CPLM-004348

Genbank Nucleotide ID

Nucleoside diphosphate kinase A

Protein Synonyms/Alias

NDK A; NDP kinase A; Granzyme A-activated DNase; GAAD; Metastasis inhibition factor nm23; Tumor metastatic process-associated protein; nm23-H1

Homo sapiens (Human)

Position	Peptide	Type	References
12	ERTFIAIKPDGVQRG	acetylation	[1]
12	ERTFIAIKPDGVQRG	ubiquitination	[2, 3, 4, 5]
26	GLVGEIIKRFEQKGF	ubiquitination	[3, 4]
39	GFRLVGLKFMQASED	ubiquitination	[4]
49	QASEDLLKEHYVDLK	ubiquitination	[3, 4]
56	KEHYVDLKDRPFFAG	acetylation	[1]
56	KEHYVDLKDRPFFAG	ubiquitination	[2, 3, 4, 6]
85	WEGLNVVKTGRVMLG	ubiquitination	[4]
100	ETNPADSKPGTIRGD	ubiquitination	[2, 3, 4, 5, 7, 8]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
[7] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
Meierhofer D, Wang X, Huang L, Kaiser P.
J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
[8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]

Functional Description

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.

ACT_SITE 118 118 Pros-phosphohistidine intermediate.
BINDING 12 12 ATP.
BINDING 60 60 ATP.
BINDING 88 88 ATP.
BINDING 94 94 ATP.
BINDING 105 105 ATP.
BINDING 115 115 ATP.
MOD_RES 2 2 N-acetylalanine.
CROSSLNK 100 100 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Differentiation; Direct protein sequencing; Endocytosis; Isopeptide bond; Kinase; Magnesium; Metal-binding; Neurogenesis; Nucleotide metabolism; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Transferase; Ubl conjugation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005813; C:centrosome; IEA:Compara.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0016020; C:membrane; IEA:Compara.
GO:0005739; C:mitochondrion; IEA:Compara.
GO:0005634; C:nucleus; TAS:UniProtKB.
GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
GO:0005524; F:ATP binding; IDA:UniProtKB.
GO:0004536; F:deoxyribonuclease activity; IDA:UniProtKB.
GO:0005525; F:GTP binding; IDA:UniProtKB.
GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB.
GO:0043024; F:ribosomal small subunit binding; IPI:UniProtKB.
GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Compara.
GO:0003697; F:single-stranded DNA binding; IEA:Compara.
GO:0035690; P:cellular response to drug; IEA:Compara.
GO:0071398; P:cellular response to fatty acid; IEA:Compara.
GO:0071333; P:cellular response to glucose stimulus; IEA:Compara.
GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
GO:0021766; P:hippocampus development; IEA:Compara.
GO:0007595; P:lactation; IEA:Compara.
GO:0008285; P:negative regulation of cell proliferation; TAS:UniProtKB.
GO:0010629; P:negative regulation of gene expression; IEA:Compara.
GO:0002762; P:negative regulation of myeloid leukocyte differentiation; IEA:Compara.
GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:HGNC.
GO:0010976; P:positive regulation of neuron projection development; IEA:Compara.
GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO:0014075; P:response to amine stimulus; IEA:Compara.
GO:0051591; P:response to cAMP; IEA:Compara.
GO:0033574; P:response to testosterone stimulus; IEA:Compara.
GO:0006228; P:UTP biosynthetic process; IEA:InterPro.

IPR001564; Nucleoside_diP_kinase.
IPR023005; Nucleoside_diP_kinase_AS.

PS00469; NDP_KINASES

PR01243; NUCDPKINASE.