[1]	PROTEIN SEQUENCE, SUBUNIT, AND ACTIVE SITE. PubMed=1851158 [NCBI, ExPASy, EBI, Israel, Japan] Gilles A.-M., Presecan E., Vonica A., Lascu I.; "Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme."; J. Biol. Chem. 266:8784-8789(1991).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1988104 [NCBI, ExPASy, EBI, Israel, Japan] Stahl J.A., Leone A., Rosengard A.M., Porter L., Liotta L.A., Steeg P.S., King C.R.; "Identification of a second human nm23 gene, nm23-H2."; Cancer Res. 51:445-449(1991).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8392752 [NCBI, ExPASy, EBI, Israel, Japan] Postel E.H., Berberich S.J., Flint S.J., Ferrone C.A.; "Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis."; Science 261:478-480(1993).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Eye; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	FUNCTION, AND INTERACTION WITH AKAP13. DOI=10.1016/j.bbrc.2004.06.067; PubMed=15249197 [NCBI, ExPASy, EBI, Israel, Japan] Iwashita S., Fujii M., Mukai H., Ono Y., Miyamoto M.; "Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2."; Biochem. Biophys. Res. Commun. 320:1063-1068(2004).
[6]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). DOI=10.1006/jmbi.1995.0457; PubMed=7658474 [NCBI, ExPASy, EBI, Israel, Japan] Webb P.A., Perisic O., Mendola C.E., Backer J.M., Williams R.L.; "The crystal structure of a human nucleoside diphosphate kinase, NM23-H2."; J. Mol. Biol. 251:574-587(1995).
[7]	X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS). DOI=10.1016/S0969-2126(01)00268-4; PubMed=8747457 [NCBI, ExPASy, EBI, Israel, Japan] Morera S., Lacombe M.-L., Xu Y., Lebras G., Janin J.; "X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2-A resolution."; Structure 3:1307-1314(1995).

Comments

FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC.
FUNCTION: Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3).
CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
COFACTOR: Magnesium (By similarity).
SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with CAPN8 (By similarity). Interacts with AKAP13.
INTERACTION:
P01616:-; NbExp=1; IntAct=EBI-713693, EBI-1053880;
Q65ZQ1:-; NbExp=1; IntAct=EBI-713693, EBI-1054063;
P53396:ACLY; NbExp=1; IntAct=EBI-713693, EBI-1042794;
P31939:ATIC; NbExp=1; IntAct=EBI-713693, EBI-1048599;
Q14204:DYNC1H1; NbExp=1; IntAct=EBI-713693, EBI-356015;
P58107:EPPK1; NbExp=1; IntAct=EBI-713693, EBI-297954;
P62807:HIST1H2BC; NbExp=1; IntAct=EBI-713693, EBI-354552;
P28222:HTR1B; NbExp=1; IntAct=EBI-713693, EBI-1056863;
P33176:KIF5B; NbExp=1; IntAct=EBI-713693, EBI-355878;
P61626:LYZ; NbExp=1; IntAct=EBI-713693, EBI-355360;
Q15084:PDIA6; NbExp=1; IntAct=EBI-713693, EBI-1043087;
P52434:POLR2H; NbExp=1; IntAct=EBI-713693, EBI-359505;
Q15435:PPP1R7; NbExp=1; IntAct=EBI-713693, EBI-1024281;
Q12972:PPP1R8; NbExp=1; IntAct=EBI-713693, EBI-716633;
P25787:PSMA2; NbExp=1; IntAct=EBI-713693, EBI-603262;
O14818:PSMA7; NbExp=1; IntAct=EBI-713693, EBI-603272;
P63173:RPL38; NbExp=1; IntAct=EBI-713693, EBI-359141;
Q9Y230:RUVBL2; NbExp=1; IntAct=EBI-713693, EBI-352939;
Q5TZU9:STIP1; NbExp=1; IntAct=EBI-713693, EBI-1054052;
Q9NZ23:YA61; NbExp=1; IntAct=EBI-713693, EBI-1047727;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
PTM: The N-terminus is blocked.
DISEASE: This protein is found in reduced amount in tumor cells of high metastatic potential.
SIMILARITY: Belongs to the NDK family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X58965; CAB37870.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M36981; AAA36369.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L16785; AAA60228.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002476; AAH02476.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A49798; A49798.

RefSeq

NP_001018146.1; -.
NP_001018147.1; -.
NP_001018148.1; -.
NP_001018149.1; -.
NP_002503.1; -.

UniGene

Hs.463456

3D structure databases

PDB

1NSK; X-ray; 2.80 A; L/N/O/R/T/U=1-152.	[ExPASy / RCSB / EBI]
1NUE; X-ray; 2.00 A; A/B/C/D/E/F=2-152.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1NSK; -.
1NUE; -.

ModBase

P22392.

Protein-protein interaction databases

IntAct

P22392; -.

PTM databases

PhosphoSite

P22392; -.

Enzyme and pathway databases

Reactome

REACT_1698; Nucleotide metabolism.

2D gel databases

DOSAC-COBS-2DPAGE

P22392; -.

OGP

P22392; -.

Organism-specific databases

H-InvDB

HIX0013992; -.
HIX0036862; -.

HGNC:7850; NME2.

156491; gene. [NCBI / EBI]

PharmGKB

PA250; -.

GeneCards

P22392.

Gene expression databases

ArrayExpress

P22392; -.

GermOnline

ENSG00000011052; Homo sapiens.

Ontologies

GO:0030027;	Cellular component: lamellipodium (inferred from direct assay from HGNC).
GO:0005634;	Cellular component: nucleus (non-traceable author statement from UniProtKB).
GO:0001726;	Cellular component: ruffle (inferred from direct assay from HGNC).
GO:0005524;	Molecular function: ATP binding (non-traceable author statement from UniProtKB).
GO:0004550;	Molecular function: nucleoside diphosphate kinase activity (traceable author statement from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003700;	Molecular function: transcription factor activity (traceable author statement from UniProtKB).
GO:0007155;	Biological process: cell adhesion (traceable author statement from HGNC).
GO:0043066;	Biological process: negative regulation of apoptosis (inferred from mutant phenotype from HGNC).
GO:0008285;	Biological process: negative regulation of cell proliferation (traceable author statement from UniProtKB).
GO:0009142;	Biological process: nucleoside triphosphate biosynthetic process (non-traceable author statement from UniProtKB).
GO:0050679;	Biological process: positive regulation of epithelial cell proliferation (inferred from mutant phenotype from HGNC).
GO:0045618;	Biological process: positive regulation of keratinocyte differentiation (inferred from mutant phenotype from HGNC).
GO:0045682;	Biological process: regulation of epidermis development (inferred from mutant phenotype from HGNC).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001564; Nuc_diP_kinase_core.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.70.141; NDK; 1.

PANTHER

PTHR11349; Nuc_diP_kinase_core; 1.

Pfam

PF00334; NDK; 1.
Pfam graphical view of domain structure.

PRINTS

PR01243; NUCDPKINASE.

ProDom

PD001018; NDK; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00562; NDK; 1.
SMART graphical view of domain structure.

PROSITE

PS00469; NDP_KINASES; 1.

BLOCKS

P22392.

Genome annotation databases

Ensembl

ENSG00000011052; Homo sapiens. [Contig view]

GeneID

4831; -.
654364; -.

KEGG

hsa:4831; -.
hsa:654364; -.

Phylogenomic databases

HOVERGEN

P22392; -.

Other

P22392; -.

NME2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Activator; Anti-oncogene; ATP-binding; Cell cycle; Cytoplasm; Direct protein sequencing; DNA-binding; Kinase; Magnesium; Metal-binding; Nucleotide metabolism; Nucleotide-binding; Nucleus; Phosphoprotein; Transcription; Transcription regulation; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 152`	`152`	`Nucleoside diphosphate kinase B.`	`PRO_0000137117`
`REGION`	`1 66`	`66`	`Interaction with AKAP13.`
`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.`
`STRAND`	`6 11`	`6`
`HELIX`	`13 17`	`5`
`HELIX`	`21 31`	`11`
`STRAND`	`34 41`	`8`
`HELIX`	`45 51`	`7`
`HELIX`	`53 55`	`3`
`HELIX`	`61 69`	`9`
`STRAND`	`73 79`	`7`
`HELIX`	`83 91`	`9`
`HELIX`	`96 98`	`3`
`HELIX`	`104 108`	`5`
`HELIX`	`112 114`	`3`
`STRAND`	`117 119`	`3`
`HELIX`	`123 133`	`11`
`HELIX`	`136 138`	`3`
`HELIX`	`147 150`	`4`

Sequence information

Length: 152 AA [This is the length of the unprocessed precursor]

Molecular weight: 17298 Da [This is the MW of the unprocessed precursor]

CRC64: 1A5C3F84D7AD272C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF 

        70         80         90        100        110        120 
FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS 

       130        140        150 
DSVKSAEKEI SLWFKPEELV DYKSCAHDWV YE

P22392 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools