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 24-JAN-2024, entry version 206. 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 NCPH1 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; LYS-154 AND ARG-170, RP CHARACTERIZATION OF VARIANTS PEOB4 LYS-44 AND LYS-154, 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 NCPH1, AND VARIANT NCPH1 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, 1 (NCPH1) [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. NCPH1 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 91. 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; 9606-ENSP00000264093; -. DR PeptideAtlas; 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 Pumba; Q16854; -. DR Antibodypedia; 31404; 240 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 AGR; HGNC:2858; -. 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; DWHTFLL; -. DR OrthoDB; 315858at2759; -. DR PhylomeDB; Q16854; -. DR TreeFam; TF324413; -. DR BioCyc; MetaCyc:HS03819-MONOMER; -. 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; 16 hits in 1163 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 208 other cell types or tissues. DR ExpressionAtlas; Q16854; baseline and differential. 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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0046122; P:purine deoxyribonucleoside metabolic process; IDA:UniProtKB. DR CDD; cd01673; dNK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR002624; DCK/DGK. DR InterPro; IPR031314; DNK_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10513:SF8; DEOXYGUANOSINE KINASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1. DR Pfam; PF01712; dNK; 1. DR PIRSF; PIRSF000705; DNK; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q16854; HS. 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 NCPH1; 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 (in PEOB4; likely benign; 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 //