NDKB_BOVIN
ID NDKB_BOVIN Reviewed; 152 AA.
AC Q3T0Q4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION AS HISTIDINE PROTEIN KINASE.
RX PubMed=12486123; DOI=10.1074/jbc.m210304200;
RA Cuello F., Schulze R.A., Heemeyer F., Meyer H.E., Lutz S., Jakobs K.H.,
RA Niroomand F., Wieland T.;
RT "Activation of heterotrimeric G proteins by a high energy phosphate
RT transfer via nucleoside diphosphate kinase (NDPK) B and Gbeta subunits.
RT Complex formation of NDPK B with Gbeta gamma dimers and phosphorylation of
RT His-266 IN Gbeta.";
RL J. Biol. Chem. 278:7220-7226(2003).
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 (By similarity). Exhibits histidine protein kinase activity
CC (PubMed:12486123). {ECO:0000250|UniProtKB:P22392,
CC ECO:0000250|UniProtKB:P36010, ECO:0000269|PubMed:12486123}.
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:0000269|PubMed:12486123};
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 -!- INTERACTION:
CC Q3T0Q4; P62871: GNB1; NbExp=3; IntAct=EBI-8577979, EBI-357141;
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; BC102300; AAI02301.1; -; mRNA.
DR RefSeq; NP_001069844.1; NM_001076376.1.
DR AlphaFoldDB; Q3T0Q4; -.
DR SMR; Q3T0Q4; -.
DR CORUM; Q3T0Q4; -.
DR IntAct; Q3T0Q4; 1.
DR MINT; Q3T0Q4; -.
DR STRING; 9913.ENSBTAP00000041066; -.
DR PaxDb; Q3T0Q4; -.
DR PeptideAtlas; Q3T0Q4; -.
DR PRIDE; Q3T0Q4; -.
DR Ensembl; ENSBTAT00000043502; ENSBTAP00000041066; ENSBTAG00000047186.
DR GeneID; 615447; -.
DR KEGG; bta:615447; -.
DR CTD; 4831; -.
DR VEuPathDB; HostDB:ENSBTAG00000047186; -.
DR VGNC; VGNC:108102; NME2.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000161569; -.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; Q3T0Q4; -.
DR OMA; ALWFGEQ; -.
DR OrthoDB; 1334716at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000047186; Expressed in caput epididymis and 107 other tissues.
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:0019003; F:GDP binding; IEA:Ensembl.
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:0003713; F:transcription coactivator activity; IEA:Ensembl.
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:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
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: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 1: Evidence at protein 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_0000250199"
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; 17316 MW; C3EB0D24AEFA4183 CRC64;
MAHAERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LQASEELLKQ HYIDLKDRPF
FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
DSVKSAEKEI NLWFKPEELI EYKPCAFDWI YE
