NDKB_MOUSE
ID NDKB_MOUSE Reviewed; 152 AA.
AC Q01768;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Nucleoside diphosphate kinase B;
DE Short=NDK B;
DE Short=NDP kinase B;
DE EC=2.7.4.6 {ECO:0000250|UniProtKB:P22392};
DE AltName: Full=Histidine protein kinase NDKB;
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P22392};
DE AltName: Full=P18;
DE AltName: Full=nm23-M2;
GN Name=Nme2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=1325378; DOI=10.1016/0014-5793(92)80807-s;
RA Urano T., Takamiya K., Furukawa K., Shiku H.;
RT "Molecular cloning and functional expression of the second mouse nm23/NDP
RT kinase gene, nm23-M2.";
RL FEBS Lett. 309:358-362(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Takeshi U.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Heart;
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 [5]
RP PROTEIN SEQUENCE OF 7-26; 57-66 AND 89-143, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH CAPN8, AND TISSUE SPECIFICITY.
RX PubMed=16476741; DOI=10.1074/jbc.m509244200;
RA Hata S., Koyama S., Kawahara H., Doi N., Maeda T., Toyama-Sorimachi N.,
RA Abe K., Suzuki K., Sorimachi H.;
RT "Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes
RT the beta-subunit of coatomer complex, beta-COP.";
RL J. Biol. Chem. 281:11214-11224(2006).
RN [7]
RP INTERACTION WITH BCL2L10.
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20884616; DOI=10.1074/jbc.m110.168070;
RA Di L., Srivastava S., Zhdanova O., Sun Y., Li Z., Skolnik E.Y.;
RT "Nucleoside diphosphate kinase B knock-out mice have impaired activation of
RT the K+ channel KCa3.1, resulting in defective T cell activation.";
RL J. Biol. Chem. 285:38765-38771(2010).
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. Acts as a transcriptional activator of the
CC MYC gene; binds DNA non-specifically. 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). Has G-quadruplex (G4) DNA-binding activity, which is
CC independent of its nucleotide-binding and kinase activity. Binds both
CC folded and unfolded G4 with similar low nanomolar affinities.
CC Stabilizes folded G4s regardless of whether they are prefolded or not.
CC Exhibits histidine protein kinase activity (By similarity).
CC {ECO:0000250|UniProtKB:P22392, ECO:0000250|UniProtKB:P36010,
CC ECO:0000269|PubMed:20884616}.
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:0000250|UniProtKB:P22392};
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:0000250|UniProtKB:P22392};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P22392};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P22392};
CC -!- SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3,
CC A2B4, AB5, B6) (By similarity). Interacts with CAPN8 (PubMed:16476741).
CC Interacts with AKAP13 (By similarity). Interacts ITGB1BP1 (via C-
CC terminal domain region) (By similarity). Interacts with BCL2L10
CC (PubMed:17532299). {ECO:0000250|UniProtKB:P22392,
CC ECO:0000269|PubMed:16476741, ECO:0000269|PubMed:17532299}.
CC -!- INTERACTION:
CC Q01768; P09055: Itgb1; NbExp=3; IntAct=EBI-642573, EBI-644224;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22392}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:P22392}. Cell
CC projection, ruffle {ECO:0000250|UniProtKB:P22392}. Nucleus
CC {ECO:0000250|UniProtKB:P22392}. Note=Colocalizes with ITGB1 and
CC ITGB1BP1 at the edge or peripheral ruffles and lamellipodia during the
CC early stages of cell spreading on fibronectin or collagen but not on
CC vitronectin or laminin substrates. {ECO:0000250|UniProtKB:P22392}.
CC -!- TISSUE SPECIFICITY: Expressed in the base region of the oxyntic and
CC pyloric mucosae. {ECO:0000269|PubMed:16476741}.
CC -!- DISRUPTION PHENOTYPE: Impaired activation of the K(+) channel Kcnn4,
CC resulting in defective T-cell activation.
CC {ECO:0000269|PubMed:20884616}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; X68193; CAA48275.1; -; mRNA.
DR EMBL; AK012447; BAB28246.1; -; mRNA.
DR EMBL; BC066995; AAH66995.1; -; mRNA.
DR EMBL; BC086892; AAH86892.1; -; mRNA.
DR EMBL; BC086893; AAH86893.1; -; mRNA.
DR CCDS; CCDS25246.1; -.
DR PIR; S29241; S29241.
DR RefSeq; NP_001070997.1; NM_001077529.2.
DR RefSeq; NP_032731.1; NM_008705.5.
DR AlphaFoldDB; Q01768; -.
DR SMR; Q01768; -.
DR BioGRID; 201789; 20.
DR IntAct; Q01768; 10.
DR STRING; 10090.ENSMUSP00000021217; -.
DR iPTMnet; Q01768; -.
DR PhosphoSitePlus; Q01768; -.
DR SwissPalm; Q01768; -.
DR REPRODUCTION-2DPAGE; Q01768; -.
DR SWISS-2DPAGE; Q01768; -.
DR CPTAC; non-CPTAC-3595; -.
DR EPD; Q01768; -.
DR jPOST; Q01768; -.
DR PaxDb; Q01768; -.
DR PeptideAtlas; Q01768; -.
DR PRIDE; Q01768; -.
DR ProteomicsDB; 252935; -.
DR Antibodypedia; 35045; 355 antibodies from 23 providers.
DR DNASU; 18103; -.
DR Ensembl; ENSMUST00000021217; ENSMUSP00000021217; ENSMUSG00000020857.
DR Ensembl; ENSMUST00000072566; ENSMUSP00000103476; ENSMUSG00000020857.
DR GeneID; 18103; -.
DR KEGG; mmu:18103; -.
DR UCSC; uc007kxs.2; mouse.
DR CTD; 4831; -.
DR MGI; MGI:97356; Nme2.
DR VEuPathDB; HostDB:ENSMUSG00000020857; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000161569; -.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; Q01768; -.
DR OMA; ALWFGEQ; -.
DR OrthoDB; 1334716at2759; -.
DR PhylomeDB; Q01768; -.
DR TreeFam; TF106373; -.
DR BRENDA; 2.7.4.6; 3474.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9748787; Azathioprine ADME.
DR BioGRID-ORCS; 18103; 6 hits in 45 CRISPR screens.
DR ChiTaRS; Nme2; mouse.
DR PRO; PR:Q01768; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q01768; protein.
DR Bgee; ENSMUSG00000020857; Expressed in right kidney and 101 other tissues.
DR ExpressionAtlas; Q01768; baseline and differential.
DR Genevisible; Q01768; MM.
DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019215; F:intermediate filament binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISO:MGI.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006241; P:CTP biosynthetic process; ISO:MGI.
DR GO; GO:0006231; P:dTMP biosynthetic process; NAS:MGI.
DR GO; GO:0006183; P:GTP biosynthetic process; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0002762; P:negative regulation of myeloid leukocyte differentiation; ISO:MGI.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0006228; P:UTP biosynthetic process; ISO:MGI.
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 ATP-binding; Cell projection; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Kinase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..152
FT /note="Nucleoside diphosphate kinase B"
FT /id="PRO_0000137118"
FT REGION 1..66
FT /note="Interaction with AKAP13"
FT /evidence="ECO:0000250|UniProtKB:P22392"
FT ACT_SITE 118
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P22392"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22392"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22392"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22392"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22392"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22392"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P22392"
SQ SEQUENCE 152 AA; 17363 MW; 1A5C3F84C1FFC83C CRC64;
MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF
FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVESAEKEI HLWFKPEELI DYKSCAHDWV YE
