Reviewed, UniProtKB/Swiss-Prot P15531 (NDKA_HUMAN)

Names and origin

Protein names

Recommended name:
    Nucleoside diphosphate kinase A
      Short name=NDP kinase A
      Short name=NDK A
    EC=2.7.4.6
Alternative name(s):
    Tumor metastatic process-associated protein
    Metastasis inhibition factor nm23
    nm23-H1
    Granzyme A-activated DNase
      Short name=GAAD

Gene names

Name:	NME1
Synonyms:	NDPKA, NM23

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Has tumor metastasis-suppressive capacity.
Catalytic activity	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
Cofactor	Magnesium.
Enzyme regulation	Autophosphorylation at His-118 increases serine/threonine protein kinase activity of the enzyme. Interaction with the SET complex inhibits exonuclease activity.
Subunit structure	Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with SET and PRUNE. Ref.2 Ref.15 Ref.18
Subcellular location	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. Ref.16
Tissue specificity	Isoform 1 is expressed in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, spleen and thymus. Expressed in lung carcinoma cell lines but not in normal lung tissues. Isoform 2 is ubiquitously expressed and its expression is also related to tumor differentiation. Isoform 3 is ubiquitously expressed. Ref.16 Ref.5 Ref.14
Post-translational modification	The N-terminus is blocked.
Involvement in disease	This protein is found in reduced amount in tumor cells of high metastatic potential. Somatic mutations of NME1 are found in neuroblastoma. Increased NME1 in neuroblastoma is correlated with features of the disease that are associated with aggressive tumors. May therefore have distinct if not opposite roles in different tumors. Ref.11
Sequence similarities	Belongs to the NDK family.

Ontologies

Keywords
Biological process	Cell cycle Differentiation Endocytosis Neurogenesis Nucleotide metabolism
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Anti-oncogene Kinase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	CTP biosynthetic process Inferred from electronic annotation. Source: InterPro GTP biosynthetic process Inferred from electronic annotation. Source: InterPro UTP biosynthetic process Inferred from electronic annotation. Source: InterPro cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW endocytosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell proliferation Ref.2 Traceable author statement. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of DNA binding Inferred from direct assay. Source: UniProtKB positive regulation of epithelial cell proliferation Inferred from mutant phenotype. Source: HGNC regulation of apoptosis Traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Traceable author statement. Source: UniProtKB nucleus Traceable author statement. Source: UniProtKB
Molecular function	ATP binding Ref.22 Inferred from direct assay. Source: UniProtKB DNA binding Inferred by curator. Source: UniProtKB GTP binding Ref.22 Inferred from direct assay. Source: UniProtKB deoxyribonuclease activity Inferred from direct assay. Source: UniProtKB identical protein binding Inferred from physical interaction. Source: IntAct magnesium ion binding Inferred from direct assay. Source: UniProtKB nucleoside diphosphate kinase activity Ref.22 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-741141,EBI-741141
Ksr1	Q61097	2	EBI-741141,EBI-1536336	From a different organism.
MCF2	P10911	4	EBI-741141,EBI-1914514
NME2	P22392	1	EBI-741141,EBI-713693
PRUNE	Q86TP1	1	EBI-741141,EBI-2127112
STRAP	Q9Y3F4	6	EBI-741141,EBI-727414

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P15531-1)

Also known as: NM23-H1A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P15531-2)

Also known as: NM23-H1B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVLLSTLGIVFQGEGPPISSCDTGTM

Isoform 3 (identifier: P22392-2)

Also known as: NM23-LV;

The sequence of this isoform can be found in the external entry P22392-2.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Based on a naturally occurring readthrough transcript which produces an NME1-NME2 fusion protein.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 152

152

Nucleoside diphosphate kinase A

PRO_0000137114

Sites

Active site

118

1

Pros-phosphohistidine intermediate Ref.2

Binding site

12

1

ATP

Binding site

60

1

ATP

Binding site

88

1

ATP

Binding site

94

1

ATP

Binding site

105

1

ATP

Binding site

115

1

ATP

Amino acid modifications

Modified residue

94

1

Phosphothreonine Ref.19

Cross-link

100

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17

Natural variations

Alternative sequence

1

1

M → MVLLSTLGIVFQGEGPPISS CDTGTM in isoform 2.

VSP_036707

Natural variant

120

1

S → G in neuroblastoma; increased motility of carcinoma cells.

VAR_004625

Experimental info

Mutagenesis

60

1

F → W: No loss of activity or substrate binding. Ref.22

Mutagenesis

96

1

P → S: Increased motility of carcinoma cells.

Mutagenesis

118

1

H → F: Loss of serine/threonine kinase activity. Some loss of motility of carcinoma cells.

Mutagenesis

118

1

H → G: Loss of activity. Ref.22

Mutagenesis

120

1

S → A: Limited increase in motility of carcinoma cells.

Secondary structure

1

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152

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Helix

13 – 17

5

Helix

21 – 31

11

Beta strand

34 – 41

8

Helix

45 – 51

7

Helix

53 – 55

3

Helix

61 – 69

9

Beta strand

73 – 80

8

Helix

83 – 91

9

Helix

96 – 98

3

Helix

104 – 108

5

Beta strand

117 – 119

3

Helix

123 – 133

11

Helix

136 – 138

3

Helix

147 – 150

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NM23-H1A) [UniParc]. Last modified April 1, 1990. Version 1. Checksum: AAE9C0DF63CB70A1	FASTA	152	17,149
	10 20 30 40 50 60 MANCERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF MQASEDLLKE HYVDLKDRPF 70 80 90 100 110 120 FAGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS 130 140 150 DSVESAEKEI GLWFHPEELV DYTSCAQNWI YE
	Isoform 2 (NM23-H1B). Checksum: DEA9961E992D0378	FASTA	177	19,654
	10 20 30 40 50 60 MVLLSTLGIV FQGEGPPISS CDTGTMANCE RTFIAIKPDG VQRGLVGEII KRFEQKGFRL 70 80 90 100 110 120 VGLKFMQASE DLLKEHYVDL KDRPFFAGLV KYMHSGPVVA MVWEGLNVVK TGRVMLGETN 130 140 150 160 170 PADSKPGTIR GDFCIQVGRN IIHGSDSVES AEKEIGLWFH PEELVDYTSC AQNWIYE
	Isoform 3 (NM23-LV). See P22392.	FASTA	–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development." Rosengard A.M., Krutzsch H.C., Shearn A., Biggs J.R., Barker E., Margulies I.M.K., King C.R., Liotta L.A., Steeg P.S. Nature 342:177-180(1989) [PubMed: 2509941] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme." Gilles A.-M., Presecan E., Vonica A., Lascu I. J. Biol. Chem. 266:8784-8789(1991) [PubMed: 1851158] [Abstract] Cited for: PROTEIN SEQUENCE (ISOFORM 1), SUBUNIT, ACTIVE SITE.
[3]	"Mutation in the nm23 gene is associated with metastasis in colorectal cancer." Wang L., Patel U., Ghosh L., Chen H.C., Banerjee S. Cancer Res. 53:717-720(1993) [PubMed: 7916650] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1." Dooley S., Seib T., Engel M., Theisinger B., Janz H., Piontek K., Zang K.D., Welter C. Hum. Genet. 93:63-66(1994) [PubMed: 8270257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]	"Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1." Ni X., Gu S., Dai J., Cheng H., Guo L., Li L., Ji C., Xie Y., Ying K., Mao Y. J. Hum. Genet. 48:96-100(2003) [PubMed: 12601555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain and Lung.
[11]	"High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification." Hailat N., Keim D.R., Melhem R.F., Zhu X.X., Eckerskorn C., Brodeur G.M., Reynolds C.P., Seeger R.C., Lottspeich F., Strahler J.R., Hanash S.J. J. Clin. Invest. 88:341-345(1991) [PubMed: 2056128] [Abstract] Cited for: PROTEIN SEQUENCE OF 7-18; 40-49 AND 89-94 (ISOFORMS 1/2), DISEASE.
[12]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 7-26; 40-49; 57-85 AND 89-128 (ISOFORMS 1/2), MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[13]	"Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells." MacDonald N.J., Freije J.M., Stracke M.L., Manrow R.E., Steeg P.S. J. Biol. Chem. 271:25107-25116(1996) [PubMed: 8810265] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF PRO-96; HIS-118 AND SER-120.
[14]	"Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display." Manda R., Kohno T., Matsuno Y., Takenoshita S., Kuwano H., Yokota J. Genomics 61:5-14(1999) [PubMed: 10512675] [Abstract] Cited for: TISSUE SPECIFICITY.
[15]	"Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor." Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J. Cell 112:659-672(2003) [PubMed: 12628186] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SET.
[16]	"Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV." Valentijn L.J., Koster J., Versteeg R. Genomics 87:483-489(2006) [PubMed: 16442775] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[17]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-100, MASS SPECTROMETRY.
[18]	"Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility." Garzia L., D'Angelo A., Amoresano A., Knauer S.K., Cirulli C., Campanella C., Stauber R.H., Steegborn C., Iolascon A., Zollo M. Oncogene 27:1853-1864(2008) [PubMed: 17906697] [Abstract] Cited for: INTERACTION WITH PRUNE.
[19]	"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) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94, MASS SPECTROMETRY.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor." Min K., Song H.K., Chang C., Kim S.Y., Lee K.J., Suh S.W. Proteins 46:340-342(2002) [PubMed: 11835509] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[22]	"Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases." Chen Y., Gallois-Montbrun S., Schneider B., Veron M., Morera S., Deville-Bonne D., Janin J. J. Mol. Biol. 332:915-926(2003) [PubMed: 12972261] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF PHE-60 AND HIS-118.
[23]	"Nm23-H1 mutation in neuroblastoma." Chang C.L., Zhu X.-X., Thoraval D.H., Ungar D., Rawwas J., Hora N., Strahler J.R., Hanash S.M. Nature 370:335-336(1994) [PubMed: 8047138] [Abstract] Cited for: VARIANT NEUROBLASTOMA GLY-120.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X17620 mRNA. Translation: CAA35621.1. Different initiation.
X73066 mRNA. Translation: CAA51527.1.
X75598 Genomic DNA. Translation: CAA53270.1.
AF487339 mRNA. Translation: AAO85436.1.
AK291105 mRNA. Translation: BAF83794.1.
CR542104 mRNA. Translation: CAG46901.1.
CR542115 mRNA. Translation: CAG46912.1.
AC005839 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94568.1.
BC000293 mRNA. Translation: AAH00293.1.
BC018994 mRNA. Translation: AAH18994.1.

IPI

IPI00012048.
IPI00375531.

PIR

A33386.

RefSeq

NP_000260.1.
NP_937818.1.

UniGene

Hs.463456

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JXV	X-ray	2.20	A/B/C/D/E/F	1-152	[»]
1UCN	X-ray	2.00	A/B/C	1-152	[»]
2HVD	X-ray	2.15	A/B/C	1-152	[»]
2HVE	X-ray	2.40	A/B/C	1-152	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P15531. 13 interactions.

PTM databases

PhosphoSite

P15531.

2-D gel databases

Aarhus/Ghent-2DPAGE

4115. IEF.
5112. IEF.

DOSAC-COBS-2DPAGE

P15531.

OGP

P15531.

PMMA-2DPAGE

P15531.

Proteomic databases

PRIDE

P15531.

Genome annotation databases

Ensembl

ENSG00000011052. Homo sapiens. [Contig view]

GeneID

4830.

KEGG

hsa:4830.

NMPDR

fig|9606.3.peg.14075.
fig|9606.3.peg.14076.

Organism-specific databases

GeneCards

GC17P046585.
GC17P046586.

HGNC

HGNC:7849. NME1.

HPA

CAB002169.
HPA008467.

MIM

156490. gene.

Orphanet

635. Neuroblastoma.

PharmGKB

PA249.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P15531.

OMA

P15531. YDELCEF.

Enzyme and pathway databases

BRENDA

2.7.4.6. 247.

Pathway_Interaction_DB

arf6downstreampathway. Arf6 downstream pathway.
arf6_traffickingpathway. Arf6 trafficking events.

Reactome

REACT_1698. Nucleotide metabolism.

Gene expression databases

ArrayExpress

P15531.

Bgee

P15531.

CleanEx

HS_NME1.

GermOnline

ENSG00000011052. Homo sapiens.

Family and domain databases

InterPro

IPR001564. Nuc_diP_kinase_core.
[Graphical view]

Gene3D

G3DSA:3.30.70.141. NDK. 1 hit.

PANTHER

PTHR11349. Nuc_diP_kinase_core. 1 hit.

Pfam

PF00334. NDK. 1 hit.
[Graphical view]

PRINTS

PR01243. NUCDPKINASE.

ProDom

PD001018. NDK. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00562. NDK. 1 hit.
[Graphical view]

PROSITE

PS00469. NDP_KINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00441. Gemcitabine.
DB00396. Progesterone.

NextBio

18606.

SOURCE

Search...

Entry information

Entry name

NDKA_HUMAN

Accession

Primary (citable) accession number: P15531
Secondary accession number(s): Q6FGK3, Q86XQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)