Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Glycylpeptide N-tetradecanoyltransferase 1  

UniProtKB / Swiss-Prot ID :  NMT1_HUMAN

Gene Name (Synonyms) : 
NMT1, NMT  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. 

Protein Sequence MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKKQKKKKEKGSE...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHCCCCCCCC...
Protein Variant
LocationDescription
61Q -> K (in dbSNP:rs3087878). VAR_050286
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
47PhosphoserineRGGLSPAND
CCCCCCCCC
25.82HPRD
Link-
47PhosphoserineRGGLSPAND
CCCCCCCCC
25.82PhosphoELM
Link-
47PhosphoserineRGGLSPAND
CCCCCCCCC
25.82Phosphositeplus
Link-
47PhosphoserineRGGLSPAND
CCCCCCCCC
25.82SysPTM
Link-
47Phosphoserine.RGGLSPAND
CCCCCCCCC
25.82UniProtKB
Link-
80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DQPVKMNSL
CCCCCHHHH
38.76Phosphositeplus
Link-
94Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QEIQKAIEL
HHHHHHHHH
57.92Phosphositeplus
Link-
117Phosphotyrosine (Lyn)SKRSYQFWD
HHHHCCCCC
16.26PhosphoELM
Link-
180PhosphotyrosineLNENYVEDD
HHHCCCCCC
10.07Phosphositeplus
Link
180Phosphotyrosine (FYN)LNENYVEDD
HHHCCCCCC
10.07HPRD
Link
180Phosphotyrosine (Fyn;Lyn)LNENYVEDD
HHHCCCCCC
10.07PhosphoELM
Link
180Phosphotyrosine (LYN)LNENYVEDD
HHHCCCCCC
10.07HPRD
Link
343PhosphothreonineRPMETKDIP
CCCCHHHHH
27.97Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
P53_HUMANphysical interactionMINT-1795431MINT16530191
FYN_HUMANin vitro
in vivo
HPRD:01187HPRD11423543
11594778
GNAZ_HUMANin vitroHPRD:01187HPRD2153964
HPCA_HUMANin vitroHPRD:01187HPRD8360179
NOS3_HUMANin vivoHPRD:01187HPRD7512951
SRC_HUMANin vitroHPRD:01187HPRD3917576
7527558
ANX13_HUMANin vitroHPRD:01187HPRD1530946
CABP2_HUMANin vitro
in vivo
HPRD:01187HPRD10625670
ARL5A_HUMANin vitro
in vivo
HPRD:01187HPRD12414990
P53_HUMANENSP00000258960STRING
BID_HUMANENSP00000258960STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures