Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  N-acetyl-D-glucosamine kinase  

UniProtKB / Swiss-Prot ID :  NAGK_HUMAN

Gene Name (Synonyms) : 
NAGK  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Also has ManNAc kinase activity (By similarity). 

Protein Sequence MAAIYGGVEGGGTRSEVLLVSEDGKILAEADGLSTNHWLIGTDKCVERINEMVNRAKRKAGVDPLVPLRS...
Predicted Secondary Structure CEEEEECCCCCCCCEEEEEEECCCCEEEECCCCCCCCEEEECCHHHHHHHHHHHHHHHHCCCCCCCCHHH...
Protein Variant
LocationDescription
38W -> R (in dbSNP:rs17856147). VAR_029763
60A -> V (in dbSNP:rs17849984). VAR_029764
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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
74PhosphoserineSLGLSLSGG
HCCEEECCC
20.77HPRD
Link
74PhosphoserineSLGLSLSGG
HCCEEECCC
20.77Phosphositeplus
Link
76PhosphoserineGLSLSGGDQ
CEEECCCCH
37.04HPRD
Link
76PhosphoserineGLSLSGGDQ
CEEECCCCH
37.04PhosphoELM
Link
76PhosphoserineGLSLSGGDQ
CEEECCCCH
37.04Phosphositeplus
Link
76Phosphoserine.GLSLSGGDQ
CEEECCCCH
37.04UniProtKB
Link
205PhosphotyrosineLTHLYRDFD
HHHHHHHHH
10.67Phosphositeplus
Link
205Phosphotyrosine.LTHLYRDFD
HHHHHHHHH
10.67UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SMAD2_HUMANphysical interactionMINT-60929MINT15231748
Q8N7E3_HUMANphysical interactionMINT-67891MINT16189514
LNX1_HUMANphysical interactionMINT-67311MINT16189514
NAGK_HUMANphysical interactionMINT-67601MINT16189514
LNX1_HUMANphysical interaction
physical interaction
EBI-756646
EBI-760931
intact16189514
16189514
Q8IYQ1_HUMANphysical interactionEBI-758572
intact16189514
NAGK_HUMANphysical interactionEBI-757597
intact16189514
STK16_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:08441HPRD11741987
LSM8_HUMANyeast 2-hybridHPRD:08441HPRD15231747
NAGK_HUMANyeast 2-hybridHPRD:08441HPRD16189514
DACH1_HUMANyeast 2-hybridHPRD:08441HPRD16189514
LNX1_HUMANyeast 2-hybridHPRD:08441HPRD16189514
SMAD9_HUMANyeast 2-hybridHPRD:08441HPRD15231748
GNA1_HUMANENSP00000244204STRING
RENBP_HUMANENSP00000244204STRING
HEXB_HUMANENSP00000244204STRING
HEXA_HUMANENSP00000244204STRING
AGM1_HUMANENSP00000244204STRING
NAGA_HUMANENSP00000244204STRING
CHIA_HUMANENSP00000244204STRING
CHIA_HUMANENSP00000244204STRING
CHIA_HUMANENSP00000244204STRING
CHIA_HUMANENSP00000244204STRING
CHIA_HUMANENSP00000244204STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00141N-Acetyl-D-glucosamine
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-76, 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-76, AND MASSSPECTROMETRY.
"Identification of the phosphotyrosine proteome from thrombinactivated platelets.";
Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,Fitzgerald D.J.;
Proteomics 2:642-648(2002).
Cited for: PHOSPHORYLATION AT TYR-205.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures