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 02-SEP-2026, entry version 259. DE RecName: Full=Nucleoside diphosphate kinase A {ECO:0000303|PubMed:16944299}; DE Short=NDP kinase A {ECO:0000303|PubMed:1851158}; DE Short=NDPK A {ECO:0000303|PubMed:1851158}; DE EC=2.7.4.6 {ECO:0000269|PubMed:10952986, ECO:0000269|PubMed:14960567, ECO:0000269|PubMed:16313181, ECO:0000269|PubMed:1851158, ECO:0000269|PubMed:23519676, ECO:0000269|PubMed:33903070, ECO:0000269|PubMed:8810265, ECO:0000269|PubMed:9038158}; DE AltName: Full=Farnesyl diphosphate kinase NME1 {ECO:0000305|PubMed:10952986}; DE EC=2.7.4.18 {ECO:0000269|PubMed:10952986}; DE AltName: Full=Histidine protein kinase NME1 {ECO:0000305|PubMed:9038158}; DE EC=2.7.13.3 {ECO:0000269|PubMed:9038158}; DE AltName: Full=Metastasis inhibition factor nm23; DE AltName: Full=NM23-H1 {ECO:0000303|PubMed:8270257}; DE AltName: Full=Non-specific serine/threonine protein kinase NME1 {ECO:0000305|PubMed:8529641}; DE EC=2.7.11.1 {ECO:0000269|PubMed:8529641}; DE AltName: Full=Nucleoside diphoshate kinase 1 {ECO:0000303|PubMed:16313181}; DE Short=NDK1 {ECO:0000303|PubMed:16313181}; DE AltName: Full=Putative 3'-5'-DNA exonuclease NDK1 {ECO:0000305|PubMed:14960567}; DE EC=3.1.11.- {ECO:0000269|PubMed:14960567, ECO:0000269|PubMed:16313181}; DE AltName: Full=Putative granzyme A-activated DNA endonuclease {ECO:0000305|PubMed:12628186}; DE Short=GAAD {ECO:0000303|PubMed:12628186}; DE EC=3.1.24.- {ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237}; DE AltName: Full=Tumor metastatic process-associated protein; GN Name=NME1 {ECO:0000312|HGNC:HGNC:7849}; GN Synonyms=NDPKA, NM23 {ECO:0000303|PubMed:2509941}; 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), AND SUBCELLULAR LOCATION. 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), FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, 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, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND ACTIVE SITE. RX PubMed=8529641; DOI=10.1111/j.1432-1033.1995.200_c.x; RA Engel M., Veron M., Theisinger B., Lacombe M.L., Seib T., Dooley S., RA Welter C.; RT "A novel serine/threonine-specific protein phosphotransferase activity of RT Nm23/nucleoside-diphosphate kinase."; RL Eur. J. Biochem. 234:200-207(1995). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PRO-96; HIS-118 AND SER-120, RP AND ACTIVE SITE. 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 [15] RP FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT GLY-120, AND RP MUTAGENESIS OF SER-44; PRO-96; HIS-118 AND SER-120. RX PubMed=9038158; DOI=10.1074/jbc.272.9.5525; RA Freije J.M., Blay P., MacDonald N.J., Manrow R.E., Steeg P.S.; RT "Site-directed mutation of Nm23-H1. Mutations lacking motility suppressive RT capacity upon transfection are deficient in histidine-dependent protein RT phosphotransferase pathways in vitro."; RL J. Biol. Chem. 272:5525-5532(1997). RN [16] 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 [17] RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PRO-96 AND HIS-118, AND RP CHARACTERIZATION OF VARIANT GLY-120. RX PubMed=10952986; DOI=10.1074/jbc.m006106200; RA Wagner P.D., Vu N.D.; RT "Phosphorylation of geranyl and farnesyl pyrophosphates by Nm23 RT proteins/nucleoside diphosphate kinases."; RL J. Biol. Chem. 275:35570-35576(2000). RN [18] RP FUNCTION. RX PubMed=11694515; DOI=10.1074/jbc.m108359200; RA Ma D., Xing Z., Liu B., Pedigo N.G., Zimmer S.G., Bai Z., Postel E.H., RA Kaetzel D.M.; RT "NM23-H1 and NM23-H2 repress transcriptional activities of nuclease- RT hypersensitive elements in the platelet-derived growth factor-A promoter."; RL J. Biol. Chem. 277:1560-1567(2002). RN [19] RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH SET, RP AND IDENTIFICATION IN 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 [20] RP FUNCTION, COFACTOR, AND MUTAGENESIS OF LYS-12; ARG-34 AND HIS-118. RX PubMed=14960567; DOI=10.1074/jbc.m400185200; RA Ma D., McCorkle J.R., Kaetzel D.M.; RT "The metastasis suppressor NM23-H1 possesses 3'-5' exonuclease activity."; RL J. Biol. Chem. 279:18073-18084(2004). RN [21] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-5; LYS-12; PHE-33; RP ASP-54; HIS-118; ASP-121 AND GLU-129. RX PubMed=16313181; DOI=10.1021/bi0515974; RA Yoon J.H., Singh P., Lee D.H., Qiu J., Cai S., O'Connor T.R., Chen Y., RA Shen B., Pfeifer G.P.; RT "Characterization of the 3' --> 5' exonuclease activity found in human RT nucleoside diphosphate kinase 1 (NDK1) and several of its homologues."; RL Biochemistry 44:15774-15786(2005). RN [22] 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 [23] 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 [24] 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 [25] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, IDENTIFICATION RP BY MASS SPECTROMETRY, INTERACTION WITH TXNRD1, GLUTATHIONYLATION AT RP CYS-109, OXIDATION AT CYS-109, DISULFIDE BOND, AND MUTAGENESIS OF CYS-109 RP AND HIS-118. RX PubMed=19956735; DOI=10.1371/journal.pone.0007949; RA Lee E., Jeong J., Kim S.E., Song E.J., Kang S.W., Lee K.J.; RT "Multiple functions of Nm23-H1 are regulated by oxido-reduction system."; RL PLoS ONE 4:e7949-e7949(2009). RN [26] 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 [27] 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 [28] 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 [29] 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 [30] RP FUNCTION, UBIQUITINATION AT LYS-85, MUTAGENESIS OF LYS-56 AND LYS-85, RP ACETYLATION AT LYS-56, AND INTERACTION WITH FBXO24. RX PubMed=25582197; DOI=10.1128/mcb.01185-14; RA Chen W., Xiong S., Li J., Li X., Liu Y., Zou C., Mallampalli R.K.; RT "The ubiquitin E3 ligase SCF-FBXO24 recognizes deacetylated nucleoside RT diphosphate kinase A to enhance its degradation."; RL Mol. Cell. Biol. 35:1001-1013(2015). RN [31] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COALATION AT CYS-109, RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-109. RX PubMed=33903070; DOI=10.1016/j.redox.2021.101978; RA Yu B.Y.K., Tossounian M.A., Hristov S.D., Lawrence R., Arora P., RA Tsuchiya Y., Peak-Chew S.Y., Filonenko V., Oxenford S., Angell R., RA Gouge J., Skehel M., Gout I.; RT "Regulation of metastasis suppressor NME1 by a key metabolic cofactor RT coenzyme A."; RL Redox Biol. 44:101978-101978(2021). RN [32] {ECO:0007744|PDB:1JXV} RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT. 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 [33] {ECO:0007744|PDB:1UCN} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS TRP-60 AND GLY-118 IN RP COMPLEX WITH ADP AND CA(2+), COFACTOR, 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 [34] {ECO:0007744|PDB:2HVD, ECO:0007744|PDB:2HVE} RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF WILD TYPE AND MUTANT GLY-120 IN RP COMPLEX WITH ADP. RX PubMed=16944299; DOI=10.1007/s10863-006-9043-0; RA Giraud M.F., Georgescauld F., Lascu I., Dautant A.; RT "Crystal structures of S120G mutant and wild type of human nucleoside RT diphosphate kinase A in complex with ADP."; RL J. Bioenerg. Biomembr. 38:261-264(2006). RN [35] {ECO:0007744|PDB:4ENO} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF OXIDIZED FORM, FUNCTION, RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, IDENTIFICATION BY MASS RP SPECTROMETRY, MUTAGENESIS OF CYS-4; CYS-109 AND CYS-145, OXIDATION AT RP CYS-109, DISULFIDE BOND, AND SUBUNIT. RX PubMed=23519676; DOI=10.1107/s0907444913001194; RA Kim M.S., Jeong J., Jeong J., Shin D.H., Lee K.J.; RT "Structure of Nm23-H1 under oxidative conditions."; RL Acta Crystallogr. D 69:669-680(2013). RN [36] {ECO:0007744|PDB:8OOV} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH COENZYME A, SUBUNIT, RP AND MUTAGENESIS OF ARG-58 AND THR-94. RX PubMed=37298313; DOI=10.3390/ijms24119359; RA Tossounian M.A., Hristov S.D., Semelak J.A., Yu B.Y.K., Baczynska M., RA Zhao Y., Estrin D.A., Trujillo M., Filonenko V., Gouge J., Gout I.; RT "A Unique Mode of Coenzyme A Binding to the Nucleotide Binding Pocket of RT Human Metastasis Suppressor NME1."; RL Int. J. Mol. Sci. 24:9359-9359(2023). RN [37] 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: Catalyzes the transfer of a gamma-phosphoryl group from a CC nucleoside triphosphate, mainly ATP, to a nucleoside diphosphate via a CC ping-pong mechanism involving a phosphohistidine intermediate, CC therefore contributing to the nucleoside triphosphate homeostasis CC (PubMed:10952986, PubMed:14960567, PubMed:16313181, PubMed:1851158, CC PubMed:23519676, PubMed:33903070, PubMed:8810265, PubMed:9038158). Also CC phosphorylates geranyl pyrophosphate (GPP) and farnesyl pyrophosphate CC (FPP), linking it to isoprenoid metabolism (PubMed:10952986). CC Additionally, functions as a non-specific serine/threonine kinase and CC histidine protein kinase, transferring phosphoryl groups from its CC active site to target proteins (PubMed:8529641, PubMed:9038158). May CC function as a Mg(2+)-dependent single-stranded DNA endonuclease as part CC of the SET complex, cooperating with the 3'-5' exonuclease TREX1 to CC mediate apoptotic DNA fragmentation in cytotoxic T lymphocytes CC (PubMed:12628186, PubMed:16818237). Reported to nick one DNA strand, CC enabling TREX1 to remove nucleotides from the free 3' end, enhancing CC DNA damage and suppressing DNA end reannealing and repair CC (PubMed:16818237). Has been shown to cleave double strands DNA within CC the 3'-portions of both 5'-SHS silencer and NHE basal promoter element CC of the PDGFA gene, potentially repressing its transcription CC (PubMed:11694515). May also function as a Mg(2+)-dependent 3'-5' DNA CC exonuclease, excising nucleotides from 3' single-stranded DNA or DNA CC with 3' single strand overhangs, suggesting a role in DNA nucleolytic CC processing (PubMed:14960567, PubMed:16313181). Involved in the CC regulation of tumor metastasis and cellular differentiation (By CC similarity). Also required for cell motility (PubMed:8270257, CC PubMed:25582197). May control, with NME2, AcCoA usage between histone CC acetylation and fatty acid synthesis, possibly by binding and releasing CC AcCoA at transcriptionally active chromatin regions in proximity to CC histone acetyltransferase (HAT) (By similarity). CC {ECO:0000250|UniProtKB:P15532, ECO:0000269|PubMed:10952986, CC ECO:0000269|PubMed:11694515, ECO:0000269|PubMed:12628186, CC ECO:0000269|PubMed:14960567, ECO:0000269|PubMed:16313181, CC ECO:0000269|PubMed:16818237, ECO:0000269|PubMed:1851158, CC ECO:0000269|PubMed:23519676, ECO:0000269|PubMed:25582197, CC ECO:0000269|PubMed:33903070, ECO:0000269|PubMed:8270257, CC ECO:0000269|PubMed:8529641, ECO:0000269|PubMed:8810265, CC ECO:0000269|PubMed:9038158}. 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 Evidence={ECO:0000269|PubMed:14960567, ECO:0000269|PubMed:16313181, CC ECO:0000269|PubMed:33903070}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44641; CC Evidence={ECO:0000269|PubMed:14960567, ECO:0000269|PubMed:16313181, CC ECO:0000269|PubMed:33903070}; 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 Evidence={ECO:0000269|PubMed:10952986, ECO:0000269|PubMed:14960567, CC ECO:0000269|PubMed:16313181, ECO:0000269|PubMed:1851158, CC ECO:0000269|PubMed:23519676, ECO:0000269|PubMed:8810265, CC ECO:0000269|PubMed:9038158}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18114; CC Evidence={ECO:0000269|PubMed:10952986, ECO:0000269|PubMed:14960567, CC ECO:0000269|PubMed:16313181, ECO:0000269|PubMed:1851158, CC ECO:0000269|PubMed:23519676, ECO:0000269|PubMed:8810265, CC ECO:0000269|PubMed:9038158}; CC -!- CATALYTIC ACTIVITY: CC Reaction=IDP + ATP = ITP + ADP; Xref=Rhea:RHEA:30347, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58280, ChEBI:CHEBI:61402, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:1851158}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30348; CC Evidence={ECO:0000269|PubMed:1851158}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GDP + ATP = GTP + ADP; Xref=Rhea:RHEA:27686, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000269|PubMed:8810265, CC ECO:0000269|PubMed:9038158}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27687; CC Evidence={ECO:0000269|PubMed:8810265, ECO:0000269|PubMed:9038158}; CC -!- CATALYTIC ACTIVITY: CC Reaction=UDP + ATP = UTP + ADP; Xref=Rhea:RHEA:25098, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:19956735, ECO:0000269|PubMed:23519676}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25099; CC Evidence={ECO:0000269|PubMed:19956735, ECO:0000269|PubMed:33903070}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP + ATP = ADP + ATP; Xref=Rhea:RHEA:84315, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q05982}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84316; CC Evidence={ECO:0000250|UniProtKB:Q05982}; CC -!- CATALYTIC ACTIVITY: CC Reaction=CDP + ATP = CTP + ADP; Xref=Rhea:RHEA:25237, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:58069, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000250|UniProtKB:P52175}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25238; CC Evidence={ECO:0000250|UniProtKB:P52175}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dTDP + ATP = dTTP + ADP; Xref=Rhea:RHEA:27682, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:14960567, ECO:0000269|PubMed:16313181}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27683; CC Evidence={ECO:0000269|PubMed:14960567, ECO:0000269|PubMed:16313181}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dCDP + ATP = dCTP + ADP; Xref=Rhea:RHEA:27678, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58593, ChEBI:CHEBI:61481, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:33903070}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27679; CC Evidence={ECO:0000269|PubMed:33903070}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + ATP = (2E,6E)-farnesyl CC triphosphate + ADP; Xref=Rhea:RHEA:21544, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61563, ChEBI:CHEBI:175763, ChEBI:CHEBI:456216; CC EC=2.7.4.18; Evidence={ECO:0000269|PubMed:10952986}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21545; CC Evidence={ECO:0000269|PubMed:10952986}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-geranyl diphosphate + ATP = (2E)-geranyl triphosphate + CC ADP; Xref=Rhea:RHEA:84295, ChEBI:CHEBI:30616, ChEBI:CHEBI:58057, CC ChEBI:CHEBI:233664, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:10952986}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84296; CC Evidence={ECO:0000269|PubMed:10952986}; CC -!- CATALYTIC ACTIVITY: CC Reaction=geranylgeranyl diphosphate + ATP = geranylgeranyl triphosphate CC + ADP; Xref=Rhea:RHEA:84299, ChEBI:CHEBI:30616, ChEBI:CHEBI:57533, CC ChEBI:CHEBI:233665, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:10952986}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84300; CC Evidence={ECO:0000269|PubMed:10952986}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:8529641}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000269|PubMed:8529641}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:8529641}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000269|PubMed:8529641}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:9038158}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12972261, ECO:0000269|PubMed:14960567, CC ECO:0000269|Ref.7}; CC -!- ACTIVITY REGULATION: Autophosphorylation at His-118 increases CC nucleoside diphosphate kinase activity and serine/threonine protein CC kinase activity (Probable) (PubMed:1851158, PubMed:8810265). Under CC cellular stress conditions, nucleoside diphosphate kinase activity is CC inhibited through both covalent and non-covalent binding by CoenzymeA CC (CoA); a non-covalent binding of coenzyme A (CoA) via its ADP moiety to CC the nucleotide-binding pocket of NME1 and a covalent binding of CoA CC through CoAlation (disulfide linkage to cysteine) at Cys-109 CC (PubMed:33903070). Nucleoside diphosphate kinase activity is regulated CC by oxido-reduction system coupled to its oligomeric state; disulfide CC bond formation, glutathionylation and oxidation at Cys-109 inhibit the CC nucleoside diphosphate kinase activity; intra- and specific inter- CC disulfide bonds are reduced through the NADPH-TXNRD1-TXN system thus CC activating nucleoside diphosphate kinase activity (PubMed:19956735, CC PubMed:23519676). Interaction with the SET complex inhibits the DNA CC endonuclease activity (PubMed:12628186). 3'-5'-DNA exonuclease activity CC is inhibited by potassium chloride (KCL), with the optimal KCl CC concentration less than or equal to 20 mM and ATP (PubMed:14960567). CC {ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:14960567, CC ECO:0000269|PubMed:1851158, ECO:0000269|PubMed:19956735, CC ECO:0000269|PubMed:23519676, ECO:0000269|PubMed:33903070, CC ECO:0000269|PubMed:8810265, ECO:0000305|PubMed:8529641}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=33 uM for IDP {ECO:0000269|PubMed:1851158}; CC -!- SUBUNIT: Homohexamer (PubMed:11835509, PubMed:1851158). Homodimer; CC disulfide-linked; under oxidative stress, the hexameric form is CC dissociated into dimers (PubMed:19956735, PubMed:23519676). Homotrimer CC (PubMed:37298313). Heterohexamer of two different chains: A/NME1 and CC B/NME2 resulting in different ratios of the respective subunits (A5B or CC A4B2 or A3B3 or A2B4 or AB5) (PubMed:1851158). Interacts (hexameric CC form) with PRUNE1: this interaction requires phosphorylation of NME1 CC (PubMed:17906697). Component of the SET complex, composed of at least CC ANP32A, APEX1, HMGB2, NME1, SET and TREX1 (PubMed:12628186, CC PubMed:16818237). Interacts directly with SET; this interaction CC inhibits single-stranded DNA endonuclease activity of NME1 and this CC inhibition is released by GZMA cleavage of SET (PubMed:12628186). CC Interacts with TREX1; this interaction is initiated only following CC translocation to the nucleus (PubMed:16818237). NDP kinase isoenzymes CC result from random association of two different kinds of polypeptides CC (PubMed:1851158). Interacts (oxidized form) with TXNRD1; this CC interaction is probably indirect and TXN is necessary for reduction of CC oxidized form through the NADPH-TXNRD1-TXN system (PubMed:19956735). CC Interacts with FBXO24 (PubMed:25582197). {ECO:0000269|PubMed:11835509, CC ECO:0000269|PubMed:12628186, ECO:0000269|PubMed:16818237, CC ECO:0000269|PubMed:17906697, ECO:0000269|PubMed:1851158, CC ECO:0000269|PubMed:19956735, ECO:0000269|PubMed:23519676, CC ECO:0000269|PubMed:25582197, ECO:0000269|PubMed:37298313}. 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=7; IntAct=EBI-741141, EBI-713693; CC P15531; Q13232: NME3; NbExp=7; IntAct=EBI-741141, EBI-713684; CC P15531; O00746: NME4; NbExp=12; 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:12628186, CC ECO:0000269|PubMed:16313181, ECO:0000269|PubMed:16442775, CC ECO:0000269|PubMed:2509941}. Nucleus {ECO:0000269|PubMed:12628186, CC ECO:0000269|PubMed:16313181, ECO:0000269|PubMed:16442775, CC ECO:0000269|PubMed:2509941}. Cell membrane CC {ECO:0000250|UniProtKB:P52175}. Note=Cell-cycle dependent nuclear CC localization which can be induced by degradation of the SET complex by CC GzmA (PubMed:12628186). In response to DNA damage, translocates to the CC nucleus where it might participate in DNA nucleolytic processing CC (PubMed:16313181). {ECO:0000269|PubMed:12628186, CC ECO:0000269|PubMed:16313181}. 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 {ECO:0000303|PubMed:16442775}; CC IsoId=P22392-2; Sequence=External; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:12601555, CC PubMed:16442775). Expressed in tumor cell lines (PubMed:10512675, CC PubMed:16442775). {ECO:0000269|PubMed:10512675, CC ECO:0000269|PubMed:12601555, ECO:0000269|PubMed:16442775}. CC -!- PTM: Autophosphorylated at His-118 results in the formation of a CC phospho-enzyme intermediate and consequently activation of nucleoside CC diphosphate kinase activity and serine/threonine protein kinase CC activity. {ECO:0000269|PubMed:1851158, ECO:0000269|PubMed:8810265, CC ECO:0000305|PubMed:8529641}. CC -!- PTM: Cys-109 is oxidized to various oxidation states including CC intra- and inter-disulfide cross-links, glutathionylation and sulfonic CC acid formation in response to oxidative stress (PubMed:19956735). CC Glutathionylation and sulfonic acid formation lead to the loss of CC nucleoside diphosphate activity (PubMed:19956735). Glutathionylation, CC and sulfonic acid formation are dependent of dimeric state and CC intramolecular disulfide bond formation between Cys-4 and Cys-145 CC (PubMed:23519676). {ECO:0000269|PubMed:19956735, CC ECO:0000269|PubMed:23519676}. CC -!- PTM: The intramolecular disulfide bond between Cys-4 and Cys-145 is CC formed under oxidative stress and triggers a large conformational CC change that destabilizes and dissociates the hexamer into dimers thus CC creating a suitable environment for the oxidation of Cys-109 to CC sulfonic acid and glutathionylation. {ECO:0000269|PubMed:19956735, CC ECO:0000269|PubMed:23519676}. CC -!- PTM: An intra-disulfide cross-link can be reduced through the NADPH- CC TXNRD1-TXN system resulting into a fully activated hexamer; this system CC reduces the Cys-4-Cys-145 intra-disulfide bond to free sulfhydryls by CC interacting with the redox-active center of TXN that can be CC sequentially reduced by TXNRD1 and NADPH. CC {ECO:0000269|PubMed:19956735}. CC -!- PTM: CoAlation at Cys-109, in response to oxidative stress, negatively CC regulates the nucleoside diphosphate kinase activity. CC {ECO:0000269|PubMed:33903070}. CC -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:P52175}. CC -!- PTM: Acetylated by GCN5, which prevents recognition by the SCF-FBXO24 CC E3 ubiquitin ligase, thereby protecting the protein from ubiquitination CC and proteasomal degradation. {ECO:0000269|PubMed:25582197}. CC -!- PTM: Ubiquitinated by the SCF-FBXO24 E3 ubiquitin ligase, leading to CC proteasomal degradation. {ECO:0000269|PubMed:25582197}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_000269.3. [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 PDB; 8OOV; X-ray; 1.70 A; A/B/C=1-152. DR PDB; 9GD6; EM; 2.80 A; A/B/C/D/E/F=1-152. DR PDB; 9GD8; EM; 3.30 A; A/B/C/D/E/F=1-152. DR PDB; 9GD9; EM; 3.80 A; A/B/C/D/E/F=1-143. DR AlphaFoldDB; P15531; -. DR EMDB; EMD-51248; -. DR EMDB; EMD-51250; -. DR EMDB; EMD-51251; -. DR MDposit; P15531; -. DR MDRepo; P15531; -. DR SMR; P15531; -. DR BioGRID; 110894; 218. DR ComplexPortal; CPX-26715; SET complex. DR CORUM; P15531; -. DR DIP; DIP-39164N; -. DR FunCoup; P15531; 1706. DR IntAct; P15531; 105. DR MINT; P15531; -. DR NDEx; IQUERY-CP-NME1; 8 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000337060; -. DR BindingDB; P15531; -. 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 GlyGen; P15531; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P15531; -. DR MetOSite; P15531; -. DR PhosphoSitePlus; P15531; -. DR SwissPalm; P15531; -. DR BioMuta; NME1; -. DR DMDM; 127981; -. DR OGP; P15531; -. DR jPOST; P15531; -. DR MassIVE; P15531; -. DR PaxDb; 9606-ENSP00000337060; -. DR PeptideAtlas; P15531; -. DR ProteomicsDB; 53183; -. [P15531-1] DR ProteomicsDB; 53184; -. [P15531-2] DR Pumba; P15531; -. DR TopDownProteomics; P15531-1; -. [P15531-1] DR Antibodypedia; 35046; 1496 antibodies from 46 providers. DR CPTC; P15531; 4 antibodies. DR DNASU; 4830; -. DR Ensembl; ENST00000013034.3; ENSP00000013034.3; ENSG00000239672.9. [P15531-2] DR Ensembl; ENST00000336097.7; ENSP00000337060.3; ENSG00000239672.9. [P15531-2] DR Ensembl; ENST00000393196.8; ENSP00000376892.3; ENSG00000239672.9. [P15531-1] DR Ensembl; ENST00000880221.1; ENSP00000550280.1; ENSG00000239672.9. [P15531-1] DR Ensembl; ENST00000880222.1; ENSP00000550281.1; ENSG00000239672.9. [P15531-1] DR Ensembl; ENST00000911790.1; ENSP00000581849.1; ENSG00000239672.9. [P15531-1] DR Ensembl; ENST00000911792.1; ENSP00000581851.1; ENSG00000239672.9. [P15531-1] DR Ensembl; ENST00000911797.1; ENSP00000581856.1; ENSG00000239672.9. [P15531-1] DR Ensembl; ENST00000911798.1; ENSP00000581857.1; ENSG00000239672.9. [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 AGR; HGNC:7849; -. DR ClinPGx; PA249; -. DR CTD; 4830; -. DR DisGeNET; 4830; -. DR GeneCards; NME1; -. DR HGNC; HGNC:7849; NME1. DR HPA; ENSG00000239672; Low tissue specificity. DR MalaCards; NME1; -. DR MIM; 156490; gene. DR OpenTargets; ENSG00000239672; -. DR VEuPathDB; HostDB:ENSG00000239672; -. DR eggNOG; KOG0888; Eukaryota. DR GeneTree; ENSGT00940000162213; -. DR InParanoid; P15531; -. DR OrthoDB; 2162449at2759; -. DR PAN-GO; P15531; 1 GO annotation based on evolutionary models. DR PhylomeDB; P15531; -. DR BioCyc; MetaCyc:ENSG00000011052-MONOMER; -. 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 Reactome; R-HSA-9755088; Ribavirin ADME. DR SignaLink; P15531; -. DR SIGNOR; P15531; -. DR Agora; ENSG00000239672; -. DR BioGRID-ORCS; 4830; 12 hits in 1131 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. 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 113 other cell types or tissues. DR ExpressionAtlas; P15531; baseline and differential. DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; NAS:ComplexPortal. 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:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB. DR GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IDA:UniProtKB. DR GO; GO:1905502; F:acetyl-CoA binding; ISS:UniProtKB. DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB. DR GO; GO:0120225; F:coenzyme A binding; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0004520; F:DNA endonuclease activity; IDA:UniProtKB. DR GO; GO:0004536; F:DNA nuclease activity; IDA:UniProtKB. DR GO; GO:0047887; F:farnesyl diphosphate kinase activity; IDA:UniProtKB. DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB. DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IDA:UniProtKB. DR GO; GO:0004673; F:protein histidine kinase activity; EXP:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; EXP:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0043024; F:ribosomal small subunit binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0120226; F:succinyl-CoA binding; ISS:UniProtKB. DR GO; GO:0046356; P:acetyl-CoA catabolic process; ISS:UniProtKB. DR GO; GO:0006309; P:apoptotic DNA fragmentation; IDA:UniProtKB. DR GO; GO:0006284; P:base-excision repair; NAS:ComplexPortal. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro. DR GO; GO:0006308; P:DNA catabolic process; IDA:UniProtKB. DR GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; NAS:ComplexPortal. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro. DR GO; GO:0006720; P:isoprenoid metabolic process; IDA:UniProtKB. DR GO; GO:0046042; P:ITP biosynthetic process; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:UniProtKB. DR GO; GO:0009132; P:nucleoside diphosphate metabolic process; IDA:UniProtKB. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IDA:UniProtKB. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:HGNC-UCL. DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB. DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; ISS:UniProtKB. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro. DR CDD; cd04413; NDPk_I; 1. DR FunFam; 3.30.70.141:FF:000039; Nucleoside diphosphate kinase B; 1. DR Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 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 NCBIfam; NF001908; PRK00668.1; 1. DR PANTHER; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1. DR Pfam; PF00334; NDK; 1. DR PRINTS; PR01243; NUCDPKINASE. DR SMART; SM00562; NDK; 1. DR SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1. DR PROSITE; PS00469; NDPK; 1. DR PROSITE; PS51374; NDPK_LIKE; 1. DR PDBsum; 1JXV; -. DR PDBsum; 1UCN; -. DR PDBsum; 2HVD; -. DR PDBsum; 2HVE; -. DR PDBsum; 3L7U; -. DR PDBsum; 4ENO; -. DR PDBsum; 5UI4; -. DR PDBsum; 8OOV; -. DR PDBsum; 9GD6; -. DR PDBsum; 9GD8; -. DR PDBsum; 9GD9; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Cell membrane; Cytoplasm; Differentiation; Direct protein sequencing; KW Disulfide bond; Endocytosis; Glutathionylation; Hydrolase; Isopeptide bond; KW Kinase; Magnesium; Membrane; Metal-binding; Neurogenesis; KW Nucleotide metabolism; Nucleotide-binding; Nucleus; Oxidation; KW Phosphoprotein; Proteomics identification; Reference proteome; Transferase; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P52175" FT CHAIN 2..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 ECO:0000269|PubMed:8810265, ECO:0000305|PubMed:8529641" FT BINDING 12 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /ligand_note="competitive inhibitor" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 12 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:12972261, FT ECO:0000269|PubMed:16944299, ECO:0007744|PDB:1UCN, FT ECO:0007744|PDB:2HVD, ECO:0007744|PDB:2HVE" FT BINDING 12 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:37298313, FT ECO:0007744|PDB:8OOV" FT BINDING 12 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 12 FT /ligand="succinyl-CoA" FT /ligand_id="ChEBI:CHEBI:57292" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 52 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /ligand_note="competitive inhibitor" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 52 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 52 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:37298313, FT ECO:0007744|PDB:8OOV" FT BINDING 52 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 52 FT /ligand="succinyl-CoA" FT /ligand_id="ChEBI:CHEBI:57292" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 58 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:37298313, FT ECO:0007744|PDB:8OOV" FT BINDING 58 FT /ligand="succinyl-CoA" FT /ligand_id="ChEBI:CHEBI:57292" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 88 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:12972261, FT ECO:0000269|PubMed:16944299, ECO:0007744|PDB:1UCN, FT ECO:0007744|PDB:2HVD, ECO:0007744|PDB:2HVE" FT BINDING 88 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:37298313, FT ECO:0007744|PDB:8OOV" FT BINDING 88 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 88 FT /ligand="succinyl-CoA" FT /ligand_id="ChEBI:CHEBI:57292" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 94 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:12972261, FT ECO:0000269|PubMed:16944299, ECO:0007744|PDB:1UCN, FT ECO:0007744|PDB:2HVD, ECO:0007744|PDB:2HVE" FT BINDING 94 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:37298313, FT ECO:0007744|PDB:8OOV" FT BINDING 94 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 94 FT /ligand="succinyl-CoA" FT /ligand_id="ChEBI:CHEBI:57292" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 105 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:12972261, FT ECO:0007744|PDB:1UCN" FT BINDING 105 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 105 FT /ligand="succinyl-CoA" FT /ligand_id="ChEBI:CHEBI:57292" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 112 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /ligand_note="competitive inhibitor" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 112 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 112 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 115 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /ligand_note="competitive inhibitor" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 115 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:12972261, FT ECO:0000269|PubMed:16944299, ECO:0007744|PDB:1UCN, FT ECO:0007744|PDB:2HVD, ECO:0007744|PDB:2HVE" FT BINDING 115 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:37298313, FT ECO:0007744|PDB:8OOV" FT BINDING 115 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 115 FT /ligand="succinyl-CoA" FT /ligand_id="ChEBI:CHEBI:57292" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 118 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /ligand_note="competitive inhibitor" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 118 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /ligand_note="inhibitor" FT /evidence="ECO:0000269|PubMed:37298313, FT ECO:0007744|PDB:8OOV" FT BINDING 118 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 118 FT /ligand="succinyl-CoA" FT /ligand_id="ChEBI:CHEBI:57292" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P15532" FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305|PubMed:12972261, FT ECO:0007744|PDB:1UCN" FT BINDING 121 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000305|PubMed:12972261, FT ECO:0007744|PDB:1UCN" FT BINDING 152 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /ligand_note="competitive inhibitor" FT /evidence="ECO:0000250|UniProtKB:P52175" FT BINDING 152 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007744|PDB:2HVE" FT MOD_RES 56 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:25582197" FT MOD_RES 109 FT /note="Cysteine sulfonic acid (-SO3H); alternate" FT /evidence="ECO:0000269|PubMed:19956735, FT ECO:0000269|PubMed:23519676" FT MOD_RES 109 FT /note="L-cysteine coenzyme A disulfide; alternate" FT /evidence="ECO:0000269|PubMed:33903070" FT MOD_RES 109 FT /note="S-glutathionyl cysteine; alternate" FT /evidence="ECO:0000269|PubMed:19956735" 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 DISULFID 4..145 FT /evidence="ECO:0000269|PubMed:19956735, FT ECO:0000269|PubMed:23519676, ECO:0000312|PDB:4ENO" FT DISULFID 4..109 FT /note="alternate" FT /evidence="ECO:0000269|PubMed:19956735" FT DISULFID 109..145 FT /note="alternate" FT /evidence="ECO:0000269|PubMed:19956735" FT DISULFID 109 FT /note="Interchain; alternate" FT /evidence="ECO:0000269|PubMed:19956735" FT CROSSLNK 85 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:25582197" 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; decreases farnesyl diphosphate FT kinase activity; decreases geranyl-diphosphate kinase FT activity; significantly decreases nucleoside diphosphate FT kinase activity; decreases autophosphorylation, slighly FT decreases histidine kinase activity; dbSNP:rs121917887)" FT /evidence="ECO:0000269|PubMed:10952986, FT ECO:0000269|PubMed:8047138, ECO:0000269|PubMed:9038158" FT /id="VAR_004625" FT MUTAGEN 4 FT /note="C->S: Increases resistance to oxidative stress. FT Impairs intramolecular disulfide bonds formation under FT oxidative stress. Decreases oxidative modification at FT Cys-109." FT /evidence="ECO:0000269|PubMed:23519676" FT MUTAGEN 5 FT /note="E->A: Almost completely loss of 3'-5'-DNA FT exonuclease activity. Slightly decreases nucleoside FT diphoshate kinase activity." FT /evidence="ECO:0000269|PubMed:16313181" FT MUTAGEN 5 FT /note="E->Q: Reduces of about 80% of wild type 3'-5'-DNA FT exonuclease activity. Slightly decreases nucleoside FT diphoshate kinase activity." FT /evidence="ECO:0000269|PubMed:16313181" FT MUTAGEN 12 FT /note="K->Q: Does not affect homohexamer formation. FT Dramatically reduces nucleoside diphosphate kinase FT activity. Markedly decreases 3'-5'-DNA exonuclease FT activity." FT /evidence="ECO:0000269|PubMed:14960567, FT ECO:0000269|PubMed:16313181" FT MUTAGEN 33 FT /note="F->A: Almost completely loss of 3'-5'-DNA FT exonuclease activity." FT /evidence="ECO:0000269|PubMed:16313181" FT MUTAGEN 34 FT /note="R->A: Does not affect homohexamer formation. FT Slightly reduces nucleoside diphosphate kinase activity. FT Markedly decreases 3'-5'-DNA exonuclease activity." FT /evidence="ECO:0000269|PubMed:14960567" FT MUTAGEN 44 FT /note="S->A: Does not affect autophosphorylation. FT Significantly decreases nucleoside diphosphate kinase FT activity." FT /evidence="ECO:0000269|PubMed:9038158" FT MUTAGEN 54 FT /note="D->A: Almost completely loss of 3'-5'-DNA FT exonuclease activity. Slightly decreases nucleoside FT diphoshate kinase activity." FT /evidence="ECO:0000269|PubMed:16313181" FT MUTAGEN 56 FT /note="K->Q: Reduced interaction with FBXO24." FT /evidence="ECO:0000269|PubMed:25582197" FT MUTAGEN 56 FT /note="K->R: Increased interaction with FBXO24." FT /evidence="ECO:0000269|PubMed:25582197" FT MUTAGEN 58 FT /note="R->E: Abolishes CoA binding." FT /evidence="ECO:0000269|PubMed:37298313" FT MUTAGEN 60 FT /note="F->W: Does not affect GTP binding; when associated FT with Gly-118. Does not affect ATP binding; when associated FT with Gly-118." FT /evidence="ECO:0000269|PubMed:12972261" FT MUTAGEN 85 FT /note="K->A: Less ubiquitinated than WT in vitro." FT /evidence="ECO:0000269|PubMed:25582197" FT MUTAGEN 94 FT /note="T->D: Abolishes CoA binding." FT /evidence="ECO:0000269|PubMed:37298313" FT MUTAGEN 96 FT /note="P->S: Increases motility of carcinoma cells. FT Decreases farnesyl diphosphate kinase activity. Decreases FT geranyl-diphosphate kinase activity. Does not affect FT autophosphorylation. Significantly decreases histidine FT kinase activity." FT /evidence="ECO:0000269|PubMed:10952986, FT ECO:0000269|PubMed:8810265, ECO:0000269|PubMed:9038158" FT MUTAGEN 109 FT /note="C->A: Does not affect nucleoside diphosphate kinase FT activity. Impairs glutathionylation. Does not affect FT nucleoside diphosphate kinase activity under oxidative FT stress. Does not affect metastasis suppressor activity FT under oxidative stress." FT /evidence="ECO:0000269|PubMed:19956735, FT ECO:0000269|PubMed:33903070" FT MUTAGEN 109 FT /note="C->S: Significantly increases resistance to FT oxidative stress. Does not affect intramolecular disulfide FT bonds formation under oxidative stress." FT /evidence="ECO:0000269|PubMed:23519676" FT MUTAGEN 118 FT /note="H->F: Decreases autophosphorylation. Some loss of FT motility of carcinoma cells. Loss of farnesyl diphosphate FT kinase activity. Loss of geranyl-diphosphate kinase FT activity. Does not affect homohexamer formation. FT Dramatically reduces nucleoside diphosphate kinase FT activity. Significantly decreases 3'-5'-DNA exonuclease FT activity. Loss of autophosphorylation. Loss of histidine FT kinase activity. Loss of nucleoside diphosphate kinase FT activity under this oxidative stress." FT /evidence="ECO:0000269|PubMed:10952986, FT ECO:0000269|PubMed:14960567, ECO:0000269|PubMed:16313181, FT ECO:0000269|PubMed:19956735, ECO:0000269|PubMed:8810265, FT ECO:0000269|PubMed:9038158" FT MUTAGEN 118 FT /note="H->G: Does not affect GTP binding; when associated FT with Trp-60. Does not affect ATP binding; when associated FT with Trp-60." FT /evidence="ECO:0000269|PubMed:12972261" FT MUTAGEN 120 FT /note="S->A: Limited increase in motility of carcinoma FT cells. Increases farnesyl diphosphate kinase activity. FT Increases geranyl-diphosphate kinase activity. FT Significantly decreases autophosphorylation." FT /evidence="ECO:0000269|PubMed:10952986, FT ECO:0000269|PubMed:8810265, ECO:0000269|PubMed:9038158" FT MUTAGEN 121 FT /note="D->A: Almost completely loss of 3'-5'-DNA FT exonuclease activity." FT /evidence="ECO:0000269|PubMed:16313181" FT MUTAGEN 129 FT /note="E->A: Almost completely loss of 3'-5'-DNA FT exonuclease activity. Completely lost nucleoside diphoshate FT kinase activity." FT /evidence="ECO:0000269|PubMed:16313181" FT MUTAGEN 129 FT /note="E->Q: Almost completely loss of 3'-5'-DNA FT exonuclease activity. Completely lost nucleoside diphoshate FT kinase activity." FT /evidence="ECO:0000269|PubMed:16313181" FT MUTAGEN 145 FT /note="C->S: Increases resistance to oxidative stress. FT Impairs intramolecular disulfide bonds formation under FT oxidative stress. Decreases oxidative modification at FT Cys-109." FT /evidence="ECO:0000269|PubMed:23519676" FT HELIX 2..4 FT /evidence="ECO:0007829|PDB:8OOV" FT STRAND 6..11 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 13..17 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 21..31 FT /evidence="ECO:0007829|PDB:8OOV" FT STRAND 34..41 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 42..44 FT /evidence="ECO:0007829|PDB:5UI4" FT HELIX 45..51 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:8OOV" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:4ENO" FT HELIX 61..69 FT /evidence="ECO:0007829|PDB:8OOV" FT STRAND 73..80 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 83..91 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 104..108 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:1UCN" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 123..133 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:8OOV" FT HELIX 147..150 FT /evidence="ECO:0007829|PDB:8OOV" SQ SEQUENCE 152 AA; 17149 MW; AAE9C0DF63CB70A1 CRC64; MANCERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF MQASEDLLKE HYVDLKDRPF FAGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS DSVESAEKEI GLWFHPEELV DYTSCAQNWI YE //