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 02-SEP-2026, entry version 232. DE RecName: Full=Adenosine kinase {ECO:0000303|PubMed:6246102}; DE Short=AK; DE EC=2.7.1.20 {ECO:0000269|PubMed:21963049, ECO:0000269|PubMed:6246102, ECO:0000269|PubMed:8577746, ECO:0000269|PubMed:9070863}; DE AltName: Full=Adenosine 5'-phosphotransferase; DE AltName: Full=N6,N6-dimethyladenosine kinase {ECO:0000305}; DE EC=2.7.1.- {ECO:0000269|PubMed:40840445}; DE AltName: Full=N6-isopentenyladenosine kinase {ECO:0000305}; DE EC=2.7.1.- {ECO:0000269|PubMed:40840445}; DE AltName: Full=N6-methyladenosine kinase {ECO:0000305}; DE EC=2.7.1.- {ECO:0000269|PubMed:40840445}; GN Name=ADK {ECO:0000303|PubMed:19635462, 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, SUBCELLULAR LOCATION, AND RP BIOPHYSICOCHEMICAL 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, RP PATHWAY, AND 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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR. RX PubMed=6246102; DOI=10.1016/s0021-9258(19)70780-7; RA Palella T.D., Andres C.M., Fox I.H.; RT "Human placental adenosine kinase. Kinetic mechanism and inhibition."; RL J. Biol. Chem. 255:5264-5269(1980). RN [9] 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 [10] 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LEU-33; ASP-35; LEU-57; RP ALA-153; LEU-155; PHE-187; PHE-218; ASN-313 AND ASP-317, AND RP CHARACTERIZATION OF VARIANTS HMAKD GLU-30; ALA-235; GLU-318; SER-319 AND RP ARG-341. RX PubMed=40840445; DOI=10.1016/j.cell.2025.07.041; RA Ogawa A., Watanabe S., Ozerova I., Tsai A.Y., Kuchitsu Y., Chong H.B., RA Kawakami T., Fuse J., Han W., Kudo R., Naito T., Sato K., Nakazawa T., RA Saheki Y., Hirayama A., Stadler P.F., Arisawa M., Araki K., Bar-Peled L., RA Taguchi T., Sawa S., Inaba K., Wei F.Y.; RT "Adenosine kinase and ADAL coordinate detoxification of modified adenosines RT to safeguard metabolism."; RL Cell 0:0-0(2025). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF ISOFORM 2 IN COMPLEX WITH RP MAGNESIUM AND ADENOSINE, ACTIVE SITE, AND SUBUNIT. 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 [17] {ECO:0007744|PDB:2I6A, ECO:0007744|PDB:2I6B} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-362, AND ACTIVITY REGULATION. RX PubMed=17154503; DOI=10.1021/jm060189a; RA Muchmore S.W., Smith R.A., Stewart A.O., Cowart M.D., Gomtsyan A., RA Matulenko M.A., Yu H., Severin J.M., Bhagwat S.S., Lee C.H., Kowaluk E.A., RA Jarvis M.F., Jakob C.L.; RT "Crystal structures of human adenosine kinase inhibitor complexes reveal RT two distinct binding modes."; RL J. Med. Chem. 49:6726-6731(2006). RN [18] 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). RN [19] RP VARIANT HMAKD 177-GLU--HIS-362 DEL. RX PubMed=27500280; DOI=10.12715/ard.2014.3.2; RA Shakiba M., Mahjoub F., Fazilaty H., Rezagholizadeh F., Shakiba A., RA Ziadlou M., Gahl W.A., Behnam B.; RT "Adenosine kinase deficiency with neurodevelopemental delay and recurrent RT hepatic dysfunction: A case report."; RL Adv. Rare Dis. 3:0-0(2016). RN [20] RP VARIANTS HMAKD 84-GLN--HIS-362 DEL; SER-319; 326-GLN--HIS-362 DEL AND RP ARG-341. RX PubMed=26642971; DOI=10.1007/s10545-015-9904-y; RA Staufner C., Lindner M., Dionisi-Vici C., Freisinger P., Dobbelaere D., RA Douillard C., Makhseed N., Straub B.K., Kahrizi K., Ballhausen D., RA la Marca G., Koelker S., Haas D., Hoffmann G.F., Gruenert S.C., Blom H.J.; RT "Adenosine kinase deficiency: expanding the clinical spectrum and RT evaluating therapeutic options."; RL J. Inherit. Metab. Dis. 39:273-283(2016). RN [21] RP VARIANT HMAKD THR-172. RX PubMed=39899686; DOI=10.1097/mph.0000000000002993; RA Oez A., Oezdemir A.M., Ceylaner S., Aydin S.; RT "Rare etiology of isolated macrocytosis: adenosine kinase deficiency with a RT novel mutation."; RL J. Pediatr. Hematol. Oncol. 47:e96-e98(2025). RN [22] RP VARIANTS HMAKD 173-TRP--HIS-362 DEL AND 277-ARG--HIS-362 DEL. RX PubMed=33309011; DOI=10.1016/j.ymgme.2020.11.007; RA Becker P.H., Demir Z., Mozer Glassberg Y., Sevin C., Habes D., Imbard A., RA Mussini C., Rozenfeld Bar Lev M., Davit-Spraul A., Benoist J.F., RA Therond P., Slama A., Jacquemin E., Gonzales E., Gaignard P.; RT "Adenosine kinase deficiency: Three new cases and diagnostic value of RT hypermethioninemia."; RL Mol. Genet. Metab. 132:38-43(2021). CC -!- FUNCTION: Adenosine kinase that mediates the phosphorylation of the CC purine nucleoside adenosine at the 5' position in an ATP-dependent CC manner: catalyzes phosphorylation of both unmodified and modified CC adenosines (PubMed:21963049, PubMed:40840445, PubMed:6246102, CC PubMed:8577746, PubMed:9070863). Plays a key role in the detoxification CC of modified adenosines containing N(6)-methylated adenine (m6A) post- CC transcriptional modification (PubMed:40840445). Modified nucleosides CC are derived from the degradation of RNAs (mRNAs, rRNAs and tRNAs) and CC possess intrinsic cytotoxicity and must be cleared to prevent metabolic CC dysfunction (PubMed:40840445). Catalyzes the phosphorylation of the CC free cytosolic methylated adenosine nucleotides N(6)-methyladenosine CC (m6A), N(6),N(6)-dimethyladenosine (m6,6A) and N(6)- CC isopentenyladenosine (i6A) into adenosine monophosphate (AMP) CC intermediates that are further detoxified by MAPDA/ADAL CC (PubMed:40840445). {ECO:0000269|PubMed:21963049, CC ECO:0000269|PubMed:40840445, ECO:0000269|PubMed:6246102, CC ECO:0000269|PubMed:8577746, ECO:0000269|PubMed:9070863}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + ATP = AMP + ADP + 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:40840445, CC ECO:0000269|PubMed:6246102, 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 -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-methyladenosine + ATP = N(6)-methyl-AMP + ADP + H(+); CC Xref=Rhea:RHEA:86211, ChEBI:CHEBI:15378, ChEBI:CHEBI:21891, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:144842, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:40840445}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86212; CC Evidence={ECO:0000269|PubMed:40840445}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6),N(6)-dimethyladenosine + ATP = N(6),N(6)-dimethyl-AMP + CC ADP + H(+); Xref=Rhea:RHEA:86215, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28284, ChEBI:CHEBI:30616, ChEBI:CHEBI:235457, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:40840445}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86216; CC Evidence={ECO:0000269|PubMed:40840445}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-(dimethylallyl)adenosine + ATP = N(6)- CC (dimethylallyl)adenosine 5'-phosphate + ADP + H(+); CC Xref=Rhea:RHEA:86219, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57526, ChEBI:CHEBI:62881, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:40840445}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86220; CC Evidence={ECO:0000269|PubMed:40840445}; CC -!- CATALYTIC ACTIVITY: [Isoform 1]: CC Reaction=N(6)-methyladenosine + ATP = N(6)-methyl-AMP + ADP + H(+); CC Xref=Rhea:RHEA:86211, ChEBI:CHEBI:15378, ChEBI:CHEBI:21891, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:144842, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:40840445}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86212; CC Evidence={ECO:0000269|PubMed:40840445}; CC -!- CATALYTIC ACTIVITY: [Isoform 1]: CC Reaction=N(6),N(6)-dimethyladenosine + ATP = N(6),N(6)-dimethyl-AMP + CC ADP + H(+); Xref=Rhea:RHEA:86215, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28284, ChEBI:CHEBI:30616, ChEBI:CHEBI:235457, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:40840445}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86216; CC Evidence={ECO:0000269|PubMed:40840445}; CC -!- CATALYTIC ACTIVITY: [Isoform 1]: CC Reaction=N(6)-(dimethylallyl)adenosine + ATP = N(6)- CC (dimethylallyl)adenosine 5'-phosphate + ADP + H(+); CC Xref=Rhea:RHEA:86219, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57526, ChEBI:CHEBI:62881, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:40840445}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86220; CC Evidence={ECO:0000269|PubMed:40840445}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=N(6)-methyladenosine + ATP = N(6)-methyl-AMP + ADP + H(+); CC Xref=Rhea:RHEA:86211, ChEBI:CHEBI:15378, ChEBI:CHEBI:21891, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:144842, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:40840445}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86212; CC Evidence={ECO:0000269|PubMed:40840445}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=N(6),N(6)-dimethyladenosine + ATP = N(6),N(6)-dimethyl-AMP + CC ADP + H(+); Xref=Rhea:RHEA:86215, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28284, ChEBI:CHEBI:30616, ChEBI:CHEBI:235457, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:40840445}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86216; CC Evidence={ECO:0000269|PubMed:40840445}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=N(6)-(dimethylallyl)adenosine + ATP = N(6)- CC (dimethylallyl)adenosine 5'-phosphate + ADP + H(+); CC Xref=Rhea:RHEA:86219, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57526, ChEBI:CHEBI:62881, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:40840445}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86220; CC Evidence={ECO:0000269|PubMed:40840445}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:6246102, 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 (PubMed:17154503, PubMed:9070863). Also CC inhibited by 5-(4-(Dimethylamino)phenyl)-6-(6-morpholin- 4-ylpyridin-3- CC ylethynyl)pyrimidin-4-ylamine, a alkynylpyrimidine class small-molecule CC (PubMed:17154503). {ECO:0000269|PubMed:17154503, CC ECO:0000269|PubMed:9070863}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.4 uM for adenosine {ECO:0000269|PubMed:6246102}; CC KM=10 uM for adenosine {ECO:0000269|PubMed:40840445}; CC KM=15 uM for N(6)-methyladenosine (m6A) CC {ECO:0000269|PubMed:40840445}; CC KM=6.1 uM for N(6),N(6)-dimethyladenosine (m6,6A) CC {ECO:0000269|PubMed:40840445}; CC KM=10 uM for N(6)-isopentenyladenosine (i6A) CC {ECO:0000269|PubMed:40840445}; CC Note=kcat is 0.19 sec(-1) with adenosine as substrate. kcat is 0.28 CC sec(-1) with N(6)-methyladenosine (m6A) as substrate. kcat is 0.27 CC sec(-1) with N(6),N(6)-dimethyladenosine as substrate. kcat is 0.18 CC sec(-1) with N(6)-isopentenyladenosine (i6A) as substrate.; CC pH dependence: CC Optimum pH is 6.5. {ECO:0000269|PubMed:6246102}; 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. {ECO:0000305|PubMed:9070863}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9843365}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:8577746}. 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, ECO:0000269|PubMed:26642971, CC ECO:0000269|PubMed:27500280, ECO:0000269|PubMed:33309011, CC ECO:0000269|PubMed:39899686, ECO:0000269|PubMed:40840445}. Note=The CC disease is caused by variants affecting the gene represented in this CC 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_001123.4. [P55263-2] DR RefSeq; NP_001189378.1; NM_001202449.2. [P55263-4] DR RefSeq; NP_001189379.1; NM_001202450.2. [P55263-3] DR RefSeq; NP_006712.2; NM_006721.4. [P55263-1] DR PDB; 1BX4; X-ray; 1.50 A; A=20-362. DR PDB; 2I6A; X-ray; 2.20 A; A/B/C/D=20-362. DR PDB; 2I6B; X-ray; 2.30 A; A/B=20-362. DR PDB; 4O1L; X-ray; 2.50 A; A/B=17-362. DR PDB; 9O7P; X-ray; 2.51 A; A=20-362. DR PDB; 9O7Q; X-ray; 2.81 A; A=20-362. DR PDB; 9O7R; X-ray; 2.41 A; A=20-362. DR AlphaFoldDB; P55263; -. DR SMR; P55263; -. DR BioGRID; 106644; 63. DR FunCoup; P55263; 3281. DR IntAct; P55263; 22. DR MINT; P55263; -. DR NDEx; IQUERY-CP-ADK; 1 NDEx IQuery Curated Pathway. 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 jPOST; P55263; -. DR MassIVE; P55263; -. DR PaxDb; 9606-ENSP00000443965; -. 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; 469 antibodies from 40 providers. DR DNASU; 132; -. DR Ensembl; ENST00000372734.5; ENSP00000361819.3; ENSG00000156110.16. [P55263-2] DR Ensembl; ENST00000539909.6; ENSP00000443965.2; ENSG00000156110.16. [P55263-1] DR Ensembl; ENST00000672429.1; ENSP00000500292.1; ENSG00000156110.16. [P55263-3] DR Ensembl; ENST00000673027.1; ENSP00000500201.1; ENSG00000156110.16. [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 ClinPGx; PA24579; -. 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 OpenTargets; ENSG00000156110; -. DR Orphanet; 289290; Hypermethioninemia encephalopathy due to adenosine kinase deficiency. DR VEuPathDB; HostDB:ENSG00000156110; -. DR eggNOG; KOG2854; Eukaryota. DR GeneTree; ENSGT00390000014320; -. DR HOGENOM; CLU_045832_0_0_1; -. DR InParanoid; P55263; -. DR OMA; YCATECI; -. DR OrthoDB; 432447at2759; -. DR PAN-GO; P55263; 4 GO annotations based on evolutionary models. DR PhylomeDB; P55263; -. 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 Agora; ENSG00000156110; -. DR BioGRID-ORCS; 132; 11 hits in 1173 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. 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:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0004001; F:adenosine kinase activity; IDA:UniProtKB. DR GO; GO:0004136; F:deoxyadenosine kinase activity; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0032263; P:GMP salvage; IEA:Ensembl. DR GO; GO:0006144; P:purine nucleobase metabolic process; IDA:UniProtKB. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:InterPro. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; TAS:ProtInc. DR GO; GO:0110052; P:toxic metabolite repair; IDA:UniProtKB. DR CDD; cd01168; adenosine_kinase; 1. DR DisProt; DP03960; -. DR FunFam; 3.40.1190.20:FF:000175; Adenosine kinase; 1. DR FunFam; 3.30.1110.10:FF:000001; Adenosine kinase a; 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 PDBsum; 1BX4; -. DR PDBsum; 2I6A; -. DR PDBsum; 2I6B; -. DR PDBsum; 4O1L; -. DR PDBsum; 9O7P; -. DR PDBsum; 9O7Q; -. DR PDBsum; 9O7R; -. 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; KW Proteomics identification; Purine salvage; 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 31 FT /ligand="adenosine" FT /ligand_id="ChEBI:CHEBI:16335" 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 81 FT /ligand="adenosine" FT /ligand_id="ChEBI:CHEBI:16335" FT /evidence="ECO:0000269|PubMed:9843365, FT ECO:0007744|PDB:1BX4" FT BINDING 85 FT /ligand="adenosine" FT /ligand_id="ChEBI:CHEBI:16335" 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 317 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; abolished ability to mediate FT phosphorylation of unmodified and modified adenosines; FT dbSNP:rs397514454)" FT /evidence="ECO:0000269|PubMed:21963049, FT ECO:0000269|PubMed:40840445" FT /id="VAR_066640" FT VARIANT 84..362 FT /note="Missing (in HMAKD)" FT /evidence="ECO:0000269|PubMed:26642971" FT /id="VAR_091016" FT VARIANT 172 FT /note="N -> T (in HMAKD; uncertain significance)" FT /evidence="ECO:0000269|PubMed:39899686" FT /id="VAR_091017" FT VARIANT 173..362 FT /note="Missing (in HMAKD)" FT /evidence="ECO:0000269|PubMed:33309011" FT /id="VAR_091018" FT VARIANT 177..362 FT /note="Missing (in HMAKD)" FT /evidence="ECO:0000269|PubMed:27500280" FT /id="VAR_091019" FT VARIANT 235 FT /note="D -> A (in HMAKD; abolished ability to mediate FT phosphorylation of unmodified and modified adenosines; FT dbSNP:rs397514453)" FT /evidence="ECO:0000269|PubMed:21963049, FT ECO:0000269|PubMed:40840445" FT /id="VAR_066641" FT VARIANT 277..362 FT /note="Missing (in HMAKD)" FT /evidence="ECO:0000269|PubMed:33309011" FT /id="VAR_091020" FT VARIANT 318 FT /note="A -> E (in HMAKD; abolished ability to mediate FT phosphorylation of unmodified and modified adenosines; FT dbSNP:rs397514452)" FT /evidence="ECO:0000269|PubMed:21963049, FT ECO:0000269|PubMed:40840445" FT /id="VAR_066642" FT VARIANT 319 FT /note="F -> S (in HMAKD; abolished ability to mediate FT phosphorylation of unmodified and modified adenosines)" FT /evidence="ECO:0000269|PubMed:26642971, FT ECO:0000269|PubMed:40840445" FT /id="VAR_091021" FT VARIANT 326..362 FT /note="Missing (in HMAKD)" FT /evidence="ECO:0000269|PubMed:26642971" FT /id="VAR_091022" FT VARIANT 341 FT /note="H -> R (in HMAKD; decreased ability to mediate FT phosphorylation of unmodified and modified adenosines; FT dbSNP:rs886039772)" FT /evidence="ECO:0000269|PubMed:26642971, FT ECO:0000269|PubMed:40840445" FT /id="VAR_091023" FT MUTAGEN 11..12 FT /note="KK->AA,AD: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:19635462" FT MUTAGEN 33 FT /note="L->A: Abolished ability to mediate phosphorylation FT of unmodified and modified adenosines." FT /evidence="ECO:0000269|PubMed:40840445" FT MUTAGEN 35 FT /note="D->A: Abolished ability to mediate phosphorylation FT of unmodified and modified adenosines." FT /evidence="ECO:0000269|PubMed:40840445" FT MUTAGEN 57 FT /note="L->A: Abolished ability to mediate phosphorylation FT of unmodified and modified adenosines." FT /evidence="ECO:0000269|PubMed:40840445" FT MUTAGEN 153 FT /note="A->T: Increased ability to phosphorylate FT N(6)-methyladenosine (m6A), N(6),N(6)-dimethyladenosine FT (m6,6A), N(6)-isopentenyladenosine (i6A) and adenosine." FT /evidence="ECO:0000269|PubMed:40840445" FT MUTAGEN 155 FT /note="L->A: Decreased ability to phosphorylate FT N(6),N(6)-dimethyladenosine (m6,6A) and FT N(6)-isopentenyladenosine (i6A), but not FT N(6)-methyladenosine (m6A) or adenosine." FT /evidence="ECO:0000269|PubMed:40840445" FT MUTAGEN 187 FT /note="F->L: Abolished ability to mediate phosphorylation FT of unmodified and modified adenosines." FT /evidence="ECO:0000269|PubMed:40840445" FT MUTAGEN 218 FT /note="F->A: Decreased ability to phosphorylate FT N(6)-methyladenosine (m6A) and N(6),N(6)-dimethyladenosine FT (m6,6A)." FT /evidence="ECO:0000269|PubMed:40840445" FT MUTAGEN 313 FT /note="N->A: Decreased ability to phosphorylate FT N(6),N(6)-dimethyladenosine (m6,6A) and FT N(6)-isopentenyladenosine (i6A)." FT /evidence="ECO:0000269|PubMed:40840445" FT MUTAGEN 317 FT /note="D->A: Abolished ability to mediate phosphorylation FT of unmodified and modified adenosines." FT /evidence="ECO:0000269|PubMed:40840445" 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 HELIX 136..138 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 300..302 FT /evidence="ECO:0007829|PDB:2I6A" 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 //