DGUOK_HUMAN
ID DGUOK_HUMAN Reviewed; 277 AA.
AC Q16854; P78532; Q16759; Q4ZG09; Q7L1W9; Q96BC1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Deoxyguanosine kinase, mitochondrial;
DE EC=2.7.1.113 {ECO:0000269|PubMed:11687801, ECO:0000269|PubMed:17073823, ECO:0000269|PubMed:23043144, ECO:0000269|PubMed:8692979, ECO:0000269|PubMed:8706825};
DE AltName: Full=Deoxyadenosine kinase, mitochondrial;
DE EC=2.7.1.76 {ECO:0000269|PubMed:17073823, ECO:0000269|PubMed:8692979, ECO:0000269|PubMed:8706825};
DE Flags: Precursor;
GN Name=DGUOK; Synonyms=DGK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Brain;
RX PubMed=8692979; DOI=10.1073/pnas.93.14.7258;
RA Johansson M., Karlsson A.;
RT "Cloning and expression of human deoxyguanosine kinase cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7258-7262(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC TISSUE=B-cell, and Urinary bladder;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 18-277, CATALYTIC ACTIVITY, FUNCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8706825; DOI=10.1016/0014-5793(96)00623-0;
RA Wang L., Hellman U., Eriksson S.;
RT "Cloning and expression of human mitochondrial deoxyguanosine kinase
RT cDNA.";
RL FEBS Lett. 390:39-43(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
RA Stegmann A.P.A., Mitchell B.S.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11687801; DOI=10.1038/ng751;
RA Saada A., Shaag A., Mandel H., Nevo Y., Eriksson S., Elpeleg O.;
RT "Mutant mitochondrial thymidine kinase in mitochondrial DNA depletion
RT myopathy.";
RL Nat. Genet. 29:342-344(2001).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT NCPH SER-46, AND
RP CHARACTERIZATION OF VARIANT ARG-266.
RX PubMed=17073823; DOI=10.1042/bj20060705;
RA Mousson de Camaret B., Taanman J.W., Padet S., Chassagne M., Mayencon M.,
RA Clerc-Renaud P., Mandon G., Zabot M.T., Lachaux A., Bozon D.;
RT "Kinetic properties of mutant deoxyguanosine kinase in a case of reversible
RT hepatic mtDNA depletion.";
RL Biochem. J. 402:377-385(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 37-277 IN COMPLEX WITH
RP DEOXYADENOSINE 5'-TRIPHOSPHATE, AND SUBUNIT.
RX PubMed=11427893; DOI=10.1038/89661;
RA Johansson K., Ramaswamy S., Ljungcrantz C., Knecht W., Piskur J.,
RA Munch-Petersen B., Eriksson S., Eklund H.;
RT "Structural basis for substrate specificities of cellular
RT deoxyribonucleoside kinases.";
RL Nat. Struct. Biol. 8:616-620(2001).
RN [11]
RP VARIANTS MTDPS3 LYS-142 AND LYS-227.
RX PubMed=12205643; DOI=10.1002/ana.10284;
RA Salviati L., Sacconi S., Mancuso M., Otaegui D., Camano P., Marina A.,
RA Rabinowitz S., Shiffman R., Thompson K., Wilson C.M., Feigenbaum A.,
RA Naini A.B., Hirano M., Bonilla E., DiMauro S., Vu T.H.;
RT "Mitochondrial DNA depletion and dGK gene mutations.";
RL Ann. Neurol. 52:311-317(2002).
RN [12]
RP VARIANT MTDPS3 SER-250, AND CHARACTERIZATION OF VARIANT MTDPS3 SER-250.
RX PubMed=15639197; DOI=10.1016/j.ymgme.2004.09.005;
RA Wang L., Limongelli A., Vila M.R., Carrara F., Zeviani M., Eriksson S.;
RT "Molecular insight into mitochondrial DNA depletion syndrome in two
RT patients with novel mutations in the deoxyguanosine kinase and thymidine
RT kinase 2 genes.";
RL Mol. Genet. Metab. 84:75-82(2005).
RN [13]
RP INVOLVEMENT IN PEOB4, VARIANTS PEOB4 LYS-44 AND LYS-154, CHARACTERIZATION
RP OF VARIANTS PEOB4 LYS-44 AND LYS-154, VARIANT ARG-170, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=23043144; DOI=10.1093/brain/aws258;
RA Ronchi D., Garone C., Bordoni A., Gutierrez Rios P., Calvo S.E.,
RA Ripolone M., Ranieri M., Rizzuti M., Villa L., Magri F., Corti S.,
RA Bresolin N., Mootha V.K., Moggio M., DiMauro S., Comi G.P., Sciacco M.;
RT "Next-generation sequencing reveals DGUOK mutations in adult patients with
RT mitochondrial DNA multiple deletions.";
RL Brain 135:3404-3415(2012).
RN [14]
RP INVOLVEMENT IN NCPH, AND VARIANT NCPH SER-46.
RX PubMed=26874653; DOI=10.1002/hep.28499;
RA Vilarinho S., Sari S., Yilmaz G., Stiegler A.L., Boggon T.J., Jain D.,
RA Akyol G., Dalgic B., Guenel M., Lifton R.P.;
RT "Recurrent recessive mutation in deoxyguanosine kinase causes idiopathic
RT noncirrhotic portal hypertension.";
RL Hepatology 63:1977-1986(2016).
CC -!- FUNCTION: Phosphorylates deoxyguanosine and deoxyadenosine in the
CC mitochondrial matrix, with the highest efficiency for deoxyguanosine
CC (PubMed:8692979, PubMed:8706825, PubMed:11687801, PubMed:17073823,
CC PubMed:23043144). In non-replicating cells, where cytosolic dNTP
CC synthesis is down-regulated, mtDNA synthesis depends solely on DGUOK
CC and TK2. Phosphorylates certain nucleoside analogs (By similarity).
CC Widely used as target of antiviral and chemotherapeutic agents.
CC {ECO:0000250|UniProtKB:Q9QX60, ECO:0000269|PubMed:11687801,
CC ECO:0000269|PubMed:17073823, ECO:0000269|PubMed:23043144,
CC ECO:0000269|PubMed:8692979, ECO:0000269|PubMed:8706825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+);
CC Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216;
CC EC=2.7.1.113; Evidence={ECO:0000269|PubMed:11687801,
CC ECO:0000269|PubMed:17073823, ECO:0000269|PubMed:23043144,
CC ECO:0000269|PubMed:8692979, ECO:0000269|PubMed:8706825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+);
CC Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216;
CC EC=2.7.1.76; Evidence={ECO:0000269|PubMed:17073823,
CC ECO:0000269|PubMed:8692979, ECO:0000269|PubMed:8706825};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11427893}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9QX60}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q16854-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16854-2; Sequence=VSP_003025;
CC Name=3;
CC IsoId=Q16854-3; Sequence=VSP_003024;
CC Name=4;
CC IsoId=Q16854-4; Sequence=VSP_003024, VSP_003025;
CC Name=5;
CC IsoId=Q16854-5; Sequence=VSP_003026, VSP_003024;
CC Name=6;
CC IsoId=Q16854-6; Sequence=VSP_056026, VSP_056027;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in muscle, brain,
CC liver and lymphoid tissues. {ECO:0000269|PubMed:8706825}.
CC -!- DISEASE: Mitochondrial DNA depletion syndrome 3 (MTDPS3) [MIM:251880]:
CC A disorder due to mitochondrial dysfunction characterized by onset in
CC infancy of progressive liver failure, hypoglycemia, increased lactate
CC in body fluids, and neurologic abnormalities including hypotonia,
CC encephalopathy, peripheral neuropathy. Affected tissues show both
CC decreased activity of the mtDNA-encoded respiratory chain complexes and
CC mtDNA depletion. {ECO:0000269|PubMed:12205643,
CC ECO:0000269|PubMed:15639197}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Portal hypertension, non-cirrhotic (NCPH) [MIM:617068]: An
CC autosomal recessive disorder characterized by portal hypertension
CC associated with hepatosplenomegaly, in absence of cirrhosis,
CC extrahepatic diseases, and splanchnic venous thrombosis. Portal
CC hypertension is defined by a portal venous system pressure that is at
CC least 5 mm Hg higher than the pressure in the inferior vena cava. High
CC pressure in the portal venous system leads to shunting of blood through
CC vessels that are poorly suited to carrying large blood volumes,
CC resulting in collateral circulation and splenomegaly. NCPH patients
CC show normal liver function. {ECO:0000269|PubMed:17073823,
CC ECO:0000269|PubMed:26874653}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA
CC deletions, autosomal recessive 4 (PEOB4) [MIM:617070]: A form of
CC progressive external ophthalmoplegia, a mitochondrial myopathy
CC characterized by progressive paralysis of the levator palpebrae,
CC orbicularis oculi, and extraocular muscles. PEOB4 patients manifest
CC clinically variable features including mitochondrial myopathy with or
CC without progressive external ophthalmoplegia, recurrent rhabdomyolysis,
CC and adult-onset lower motor neuron syndrome with mild cognitive
CC impairment. {ECO:0000269|PubMed:23043144}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; U41668; AAC50624.1; -; mRNA.
DR EMBL; AC073046; AAX88910.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99704.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99707.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99709.1; -; Genomic_DNA.
DR EMBL; BC015757; AAH15757.1; -; mRNA.
DR EMBL; BC024019; AAH24019.1; -; mRNA.
DR EMBL; X97386; CAA66054.1; -; mRNA.
DR EMBL; U81499; AAB39858.1; -; Genomic_DNA.
DR CCDS; CCDS1931.1; -. [Q16854-1]
DR CCDS; CCDS1932.1; -. [Q16854-2]
DR PIR; JC6142; JC6142.
DR PIR; S71315; S71315.
DR RefSeq; NP_001305788.1; NM_001318859.1.
DR RefSeq; NP_001305789.1; NM_001318860.1.
DR RefSeq; NP_001305790.1; NM_001318861.1.
DR RefSeq; NP_001305791.1; NM_001318862.1.
DR RefSeq; NP_001305792.1; NM_001318863.1.
DR RefSeq; NP_550438.1; NM_080916.2. [Q16854-1]
DR RefSeq; NP_550440.1; NM_080918.2. [Q16854-2]
DR PDB; 2OCP; X-ray; 2.80 A; A/B/C/D/E/F/G/H=37-277.
DR PDBsum; 2OCP; -.
DR AlphaFoldDB; Q16854; -.
DR SMR; Q16854; -.
DR BioGRID; 108062; 86.
DR IntAct; Q16854; 56.
DR STRING; 9606.ENSP00000264093; -.
DR BindingDB; Q16854; -.
DR ChEMBL; CHEMBL5997; -.
DR DrugBank; DB01280; Nelarabine.
DR DrugCentral; Q16854; -.
DR iPTMnet; Q16854; -.
DR PhosphoSitePlus; Q16854; -.
DR BioMuta; DGUOK; -.
DR DMDM; 23503050; -.
DR EPD; Q16854; -.
DR jPOST; Q16854; -.
DR MassIVE; Q16854; -.
DR MaxQB; Q16854; -.
DR PaxDb; Q16854; -.
DR PeptideAtlas; Q16854; -.
DR PRIDE; Q16854; -.
DR ProteomicsDB; 61106; -. [Q16854-1]
DR ProteomicsDB; 61107; -. [Q16854-2]
DR ProteomicsDB; 61108; -. [Q16854-3]
DR ProteomicsDB; 61109; -. [Q16854-4]
DR ProteomicsDB; 61110; -. [Q16854-5]
DR ProteomicsDB; 68753; -.
DR Antibodypedia; 31404; 216 antibodies from 25 providers.
DR DNASU; 1716; -.
DR Ensembl; ENST00000264093.9; ENSP00000264093.4; ENSG00000114956.20. [Q16854-1]
DR Ensembl; ENST00000348222.3; ENSP00000306964.3; ENSG00000114956.20. [Q16854-2]
DR Ensembl; ENST00000418996.5; ENSP00000408209.1; ENSG00000114956.20. [Q16854-6]
DR Ensembl; ENST00000629438.2; ENSP00000487122.1; ENSG00000114956.20. [Q16854-6]
DR GeneID; 1716; -.
DR KEGG; hsa:1716; -.
DR MANE-Select; ENST00000264093.9; ENSP00000264093.4; NM_080916.3; NP_550438.1.
DR UCSC; uc002sjx.3; human. [Q16854-1]
DR CTD; 1716; -.
DR DisGeNET; 1716; -.
DR GeneCards; DGUOK; -.
DR GeneReviews; DGUOK; -.
DR HGNC; HGNC:2858; DGUOK.
DR HPA; ENSG00000114956; Low tissue specificity.
DR MalaCards; DGUOK; -.
DR MIM; 251880; phenotype.
DR MIM; 601465; gene.
DR MIM; 617068; phenotype.
DR MIM; 617070; phenotype.
DR neXtProt; NX_Q16854; -.
DR OpenTargets; ENSG00000114956; -.
DR Orphanet; 329314; Adult-onset multiple mitochondrial DNA deletion syndrome due to DGUOK deficiency.
DR Orphanet; 279934; Mitochondrial DNA depletion syndrome, hepatocerebral form due to DGUOK deficiency.
DR PharmGKB; PA27319; -.
DR VEuPathDB; HostDB:ENSG00000114956; -.
DR eggNOG; KOG4235; Eukaryota.
DR GeneTree; ENSGT00940000159627; -.
DR HOGENOM; CLU_030466_1_1_1; -.
DR InParanoid; Q16854; -.
DR OMA; LMIYLRC; -.
DR PhylomeDB; Q16854; -.
DR TreeFam; TF324413; -.
DR BioCyc; MetaCyc:HS03819-MON; -.
DR BRENDA; 2.7.1.113; 2681.
DR PathwayCommons; Q16854; -.
DR Reactome; R-HSA-74217; Purine salvage.
DR SABIO-RK; Q16854; -.
DR SignaLink; Q16854; -.
DR BioGRID-ORCS; 1716; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; DGUOK; human.
DR EvolutionaryTrace; Q16854; -.
DR GeneWiki; DGUOK; -.
DR GenomeRNAi; 1716; -.
DR Pharos; Q16854; Tbio.
DR PRO; PR:Q16854; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q16854; protein.
DR Bgee; ENSG00000114956; Expressed in adenohypophysis and 206 other tissues.
DR ExpressionAtlas; Q16854; baseline and differential.
DR Genevisible; Q16854; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004136; F:deoxyadenosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; IDA:UniProtKB.
DR GO; GO:0019136; F:deoxynucleoside kinase activity; IBA:GO_Central.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:Ensembl.
DR GO; GO:0106383; P:dAMP salvage; IDA:MGI.
DR GO; GO:0046070; P:dGTP metabolic process; IEA:Ensembl.
DR GO; GO:0008617; P:guanosine metabolic process; TAS:ProtInc.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0046122; P:purine deoxyribonucleoside metabolic process; IDA:UniProtKB.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Disease variant; Kinase; Mitochondrion; Neuropathy; Nucleotide-binding;
KW Primary mitochondrial disease; Progressive external ophthalmoplegia;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..277
FT /note="Deoxyguanosine kinase, mitochondrial"
FT /id="PRO_0000016840"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11427893,
FT ECO:0007744|PDB:2OCP"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11427893,
FT ECO:0007744|PDB:2OCP"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11427893,
FT ECO:0007744|PDB:2OCP"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11427893,
FT ECO:0007744|PDB:2OCP"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11427893,
FT ECO:0007744|PDB:2OCP"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11427893,
FT ECO:0007744|PDB:2OCP"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 206..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:11427893,
FT ECO:0007744|PDB:2OCP"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11427893,
FT ECO:0007744|PDB:2OCP"
FT BINDING 254..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 275
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 47
FT /note="I -> IGNILKQIRGRAPIQET (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003026"
FT VAR_SEQ 48..89
FT /note="AVGKSTFVKLLTKTYPEWHVATEPVATWQNIQAAGTQKACTA -> GLHCPK
FT SWKLAGYDVPGASTMVLHIPDIFLFEPPESTAGALP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056026"
FT VAR_SEQ 48..85
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003024"
FT VAR_SEQ 90..277
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056027"
FT VAR_SEQ 149..236
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003025"
FT VARIANT 44
FT /note="E -> K (in PEOB4; decreased protein levels;
FT dbSNP:rs762550967)"
FT /evidence="ECO:0000269|PubMed:23043144"
FT /id="VAR_076979"
FT VARIANT 46
FT /note="N -> S (in NCPH; impairs adenosine triphosphate
FT binding; reduction of activity; dbSNP:rs763615602)"
FT /evidence="ECO:0000269|PubMed:17073823,
FT ECO:0000269|PubMed:26874653"
FT /id="VAR_076980"
FT VARIANT 142
FT /note="R -> K (in MTDPS3; dbSNP:rs104893631)"
FT /evidence="ECO:0000269|PubMed:12205643"
FT /id="VAR_019417"
FT VARIANT 154
FT /note="N -> K (in PEOB4; decreased protein levels;
FT dbSNP:rs144181978)"
FT /evidence="ECO:0000269|PubMed:23043144"
FT /id="VAR_076981"
FT VARIANT 170
FT /note="Q -> R (unknown pathological significance;
FT dbSNP:rs74874677)"
FT /evidence="ECO:0000269|PubMed:23043144"
FT /id="VAR_076982"
FT VARIANT 227
FT /note="E -> K (in MTDPS3; dbSNP:rs104893632)"
FT /evidence="ECO:0000269|PubMed:12205643"
FT /id="VAR_019418"
FT VARIANT 250
FT /note="L -> S (in MTDPS3; significant reduction of
FT activity; dbSNP:rs749464475)"
FT /evidence="ECO:0000269|PubMed:15639197"
FT /id="VAR_023789"
FT VARIANT 266
FT /note="L -> R (reduction of activity; dbSNP:rs886037846)"
FT /evidence="ECO:0000269|PubMed:17073823"
FT /id="VAR_076983"
FT CONFLICT 83
FT /note="T -> N (in Ref. 1; AAC50624)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="G -> D (in Ref. 5; CAA66054)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="K -> E (in Ref. 5; CAA66054)"
FT /evidence="ECO:0000305"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:2OCP"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 103..123
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2OCP"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:2OCP"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:2OCP"
FT TURN 209..213
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 216..230
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2OCP"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:2OCP"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:2OCP"
FT HELIX 260..275
FT /evidence="ECO:0007829|PDB:2OCP"
SQ SEQUENCE 277 AA; 32056 MW; 53E4514BFC2CB5E5 CRC64;
MAAGRLFLSR LRAPFSSMAK SPLEGVSSSR GLHAGRGPRR LSIEGNIAVG KSTFVKLLTK
TYPEWHVATE PVATWQNIQA AGTQKACTAQ SLGNLLDMMY REPARWSYTF QTFSFLSRLK
VQLEPFPEKL LQARKPVQIF ERSVYSDRYI FAKNLFENGS LSDIEWHIYQ DWHSFLLWEF
ASRITLHGFI YLQASPQVCL KRLYQRAREE EKGIELAYLE QLHGQHEAWL IHKTTKLHFE
ALMNIPVLVL DVNDDFSEEV TKQEDLMREV NTFVKNL
