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Nucleoside diphosphate kinase A (NDK A) (NDP kinase A) (EC 2.7.4.6) (Granzyme A-activated DNase) (GAAD) (Metastasis inhibition factor nm23) (NM23-H1) (Tumor metastatic process-associated protein)

 NDKA_HUMAN              Reviewed;         152 AA.
P15531; Q6FGK3; Q86XQ2; Q9UDJ6;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
30-AUG-2017, entry version 203.
RecName: Full=Nucleoside diphosphate kinase A;
Short=NDK A;
Short=NDP kinase A;
EC=2.7.4.6;
AltName: Full=Granzyme A-activated DNase;
Short=GAAD;
AltName: Full=Metastasis inhibition factor nm23;
AltName: Full=NM23-H1;
AltName: Full=Tumor metastatic process-associated protein;
Name=NME1; Synonyms=NDPKA, NM23;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2509941; DOI=10.1038/342177a0;
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.;
"Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila
development.";
Nature 342:177-180(1989).
[2]
PROTEIN SEQUENCE (ISOFORM 1), SUBUNIT, AND ACTIVE SITE.
PubMed=1851158;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7916650;
Wang L., Patel U., Ghosh L., Chen H.C., Banerjee S.;
"Mutation in the nm23 gene is associated with metastasis in colorectal
cancer.";
Cancer Res. 53:717-720(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=8270257; DOI=10.1007/BF00218915;
Dooley S., Seib T., Engel M., Theisinger B., Janz H., Piontek K.,
Zang K.D., Welter C.;
"Isolation and characterization of the human genomic locus coding for
the putative metastasis control gene nm23-H1.";
Hum. Genet. 93:63-66(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=12601555; DOI=10.1007/s100380300014;
Ni X., Gu S., Dai J., Cheng H., Guo L., Li L., Ji C., Xie Y., Ying K.,
Mao Y.;
"Isolation and characterization of a novel human NM23-H1B gene, a
different transcript of NM23-H1.";
J. Hum. Genet. 48:96-100(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
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.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[11]
PROTEIN SEQUENCE OF 7-18; 40-49 AND 89-94 (ISOFORMS 1/2), AND
DISCUSSION OF THE ROLE IN TUMOR PROGRESSION.
TISSUE=Neuroblastoma;
PubMed=2056128; DOI=10.1172/JCI115299;
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.;
"High levels of p19/nm23 protein in neuroblastoma are associated with
advanced stage disease and with N-myc gene amplification.";
J. Clin. Invest. 88:341-345(1991).
[12]
PROTEIN SEQUENCE OF 7-26; 40-49; 57-85 AND 89-128 (ISOFORMS 1/2), AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[13]
FUNCTION, AND MUTAGENESIS OF PRO-96; HIS-118 AND SER-120.
PubMed=8810265; DOI=10.1074/jbc.271.41.25107;
MacDonald N.J., Freije J.M., Stracke M.L., Manrow R.E., Steeg P.S.;
"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.";
J. Biol. Chem. 271:25107-25116(1996).
[14]
TISSUE SPECIFICITY.
PubMed=10512675; DOI=10.1006/geno.1999.5939;
Manda R., Kohno T., Matsuno Y., Takenoshita S., Kuwano H., Yokota J.;
"Identification of genes (SPON2 and C20orf2) differentially expressed
between cancerous and noncancerous lung cells by mRNA differential
display.";
Genomics 61:5-14(1999).
[15]
FUNCTION, ENZYME REGULATION, INTERACTION WITH SET, AND IDENTIFICATION
IN THE SET COMPLEX.
PubMed=12628186; DOI=10.1016/S0092-8674(03)00150-8;
Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.;
"Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-
mediated apoptosis, and the nucleosome assembly protein SET is its
inhibitor.";
Cell 112:659-672(2003).
[16]
ALTERNATIVE SPLICING (ISOFORM 3), SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=16442775; DOI=10.1016/j.ygeno.2005.11.004;
Valentijn L.J., Koster J., Versteeg R.;
"Read-through transcript from NM23-H1 into the neighboring NM23-H2
gene encodes a novel protein, NM23-LV.";
Genomics 87:483-489(2006).
[17]
FUNCTION, INTERACTION WITH TREX1, AND IDENTIFICATION IN THE SET
COMPLEX.
PubMed=16818237; DOI=10.1016/j.molcel.2006.06.005;
Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B.,
Perrino F.W., Lieberman J.;
"The exonuclease TREX1 is in the SET complex and acts in concert with
NM23-H1 to degrade DNA during granzyme A-mediated cell death.";
Mol. Cell 23:133-142(2006).
[18]
INTERACTION WITH PRUNE1.
PubMed=17906697; DOI=10.1038/sj.onc.1210822;
Garzia L., D'Angelo A., Amoresano A., Knauer S.K., Cirulli C.,
Campanella C., Stauber R.H., Steegborn C., Iolascon A., Zollo M.;
"Phosphorylation of nm23-H1 by CKI induces its complex formation with
h-prune and promotes cell motility.";
Oncogene 27:1853-1864(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-122 AND
SER-125, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[23]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=11835509; DOI=10.1002/prot.10038;
Min K., Song H.K., Chang C., Kim S.Y., Lee K.J., Suh S.W.;
"Crystal structure of human nucleoside diphosphate kinase A, a
metastasis suppressor.";
Proteins 46:340-342(2002).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND MUTAGENESIS OF PHE-60 AND
HIS-118.
PubMed=12972261; DOI=10.1016/j.jmb.2003.07.004;
Chen Y., Gallois-Montbrun S., Schneider B., Veron M., Morera S.,
Deville-Bonne D., Janin J.;
"Nucleotide binding to nucleoside diphosphate kinases: X-ray structure
of human NDPK-A in complex with ADP and comparison to protein
kinases.";
J. Mol. Biol. 332:915-926(2003).
[25]
VARIANT GLY-120.
PubMed=8047138; DOI=10.1038/370335a0;
Chang C.L., Zhu X.-X., Thoraval D.H., Ungar D., Rawwas J., Hora N.,
Strahler J.R., Hanash S.M.;
"Nm23-H1 mutation in neuroblastoma.";
Nature 370:335-336(1994).
-!- 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. {ECO:0000269|PubMed:12628186,
ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:8810265}.
-!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
nucleoside triphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Autophosphorylation at His-118 increases
serine/threonine protein kinase activity of the enzyme.
Interaction with the SET complex inhibits the endonuclease
activity. {ECO:0000269|PubMed:12628186}.
-!- SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2,
A3B3, A2B4, AB5, B6). Interacts with PRUNE1. 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. {ECO:0000269|PubMed:12628186,
ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:17906697,
ECO:0000269|PubMed:1851158}.
-!- INTERACTION:
Self; NbExp=14; IntAct=EBI-741141, EBI-741141;
Q61097:Ksr1 (xeno); NbExp=7; IntAct=EBI-741141, EBI-1536336;
P10911:MCF2; NbExp=4; IntAct=EBI-741141, EBI-1914514;
P22392:NME2; NbExp=2; IntAct=EBI-741141, EBI-713693;
Q13232:NME3; NbExp=4; IntAct=EBI-741141, EBI-713684;
O00746:NME4; NbExp=6; IntAct=EBI-741141, EBI-744871;
Q7Z2X4:PID1; NbExp=3; IntAct=EBI-741141, EBI-10256685;
O15160:POLR1C; NbExp=7; IntAct=EBI-741141, EBI-1055079;
Q86TP1:PRUNE1; NbExp=2; IntAct=EBI-741141, EBI-2127112;
Q8N9Q2:SREK1IP1; NbExp=3; IntAct=EBI-741141, EBI-10268630;
Q9Y3F4:STRAP; NbExp=9; IntAct=EBI-741141, EBI-727414;
O14787:TNPO2; NbExp=3; IntAct=EBI-741141, EBI-431907;
Q96HA8:WDYHV1; NbExp=5; IntAct=EBI-741141, EBI-741158;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16442775}.
Nucleus {ECO:0000269|PubMed:16442775}. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=NM23-H1A;
IsoId=P15531-1; Sequence=Displayed;
Name=2; Synonyms=NM23-H1B;
IsoId=P15531-2; Sequence=VSP_036707;
Name=3; Synonyms=NM23-LV;
IsoId=P22392-2; Sequence=External;
Note=Based on a naturally occurring readthrough transcript which
produces an NME1-NME2 fusion protein.;
-!- 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.
{ECO:0000269|PubMed:10512675, ECO:0000269|PubMed:12601555,
ECO:0000269|PubMed:16442775}.
-!- 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.
-!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA35621.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X17620; CAA35621.1; ALT_INIT; mRNA.
EMBL; X73066; CAA51527.1; -; mRNA.
EMBL; X75598; CAA53270.1; -; Genomic_DNA.
EMBL; AF487339; AAO85436.1; -; mRNA.
EMBL; AK291105; BAF83794.1; -; mRNA.
EMBL; CR542104; CAG46901.1; -; mRNA.
EMBL; CR542115; CAG46912.1; -; mRNA.
EMBL; AC005839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94568.1; -; Genomic_DNA.
EMBL; BC000293; AAH00293.1; -; mRNA.
EMBL; BC018994; AAH18994.1; -; mRNA.
CCDS; CCDS11578.1; -. [P15531-2]
CCDS; CCDS11579.1; -. [P15531-1]
PIR; A33386; A33386.
RefSeq; NP_000260.1; NM_000269.2. [P15531-1]
RefSeq; NP_937818.1; NM_198175.1. [P15531-2]
UniGene; Hs.463456; -.
PDB; 1JXV; X-ray; 2.20 A; A/B/C/D/E/F=1-152.
PDB; 1UCN; X-ray; 2.00 A; A/B/C=1-152.
PDB; 2HVD; X-ray; 2.15 A; A/B/C=1-152.
PDB; 2HVE; X-ray; 2.40 A; A/B/C=1-152.
PDB; 3L7U; X-ray; 2.10 A; A/B/C=1-152.
PDB; 4ENO; X-ray; 2.80 A; A/B=1-152.
PDBsum; 1JXV; -.
PDBsum; 1UCN; -.
PDBsum; 2HVD; -.
PDBsum; 2HVE; -.
PDBsum; 3L7U; -.
PDBsum; 4ENO; -.
ProteinModelPortal; P15531; -.
SMR; P15531; -.
BioGrid; 110894; 63.
DIP; DIP-39164N; -.
IntAct; P15531; 29.
MINT; MINT-221462; -.
STRING; 9606.ENSP00000013034; -.
ChEMBL; CHEMBL2159; -.
DrugBank; DB03491; 2'-Deoxyguanosine-5'-Diphosphate.
DrugBank; DB02181; 2'-Deoxyguanosine-5'-Triphosphate.
DrugBank; DB04542; 3'-Azido-3'-Deoxythymidine-5'-Diphosphate.
DrugBank; DB04366; 3'-Deoxy 3'-Amino Adenosine-5'-Diphosphate.
DrugBank; DB00718; Adefovir Dipivoxil.
DrugBank; DB02607; Adenosine Phosphonoacetic Acid.
DrugBank; DB04068; Fudp.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
DrugBank; DB00709; Lamivudine.
DrugBank; DB02345; Selenocysteine.
DrugBank; DB00300; Tenofovir.
DrugBank; DB03103; Thymidine-5'- Diphosphate.
iPTMnet; P15531; -.
PhosphoSitePlus; P15531; -.
SwissPalm; P15531; -.
BioMuta; NME1; -.
DMDM; 127981; -.
DOSAC-COBS-2DPAGE; P15531; -.
OGP; P15531; -.
EPD; P15531; -.
PaxDb; P15531; -.
PeptideAtlas; P15531; -.
PRIDE; P15531; -.
TopDownProteomics; P15531-1; -. [P15531-1]
DNASU; 4830; -.
Ensembl; ENST00000013034; ENSP00000013034; ENSG00000239672. [P15531-2]
Ensembl; ENST00000336097; ENSP00000337060; ENSG00000239672. [P15531-2]
Ensembl; ENST00000393196; ENSP00000376892; ENSG00000239672. [P15531-1]
GeneID; 4830; -.
KEGG; hsa:4830; -.
UCSC; uc002ith.3; human. [P15531-1]
CTD; 4830; -.
DisGeNET; 4830; -.
GeneCards; NME1; -.
HGNC; HGNC:7849; NME1.
HPA; CAB040571; -.
HPA; HPA008467; -.
HPA; HPA041113; -.
MalaCards; NME1; -.
MIM; 156490; gene.
neXtProt; NX_P15531; -.
OpenTargets; ENSG00000239672; -.
PharmGKB; PA249; -.
eggNOG; KOG0888; Eukaryota.
eggNOG; COG0105; LUCA.
GeneTree; ENSGT00760000119146; -.
HOGENOM; HOG000224564; -.
HOVERGEN; HBG000423; -.
InParanoid; P15531; -.
KO; K00940; -.
OMA; KIVAMKM; -.
OrthoDB; EOG091G0PLD; -.
PhylomeDB; P15531; -.
TreeFam; TF106373; -.
BioCyc; MetaCyc:ENSG00000011052-MONOMER; -.
BRENDA; 2.7.4.6; 2681.
Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
SIGNOR; P15531; -.
ChiTaRS; NME1; human.
EvolutionaryTrace; P15531; -.
GeneWiki; NME1; -.
GenomeRNAi; 4830; -.
PRO; PR:P15531; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000239672; -.
CleanEx; HS_NME1; -.
ExpressionAtlas; P15531; baseline and differential.
Genevisible; P15531; HS.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0004536; F:deoxyribonuclease activity; IDA:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; IEA:Ensembl.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019215; F:intermediate filament binding; IEA:Ensembl.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0043024; F:ribosomal small subunit binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003697; F:single-stranded DNA binding; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0002762; P:negative regulation of myeloid leukocyte differentiation; IEA:Ensembl.
GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:HGNC.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0014075; P:response to amine; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
Gene3D; 3.30.70.141; -; 1.
HAMAP; MF_00451; NDP_kinase; 1.
InterPro; IPR034907; NDK-like_dom.
InterPro; IPR001564; Nucleoside_diP_kinase.
InterPro; IPR023005; Nucleoside_diP_kinase_AS.
Pfam; PF00334; NDK; 1.
PRINTS; PR01243; NUCDPKINASE.
SMART; SM00562; NDK; 1.
SUPFAM; SSF54919; SSF54919; 1.
PROSITE; PS00469; NDP_KINASES; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Differentiation; Direct protein sequencing; Endocytosis;
Isopeptide bond; Kinase; Magnesium; Metal-binding; Neurogenesis;
Nucleotide metabolism; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transferase; Ubl conjugation.
CHAIN 1 152 Nucleoside diphosphate kinase A.
/FTId=PRO_0000137114.
ACT_SITE 118 118 Pros-phosphohistidine intermediate.
{ECO:0000269|PubMed:1851158}.
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 120 120 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 100 100 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VAR_SEQ 1 1 M -> MVLLSTLGIVFQGEGPPISSCDTGTM (in
isoform 2).
{ECO:0000303|PubMed:12601555}.
/FTId=VSP_036707.
VARIANT 120 120 S -> G (in a neuroblastoma sample;
increased motility of carcinoma cells;
dbSNP:rs121917887).
{ECO:0000269|PubMed:8047138}.
/FTId=VAR_004625.
MUTAGEN 60 60 F->W: No loss of activity or substrate
binding. {ECO:0000269|PubMed:12972261}.
MUTAGEN 96 96 P->S: Increased motility of carcinoma
cells. {ECO:0000269|PubMed:8810265}.
MUTAGEN 118 118 H->F: Loss of serine/threonine kinase
activity. Some loss of motility of
carcinoma cells.
{ECO:0000269|PubMed:12972261,
ECO:0000269|PubMed:8810265}.
MUTAGEN 118 118 H->G: Loss of activity.
{ECO:0000269|PubMed:12972261,
ECO:0000269|PubMed:8810265}.
MUTAGEN 120 120 S->A: Limited increase in motility of
carcinoma cells.
{ECO:0000269|PubMed:8810265}.
HELIX 2 4 {ECO:0000244|PDB:3L7U}.
STRAND 6 11 {ECO:0000244|PDB:1UCN}.
HELIX 13 17 {ECO:0000244|PDB:1UCN}.
HELIX 21 31 {ECO:0000244|PDB:1UCN}.
STRAND 34 41 {ECO:0000244|PDB:1UCN}.
HELIX 45 51 {ECO:0000244|PDB:1UCN}.
HELIX 53 55 {ECO:0000244|PDB:1UCN}.
STRAND 56 58 {ECO:0000244|PDB:4ENO}.
HELIX 61 69 {ECO:0000244|PDB:1UCN}.
STRAND 73 80 {ECO:0000244|PDB:1UCN}.
HELIX 83 91 {ECO:0000244|PDB:1UCN}.
HELIX 96 98 {ECO:0000244|PDB:1UCN}.
HELIX 104 108 {ECO:0000244|PDB:1UCN}.
HELIX 112 114 {ECO:0000244|PDB:1UCN}.
STRAND 116 119 {ECO:0000244|PDB:1UCN}.
HELIX 123 133 {ECO:0000244|PDB:1UCN}.
HELIX 136 138 {ECO:0000244|PDB:1UCN}.
HELIX 147 150 {ECO:0000244|PDB:1UCN}.
SEQUENCE 152 AA; 17149 MW; AAE9C0DF63CB70A1 CRC64;
MANCERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF MQASEDLLKE HYVDLKDRPF
FAGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVESAEKEI GLWFHPEELV DYTSCAQNWI YE


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