Reviewed, UniProtKB/Swiss-Prot O60551 (NMT2_HUMAN)

Names and origin

Protein names

Recommended name:
    Glycylpeptide N-tetradecanoyltransferase 2
    EC=2.3.1.97
Alternative name(s):
    Peptide N-myristoyltransferase 2
    Myristoyl-CoA:protein N-myristoyltransferase 2
      Short name=NMT 2
    Type II N-myristoyltransferase

Gene names

Name:

NMT2

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

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Sequence similarities	Belongs to the NMT family.
Caution	Ref.2 sequence is incorrectly indicated as originating from bovine.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	N-terminal protein myristoylation Inferred from electronic annotation. Source: InterPro protein lipoylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA
Molecular function	glycylpeptide N-tetradecanoyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 498	498	Glycylpeptide N-tetradecanoyltransferase 2		PRO_0000064226
Regions
	Compositional bias	46 – 56	11	Poly-Lys
Amino acid modifications
	Modified residue	38	1	Phosphoserine Ref.9
	Modified residue	66	1	Phosphoserine By similarity
	Modified residue	68	1	Phosphoserine By similarity
	Modified residue	70	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	306	1	R → K in AAP35670. Ref.3
	Sequence conflict	306	1	R → K in AAH06376. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	O60551-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 1B1486CC6559B6A9	FASTA	498	56,980
	10 20 30 40 50 60 MAEDSESAAS QQSLELDDQD TCGIDGDNEE ETEHAKGSPG GYLGAKKKKK KQKRKKEKPN 70 80 90 100 110 120 SGGTKSDSAS DSQEIKIQQP SKNPSVPMQK LQDIQRAMEL LSACQGPARN IDEAAKHRYQ 130 140 150 160 170 180 FWDTQPVPKL DEVITSHGAI EPDKDNVRQE PYSLPQGFMW DTLDLSDAEV LKELYTLLNE 190 200 210 220 230 240 NYVEDDDNMF RFDYSPEFLL WALRPPGWLL QWHCGVRVSS NKKLVGFISA IPANIRIYDS 250 260 270 280 290 300 VKKMVEINFL CVHKKLRSKR VAPVLIREIT RRVNLEGIFQ AVYTAGVVLP KPIATCRYWH 310 320 330 340 350 360 RSLNPRKLVE VKFSHLSRNM TLQRTMKLYR LPDVTKTSGL RPMEPKDIKS VRELINTYLK 370 380 390 400 410 420 QFHLAPVMDE EEVAHWFLPR EHIIDTFVVE SPNGKLTDFL SFYTLPSTVM HHPAHKSLKA 430 440 450 460 470 480 AYSFYNIHTE TPLLDLMSDA LILAKSKGFD VFNALDLMEN KTFLEKLKFG IGDGNLQYYL 490 YNWRCPGTDS EKVGLVLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 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: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00030223.
RefSeq	NP_004799.1.
UniGene	Hs.60339
3D structure databases
SMR	O60551. Positions 116-497, 157-498.
ModBase	Search...
Protein-protein interaction databases
STRING	O60551.
PTM databases
PhosphoSite	O60551.
Proteomic databases
PRIDE	O60551.
Genome annotation databases
Ensembl	ENST00000378165; ENSP00000367407; ENSG00000152465; Homo sapiens. [Genome view]
GeneID	9397.
KEGG	hsa:9397.
UCSC	uc001inz.1. human.
Organism-specific databases
CTD	9397.
GeneCards	GC10M015172.
H-InvDB	HIX0008674.
HGNC	HGNC:7858. NMT2.
HPA	HPA001303.
MIM	603801. gene.
PharmGKB	PA27444.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10827.
HOVERGEN	O60551.
PhylomeDB	O60551.
Enzyme and pathway databases
BRENDA	2.3.1.97. 247.
Gene expression databases
ArrayExpress	O60551.
Bgee	O60551.
CleanEx	HS_NMT2.
Genevestigator	O60551.
GermOnline	ENSG00000152465. Homo sapiens.
Family and domain databases
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...
Other Resources
NextBio	35199.
SOURCE	Search...

Entry information

Entry name

NMT2_HUMAN

Accession

Primary (citable) accession number: O60551
Secondary accession number(s): B0YJ49 , Q53Y38, Q5VUC8, Q9BRB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	January 19, 2010
This is version 80 of the entry and version 1 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.