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 B  

UniProtKB / Swiss-Prot ID :  NDKB_HUMAN

Gene Name (Synonyms) : 
NME2, NM23B  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Note=Isoform 2 is mainly cytoplasmic and isoform 1 and isoform 2 are excluded from the nucleolus. 

Protein Function :  Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752). Exhibits histidine protein kinase activity. 

Protein Sequence MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPFFPGLVKYMNS...
Predicted Secondary Structure CCCHHHHHHHCCCCCCCCCCHHHHHHHHHHCCCCEEHHHHCCCCHHHHHHHHHHHCCCCCHHHHHHHHCC...
Protein Variant -
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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
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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.---MANLER
---CCCHHH
29.34UniProtKB
Link
12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FIAIKPDGV
HHHCCCCCC
28.21Phosphositeplus
Link
12N6-acetyllysine.FIAIKPDGV
HHHCCCCCC
28.21UniProtKB
Link
39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVAMKFLRA
EEHHHHCCC
31.35Phosphositeplus
Link
44PhosphoserineFLRASEEHL
HCCCCHHHH
36.76PhosphoELM
Link
44Phosphoserine (NME2)FLRASEEHL
HCCCCHHHH
36.76HPRD
Link
49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEHLKQHYI
HHHHHHHHH
36.62Phosphositeplus
Link
49N6-acetyllysineEEHLKQHYI
HHHHHHHHH
36.62HPRD
Link
49N6-acetyllysineEEHLKQHYI
HHHHHHHHH
36.62Phosphositeplus
Link
49N6-acetyllysine.EEHLKQHYI
HHHHHHHHH
36.62UniProtKB
Link
52PhosphotyrosineLKQHYIDLK
HHHHHHHHC
8.14Phosphositeplus
Link
52Phosphotyrosine.LKQHYIDLK
HHHHHHHHC
8.14UniProtKB
Link
56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YIDLKDRPF
HHHHCCCCC
48.20Phosphositeplus
Link
56N6-acetyllysineYIDLKDRPF
HHHHCCCCC
48.20HPRD
Link
56N6-acetyllysineYIDLKDRPF
HHHHCCCCC
48.20Phosphositeplus
Link
56N6-acetyllysine.YIDLKDRPF
HHHHCCCCC
48.20UniProtKB
Link
85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LNVVKTGRV
CCHHHHHHH
40.76Phosphositeplus
Link
85N6-acetyllysineLNVVKTGRV
CCHHHHHHH
40.76HPRD
Link
85N6-acetyllysineLNVVKTGRV
CCHHHHHHH
40.76Phosphositeplus
Link
85N6-acetyllysine.LNVVKTGRV
CCHHHHHHH
40.76UniProtKB
Link
94PhosphothreonineMLGETNPAD
HHCCCCHHH
44.71PhosphoELM
Link
94PhosphothreonineMLGETNPAD
HHCCCCHHH
44.71Phosphositeplus
Link
100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PADSKPGTI
HHHCCCCCC
48.27Phosphositeplus
Link
100N6-acetyllysinePADSKPGTI
HHHCCCCCC
48.27Phosphositeplus
Link
100N6-acetyllysine.PADSKPGTI
HHHCCCCCC
48.27UniProtKB
Link
118PhosphohistidineRNIIHGSDS
HCEEECCCC
26.38Phosphositeplus
Link
118Phosphohistidine (NME2)RNIIHGSDS
HCEEECCCC
26.38HPRD
Link
120PhosphoserineIIHGSDSVK
EEECCCCHH
16.73HPRD
Link
120PhosphoserineIIHGSDSVK
EEECCCCHH
16.73Phosphositeplus
Link
122PhosphoserineHGSDSVKSA
ECCCCHHHH
32.89HPRD
Link
122PhosphoserineHGSDSVKSA
ECCCCHHHH
32.89Phosphositeplus
Link
124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SDSVKSAEK
CCCHHHHHH
48.15Phosphositeplus
Link
124N6-acetyllysineSDSVKSAEK
CCCHHHHHH
48.15HPRD
Link
124N6-acetyllysineSDSVKSAEK
CCCHHHHHH
48.15Phosphositeplus
Link
124N6-acetyllysine.SDSVKSAEK
CCCHHHHHH
48.15UniProtKB
Link
128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KSAEKEISL
HHHHHHHHH
61.13Phosphositeplus
Link
128N6-acetyllysineKSAEKEISL
HHHHHHHHH
61.13HPRD
Link
128N6-acetyllysineKSAEKEISL
HHHHHHHHH
61.13Phosphositeplus
Link
128N6-acetyllysine.KSAEKEISL
HHHHHHHHH
61.13UniProtKB
Link
135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SLWFKPEEL
HHHCCHHHE
39.68Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PP1R7_HUMANphysical interactionEBI-1059661
intact17353931
KV203_HUMANphysical interactionEBI-1061143
intact17353931
5HT1B_HUMANphysical interactionEBI-1061406
intact17353931
H2B1C_HUMANphysical interactionEBI-1075233
intact17353931
CYBP_HUMANphysical interactionEBI-1075281
intact17353931
RRP44_HUMANphysical interactionEBI-1083038
intact17353931
Q5TZU9_HUMANphysical interactionEBI-1083082
intact17353931
RPAB3_HUMANphysical interactionEBI-1071336
intact17353931
PP1R8_HUMANphysical interactionEBI-1064323
intact17353931
F10A1_HUMANphysical interactionEBI-1084657
intact17353931
RIB2_HUMANphysical interactionEBI-1082016
intact17353931
EPIPL_HUMANphysical interactionEBI-1082068
intact17353931
RL38_HUMANphysical interactionEBI-1075834
intact17353931
Q7L7Q8_HUMANphysical interactionEBI-1080716
intact17353931
ACLY_HUMANphysical interactionEBI-1082405
intact17353931
Q65ZQ1_HUMANphysical interactionEBI-1076843
intact17353931
UBE2N_HUMANphysical interactionEBI-1076851
intact17353931
Q9NPH2_HUMANphysical interactionEBI-1076944
intact17353931
G3BP1_HUMANphysical interactionEBI-1076964
intact17353931
SET_HUMANphysical interactionEBI-1077547
intact17353931
RD23A_HUMANphysical interactionEBI-1084508
intact17353931
PSA7_HUMANphysical interactionEBI-1084536
intact17353931
CBR1_HUMANphysical interactionEBI-1078617
intact17353931
PSB4_HUMANphysical interactionEBI-1085900
intact17353931
Q9NZ23_HUMANphysical interactionEBI-1085916
intact17353931
Q6FHQ0_HUMANphysical interactionEBI-1083767
intact17353931
PA1B2_HUMANphysical interactionEBI-1084933
intact17353931
RUVB2_HUMANphysical interactionEBI-1086002
intact17353931
EIF3M_HUMANphysical interactionEBI-1086018
intact17353931
PUR9_HUMANphysical interactionEBI-1086191
intact17353931
KINH_HUMANphysical interactionEBI-1086252
intact17353931
PGRC1_HUMANphysical interactionEBI-1075521
intact17353931
DYHC1_HUMANphysical interactionEBI-1085083
intact17353931
PDIA6_HUMANphysical interactionEBI-1079212
intact17353931
RS16_HUMANphysical interactionEBI-1079501
intact17353931
PSD12_HUMANphysical interactionEBI-1079589
intact17353931
RNBP6_HUMANphysical interactionEBI-1082514
intact17353931
LSM2_HUMANphysical interactionEBI-1082666
intact17353931
LYSC_HUMANphysical interactionEBI-1078976
intact17353931
RS19_HUMANphysical interactionEBI-1078996
intact17353931
KAD2_HUMANphysical interactionEBI-1076537
intact17353931
PCBP1_HUMANphysical interactionEBI-1081301
intact17353931
MGN_HUMANphysical interactionEBI-1082762
intact17353931
LA_HUMANphysical interactionEBI-1080231
intact17353931
PSA2_HUMANphysical interactionEBI-1077873
intact17353931
STRAP_HUMANphysical interactionEBI-1077889
intact17353931
UBC1_HUMANphysical interactionEBI-1077953
intact17353931
NDKB_HUMANin vivoHPRD:01132HPRD8245015
TERF1_HUMANin vitro
yeast 2-hybrid
HPRD:01132HPRD9480811
TERF1_HUMANENSP00000312446STRING
NDKA_HUMANENSP00000312446STRING
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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
"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-12; LYS-49; LYS-56; LYS-85;LYS-100; LYS-124 AND LYS-128, AND MASS SPECTROMETRY.
"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.
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures