NDKB_PIG
ID NDKB_PIG Reviewed; 152 AA.
AC Q2EN76;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
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};
GN Name=NME2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen C.H., Ding S.T.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250|UniProtKB:P22392,
CC ECO:0000250|UniProtKB:Q01768}.
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 -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; DQ372081; ABD18456.1; -; mRNA.
DR RefSeq; NP_001038075.1; NM_001044610.2.
DR AlphaFoldDB; Q2EN76; -.
DR SMR; Q2EN76; -.
DR STRING; 9823.ENSSSCP00000018643; -.
DR PaxDb; Q2EN76; -.
DR PeptideAtlas; Q2EN76; -.
DR PRIDE; Q2EN76; -.
DR Ensembl; ENSSSCT00000019150; ENSSSCP00000018643; ENSSSCG00000017591.
DR Ensembl; ENSSSCT00005012014; ENSSSCP00005007039; ENSSSCG00005007984.
DR Ensembl; ENSSSCT00015056918; ENSSSCP00015022802; ENSSSCG00015042663.
DR Ensembl; ENSSSCT00015057117; ENSSSCP00015022884; ENSSSCG00015042663.
DR Ensembl; ENSSSCT00025103851; ENSSSCP00025046063; ENSSSCG00025075310.
DR Ensembl; ENSSSCT00025103885; ENSSSCP00025046088; ENSSSCG00025075310.
DR Ensembl; ENSSSCT00030053120; ENSSSCP00030024238; ENSSSCG00030038134.
DR Ensembl; ENSSSCT00035079371; ENSSSCP00035032592; ENSSSCG00035059254.
DR Ensembl; ENSSSCT00040004416; ENSSSCP00040001408; ENSSSCG00040003507.
DR Ensembl; ENSSSCT00045029357; ENSSSCP00045020341; ENSSSCG00045017236.
DR Ensembl; ENSSSCT00050109056; ENSSSCP00050048536; ENSSSCG00050079003.
DR Ensembl; ENSSSCT00055043217; ENSSSCP00055034379; ENSSSCG00055022004.
DR Ensembl; ENSSSCT00060084840; ENSSSCP00060036715; ENSSSCG00060062146.
DR Ensembl; ENSSSCT00065109127; ENSSSCP00065048975; ENSSSCG00065078642.
DR Ensembl; ENSSSCT00065109143; ENSSSCP00065048991; ENSSSCG00065078642.
DR Ensembl; ENSSSCT00070046547; ENSSSCP00070039276; ENSSSCG00070023343.
DR GeneID; 733683; -.
DR KEGG; ssc:733683; -.
DR CTD; 4831; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000161569; -.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; Q2EN76; -.
DR OMA; ALWFGEQ; -.
DR OrthoDB; 1334716at2759; -.
DR TreeFam; TF106373; -.
DR Reactome; R-SSC-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-9748787; Azathioprine ADME.
DR Proteomes; UP000008227; Chromosome 12.
DR Proteomes; UP000314985; Chromosome 12.
DR Bgee; ENSSSCG00000017591; Expressed in hindlimb bud and 43 other tissues.
DR ExpressionAtlas; Q2EN76; baseline and differential.
DR Genevisible; Q2EN76; SS.
DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0051880; F:G-quadruplex DNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; ISS:UniProtKB.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
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; ISS:UniProtKB.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
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:0042981; P:regulation of apoptotic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cytoplasm; DNA-binding; Kinase; Magnesium;
KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..152
FT /note="Nucleoside diphosphate kinase B"
FT /id="PRO_0000250201"
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; 17176 MW; 446D0DFAC8D47019 CRC64;
MAHAERTFIA VKPDGVQRGL VGEIIKRFEQ KGFRLVALKF LQASEELLKQ HYIDLKDRPF
FPGLVKYMGS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVKSAEKEI SLWFKPEELV EYKSCAFDWI YE
