NDKB_RAT
ID NDKB_RAT Reviewed; 152 AA.
AC P19804;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 189.
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;
GN Name=Nme2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Wistar;
RX PubMed=2168422; DOI=10.1016/s0021-9258(18)55460-0;
RA Kimura N., Shimada N., Nomura K., Watanabe K.;
RT "Isolation and characterization of a cDNA clone encoding rat nucleoside
RT diphosphate kinase.";
RL J. Biol. Chem. 265:15744-15749(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1321145; DOI=10.1016/s0021-9258(19)49721-4;
RA Ishikawa N., Shimada N., Munakata Y., Watanabe K., Kimura N.;
RT "Isolation and characterization of a gene encoding rat nucleoside
RT diphosphate kinase.";
RL J. Biol. Chem. 267:14366-14372(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Mast cell;
RX PubMed=1316151; DOI=10.1021/bi00134a006;
RA Hemmerich S., Yarden Y., Pecht I.;
RT "A cromoglycate binding protein from rat mast cells of a leukemia line is a
RT nucleoside diphosphate kinase.";
RL Biochemistry 31:4574-4579(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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; 89-114 AND 129-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
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).
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 -!- 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 (By similarity).
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:0000250|UniProtKB:Q01768, ECO:0000269|PubMed:17532299}.
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 -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; M55331; AAA41684.1; -; mRNA.
DR EMBL; M91597; AAA42017.1; -; mRNA.
DR EMBL; BC086599; AAH86599.1; -; mRNA.
DR PIR; A41849; A38369.
DR RefSeq; NP_114021.2; NM_031833.2.
DR AlphaFoldDB; P19804; -.
DR SMR; P19804; -.
DR BioGRID; 249827; 4.
DR IntAct; P19804; 1.
DR MINT; P19804; -.
DR STRING; 10116.ENSRNOP00000003611; -.
DR iPTMnet; P19804; -.
DR PhosphoSitePlus; P19804; -.
DR SwissPalm; P19804; -.
DR World-2DPAGE; 0004:P19804; -.
DR jPOST; P19804; -.
DR PaxDb; P19804; -.
DR PRIDE; P19804; -.
DR Ensembl; ENSRNOT00000003611; ENSRNOP00000003611; ENSRNOG00000002671.
DR GeneID; 83782; -.
DR KEGG; rno:83782; -.
DR CTD; 4831; -.
DR RGD; 619877; Nme2.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000161569; -.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; P19804; -.
DR OMA; ALWFGEQ; -.
DR OrthoDB; 1334716at2759; -.
DR PhylomeDB; P19804; -.
DR TreeFam; TF106373; -.
DR Reactome; R-RNO-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR SABIO-RK; P19804; -.
DR PRO; PR:P19804; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002671; Expressed in heart and 20 other tissues.
DR Genevisible; P19804; RN.
DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:HGNC-UCL.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0001726; C:ruffle; ISS:HGNC-UCL.
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; IPI:RGD.
DR GO; GO:0005504; F:fatty acid binding; IPI:RGD.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISO:RGD.
DR GO; GO:1901363; F:heterocyclic compound binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0019215; F:intermediate filament binding; IPI:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:RGD.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
DR GO; GO:0006241; P:CTP biosynthetic process; IDA:RGD.
DR GO; GO:0006183; P:GTP biosynthetic process; IDA:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:HGNC-UCL.
DR GO; GO:0002762; P:negative regulation of myeloid leukocyte differentiation; IDA:RGD.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IDA:RGD.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISO:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:HGNC-UCL.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:HGNC-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
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; IDA:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0045682; P:regulation of epidermis development; ISS:HGNC-UCL.
DR GO; GO:0060416; P:response to growth hormone; IEP:RGD.
DR GO; GO:0006228; P:UTP biosynthetic process; IDA:RGD.
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_0000137119"
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"
FT CONFLICT 89
FT /note="V -> W (in Ref. 3; AAA42017)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 17283 MW; 1A5C3F84C1F413EC CRC64;
MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF
FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVESAEKEI GLWFKPEELI DYKSCAHDWV YE
