P15531 (NDKA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleoside diphosphate kinase A
Short name=NDK A
Short name=NDP kinase A
EC=2.7.4.6

Alternative name(s):
Granzyme A-activated DNase
Short name=GAAD
Metastasis inhibition factor nm23
Tumor metastatic process-associated protein
nm23-H1

Gene names

Name:	NME1
Synonyms:	NDPKA, NM23

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
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. Ref.11 Ref.13 Ref.15
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. Ref.15
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.5 Ref.14 Ref.16
Miscellaneous	The role of this protein in tumor development and progression is uncertain. This protein is found in reduced amount in some tumor cells of high metastatic potential. However, increased NME1 levels correlate with aggressive tumor features in neuroblastoma. May have distinct if not opposite roles in different tumors.
Sequence similarities	Belongs to the NDK family.
Sequence caution	The sequence CAA35621.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Differentiation Endocytosis Neurogenesis Nucleotide metabolism
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
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 cellular response to drug Inferred from electronic annotation. Source: Compara cellular response to fatty acid Inferred from electronic annotation. Source: Compara cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara endocytosis Inferred from electronic annotation. Source: UniProtKB-KW hippocampus development Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Traceable author statement Ref.2. Source: UniProtKB negative regulation of gene expression Inferred from electronic annotation. Source: Compara negative regulation of myeloid leukocyte differentiation Inferred from electronic annotation. Source: Compara nucleobase-containing small molecule interconversion Traceable author statement. Source: Reactome positive regulation of DNA binding Inferred from direct assay PubMed 17975005. Source: UniProtKB positive regulation of epithelial cell proliferation Inferred from mutant phenotype PubMed 16862176. Source: HGNC positive regulation of neuron projection development Inferred from electronic annotation. Source: Compara regulation of apoptotic process Traceable author statement PubMed 16130169. Source: UniProtKB response to amine stimulus Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to testosterone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	centrosome Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: Compara nucleus Traceable author statement PubMed 16130169. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from direct assay Ref.21. Source: UniProtKB GTP binding Inferred from direct assay Ref.21. Source: UniProtKB RNA polymerase II regulatory region sequence-specific DNA binding Inferred from electronic annotation. Source: Compara deoxyribonuclease activity Inferred from direct assay PubMed 11555662. Source: UniProtKB magnesium ion binding Inferred from direct assay PubMed 11555662. Source: UniProtKB nucleoside diphosphate kinase activity Inferred from direct assay Ref.21. Source: UniProtKB ribosomal small subunit binding Inferred from physical interaction PubMed 16814409. Source: UniProtKB single-stranded DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-741141,EBI-741141
Ksr1	Q61097	7	EBI-741141,EBI-1536336	From a different organism.
MCF2	P10911	4	EBI-741141,EBI-1914514
NME2	P22392	2	EBI-741141,EBI-713693
PRUNE	Q86TP1	2	EBI-741141,EBI-2127112
STRAP	Q9Y3F4	9	EBI-741141,EBI-727414
WDYHV1	Q96HA8	3	EBI-741141,EBI-741158

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.
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

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 a neuroblastoma sample; increased motility of carcinoma cells. Ref.22

VAR_004625

Experimental info

Mutagenesis

60

1

F → W: No loss of activity or substrate binding. Ref.21

Mutagenesis

96

1

P → S: Increased motility of carcinoma cells. Ref.13

Mutagenesis

118

1

H → F: Loss of serine/threonine kinase activity. Some loss of motility of carcinoma cells. Ref.13 Ref.21

Mutagenesis

118

1

H → G: Loss of activity. Ref.13 Ref.21

Mutagenesis

120

1

S → A: Limited increase in motility of carcinoma cells. Ref.13

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

152

Helix Strand Turn

Details...

Helix

2 – 4

3

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

Helix

112 – 114

3

Beta strand

116 – 119

4

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) [UniParc]. 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) [UniParc]. See P22392.		–	–

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 7-18; 40-49 AND 89-94 (ISOFORMS 1/2), DISCUSSION OF THE ROLE IN TUMOR PROGRESSION. Tissue: Neuroblastoma.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRUNE.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[21]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF PHE-60 AND HIS-118.
[22]	"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] [Europe PMC] [Abstract] Cited for: VARIANT GLY-120.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_000269.2.
NP_937818.1. NM_198175.1.

UniGene

Hs.463456.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3L7U	X-ray	2.10	A/B/C	1-152	[»]
4ENO	X-ray	2.80	A/B	1-152	[»]

ProteinModelPortal

P15531.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39164N.

IntAct

P15531. 21 interactions.

MINT

MINT-221462.

STRING

9606.ENSP00000013034.

PTM databases

PhosphoSite

P15531.

Polymorphism databases

DMDM

127981.

2D gel databases

DOSAC-COBS-2DPAGE

P15531.

OGP

P15531.

Proteomic databases

PaxDb

P15531.

PRIDE

P15531.

Protocols and materials databases

DNASU

4830.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000013034; ENSP00000013034; ENSG00000239672.
ENST00000336097; ENSP00000337060; ENSG00000239672.
ENST00000393196; ENSP00000376892; ENSG00000239672.

GeneID

4830.

KEGG

hsa:4830.

UCSC

uc002ith.2. human.
uc002iti.2. human.

Organism-specific databases

CTD

4830.

GeneCards

GC17P049231.

HGNC

HGNC:7849. NME1.

HPA

HPA008467.
HPA041113.

MIM

156490. gene.

neXtProt

NX_P15531.

PharmGKB

PA249.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0105.

HOGENOM

HOG000224564.

HOVERGEN

HBG000423.

KO

K00940.

OMA

ARQMMGK.

OrthoDB

EOG4S1T8G.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000011052-MONOMER.

Pathway_Interaction_DB

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

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P15531.

Bgee

P15531.

CleanEx

HS_NME1.

Genevestigator

P15531.

GermOnline

ENSG00000011052. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.141. 1 hit.

InterPro

IPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view]

PANTHER

PTHR11349. PTHR11349. 1 hit.

Pfam

PF00334. NDK. 1 hit.
[Graphical view]

PRINTS

PR01243. NUCDPKINASE.

SMART

SM00562. NDK. 1 hit.
[Graphical view]

SUPFAM

SSF54919. NDK. 1 hit.

PROSITE

PS00469. NDP_KINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2159.

DrugBank

DB00441. Gemcitabine.
DB00396. Progesterone.

EvolutionaryTrace

P15531.

GenomeRNAi

4830.

NextBio

18606.

SOURCE

Search...

Entry information

Entry name

NDKA_HUMAN

Accession

Primary (citable) accession number: P15531
Secondary accession number(s): Q6FGK3, Q86XQ2, Q9UDJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 29, 2013
This is version 157 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.