NDKB_HUMAN
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 03-AUG-2022, entry version 243.
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 ITGB1BP1 (via C-
CC 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}.
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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; 152.
DR BioGRID; 576341; 82.
DR DIP; DIP-50179N; -.
DR IntAct; P22392; 46.
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 UCD-2DPAGE; P22392; -.
DR EPD; P22392; -.
DR jPOST; P22392; -.
DR MassIVE; P22392; -.
DR MaxQB; P22392; -.
DR PaxDb; P22392; -.
DR PeptideAtlas; P22392; -.
DR PRIDE; P22392; -.
DR ProteomicsDB; 53986; -. [P22392-1]
DR ProteomicsDB; 53987; -. [P22392-2]
DR TopDownProteomics; P22392-1; -. [P22392-1]
DR TopDownProteomics; P22392-2; -. [P22392-2]
DR Antibodypedia; 35045; 355 antibodies from 23 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 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 GeneTree; ENSGT00940000163317; -.
DR HOGENOM; CLU_080881_1_0_1; -.
DR InParanoid; P22392; -.
DR OMA; GXASEEH; -.
DR OrthoDB; 1334716at2759; -.
DR PhylomeDB; P22392; -.
DR TreeFam; TF106373; -.
DR BioCyc; MetaCyc:HS04463-MON; -.
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 SignaLink; P22392; -.
DR SIGNOR; P22392; -.
DR BioGRID-ORCS; 4831; 38 hits in 1076 CRISPR screens.
DR BioGRID-ORCS; 654364; 20 hits in 974 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 94 other tissues.
DR ExpressionAtlas; P22392; baseline and differential.
DR Genevisible; P22392; HS.
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:0030027; C:lamellipodium; IDA:HGNC-UCL.
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:0051880; F:G-quadruplex DNA binding; IDA:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IMP:UniProtKB.
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:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:HGNC-UCL.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
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:0006165; P:nucleoside diphosphate phosphorylation; 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:0045618; P:positive regulation of keratinocyte differentiation; IMP:HGNC-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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: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; 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 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
