
UniGeneiHs.532790.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RXTX-ray3.00A/B/C/D1-496[»]
3IU1X-ray1.42A/B115-496[»]
3IU2X-ray1.73A/B115-496[»]
3IWEX-ray1.79A/B115-496[»]
3JTKX-ray1.61A/B115-496[»]
4C2YX-ray1.64A/B109-496[»]
4C2ZX-ray2.08A/B109-496[»]
ProteinModelPortaliP30419.
SMRiP30419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110899. 81 interactors.
IntActiP30419. 20 interactors.
MINTiMINT-5004170.
STRINGi9606.ENSP00000258960.

Chemistry databases

BindingDBiP30419.
ChEMBLiCHEMBL2593.
SwissLipidsiSLP:000001287.

PTM databases

iPTMnetiP30419.
PhosphoSitePlusiP30419.
SwissPalmiP30419.

Polymorphism and mutation databases

BioMutaiNMT1.
DMDMi12231020.

Proteomic databases

EPDiP30419.
MaxQBiP30419.
PaxDbiP30419.
PeptideAtlasiP30419.
PRIDEiP30419.
TopDownProteomicsiP30419-2. [P30419-2]

Protocols and materials databases

DNASUi4836.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258960; ENSP00000258960; ENSG00000136448. [P30419-1]
ENST00000592782; ENSP00000468424; ENSG00000136448. [P30419-1]
GeneIDi4836.
KEGGihsa:4836.
UCSCiuc002ihz.4. human. [P30419-1]

Organism-specific databases

CTDi4836.
DisGeNETi4836.
GeneCardsiNMT1.
HGNCiHGNC:7857. NMT1.
HPAiHPA022949.
HPA022963.
MIMi160993. gene.
neXtProtiNX_P30419.
OpenTargetsiENSG00000136448.
PharmGKBiPA31661.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2779. Eukaryota.
COG5092. LUCA.
GeneTreeiENSGT00390000017837.
HOGENOMiHOG000189123.
HOVERGENiHBG003404.
InParanoidiP30419.
KOiK00671.
OMAiEMCTEVY.
OrthoDBiEOG091G06JB.
PhylomeDBiP30419.

Enzyme and pathway databases

BioCyciZFISH:HS06161-MONOMER.
BRENDAi2.3.1.97. 2681.
ReactomeiR-HSA-162599. Late Phase of HIV Life Cycle.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-75108. Activation, myristolyation of BID and translocation to mitochondria.
SIGNORiP30419.

Miscellaneous databases

ChiTaRSiNMT1. human.
EvolutionaryTraceiP30419.
GeneWikiiN-myristoyltransferase_1.
GenomeRNAii4836.
PROiP30419.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136448.
CleanExiHS_NMT1.
ExpressionAtlasiP30419. baseline and differential.
GenevisibleiP30419. HS.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
PANTHERiPTHR11377. PTHR11377. 1 hit.
PfamiPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNMT1_HUMAN
AccessioniPrimary (citable) accession number: P30419
Secondary accession number(s): A8K7C1, Q9UE09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 11, 2001
Last modified: November 30, 2016
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.