NDK6_MOUSE
ID NDK6_MOUSE Reviewed; 189 AA.
AC O88425; Q99M53;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Nucleoside diphosphate kinase 6;
DE Short=NDK 6;
DE Short=NDP kinase 6;
DE EC=2.7.4.6;
DE AltName: Full=nm23-M6;
GN Name=Nme6;
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 TISSUE=Heart;
RX PubMed=10453732; DOI=10.1007/s004390050987;
RA Mehus J.G., Deloukas P., Lambeth D.O.;
RT "NME6: a new member of the nm23/nucleoside diphosphate kinase gene family
RT located on human chromosome 3p21.3.";
RL Hum. Genet. 104:454-459(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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.
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:0000255|PROSITE-
CC ProRule:PRU10030};
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:0000255|PROSITE-ProRule:PRU10030};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; AF051942; AAC78464.1; -; mRNA.
DR EMBL; BC002007; AAH02007.1; -; mRNA.
DR CCDS; CCDS23558.1; -.
DR RefSeq; NP_061227.1; NM_018757.1.
DR RefSeq; XP_006512260.1; XM_006512197.1.
DR RefSeq; XP_006512261.1; XM_006512198.3.
DR RefSeq; XP_006512262.1; XM_006512199.3.
DR AlphaFoldDB; O88425; -.
DR SMR; O88425; -.
DR STRING; 10090.ENSMUSP00000113692; -.
DR PhosphoSitePlus; O88425; -.
DR EPD; O88425; -.
DR MaxQB; O88425; -.
DR PaxDb; O88425; -.
DR PeptideAtlas; O88425; -.
DR PRIDE; O88425; -.
DR ProteomicsDB; 252933; -.
DR Antibodypedia; 13081; 196 antibodies from 23 providers.
DR DNASU; 54369; -.
DR Ensembl; ENSMUST00000035053; ENSMUSP00000035053; ENSMUSG00000032478.
DR Ensembl; ENSMUST00000200468; ENSMUSP00000143021; ENSMUSG00000032478.
DR GeneID; 54369; -.
DR KEGG; mmu:54369; -.
DR UCSC; uc009rst.1; mouse.
DR CTD; 10201; -.
DR MGI; MGI:1861676; Nme6.
DR VEuPathDB; HostDB:ENSMUSG00000032478; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000160284; -.
DR InParanoid; O88425; -.
DR OMA; QKWRRLM; -.
DR OrthoDB; 1395365at2759; -.
DR PhylomeDB; O88425; -.
DR TreeFam; TF354225; -.
DR BioGRID-ORCS; 54369; 11 hits in 76 CRISPR screens.
DR ChiTaRS; Nme6; mouse.
DR PRO; PR:O88425; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O88425; protein.
DR Bgee; ENSMUSG00000032478; Expressed in spermatocyte and 224 other tissues.
DR ExpressionAtlas; O88425; baseline and differential.
DR Genevisible; O88425; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR CDD; cd04414; NDPk6; 1.
DR Gene3D; 3.30.70.141; -; 1.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR037994; NDPk6.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR PANTHER; PTHR46956; PTHR46956; 1.
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; Kinase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..189
FT /note="Nucleoside diphosphate kinase 6"
FT /id="PRO_0000137128"
FT ACT_SITE 129
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10030"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 179
FT /note="E -> G (in Ref. 2; AAH02007)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="T -> A (in Ref. 2; AAH02007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21778 MW; 47D830A249902ECD CRC64;
MTSILRSPQA LQLTLALIKP DAVAHPLILE AVHQQILSNK FLIVRTRELQ WKLEDCRRFY
REHEGRFFYQ RLVEFMTSGP IRAYILAHKD AIQLWRTLMG PTRVFRARYI APDSIRGSLG
LTDTRNTTHG SDSVVSASRE IAAFFPDFSE QRWYEEEEPQ LRCGPVHYSP EEGIHCAAET
GGHKQPNKT
