NDKA_HUMAN
ID NDKA_HUMAN Reviewed; 152 AA.
AC P15531; Q6FGK3; Q86XQ2; Q9UDJ6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 240.
DE RecName: Full=Nucleoside diphosphate kinase A;
DE Short=NDK A;
DE Short=NDP kinase A;
DE EC=2.7.4.6;
DE AltName: Full=Granzyme A-activated DNase;
DE Short=GAAD;
DE AltName: Full=Metastasis inhibition factor nm23;
DE AltName: Full=NM23-H1;
DE AltName: Full=Tumor metastatic process-associated protein;
GN Name=NME1; Synonyms=NDPKA, NM23;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2509941; DOI=10.1038/342177a0;
RA Rosengard A.M., Krutzsch H.C., Shearn A., Biggs J.R., Barker E.,
RA Margulies I.M.K., King C.R., Liotta L.A., Steeg P.S.;
RT "Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila
RT development.";
RL Nature 342:177-180(1989).
RN [2]
RP PROTEIN SEQUENCE (ISOFORM 1), SUBUNIT, AND ACTIVE SITE.
RX PubMed=1851158; DOI=10.1016/s0021-9258(18)31515-1;
RA Gilles A.-M., Presecan E., Vonica A., Lascu I.;
RT "Nucleoside diphosphate kinase from human erythrocytes. Structural
RT characterization of the two polypeptide chains responsible for
RT heterogeneity of the hexameric enzyme.";
RL J. Biol. Chem. 266:8784-8789(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7916650;
RA Wang L., Patel U., Ghosh L., Chen H.C., Banerjee S.;
RT "Mutation in the nm23 gene is associated with metastasis in colorectal
RT cancer.";
RL Cancer Res. 53:717-720(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=8270257; DOI=10.1007/bf00218915;
RA Dooley S., Seib T., Engel M., Theisinger B., Janz H., Piontek K.,
RA Zang K.D., Welter C.;
RT "Isolation and characterization of the human genomic locus coding for the
RT putative metastasis control gene nm23-H1.";
RL Hum. Genet. 93:63-66(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=12601555; DOI=10.1007/s100380300014;
RA Ni X., Gu S., Dai J., Cheng H., Guo L., Li L., Ji C., Xie Y., Ying K.,
RA Mao Y.;
RT "Isolation and characterization of a novel human NM23-H1B gene, a different
RT transcript of NM23-H1.";
RL J. Hum. Genet. 48:96-100(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEIN SEQUENCE OF 7-18; 40-49 AND 89-94 (ISOFORMS 1/2), AND DISCUSSION OF
RP THE ROLE IN TUMOR PROGRESSION.
RC TISSUE=Neuroblastoma;
RX PubMed=2056128; DOI=10.1172/jci115299;
RA Hailat N., Keim D.R., Melhem R.F., Zhu X.X., Eckerskorn C., Brodeur G.M.,
RA Reynolds C.P., Seeger R.C., Lottspeich F., Strahler J.R., Hanash S.J.;
RT "High levels of p19/nm23 protein in neuroblastoma are associated with
RT advanced stage disease and with N-myc gene amplification.";
RL J. Clin. Invest. 88:341-345(1991).
RN [12]
RP PROTEIN SEQUENCE OF 7-26; 40-49; 57-85 AND 89-128 (ISOFORMS 1/2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [13]
RP FUNCTION, AND MUTAGENESIS OF PRO-96; HIS-118 AND SER-120.
RX PubMed=8810265; DOI=10.1074/jbc.271.41.25107;
RA MacDonald N.J., Freije J.M., Stracke M.L., Manrow R.E., Steeg P.S.;
RT "Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120
RT abrogates its motility inhibitory activity upon transfection into human
RT breast carcinoma cells.";
RL J. Biol. Chem. 271:25107-25116(1996).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=10512675; DOI=10.1006/geno.1999.5939;
RA Manda R., Kohno T., Matsuno Y., Takenoshita S., Kuwano H., Yokota J.;
RT "Identification of genes (SPON2 and C20orf2) differentially expressed
RT between cancerous and noncancerous lung cells by mRNA differential
RT display.";
RL Genomics 61:5-14(1999).
RN [15]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH SET, AND IDENTIFICATION IN
RP THE SET COMPLEX.
RX PubMed=12628186; DOI=10.1016/s0092-8674(03)00150-8;
RA Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.;
RT "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-
RT mediated apoptosis, and the nucleosome assembly protein SET is its
RT inhibitor.";
RL Cell 112:659-672(2003).
RN [16]
RP ALTERNATIVE SPLICING (ISOFORM 3), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16442775; DOI=10.1016/j.ygeno.2005.11.004;
RA Valentijn L.J., Koster J., Versteeg R.;
RT "Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene
RT encodes a novel protein, NM23-LV.";
RL Genomics 87:483-489(2006).
RN [17]
RP FUNCTION, INTERACTION WITH TREX1, AND IDENTIFICATION IN THE SET COMPLEX.
RX PubMed=16818237; DOI=10.1016/j.molcel.2006.06.005;
RA Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B.,
RA Perrino F.W., Lieberman J.;
RT "The exonuclease TREX1 is in the SET complex and acts in concert with NM23-
RT H1 to degrade DNA during granzyme A-mediated cell death.";
RL Mol. Cell 23:133-142(2006).
RN [18]
RP INTERACTION WITH PRUNE1.
RX PubMed=17906697; DOI=10.1038/sj.onc.1210822;
RA Garzia L., D'Angelo A., Amoresano A., Knauer S.K., Cirulli C.,
RA Campanella C., Stauber R.H., Steegborn C., Iolascon A., Zollo M.;
RT "Phosphorylation of nm23-H1 by CKI induces its complex formation with h-
RT prune and promotes cell motility.";
RL Oncogene 27:1853-1864(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-122 AND SER-125, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11835509; DOI=10.1002/prot.10038;
RA Min K., Song H.K., Chang C., Kim S.Y., Lee K.J., Suh S.W.;
RT "Crystal structure of human nucleoside diphosphate kinase A, a metastasis
RT suppressor.";
RL Proteins 46:340-342(2002).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND MUTAGENESIS OF PHE-60 AND
RP HIS-118.
RX PubMed=12972261; DOI=10.1016/j.jmb.2003.07.004;
RA Chen Y., Gallois-Montbrun S., Schneider B., Veron M., Morera S.,
RA Deville-Bonne D., Janin J.;
RT "Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of
RT human NDPK-A in complex with ADP and comparison to protein kinases.";
RL J. Mol. Biol. 332:915-926(2003).
RN [25]
RP VARIANT GLY-120.
RX PubMed=8047138; DOI=10.1038/370335a0;
RA Chang C.L., Zhu X.-X., Thoraval D.H., Ungar D., Rawwas J., Hora N.,
RA Strahler J.R., Hanash S.M.;
RT "Nm23-H1 mutation in neuroblastoma.";
RL Nature 370:335-336(1994).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other
CC than ATP. The ATP gamma phosphate is transferred to the NDP beta
CC phosphate via a ping-pong mechanism, using a phosphorylated active-site
CC intermediate. Possesses nucleoside-diphosphate kinase,
CC serine/threonine-specific protein kinase, geranyl and farnesyl
CC pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease
CC activities. Involved in cell proliferation, differentiation and
CC development, signal transduction, G protein-coupled receptor
CC endocytosis, and gene expression. Required for neural development
CC including neural patterning and cell fate determination. During GZMA-
CC mediated cell death, works in concert with TREX1. NME1 nicks one strand
CC of DNA and TREX1 removes bases from the free 3' end to enhance DNA
CC damage and prevent DNA end reannealing and rapid repair.
CC {ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237,
CC ECO:0000269|PubMed:8810265}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Autophosphorylation at His-118 increases
CC serine/threonine protein kinase activity of the enzyme. Interaction
CC with the SET complex inhibits the endonuclease activity.
CC {ECO:0000269|PubMed:12628186}.
CC -!- SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3,
CC A2B4, AB5, B6). Interacts with PRUNE1. Component of the SET complex,
CC composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Within
CC this complex, interacts directly with SET. Also interacts with TREX1,
CC but only following translocation to the nucleus.
CC {ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237,
CC ECO:0000269|PubMed:17906697, ECO:0000269|PubMed:1851158}.
CC -!- INTERACTION:
CC P15531; P51116: FXR2; NbExp=4; IntAct=EBI-741141, EBI-740459;
CC P15531; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-741141, EBI-739832;
CC P15531; P10911: MCF2; NbExp=4; IntAct=EBI-741141, EBI-1914514;
CC P15531; PRO_0000030434 [P10911]: MCF2; NbExp=9; IntAct=EBI-741141, EBI-1915491;
CC P15531; P15531: NME1; NbExp=15; IntAct=EBI-741141, EBI-741141;
CC P15531; P22392: NME2; NbExp=4; IntAct=EBI-741141, EBI-713693;
CC P15531; Q13232: NME3; NbExp=5; IntAct=EBI-741141, EBI-713684;
CC P15531; O00746: NME4; NbExp=11; IntAct=EBI-741141, EBI-744871;
CC P15531; Q96HA8: NTAQ1; NbExp=8; IntAct=EBI-741141, EBI-741158;
CC P15531; P61970: NUTF2; NbExp=3; IntAct=EBI-741141, EBI-591778;
CC P15531; Q7Z2X4: PID1; NbExp=3; IntAct=EBI-741141, EBI-10256685;
CC P15531; O15160: POLR1C; NbExp=11; IntAct=EBI-741141, EBI-1055079;
CC P15531; Q86TP1: PRUNE1; NbExp=2; IntAct=EBI-741141, EBI-2127112;
CC P15531; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-741141, EBI-10268630;
CC P15531; Q9Y3F4: STRAP; NbExp=9; IntAct=EBI-741141, EBI-727414;
CC P15531; O14787: TNPO2; NbExp=3; IntAct=EBI-741141, EBI-431907;
CC P15531; Q9Y5L0: TNPO3; NbExp=3; IntAct=EBI-741141, EBI-1042571;
CC P15531; Q61097: Ksr1; Xeno; NbExp=7; IntAct=EBI-741141, EBI-1536336;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16442775}. Nucleus
CC {ECO:0000269|PubMed:16442775}. Note=Cell-cycle dependent nuclear
CC localization which can be induced by interaction with Epstein-barr
CC viral proteins or by degradation of the SET complex by GzmA.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NM23-H1A;
CC IsoId=P15531-1; Sequence=Displayed;
CC Name=2; Synonyms=NM23-H1B;
CC IsoId=P15531-2; Sequence=VSP_036707;
CC Name=3; Synonyms=NM23-LV;
CC IsoId=P22392-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in heart, brain, placenta,
CC lung, liver, skeletal muscle, pancreas, spleen and thymus. Expressed in
CC lung carcinoma cell lines but not in normal lung tissues. Isoform 2 is
CC ubiquitously expressed and its expression is also related to tumor
CC differentiation. {ECO:0000269|PubMed:10512675,
CC ECO:0000269|PubMed:12601555, ECO:0000269|PubMed:16442775}.
CC -!- MISCELLANEOUS: The role of this protein in tumor development and
CC progression is uncertain. This protein is found in reduced amount in
CC some tumor cells of high metastatic potential. However, increased NME1
CC levels correlate with aggressive tumor features in neuroblastoma. May
CC have distinct if not opposite roles in different tumors.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35621.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X17620; CAA35621.1; ALT_INIT; mRNA.
DR EMBL; X73066; CAA51527.1; -; mRNA.
DR EMBL; X75598; CAA53270.1; -; Genomic_DNA.
DR EMBL; AF487339; AAO85436.1; -; mRNA.
DR EMBL; AK291105; BAF83794.1; -; mRNA.
DR EMBL; CR542104; CAG46901.1; -; mRNA.
DR EMBL; CR542115; CAG46912.1; -; mRNA.
DR EMBL; AC005839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94568.1; -; Genomic_DNA.
DR EMBL; BC000293; AAH00293.1; -; mRNA.
DR EMBL; BC018994; AAH18994.1; -; mRNA.
DR CCDS; CCDS11578.1; -. [P15531-2]
DR CCDS; CCDS11579.1; -. [P15531-1]
DR PIR; A33386; A33386.
DR RefSeq; NP_000260.1; NM_000269.2. [P15531-1]
DR RefSeq; NP_937818.1; NM_198175.1. [P15531-2]
DR PDB; 1JXV; X-ray; 2.20 A; A/B/C/D/E/F=1-152.
DR PDB; 1UCN; X-ray; 2.00 A; A/B/C=1-152.
DR PDB; 2HVD; X-ray; 2.15 A; A/B/C=1-152.
DR PDB; 2HVE; X-ray; 2.40 A; A/B/C=1-152.
DR PDB; 3L7U; X-ray; 2.10 A; A/B/C=1-152.
DR PDB; 4ENO; X-ray; 2.80 A; A/B=1-152.
DR PDB; 5UI4; X-ray; 2.75 A; A/B/C/D/E/F=1-152.
DR PDBsum; 1JXV; -.
DR PDBsum; 1UCN; -.
DR PDBsum; 2HVD; -.
DR PDBsum; 2HVE; -.
DR PDBsum; 3L7U; -.
DR PDBsum; 4ENO; -.
DR PDBsum; 5UI4; -.
DR AlphaFoldDB; P15531; -.
DR SMR; P15531; -.
DR BioGRID; 110894; 161.
DR CORUM; P15531; -.
DR DIP; DIP-39164N; -.
DR IntAct; P15531; 92.
DR MINT; P15531; -.
DR STRING; 9606.ENSP00000337060; -.
DR ChEMBL; CHEMBL2159; -.
DR DrugBank; DB02569; 2',3'-Dehydro-2',3'-Deoxy-Thymidine 5'-Diphosphate.
DR DrugBank; DB04068; 2',3'-dideoxy-3'-fluoro-urididine-5'-diphosphate.
DR DrugBank; DB03491; 2'-Deoxyguanosine-5'-Diphosphate.
DR DrugBank; DB02181; 2'-Deoxyguanosine-5'-Triphosphate.
DR DrugBank; DB04366; 3'-Deoxy 3'-Amino Adenosine-5'-Diphosphate.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB00718; Adefovir dipivoxil.
DR DrugBank; DB00640; Adenosine.
DR DrugBank; DB02607; Adenosine Phosphonoacetic Acid.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01262; Decitabine.
DR DrugBank; DB00441; Gemcitabine.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB00709; Lamivudine.
DR DrugBank; DB02345; Selenocysteine.
DR DrugBank; DB08934; Sofosbuvir.
DR DrugBank; DB02887; Stavudine triphosphate.
DR DrugBank; DB14126; Tenofovir.
DR DrugBank; DB09299; Tenofovir alafenamide.
DR DrugBank; DB00300; Tenofovir disoproxil.
DR DrugBank; DB03103; Thymidine-5'- Diphosphate.
DR DrugBank; DB04542; Zidovudine diphosphate.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR iPTMnet; P15531; -.
DR MetOSite; P15531; -.
DR PhosphoSitePlus; P15531; -.
DR SwissPalm; P15531; -.
DR BioMuta; NME1; -.
DR DMDM; 127981; -.
DR DOSAC-COBS-2DPAGE; P15531; -.
DR OGP; P15531; -.
DR EPD; P15531; -.
DR jPOST; P15531; -.
DR MassIVE; P15531; -.
DR MaxQB; P15531; -.
DR PaxDb; P15531; -.
DR PeptideAtlas; P15531; -.
DR PRIDE; P15531; -.
DR ProteomicsDB; 53183; -. [P15531-1]
DR ProteomicsDB; 53184; -. [P15531-2]
DR TopDownProteomics; P15531-1; -. [P15531-1]
DR Antibodypedia; 35046; 1422 antibodies from 43 providers.
DR CPTC; P15531; 4 antibodies.
DR DNASU; 4830; -.
DR Ensembl; ENST00000013034.3; ENSP00000013034.3; ENSG00000239672.8. [P15531-2]
DR Ensembl; ENST00000336097.7; ENSP00000337060.3; ENSG00000239672.8. [P15531-2]
DR Ensembl; ENST00000393196.8; ENSP00000376892.3; ENSG00000239672.8. [P15531-1]
DR GeneID; 4830; -.
DR KEGG; hsa:4830; -.
DR MANE-Select; ENST00000393196.8; ENSP00000376892.3; NM_000269.3; NP_000260.1.
DR UCSC; uc002ith.3; human. [P15531-1]
DR CTD; 4830; -.
DR DisGeNET; 4830; -.
DR GeneCards; NME1; -.
DR HGNC; HGNC:7849; NME1.
DR HPA; ENSG00000239672; Low tissue specificity.
DR MIM; 156490; gene.
DR neXtProt; NX_P15531; -.
DR OpenTargets; ENSG00000239672; -.
DR PharmGKB; PA249; -.
DR VEuPathDB; HostDB:ENSG00000239672; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000162213; -.
DR InParanoid; P15531; -.
DR PhylomeDB; P15531; -.
DR TreeFam; TF106373; -.
DR BioCyc; MetaCyc:ENSG00000011052-MON; -.
DR BRENDA; 2.7.13.3; 2681.
DR BRENDA; 2.7.4.6; 2681.
DR PathwayCommons; P15531; -.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-HSA-9748787; Azathioprine ADME.
DR SignaLink; P15531; -.
DR SIGNOR; P15531; -.
DR BioGRID-ORCS; 4830; 11 hits in 1051 CRISPR screens.
DR EvolutionaryTrace; P15531; -.
DR GeneWiki; NME1; -.
DR GenomeRNAi; 4830; -.
DR Pharos; P15531; Tbio.
DR PRO; PR:P15531; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P15531; protein.
DR Bgee; ENSG00000239672; Expressed in cortical plate and 111 other tissues.
DR ExpressionAtlas; P15531; baseline and differential.
DR Genevisible; P15531; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004536; F:deoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0043024; F:ribosomal small subunit binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:HGNC-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.141; -; 1.
DR HAMAP; MF_00451; NDP_kinase; 1.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00562; NDK; 1.
DR SUPFAM; SSF54919; SSF54919; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm;
KW Differentiation; Direct protein sequencing; Endocytosis; Isopeptide bond;
KW Kinase; Magnesium; Metal-binding; Neurogenesis; Nucleotide metabolism;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation.
FT CHAIN 1..152
FT /note="Nucleoside diphosphate kinase A"
FT /id="PRO_0000137114"
FT ACT_SITE 118
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:1851158"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 100
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT VAR_SEQ 1
FT /note="M -> MVLLSTLGIVFQGEGPPISSCDTGTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12601555"
FT /id="VSP_036707"
FT VARIANT 120
FT /note="S -> G (in a neuroblastoma sample; increased
FT motility of carcinoma cells; dbSNP:rs121917887)"
FT /evidence="ECO:0000269|PubMed:8047138"
FT /id="VAR_004625"
FT MUTAGEN 60
FT /note="F->W: No loss of activity or substrate binding."
FT /evidence="ECO:0000269|PubMed:12972261"
FT MUTAGEN 96
FT /note="P->S: Increased motility of carcinoma cells."
FT /evidence="ECO:0000269|PubMed:8810265"
FT MUTAGEN 118
FT /note="H->F: Loss of serine/threonine kinase activity. Some
FT loss of motility of carcinoma cells."
FT /evidence="ECO:0000269|PubMed:12972261,
FT ECO:0000269|PubMed:8810265"
FT MUTAGEN 118
FT /note="H->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12972261,
FT ECO:0000269|PubMed:8810265"
FT MUTAGEN 120
FT /note="S->A: Limited increase in motility of carcinoma
FT cells."
FT /evidence="ECO:0000269|PubMed:8810265"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:3L7U"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:1UCN"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1UCN"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4ENO"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:1UCN"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1UCN"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1UCN"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1UCN"
SQ SEQUENCE 152 AA; 17149 MW; AAE9C0DF63CB70A1 CRC64;
MANCERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF MQASEDLLKE HYVDLKDRPF
FAGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVESAEKEI GLWFHPEELV DYTSCAQNWI YE
