ID NDKB_HUMAN Reviewed; 152 AA. AC P22392; A8MWA3; Q1WM23; Q6LCT6; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 27-MAR-2024, entry version 252. DE RecName: Full=Nucleoside diphosphate kinase B; DE Short=NDK B; DE Short=NDP kinase B; DE EC=2.7.4.6 {ECO:0000269|PubMed:1851158, ECO:0000269|PubMed:25679041}; DE AltName: Full=C-myc purine-binding transcription factor PUF; DE AltName: Full=Histidine protein kinase NDKB; DE EC=2.7.13.3 {ECO:0000269|PubMed:20946858}; DE AltName: Full=nm23-H2; GN Name=NME2; Synonyms=NM23B; 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=1988104; RA Stahl J.A., Leone A., Rosengard A.M., Porter L., Liotta L.A., Steeg P.S., RA King C.R.; RT "Identification of a second human nm23 gene, nm23-H2."; RL Cancer Res. 51:445-449(1991). RN [2] RP PROTEIN SEQUENCE (ISOFORM 1), CATALYTIC ACTIVITY, 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=8392752; DOI=10.1126/science.8392752; RA Postel E.H., Berberich S.J., Flint S.J., Ferrone C.A.; RT "Human c-myc transcription factor PuF identified as nm23-H2 nucleoside RT diphosphate kinase, a candidate suppressor of tumor metastasis."; RL Science 261:478-480(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Neuroblastoma; 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Eye; 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18. RX PubMed=7488060; DOI=10.1006/bbrc.1995.2550; RA Seifert M., Seib T., Engel M., Dooley S., Welter C.; RT "Characterization of the human nm23-H2 promoter region and localization of RT the microsatellite D17S396."; RL Biochem. Biophys. Res. Commun. 215:910-914(1995). RN [8] RP INTERACTION WITH ITGB1BP1, AND SUBCELLULAR LOCATION. RX PubMed=11919189; DOI=10.1074/jbc.m200200200; RA Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C., RA Block M.R., Albiges-Rizo C.; RT "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha) RT interacts directly with the metastasis suppressor nm23-H2, and both RT proteins are targeted to newly formed cell adhesion sites upon integrin RT engagement."; RL J. Biol. Chem. 277:20895-20902(2002). RN [9] RP FUNCTION, AND INTERACTION WITH AKAP13. RX PubMed=15249197; DOI=10.1016/j.bbrc.2004.06.067; RA Iwashita S., Fujii M., Mukai H., Ono Y., Miyamoto M.; RT "Lbc proto-oncogene product binds to and could be negatively regulated by RT metastasis suppressor nm23-H2."; RL Biochem. Biophys. Res. Commun. 320:1063-1068(2004). RN [10] RP INTERACTION WITH BCL2L10, AND SUBCELLULAR LOCATION. RX PubMed=17532299; DOI=10.1016/j.bbrc.2007.05.090; RA Kang Y., Lee D.C., Han J., Yoon S., Won M., Yeom J.H., Seong M.J., Ko J.J., RA Lee K.A., Lee K., Bae J.; RT "NM23-H2 involves in negative regulation of Diva and Bcl2L10 in apoptosis RT signaling."; RL Biochem. Biophys. Res. Commun. 359:76-82(2007). RN [11] RP FUNCTION AS HISTIDINE PROTEIN KINASE. RX PubMed=20946858; DOI=10.1016/s0076-6879(10)71020-x; RA Wieland T., Hippe H.J., Ludwig K., Zhou X.B., Korth M., Klumpp S.; RT "Reversible histidine phosphorylation in mammalian cells: a teeter-totter RT formed by nucleoside diphosphate kinase and protein histidine phosphatase RT 1."; RL Methods Enzymol. 471:379-402(2010). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=25679041; DOI=10.1021/bi501284g; RA Kopylov M., Bass H.W., Stroupe M.E.; RT "The maize (Zea mays L.) nucleoside diphosphate kinase1 (ZmNDPK1) gene RT encodes a human NM23-H2 homologue that binds and stabilizes G-quadruplex RT DNA."; RL Biochemistry 54:1743-1757(2015). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=7658474; DOI=10.1006/jmbi.1995.0457; RA Webb P.A., Perisic O., Mendola C.E., Backer J.M., Williams R.L.; RT "The crystal structure of a human nucleoside diphosphate kinase, NM23-H2."; RL J. Mol. Biol. 251:574-587(1995). RN [14] RP X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS). RX PubMed=8747457; DOI=10.1016/s0969-2126(01)00268-4; RA Morera S., Lacombe M.-L., Xu Y., Lebras G., Janin J.; RT "X-ray structure of human nucleoside diphosphate kinase B complexed with RT GDP at 2-A resolution."; RL Structure 3:1307-1314(1995). RN [15] {ECO:0007744|PDB:3BBB, ECO:0007744|PDB:3BBC, ECO:0007744|PDB:3BBF} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 2-152 IN COMPLEX WITH GDP AND RP DINUCLEOTIDE AND OF 2-152 OF MUTANT ALA-88, FUNCTION, COFACTOR, AND RP MUTAGENESIS OF ARG-88. RX PubMed=19435876; DOI=10.1158/1535-7163.mct-08-1093; RA Dexheimer T.S., Carey S.S., Zuohe S., Gokhale V.M., Hu X., Murata L.B., RA Maes E.M., Weichsel A., Sun D., Meuillet E.J., Montfort W.R., Hurley L.H.; RT "NM23-H2 may play an indirect role in transcriptional activation of c-myc RT gene expression but does not cleave the nuclease hypersensitive element RT III(1)."; RL Mol. Cancer Ther. 8:1363-1377(2009). 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 (By similarity). Negatively regulates Rho activity by CC interacting with AKAP13/LBC (PubMed:15249197). Acts as a CC transcriptional activator of the MYC gene; binds DNA non-specifically CC (PubMed:8392752, PubMed:19435876). Binds to both single-stranded CC guanine- and cytosine-rich strands within the nuclease hypersensitive CC element (NHE) III(1) region of the MYC gene promoter. Does not bind to CC duplex NHE III(1) (PubMed:19435876). Has G-quadruplex (G4) DNA-binding CC activity, which is independent of its nucleotide-binding and kinase CC activity. Binds both folded and unfolded G4 with similar low nanomolar CC affinities. Stabilizes folded G4s regardless of whether they are CC prefolded or not (PubMed:25679041). Exhibits histidine protein kinase CC activity (PubMed:20946858). {ECO:0000250|UniProtKB:P36010, CC ECO:0000269|PubMed:15249197, ECO:0000269|PubMed:19435876, CC ECO:0000269|PubMed:20946858, ECO:0000269|PubMed:25679041, CC ECO:0000269|PubMed:8392752}. 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; Evidence={ECO:0000269|PubMed:1851158, CC ECO:0000269|PubMed:25679041}; 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:1851158, ECO:0000269|PubMed:25679041}; 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:20946858}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:19435876}; CC -!- SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, CC A2B4, AB5, B6) (PubMed:1851158). Interacts with CAPN8 (By similarity). CC Interacts with AKAP13 (PubMed:15249197). Interacts with ITGB1BP1 (via CC C-terminal domain region) (PubMed:11919189). Interacts with BCL2L10 CC (PubMed:17532299). {ECO:0000250|UniProtKB:Q01768, CC ECO:0000269|PubMed:11919189, ECO:0000269|PubMed:15249197, CC ECO:0000269|PubMed:17532299, ECO:0000269|PubMed:1851158}. CC -!- INTERACTION: CC P22392; P50570: DNM2; NbExp=2; IntAct=EBI-713693, EBI-346547; CC P22392; O14713-1: ITGB1BP1; NbExp=7; IntAct=EBI-713693, EBI-2127367; CC P22392; P15531: NME1; NbExp=4; IntAct=EBI-713693, EBI-741141; CC P22392; O00746: NME4; NbExp=5; IntAct=EBI-713693, EBI-744871; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17532299}. Cell CC projection, lamellipodium {ECO:0000269|PubMed:11919189}. Cell CC projection, ruffle {ECO:0000269|PubMed:11919189}. Note=Colocalizes with CC ITGB1 and ITGB1BP1 at the edge or peripheral ruffles and lamellipodia CC during the early stages of cell spreading on fibronectin or collagen CC but not on vitronectin or laminin substrates. CC {ECO:0000269|PubMed:11919189}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm CC {ECO:0000269|PubMed:16442775}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:16442775}. Nucleus {ECO:0000269|PubMed:16442775}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm CC {ECO:0000269|PubMed:16442775}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:16442775}. Nucleus {ECO:0000269|PubMed:16442775}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=NM23-H2; CC IsoId=P22392-1; Sequence=Displayed; CC Name=3; Synonyms=NM23-LV; CC IsoId=P22392-2; Sequence=VSP_036708; CC -!- TISSUE SPECIFICITY: [Isoform 1]: Ubiquitously expressed. CC {ECO:0000269|PubMed:16442775}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Ubiquitously expressed. CC {ECO:0000269|PubMed:16442775}. CC -!- MISCELLANEOUS: [Isoform 3]: Based on a naturally occurring readthrough CC transcript which produces an NME1-NME2 fusion protein. CC {ECO:0000269|PubMed:16442775}. CC -!- SIMILARITY: Belongs to the NDK family. {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; X58965; CAB37870.1; -; mRNA. DR EMBL; M36981; AAA36369.1; -; mRNA. DR EMBL; L16785; AAA60228.1; -; mRNA. DR EMBL; DQ109675; AAZ82097.1; -; mRNA. DR EMBL; AC005839; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002476; AAH02476.1; -; mRNA. DR EMBL; BC133029; AAI33030.1; -; mRNA. DR EMBL; BC133031; AAI33032.1; -; mRNA. DR EMBL; U29200; AAA86745.1; -; Genomic_DNA. DR CCDS; CCDS11580.1; -. [P22392-1] DR PIR; A49798; A49798. DR RefSeq; NP_001018146.1; NM_001018136.2. [P22392-2] DR RefSeq; NP_001018147.1; NM_001018137.2. [P22392-1] DR RefSeq; NP_001018148.1; NM_001018138.1. [P22392-1] DR RefSeq; NP_001018149.1; NM_001018139.2. [P22392-1] DR RefSeq; NP_002503.1; NM_002512.3. [P22392-1] DR PDB; 1NSK; X-ray; 2.80 A; L/N/O/R/T/U=1-152. DR PDB; 1NUE; X-ray; 2.00 A; A/B/C/D/E/F=2-152. DR PDB; 3BBB; X-ray; 1.30 A; A/B/C/D/E/F=2-152. DR PDB; 3BBC; X-ray; 1.70 A; A/B/C/D/E/F=2-152. DR PDB; 3BBF; X-ray; 1.70 A; A/B/C/D/E/F=2-152. DR PDB; 7KPF; X-ray; 2.23 A; A/B/C/D/E/F=1-152. DR PDBsum; 1NSK; -. DR PDBsum; 1NUE; -. DR PDBsum; 3BBB; -. DR PDBsum; 3BBC; -. DR PDBsum; 3BBF; -. DR PDBsum; 7KPF; -. DR AlphaFoldDB; P22392; -. DR SMR; P22392; -. DR BioGRID; 110895; 180. DR BioGRID; 576341; 86. DR DIP; DIP-50179N; -. DR IntAct; P22392; 51. DR MINT; P22392; -. DR STRING; 9606.ENSP00000376886; -. DR BindingDB; P22392; -. DR ChEMBL; CHEMBL2160; -. DR DrugBank; DB00787; Acyclovir. DR DrugBank; DB00718; Adefovir dipivoxil. DR DrugBank; DB00640; Adenosine. DR DrugBank; DB01262; Decitabine. DR DrugBank; DB04315; Guanosine-5'-Diphosphate. DR DrugBank; DB00709; Lamivudine. DR DrugBank; DB14126; Tenofovir. DR DrugBank; DB09299; Tenofovir alafenamide. DR DrugBank; DB00300; Tenofovir disoproxil. DR GlyGen; P22392; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P22392; -. DR MetOSite; P22392; -. DR PhosphoSitePlus; P22392; -. DR SwissPalm; P22392; -. DR BioMuta; NME2; -. DR DMDM; 127983; -. DR DOSAC-COBS-2DPAGE; P22392; -. DR OGP; P22392; -. DR EPD; P22392; -. DR jPOST; P22392; -. DR MassIVE; P22392; -. DR MaxQB; P22392; -. DR PaxDb; 9606-ENSP00000376886; -. DR PeptideAtlas; P22392; -. DR PRIDE; P22392; -. DR ProteomicsDB; 53986; -. [P22392-1] DR ProteomicsDB; 53987; -. [P22392-2] DR Pumba; P22392; -. DR TopDownProteomics; P22392-1; -. [P22392-1] DR TopDownProteomics; P22392-2; -. [P22392-2] DR Antibodypedia; 35045; 411 antibodies from 24 providers. DR CPTC; P22392; 3 antibodies. DR DNASU; 4831; -. DR Ensembl; ENST00000393190.4; ENSP00000376886.1; ENSG00000243678.12. [P22392-1] DR Ensembl; ENST00000503064.5; ENSP00000426901.1; ENSG00000243678.12. [P22392-1] DR Ensembl; ENST00000512737.6; ENSP00000421064.1; ENSG00000243678.12. [P22392-1] DR Ensembl; ENST00000513177.5; ENSP00000425581.1; ENSG00000243678.12. [P22392-1] DR Ensembl; ENST00000514264.6; ENSP00000426976.2; ENSG00000243678.12. [P22392-1] DR GeneID; 4831; -. DR GeneID; 654364; -. DR KEGG; hsa:4831; -. DR KEGG; hsa:654364; -. DR MANE-Select; ENST00000512737.6; ENSP00000421064.1; NM_002512.4; NP_002503.1. DR UCSC; uc002itj.4; human. [P22392-1] DR AGR; HGNC:33531; -. DR AGR; HGNC:7850; -. DR CTD; 4831; -. DR CTD; 654364; -. DR DisGeNET; 4831; -. DR DisGeNET; 654364; -. DR GeneCards; NME2; -. DR HGNC; HGNC:7850; NME2. DR HPA; ENSG00000243678; Low tissue specificity. DR MIM; 156491; gene. DR neXtProt; NX_P22392; -. DR OpenTargets; ENSG00000011052; -. DR OpenTargets; ENSG00000243678; -. DR PharmGKB; PA162398077; -. DR VEuPathDB; HostDB:ENSG00000243678; -. DR eggNOG; KOG0888; Eukaryota. DR GeneTree; ENSGT00940000161569; -. DR HOGENOM; CLU_080881_1_0_1; -. DR InParanoid; P22392; -. DR OMA; TESMANT; -. DR OrthoDB; 3075753at2759; -. DR PhylomeDB; P22392; -. DR TreeFam; TF106373; -. DR BioCyc; MetaCyc:HS04463-MONOMER; -. DR BRENDA; 2.7.4.6; 2681. DR PathwayCommons; P22392; -. DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-9748787; Azathioprine ADME. DR Reactome; R-HSA-9755088; Ribavirin ADME. DR SignaLink; P22392; -. DR SIGNOR; P22392; -. DR BioGRID-ORCS; 4831; 39 hits in 1156 CRISPR screens. DR BioGRID-ORCS; 654364; 20 hits in 1029 CRISPR screens. DR EvolutionaryTrace; P22392; -. DR GeneWiki; NME1-NME2; -. DR GeneWiki; NME2; -. DR Pharos; P22392; Tbio. DR PRO; PR:P22392; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P22392; Protein. DR Bgee; ENSG00000243678; Expressed in left ovary and 96 other cell types or tissues. DR ExpressionAtlas; P22392; baseline and differential. DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0005882; C:intermediate filament; IEA:Ensembl. DR GO; GO:0030027; C:lamellipodium; IDA:HGNC-UCL. DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0001726; C:ruffle; IDA:HGNC-UCL. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl. DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl. DR GO; GO:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB. DR GO; GO:0019003; F:GDP binding; IMP:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0019215; F:intermediate filament binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB. DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:Ensembl. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; TAS:HGNC-UCL. DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:Ensembl. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:Ensembl. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:HGNC-UCL. DR GO; GO:0002762; P:negative regulation of myeloid leukocyte differentiation; IEA:Ensembl. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:HGNC-UCL. DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:HGNC-UCL. DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0045682; P:regulation of epidermis development; IMP:HGNC-UCL. DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:Ensembl. DR CDD; cd04413; NDPk_I; 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 PANTHER; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1. DR PANTHER; PTHR11349:SF57; NUCLEOSIDE DIPHOSPHATE KINASE B; 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 UCD-2DPAGE; P22392; -. DR Genevisible; P22392; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; ATP-binding; KW Cell projection; Cytoplasm; Direct protein sequencing; DNA-binding; Kinase; KW Magnesium; Metal-binding; Nucleotide metabolism; Nucleotide-binding; KW Nucleus; Reference proteome; Transcription; Transcription regulation; KW Transferase. FT CHAIN 1..152 FT /note="Nucleoside diphosphate kinase B" FT /id="PRO_0000137117" FT REGION 1..66 FT /note="Interaction with AKAP13" FT /evidence="ECO:0000269|PubMed:15249197" 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 /evidence="ECO:0000269|PubMed:19435876, FT ECO:0007744|PDB:3BBF" FT BINDING 60 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:19435876, FT ECO:0007744|PDB:3BBF" FT BINDING 88 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:19435876, FT ECO:0007744|PDB:3BBF" FT BINDING 94 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:19435876, FT ECO:0007744|PDB:3BBF" FT BINDING 105 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:19435876, FT ECO:0007744|PDB:3BBF" FT BINDING 115 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:19435876, FT ECO:0007744|PDB:3BBF" FT VAR_SEQ 1 FT /note="M -> MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDL FT LKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRG FT DFCIQVGRTM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16442775" FT /id="VSP_036708" FT MUTAGEN 88 FT /note="R->A: Decreased single-stranded DNA-binding and FT nucleotide-binding activity. No effect on 3D-structure." FT /evidence="ECO:0000269|PubMed:19435876" FT HELIX 2..4 FT /evidence="ECO:0007829|PDB:7KPF" FT STRAND 6..11 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 13..17 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 21..31 FT /evidence="ECO:0007829|PDB:3BBB" FT STRAND 34..41 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 45..51 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 61..68 FT /evidence="ECO:0007829|PDB:3BBB" FT STRAND 73..80 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 83..91 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 104..108 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:3BBC" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 123..133 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:3BBB" FT HELIX 147..150 FT /evidence="ECO:0007829|PDB:3BBB" SQ SEQUENCE 152 AA; 17298 MW; 1A5C3F84D7AD272C CRC64; MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS DSVKSAEKEI SLWFKPEELV DYKSCAHDWV YE //