Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Nucleoside diphosphate kinase A  

UniProtKB / Swiss-Prot ID :  NDKA_HUMAN

Gene Name (Synonyms) : 
NME1, NDPKA, NM23  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Note=Cell-cycle dependent nuclear localization which can be induced by interaction with Epstein-barr viral proteins or by degradation of the SET complex by GzmA. 

Protein Function :  Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. 

Protein Sequence MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPFFAGLVKYMHS...
Predicted Secondary Structure CCCCCEEEEEECCCCCCCCCHHHHHHHHHHCCCCEEHHHHCCCCHHHHHHHHHHHCCCCCHHHHHHHHCC...
Protein Variant
LocationDescription
120S -> G (in a neuroblastoma sample;increased motility of carcinoma cells).
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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
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
2N-acetylalanine.---MANCER
---CCCCCE
29.40UniProtKB
Link-
12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FIAIKPDGV
EEEECCCCC
28.21Phosphositeplus
Link
12N6-acetyllysineFIAIKPDGV
EEEECCCCC
28.21HPRD
Link
39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVGLKFMQA
EEHHHHCCC
32.63Phosphositeplus
Link
44PhosphoserineFMQASEDLL
HCCCCHHHH
18.10PhosphoELM
Link
44PhosphoserineFMQASEDLL
HCCCCHHHH
18.10Phosphositeplus
Link
44Phosphoserine (NME1)FMQASEDLL
HCCCCHHHH
18.10HPRD
Link
49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EDLLKEHYV
HHHHHHHHH
50.14Phosphositeplus
Link
52PhosphotyrosineLKEHYVDLK
HHHHHHHHC
9.21Phosphositeplus
Link
52Phosphotyrosine.LKEHYVDLK
HHHHHHHHC
9.21UniProtKB
Link
56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YVDLKDRPF
HHHHCCCCC
47.42Phosphositeplus
Link
56N6-acetyllysineYVDLKDRPF
HHHHCCCCC
47.42HPRD
Link
56N6-acetyllysineYVDLKDRPF
HHHHCCCCC
47.42Phosphositeplus
Link
56N6-acetyllysine.YVDLKDRPF
HHHHCCCCC
47.42UniProtKB
Link
85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LNVVKTGRV
CCHHHHHHH
40.76Phosphositeplus
Link
94PhosphothreonineMLGETNPAD
HHCCCCHHH
44.71HPRD
Link
94PhosphothreonineMLGETNPAD
HHCCCCHHH
44.71PhosphoELM
Link
94PhosphothreonineMLGETNPAD
HHCCCCHHH
44.71Phosphositeplus
Link
94PhosphothreonineMLGETNPAD
HHCCCCHHH
44.71SysPTM
Link
94Phosphothreonine.MLGETNPAD
HHCCCCHHH
44.71UniProtKB
Link
99PhosphoserineNPADSKPGT
CHHHCCCCC
42.74HPRD
Link
100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PADSKPGTI
HHHCCCCCC
48.27Phosphositeplus
Link
100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PADSKPGTI
HHHCCCCCC
48.27SysPTM
Link
100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).PADSKPGTI
HHHCCCCCC
48.27UniProtKB
Link
100N6-acetyllysinePADSKPGTI
HHHCCCCCC
48.27HPRD
Link
100N6-acetyllysinePADSKPGTI
HHHCCCCCC
48.27Phosphositeplus
Link
118PhosphohistidineRNIIHGSDS
HCEEECCCC
26.38Phosphositeplus
Link
120PhosphoserineIIHGSDSVE
EEECCCCHH
16.73PhosphoELM
Link
120PhosphoserineIIHGSDSVE
EEECCCCHH
16.73Phosphositeplus
Link
120Phosphoserine (NME1)IIHGSDSVE
EEECCCCHH
16.73HPRD
Link
122PhosphoserineHGSDSVESA
ECCCCHHHH
29.49PhosphoELM
Link
122Phosphoserine (NME1)HGSDSVESA
ECCCCHHHH
29.49HPRD
Link
125PhosphoserineDSVESAEKE
CCHHHHHHH
39.30PhosphoELM
Link
125Phosphoserine (NME1)DSVESAEKE
CCHHHHHHH
39.30HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
STK6_HUMANphysical interactionMINT-14503MINT12490715
STK6_HUMANphysical interactionMINT-14505MINT12490715
TERF1_HUMANphysical interactionMINT-17759MINT11701125
CH032_HUMANphysical interactionEBI-752854
intact16189514
RPAC1_HUMANphysical interactionEBI-756196
intact16189514
GORS2_HUMANphysical interactionEBI-756532
intact16189514
NDKM_HUMANphysical interactionEBI-754228
intact16189514
NDK3_HUMANphysical interactionEBI-760207
intact16189514
NDKA_HUMANphysical interactionEBI-760399
intact16189514
APEX1_HUMANin vitroHPRD:01131HPRD12524539
ITB1_HUMANin vitro
in vivo
HPRD:01131HPRD11919189
NDKA_HUMANin vitro
yeast 2-hybrid
HPRD:01131HPRD11835509
8245015
8810265
16189514
NDKM_HUMANyeast 2-hybridHPRD:01131HPRD16189514
CH032_HUMANyeast 2-hybridHPRD:01131HPRD16189514
GORS2_HUMANyeast 2-hybridHPRD:01131HPRD16189514
RPAC1_HUMANyeast 2-hybridHPRD:01131HPRD16189514
TERF1_HUMANin vitro
yeast 2-hybrid
HPRD:01131HPRD9480811
KSR1_HUMANin vitro
in vivo
HPRD:01131HPRD12105213
APEX1_HUMANENSP00000337060STRING
DUT_HUMANENSP00000337060STRING
PNPT1_HUMANENSP00000337060STRING
AN32A_HUMANENSP00000337060STRING
P53_HUMANENSP00000337060STRING
TERF1_HUMANENSP00000337060STRING
HMGB2_HUMANENSP00000337060STRING
RAD_HUMANENSP00000337060STRING
NDKB_HUMANENSP00000337060STRING
KGUA_HUMANENSP00000337060STRING
STK6_HUMANENSP00000337060STRING
AP4A_HUMANENSP00000337060STRING
NF1_HUMANENSP00000337060STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00718Adefovir Dipivoxil
DB00709Lamivudine
DB00300Tenofovir
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, AND MASS SPECTROMETRY.
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 THR-94, 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 TYR-52, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-100, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures