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Protein

Glycylpeptide N-tetradecanoyltransferase 2

Gene

NMT2

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.2 Publications

Catalytic activityi

Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.2 Publications

GO - Molecular functioni

  1. glycylpeptide N-tetradecanoyltransferase activity Source: UniProtKB

GO - Biological processi

  1. intracellular transport of virus Source: Reactome
  2. N-terminal peptidyl-glycine N-myristoylation Source: UniProtKB
  3. phototransduction, visible light Source: Reactome
  4. regulation of rhodopsin mediated signaling pathway Source: Reactome
  5. rhodopsin mediated signaling pathway Source: Reactome
  6. viral process Source: Reactome
  7. viral protein processing Source: Reactome
  8. virion assembly Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.97. 2681.
ReactomeiREACT_115893. Membrane binding and targetting of GAG proteins.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycylpeptide N-tetradecanoyltransferase 2 (EC:2.3.1.972 Publications)
Alternative name(s):
Myristoyl-CoA:protein N-myristoyltransferase 2
Short name:
NMT 2
Peptide N-myristoyltransferase 2
Type II N-myristoyltransferase
Gene namesi
Name:NMT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:7858. NMT2.

Subcellular locationi

Cytoplasm 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extrinsic component of membrane Source: UniProtKB
  4. Golgi apparatus Source: HPA
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31662.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Glycylpeptide N-tetradecanoyltransferase 2PRO_0000064226Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60551.
PaxDbiO60551.
PRIDEiO60551.

PTM databases

PhosphoSiteiO60551.

Expressioni

Gene expression databases

BgeeiO60551.
CleanExiHS_NMT2.
ExpressionAtlasiO60551. baseline and differential.
GenevestigatoriO60551.

Organism-specific databases

HPAiHPA001303.

Interactioni

Protein-protein interaction databases

BioGridi114794. 18 interactions.
IntActiO60551. 10 interactions.
MINTiMINT-1795376.
STRINGi9606.ENSP00000367407.

Structurei

Secondary structure

1
498
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi122 – 1243Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi158 – 1625Combined sources
Helixi168 – 18114Combined sources
Beta strandi186 – 1927Combined sources
Helixi196 – 2038Combined sources
Helixi210 – 2123Combined sources
Beta strandi213 – 2186Combined sources
Turni219 – 2213Combined sources
Beta strandi224 – 23714Combined sources
Beta strandi240 – 25213Combined sources
Helixi254 – 2563Combined sources
Helixi262 – 27413Combined sources
Turni275 – 2773Combined sources
Beta strandi281 – 2877Combined sources
Beta strandi293 – 30311Combined sources
Helixi305 – 3106Combined sources
Helixi322 – 3287Combined sources
Beta strandi340 – 3423Combined sources
Helixi345 – 3473Combined sources
Helixi348 – 35811Combined sources
Helixi359 – 3613Combined sources
Beta strandi362 – 3665Combined sources
Helixi370 – 3778Combined sources
Turni381 – 3833Combined sources
Beta strandi384 – 3907Combined sources
Beta strandi392 – 3943Combined sources
Beta strandi396 – 4049Combined sources
Beta strandi407 – 4093Combined sources
Beta strandi416 – 4183Combined sources
Beta strandi420 – 4234Combined sources
Beta strandi427 – 4315Combined sources
Helixi433 – 44513Combined sources
Turni446 – 4483Combined sources
Beta strandi450 – 4567Combined sources
Helixi460 – 4623Combined sources
Turni463 – 4686Combined sources
Beta strandi470 – 48213Combined sources
Helixi490 – 4923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2XX-ray2.33A112-498[»]
ProteinModelPortaliO60551.
SMRiO60551. Positions 119-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 1223Myristoyl-CoA binding1 Publication
Regioni250 – 2523Myristoyl-CoA binding1 Publication
Regioni258 – 2625Myristoyl-CoA binding1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi46 – 5611Poly-LysAdd
BLAST

Sequence similaritiesi

Belongs to the NMT family.Curated

Phylogenomic databases

eggNOGiCOG5092.
GeneTreeiENSGT00390000017837.
HOGENOMiHOG000189123.
HOVERGENiHBG003404.
InParanoidiO60551.
KOiK00671.
OMAiIATCRYW.
OrthoDBiEOG76DTS3.
PhylomeDBiO60551.
TreeFamiTF300701.

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]

Sequencei

Sequence statusi: Complete.

O60551-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEDSESAAS QQSLELDDQD TCGIDGDNEE ETEHAKGSPG GYLGAKKKKK
60 70 80 90 100
KQKRKKEKPN SGGTKSDSAS DSQEIKIQQP SKNPSVPMQK LQDIQRAMEL
110 120 130 140 150
LSACQGPARN IDEAAKHRYQ FWDTQPVPKL DEVITSHGAI EPDKDNVRQE
160 170 180 190 200
PYSLPQGFMW DTLDLSDAEV LKELYTLLNE NYVEDDDNMF RFDYSPEFLL
210 220 230 240 250
WALRPPGWLL QWHCGVRVSS NKKLVGFISA IPANIRIYDS VKKMVEINFL
260 270 280 290 300
CVHKKLRSKR VAPVLIREIT RRVNLEGIFQ AVYTAGVVLP KPIATCRYWH
310 320 330 340 350
RSLNPRKLVE VKFSHLSRNM TLQRTMKLYR LPDVTKTSGL RPMEPKDIKS
360 370 380 390 400
VRELINTYLK QFHLAPVMDE EEVAHWFLPR EHIIDTFVVE SPNGKLTDFL
410 420 430 440 450
SFYTLPSTVM HHPAHKSLKA AYSFYNIHTE TPLLDLMSDA LILAKSKGFD
460 470 480 490
VFNALDLMEN KTFLEKLKFG IGDGNLQYYL YNWRCPGTDS EKVGLVLQ
Length:498
Mass (Da):56,980
Last modified:August 1, 1998 - v1
Checksum:i1B1486CC6559B6A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti306 – 3061R → K in AAP35670 (Ref. 3) Curated
Sequence conflicti306 – 3061R → K in AAH06376 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043325 mRNA. Translation: AAC09295.1.
AF232826 mRNA. Translation: AAF36406.2.
BT007024 mRNA. Translation: AAP35670.1.
EF445001 Genomic DNA. Translation: ACA06028.1.
EF445001 Genomic DNA. Translation: ACA06029.1.
AL590365 Genomic DNA. Translation: CAH73971.1.
CH471072 Genomic DNA. Translation: EAW86238.1.
BC006376 mRNA. Translation: AAH06376.1.
CCDSiCCDS7109.1.
RefSeqiNP_004799.1. NM_004808.2.
UniGeneiHs.60339.

Genome annotation databases

EnsembliENST00000378165; ENSP00000367407; ENSG00000152465.
GeneIDi9397.
KEGGihsa:9397.
UCSCiuc001inz.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043325 mRNA. Translation: AAC09295.1.
AF232826 mRNA. Translation: AAF36406.2.
BT007024 mRNA. Translation: AAP35670.1.
EF445001 Genomic DNA. Translation: ACA06028.1.
EF445001 Genomic DNA. Translation: ACA06029.1.
AL590365 Genomic DNA. Translation: CAH73971.1.
CH471072 Genomic DNA. Translation: EAW86238.1.
BC006376 mRNA. Translation: AAH06376.1.
CCDSiCCDS7109.1.
RefSeqiNP_004799.1. NM_004808.2.
UniGeneiHs.60339.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C2XX-ray2.33A112-498[»]
ProteinModelPortaliO60551.
SMRiO60551. Positions 119-498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114794. 18 interactions.
IntActiO60551. 10 interactions.
MINTiMINT-1795376.
STRINGi9606.ENSP00000367407.

Chemistry

BindingDBiO60551.
ChEMBLiCHEMBL2096973.

PTM databases

PhosphoSiteiO60551.

Proteomic databases

MaxQBiO60551.
PaxDbiO60551.
PRIDEiO60551.

Protocols and materials databases

DNASUi9397.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378165; ENSP00000367407; ENSG00000152465.
GeneIDi9397.
KEGGihsa:9397.
UCSCiuc001inz.1. human.

Organism-specific databases

CTDi9397.
GeneCardsiGC10M015144.
HGNCiHGNC:7858. NMT2.
HPAiHPA001303.
MIMi603801. gene.
neXtProtiNX_O60551.
PharmGKBiPA31662.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5092.
GeneTreeiENSGT00390000017837.
HOGENOMiHOG000189123.
HOVERGENiHBG003404.
InParanoidiO60551.
KOiK00671.
OMAiIATCRYW.
OrthoDBiEOG76DTS3.
PhylomeDBiO60551.
TreeFamiTF300701.

Enzyme and pathway databases

BRENDAi2.3.1.97. 2681.
ReactomeiREACT_115893. Membrane binding and targetting of GAG proteins.
REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

ChiTaRSiNMT2. human.
GeneWikiiNMT2.
GenomeRNAii9397.
NextBioi35199.
PROiO60551.
SOURCEiSearch...

Gene expression databases

BgeeiO60551.
CleanExiHS_NMT2.
ExpressionAtlasiO60551. baseline and differential.
GenevestigatoriO60551.

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...

Publicationsi

« Hide 'large scale' publications
  1. "A second mammalian N-myristoyltransferase."
    Giang D.K., Cravatt B.F.
    J. Biol. Chem. 273:6595-6598(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Liver.
  2. Rundle D.R., Anderson R.E.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells."
    Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.
    Nat. Commun. 5:4919-4919(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 112-498 IN COMPLEX WITH SUBSTRATE ANALOG, CATALYTIC ACTIVITY, FUNCTION.

Entry informationi

Entry nameiNMT2_HUMAN
AccessioniPrimary (citable) accession number: O60551
Secondary accession number(s): B0YJ49
, Q53Y38, Q5VUC8, Q9BRB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: March 4, 2015
This is version 130 of the entry and version 1 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

Caution

Sequence AAF36406.2 was incorrectly indicated as originating from bovine.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.