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P15531 (NDKA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
NM23-H1
Tumor metastatic process-associated protein
Gene names
Name:NME1
Synonyms:NDPKA, NM23
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. 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. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair. Ref.11 Ref.13 Ref.15 Ref.17

Catalytic activity

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. HAMAP-Rule MF_00451

Cofactor

Magnesium.

Enzyme regulation

Autophosphorylation at His-118 increases serine/threonine protein kinase activity of the enzyme. Interaction with the SET complex inhibits the endonuclease activity. Ref.15

Subunit structure

Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with PRUNE. Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Within this complex, interacts directly with SET. Also interacts with TREX1, but only following translocation to the nucleus. Ref.2 Ref.15 Ref.17 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 processDifferentiation
Endocytosis
Neurogenesis
Nucleotide metabolism
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCTP biosynthetic process

Inferred from electronic annotation. Source: InterPro

DNA catabolic process

Inferred from direct assay PubMed 11555662. Source: GOC

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: Ensembl

cellular response to fatty acid

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

hippocampus development

Inferred from electronic annotation. Source: Ensembl

lactation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Traceable author statement Ref.2. Source: UniProtKB

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of myeloid leukocyte differentiation

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule interconversion

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

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: Ensembl

regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

response to amine

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 16814409. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 16814409. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

ruffle membrane

Inferred from direct assay PubMed 16814409. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.22. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.22. Source: UniProtKB

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

deoxyribonuclease activity

Inferred from direct assay PubMed 11555662. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 10602478PubMed 16189514PubMed 17314099. Source: IntAct

magnesium ion binding

Inferred from direct assay PubMed 11555662. Source: UniProtKB

nucleoside diphosphate kinase activity

Inferred from direct assay Ref.22. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17975005. Source: UniProtKB

ribosomal small subunit binding

Inferred from physical interaction PubMed 16814409. Source: UniProtKB

single-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 152151Nucleoside diphosphate kinase A HAMAP-Rule MF_00451
PRO_0000137114

Sites

Active site1181Pros-phosphohistidine intermediate Ref.2
Binding site121ATP
Binding site601ATP
Binding site881ATP
Binding site941ATP
Binding site1051ATP
Binding site1151ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.19
Cross-link100Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) HAMAP-Rule MF_00451

Natural variations

Alternative sequence11M → MVLLSTLGIVFQGEGPPISS CDTGTM in isoform 2.
VSP_036707
Natural variant1201S → G in a neuroblastoma sample; increased motility of carcinoma cells. Ref.23
Corresponds to variant rs121917887 [ dbSNP | Ensembl ].
VAR_004625

Experimental info

Mutagenesis601F → W: No loss of activity or substrate binding. Ref.22
Mutagenesis961P → S: Increased motility of carcinoma cells. Ref.13
Mutagenesis1181H → F: Loss of serine/threonine kinase activity. Some loss of motility of carcinoma cells. Ref.13 Ref.22
Mutagenesis1181H → G: Loss of activity. Ref.13 Ref.22
Mutagenesis1201S → A: Limited increase in motility of carcinoma cells. Ref.13

Secondary structure

.................................... 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NM23-H1A) [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: AAE9C0DF63CB70A1

FASTA15217,149
        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 

« Hide

Isoform 2 (NM23-H1B) [UniParc].

Checksum: DEA9961E992D0378
Show »

FASTA17719,654
Isoform 3 (NM23-LV) [UniParc].

See P22392.

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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), IDENTIFICATION BY 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, IDENTIFICATION IN THE SET COMPLEX.
[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]"The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death."
Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., Perrino F.W., Lieberman J.
Mol. Cell 23:133-142(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TREX1, IDENTIFICATION IN THE SET COMPLEX.
[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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[20]"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].
[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] [Europe PMC] [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] [Europe PMC] [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] [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.
CCDSCCDS11578.1. [P15531-2]
CCDS11579.1. [P15531-1]
PIRA33386.
RefSeqNP_000260.1. NM_000269.2. [P15531-1]
NP_937818.1. NM_198175.1. [P15531-2]
UniGeneHs.463456.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXVX-ray2.20A/B/C/D/E/F1-152[»]
1UCNX-ray2.00A/B/C1-152[»]
2HVDX-ray2.15A/B/C1-152[»]
2HVEX-ray2.40A/B/C1-152[»]
3L7UX-ray2.10A/B/C1-152[»]
4ENOX-ray2.80A/B1-152[»]
ProteinModelPortalP15531.
SMRP15531. Positions 1-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110894. 45 interactions.
DIPDIP-39164N.
IntActP15531. 22 interactions.
MINTMINT-221462.
STRING9606.ENSP00000013034.

Chemistry

ChEMBLCHEMBL2159.
DrugBankDB00441. Gemcitabine.
DB00396. Progesterone.

PTM databases

PhosphoSiteP15531.

Polymorphism databases

DMDM127981.

2D gel databases

DOSAC-COBS-2DPAGEP15531.
OGPP15531.

Proteomic databases

MaxQBP15531.
PaxDbP15531.
PRIDEP15531.

Protocols and materials databases

DNASU4830.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000013034; ENSP00000013034; ENSG00000239672. [P15531-2]
ENST00000336097; ENSP00000337060; ENSG00000239672. [P15531-2]
ENST00000393196; ENSP00000376892; ENSG00000239672. [P15531-1]
GeneID4830.
KEGGhsa:4830.
UCSCuc002ith.2. human. [P15531-2]
uc002iti.2. human. [P15531-1]

Organism-specific databases

CTD4830.
GeneCardsGC17P049231.
HGNCHGNC:7849. NME1.
HPAHPA008467.
HPA041113.
MIM156490. gene.
neXtProtNX_P15531.
PharmGKBPA249.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0105.
HOGENOMHOG000224564.
HOVERGENHBG000423.
KOK00940.
OMACAHEWIY.
OrthoDBEOG7GJ6FG.
PhylomeDBP15531.
TreeFamTF106373.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000011052-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP15531.
BgeeP15531.
CleanExHS_NME1.
GenevestigatorP15531.

Family and domain databases

Gene3D3.30.70.141. 1 hit.
HAMAPMF_00451. NDP_kinase.
InterProIPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view]
PfamPF00334. NDK. 1 hit.
[Graphical view]
PRINTSPR01243. NUCDPKINASE.
SMARTSM00562. NDK. 1 hit.
[Graphical view]
SUPFAMSSF54919. SSF54919. 1 hit.
PROSITEPS00469. NDP_KINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15531.
GeneWikiNME1.
GenomeRNAi4830.
NextBio18606.
PROP15531.
SOURCESearch...

Entry information

Entry nameNDKA_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM