ID ADK_HUMAN Reviewed; 362 AA. AC P55263; B7Z783; B7Z800; O00741; O00742; Q16710; Q5JQ10; Q5JQ11; Q9BTN2; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 222. DE RecName: Full=Adenosine kinase; DE Short=AK; DE EC=2.7.1.20 {ECO:0000269|PubMed:21963049, ECO:0000269|PubMed:8577746, ECO:0000269|PubMed:9070863}; DE AltName: Full=Adenosine 5'-phosphotransferase; GN Name=ADK {ECO:0000312|HGNC:HGNC:257}; 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 2), PROTEIN SEQUENCE OF 94-133; 175-200 RP AND 272-289, CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC TISSUE=Liver; RX PubMed=8577746; DOI=10.1073/pnas.93.3.1232; RA Spychala J., Datta N.S., Takabayashi K., Datta M., Fox I.H., Gribbin T., RA Mitchell B.S.; RT "Cloning of human adenosine kinase cDNA: sequence similarity to microbial RT ribokinases and fructokinases."; RL Proc. Natl. Acad. Sci. U.S.A. 93:1232-1237(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8917457; DOI=10.1111/j.1432-1033.1996.00564.x; RA Singh B., Hao W., Wu Z.-C., Eigl B., Gupta R.S.; RT "Cloning and characterization of cDNA for adenosine kinase from mammalian RT (Chinese hamster, mouse, human and rat) species. High frequency mutants of RT Chinese hamster ovary cells involve structural alterations in the gene."; RL Eur. J. Biochem. 241:564-571(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, RP CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND RP TISSUE SPECIFICITY. RX PubMed=9070863; DOI=10.1006/bbrc.1997.6157; RA McNally T., Helfrich R.J., Cowart M., Dorwin S.A., Meuth J.L., Idler K.B., RA Klute K.A., Simmer R.L., Kowaluk E.A., Halbert D.N.; RT "Cloning and expression of the adenosine kinase gene from rat and human RT tissues."; RL Biochem. Biophys. Res. Commun. 231:645-650(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4). RC TISSUE=Mammary gland, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skin; 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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), NUCLEAR LOCALIZATION SIGNAL, AND RP MUTAGENESIS OF 11-LYS-LYS-12. RX PubMed=19635462; DOI=10.1016/j.bbrc.2009.07.106; RA Cui X.A., Singh B., Park J., Gupta R.S.; RT "Subcellular localization of adenosine kinase in mammalian cells: The long RT isoform of AdK is localized in the nucleus."; RL Biochem. Biophys. Res. Commun. 388:46-50(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF ISOFORM 2 IN COMPLEX WITH RP MAGNESIUM AND ADENOSINE. RX PubMed=9843365; DOI=10.1021/bi9815445; RA Mathews I.I., Erion M.D., Ealick S.E.; RT "Structure of human adenosine kinase at 1.5-A resolution."; RL Biochemistry 37:15607-15620(1998). RN [14] RP PHOSPHORYLATION AT TYR-77. RX PubMed=12112843; RX DOI=10.1002/1615-9861(200206)2:6<642::aid-prot642>3.0.co;2-i; RA Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G., RA Fitzgerald D.J.; RT "Identification of the phosphotyrosine proteome from thrombin activated RT platelets."; RL Proteomics 2:642-648(2002). RN [15] RP VARIANTS HMAKD GLU-30; ALA-235 AND GLU-318, CHARACTERIZATION OF VARIANTS RP HMAKD GLU-30; ALA-235 AND GLU-318, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=21963049; DOI=10.1016/j.ajhg.2011.09.004; RA Bjursell M.K., Blom H.J., Cayuela J.A., Engvall M.L., Lesko N., RA Balasubramaniam S., Brandberg G., Halldin M., Falkenberg M., Jakobs C., RA Smith D., Struys E., von Dobeln U., Gustafsson C.M., Lundeberg J., RA Wedell A.; RT "Adenosine kinase deficiency disrupts the methionine cycle and causes RT hypermethioninemia, encephalopathy, and abnormal liver function."; RL Am. J. Hum. Genet. 89:507-515(2011). CC -!- FUNCTION: Catalyzes the phosphorylation of the purine nucleoside CC adenosine at the 5' position in an ATP-dependent manner. Serves as a CC potential regulator of concentrations of extracellular adenosine and CC intracellular adenine nucleotides. {ECO:0000269|PubMed:21963049, CC ECO:0000269|PubMed:8577746, ECO:0000269|PubMed:9070863}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + ATP = ADP + AMP + H(+); Xref=Rhea:RHEA:20824, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.1.20; CC Evidence={ECO:0000269|PubMed:21963049, ECO:0000269|PubMed:8577746, CC ECO:0000269|PubMed:9070863}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20825; CC Evidence={ECO:0000305|PubMed:8577746}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:9070863}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:9070863}; CC -!- ACTIVITY REGULATION: Activity is inhibited by 5-iodotubercidin and 5'- CC amino-5'-deoxyadenosine. {ECO:0000269|PubMed:9070863}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]: CC Kinetic parameters: CC KM=41 nM for adenosine {ECO:0000269|PubMed:8577746}; CC KM=0.13 uM for ATP {ECO:0000269|PubMed:9070863}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]: CC Kinetic parameters: CC KM=0.12 uM for ATP {ECO:0000269|PubMed:9070863}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP CC from adenosine: step 1/1. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus CC {ECO:0000269|PubMed:19635462}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm CC {ECO:0000269|PubMed:19635462}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=AK-L, Long {ECO:0000303|PubMed:9070863}; CC IsoId=P55263-1; Sequence=Displayed; CC Name=2; Synonyms=AK-S, Short {ECO:0000303|PubMed:9070863}; CC IsoId=P55263-2; Sequence=VSP_046713; CC Name=3; CC IsoId=P55263-3; Sequence=VSP_043526; CC Name=4; CC IsoId=P55263-4; Sequence=VSP_004668; CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level in placenta, liver, CC muscle and kidney. {ECO:0000269|PubMed:9070863}. CC -!- DISEASE: Hypermethioninemia due to adenosine kinase deficiency (HMAKD) CC [MIM:614300]: A metabolic disorder characterized by global CC developmental delay, early-onset seizures, mild dysmorphic features, CC and characteristic biochemical anomalies, including persistent CC hypermethioninemia with increased levels of S-adenosylmethionine and S- CC adenosylhomocysteine. Homocysteine levels are typically normal. CC {ECO:0000269|PubMed:21963049}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB01689.1; Type=Frameshift; Evidence={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; U50196; AAA97893.1; -; mRNA. DR EMBL; U33936; AAB01689.1; ALT_FRAME; mRNA. DR EMBL; U90338; AAB50234.1; -; mRNA. DR EMBL; U90339; AAB50235.1; -; mRNA. DR EMBL; AK290633; BAF83322.1; -; mRNA. DR EMBL; AK301590; BAH13519.1; -; mRNA. DR EMBL; AK302706; BAH13786.1; -; mRNA. DR EMBL; AC012046; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC022026; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC022540; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC091699; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL357037; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL731576; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471083; EAW54555.1; -; Genomic_DNA. DR EMBL; CH471083; EAW54556.1; -; Genomic_DNA. DR EMBL; BC003568; AAH03568.1; -; mRNA. DR CCDS; CCDS55716.1; -. [P55263-3] DR CCDS; CCDS55717.1; -. [P55263-4] DR CCDS; CCDS7343.1; -. [P55263-1] DR CCDS; CCDS7344.1; -. [P55263-2] DR PIR; JC5363; JC5363. DR PIR; JC5364; JC5364. DR RefSeq; NP_001114.2; NM_001123.3. [P55263-2] DR RefSeq; NP_001189378.1; NM_001202449.1. [P55263-4] DR RefSeq; NP_001189379.1; NM_001202450.1. [P55263-3] DR RefSeq; NP_006712.2; NM_006721.3. [P55263-1] DR PDB; 1BX4; X-ray; 1.50 A; A=22-362. DR PDB; 2I6A; X-ray; 2.20 A; A/B/C/D=22-362. DR PDB; 2I6B; X-ray; 2.30 A; A/B=22-362. DR PDB; 4O1L; X-ray; 2.50 A; A/B=17-362. DR PDBsum; 1BX4; -. DR PDBsum; 2I6A; -. DR PDBsum; 2I6B; -. DR PDBsum; 4O1L; -. DR AlphaFoldDB; P55263; -. DR SMR; P55263; -. DR BioGRID; 106644; 51. DR IntAct; P55263; 8. DR MINT; P55263; -. DR STRING; 9606.ENSP00000443965; -. DR BindingDB; P55263; -. DR ChEMBL; CHEMBL3589; -. DR DrugBank; DB07280; 5-[4-(DIMETHYLAMINO)PHENYL]-6-[(6-MORPHOLIN-4-YLPYRIDIN-3-YL)ETHYNYL]PYRIMIDIN-4-AMINE. DR DrugBank; DB07173; 7-(5-DEOXY-BETA-D-RIBOFURANOSYL)-5-IODO-7H-PYRROLO[2,3-D]PYRIMIDIN-4-AMINE. DR DrugBank; DB01048; Abacavir. DR DrugBank; DB00640; Adenosine. DR DrugBank; DB00131; Adenosine phosphate. DR DrugBank; DB00171; ATP. DR DrugBank; DB00811; Ribavirin. DR DrugCentral; P55263; -. DR GuidetoPHARMACOLOGY; 1231; -. DR GlyGen; P55263; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P55263; -. DR MetOSite; P55263; -. DR PhosphoSitePlus; P55263; -. DR SwissPalm; P55263; -. DR BioMuta; ADK; -. DR DMDM; 6840802; -. DR REPRODUCTION-2DPAGE; IPI00234368; -. DR CPTAC; CPTAC-162; -. DR CPTAC; CPTAC-2925; -. DR CPTAC; CPTAC-2926; -. DR EPD; P55263; -. DR jPOST; P55263; -. DR MassIVE; P55263; -. DR MaxQB; P55263; -. DR PaxDb; 9606-ENSP00000286621; -. DR PeptideAtlas; P55263; -. DR ProteomicsDB; 56823; -. [P55263-1] DR ProteomicsDB; 56824; -. [P55263-2] DR ProteomicsDB; 56825; -. [P55263-3] DR ProteomicsDB; 6910; -. DR Pumba; P55263; -. DR Antibodypedia; 29612; 511 antibodies from 37 providers. DR DNASU; 132; -. DR Ensembl; ENST00000372734.5; ENSP00000361819.3; ENSG00000156110.15. [P55263-2] DR Ensembl; ENST00000539909.6; ENSP00000443965.2; ENSG00000156110.15. [P55263-1] DR Ensembl; ENST00000672429.1; ENSP00000500292.1; ENSG00000156110.15. [P55263-3] DR Ensembl; ENST00000673027.1; ENSP00000500201.1; ENSG00000156110.15. [P55263-4] DR GeneID; 132; -. DR KEGG; hsa:132; -. DR MANE-Select; ENST00000539909.6; ENSP00000443965.2; NM_006721.4; NP_006712.2. DR UCSC; uc001jwi.4; human. [P55263-1] DR AGR; HGNC:257; -. DR CTD; 132; -. DR DisGeNET; 132; -. DR GeneCards; ADK; -. DR HGNC; HGNC:257; ADK. DR HPA; ENSG00000156110; Tissue enhanced (liver). DR MalaCards; ADK; -. DR MIM; 102750; gene. DR MIM; 614300; phenotype. DR neXtProt; NX_P55263; -. DR OpenTargets; ENSG00000156110; -. DR Orphanet; 289290; Hypermethioninemia encephalopathy due to adenosine kinase deficiency. DR PharmGKB; PA24579; -. DR VEuPathDB; HostDB:ENSG00000156110; -. DR eggNOG; KOG2854; Eukaryota. DR GeneTree; ENSGT00390000014320; -. DR HOGENOM; CLU_045832_0_0_1; -. DR InParanoid; P55263; -. DR OMA; HASAQNC; -. DR OrthoDB; 22683at2759; -. DR PhylomeDB; P55263; -. DR TreeFam; TF300745; -. DR BioCyc; MetaCyc:HS08097-MONOMER; -. DR BRENDA; 2.7.1.20; 2681. DR PathwayCommons; P55263; -. DR Reactome; R-HSA-74217; Purine salvage. DR Reactome; R-HSA-9755088; Ribavirin ADME. DR SABIO-RK; P55263; -. DR SignaLink; P55263; -. DR SIGNOR; P55263; -. DR UniPathway; UPA00588; UER00659. DR BioGRID-ORCS; 132; 11 hits in 1173 CRISPR screens. DR ChiTaRS; ADK; human. DR EvolutionaryTrace; P55263; -. DR GeneWiki; ADK_(gene); -. DR GenomeRNAi; 132; -. DR Pharos; P55263; Tchem. DR PRO; PR:P55263; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P55263; Protein. DR Bgee; ENSG00000156110; Expressed in cartilage tissue and 202 other cell types or tissues. DR ExpressionAtlas; P55263; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0004001; F:adenosine kinase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004136; F:deoxyadenosine kinase activity; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0106383; P:dAMP salvage; IEA:Ensembl. DR GO; GO:0006175; P:dATP biosynthetic process; IEA:Ensembl. DR GO; GO:0032263; P:GMP salvage; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; TAS:ProtInc. DR CDD; cd01168; adenosine_kinase; 1. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR001805; Adenokinase. DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR029056; Ribokinase-like. DR PANTHER; PTHR45769; ADENOSINE KINASE; 1. DR PANTHER; PTHR45769:SF3; ADENOSINE KINASE; 1. DR Pfam; PF00294; PfkB; 1. DR PRINTS; PR00989; ADENOKINASE. DR SUPFAM; SSF53613; Ribokinase-like; 1. DR PROSITE; PS00584; PFKB_KINASES_2; 1. DR Genevisible; P55263; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm; KW Direct protein sequencing; Disease variant; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Purine salvage; KW Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..362 FT /note="Adenosine kinase" FT /id="PRO_0000080053" FT MOTIF 8..16 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:19635462" FT ACT_SITE 317 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:9843365, FT ECO:0007744|PDB:1BX4" FT BINDING 35 FT /ligand="adenosine" FT /ligand_id="ChEBI:CHEBI:16335" FT /evidence="ECO:0000269|PubMed:9843365, FT ECO:0007744|PDB:1BX4" FT BINDING 49 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:9843365, FT ECO:0007744|PDB:1BX4" FT BINDING 147 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:9843365, FT ECO:0007744|PDB:1BX4" FT BINDING 148 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:9843365, FT ECO:0007744|PDB:1BX4" FT BINDING 306 FT /ligand="adenosine" FT /ligand_id="ChEBI:CHEBI:16335" FT /evidence="ECO:0000269|PubMed:9843365, FT ECO:0007744|PDB:1BX4" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 77 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:12112843" FT VAR_SEQ 1..65 FT /note="MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKP FT NDQILAEDKHKEL -> MTSVRENILFGMGNPLLDISAVVDKDFLDK (in isoform FT 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_004668" FT VAR_SEQ 1..21 FT /note="MAAAEEEPKPKKLKVEAPQAL -> MTSV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8577746, FT ECO:0000303|PubMed:9070863" FT /id="VSP_046713" FT VAR_SEQ 186..242 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043526" FT VARIANT 30 FT /note="G -> E (in HMAKD; the mutant shows some residual FT adenosine kinase activity; dbSNP:rs397514454)" FT /evidence="ECO:0000269|PubMed:21963049" FT /id="VAR_066640" FT VARIANT 235 FT /note="D -> A (in HMAKD; the mutant shows some residual FT adenosine kinase activity; dbSNP:rs397514453)" FT /evidence="ECO:0000269|PubMed:21963049" FT /id="VAR_066641" FT VARIANT 318 FT /note="A -> E (in HMAKD; complete loss of adenosine kinase FT activity; dbSNP:rs397514452)" FT /evidence="ECO:0000269|PubMed:21963049" FT /id="VAR_066642" FT MUTAGEN 11..12 FT /note="KK->AA,AD: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:19635462" FT CONFLICT 98 FT /note="H -> A (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 133 FT /note="N -> D (in Ref. 2; AAB01689)" FT /evidence="ECO:0000305" FT CONFLICT 171 FT /note="K -> R (in Ref. 2; AAB01689)" FT /evidence="ECO:0000305" FT CONFLICT 190 FT /note="T -> H (in Ref. 1; AAA97893)" FT /evidence="ECO:0000305" FT CONFLICT 219 FT /note="I -> F (in Ref. 7; AAH03568)" FT /evidence="ECO:0000305" FT CONFLICT 273 FT /note="S -> V (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 289 FT /note="I -> N (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 307 FT /note="K -> R (in Ref. 2; AAB01689)" FT /evidence="ECO:0000305" FT STRAND 26..29 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 33..39 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 42..47 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 52..57 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 63..72 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 82..94 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:2I6B" FT STRAND 101..110 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 111..122 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 126..135 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 139..145 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 156..160 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:1BX4" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 170..178 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 180..185 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 186..190 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 193..205 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 209..213 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 217..222 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 224..230 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 235..240 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 241..250 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 258..266 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 278..283 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 286..291 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 312..327 FT /evidence="ECO:0007829|PDB:1BX4" FT TURN 328..330 FT /evidence="ECO:0007829|PDB:1BX4" FT HELIX 333..347 FT /evidence="ECO:0007829|PDB:1BX4" FT STRAND 350..353 FT /evidence="ECO:0007829|PDB:1BX4" SQ SEQUENCE 362 AA; 40545 MW; 48AA4925865BFE70 CRC64; MAAAEEEPKP KKLKVEAPQA LRENILFGMG NPLLDISAVV DKDFLDKYSL KPNDQILAED KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA ATFFGCIGID KFGEILKRKA AEAHVDAHYY EQNEQPTGTC AACITGDNRS LIANLAAANC YKKEKHLDLE KNWMLVEKAR VCYIAGFFLT VSPESVLKVA HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN ETEAATFARE QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR TGCTFPEKPD FH //