ID ADK_HUMAN STANDARD; PRT; 362 AA. AC P55263; O00741; O00742; Q16710; Q9BTN2; DT 01-OCT-1996 (Rel. 34, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Adenosine kinase (EC 2.7.1.20) (AK) (Adenosine 5'-phosphotransferase). GN ADK. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 94-133; 175-200 AND 272-289. RC TISSUE=Liver; RX MEDLINE=96165550; PubMed=8577746; RA Spychala J., Datta N.S., Takabayashi K., Datta M., Fox I.H., RA Gribbin T., Mitchell B.S.; RT "Cloning of human adenosine kinase cDNA: sequence similarity to RT microbial ribokinases and fructokinases."; RL Proc. Natl. Acad. Sci. U.S.A. 93:1232-1237(1996). RN [2] RP SEQUENCE FROM N.A., AND CHARACTERIZATION. RX MEDLINE=97075030; PubMed=8917457; RA Singh B., Hao W., Wu Z.-C., Eigl B., Gupta R.S.; RT "Cloning and characterization of cDNA for adenosine kinase from RT mammalian (Chinese hamster, mouse, human and rat) species. High RT frequency mutants of Chinese hamster ovary cells involve structural RT alterations in the gene."; RL Eur. J. Biochem. 241:564-571(1996). RN [3] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=97224402; PubMed=9070863; RA McNally T., Helfrich R.J., Cowart M., Dorwin S.A., Meuth J.L., RA Idler K.B., Klute K.A., Simmer R.L., Kowaluk E.A., Halbert D.N.; RT "Cloning and expression of the adenosine kinase gene from rat and RT human tissues."; RL Biochem. Biophys. Res. Commun. 231:645-650(1997). RN [4] RP SEQUENCE FROM N.A. (ISOFORM SHORT). RC TISSUE=Skin; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF SHORT ISOFORM. RX MEDLINE=99060037; PubMed=9843365; 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 [6] RP PHOSPHORYLATION OF TYR-77. RX MEDLINE=22107313; PubMed=12112843; 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 RT activated platelets."; RL Proteomics 2:642-648(2002). CC -!- FUNCTION: ATP dependent phosphorylation of adenosine and other CC related nucleoside analogs to monophosphate derivatives. Serves as CC a potential regulator of concentrations of extracellular adenosine CC and intracellular adenine nucleotides. CC -!- CATALYTIC ACTIVITY: ATP + adenosine = ADP + AMP. CC -!- COFACTOR: Magnesium. CC -!- PATHWAY: Purine salvage. CC -!- SUBUNIT: Monomer. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P55263-1; Sequence=Displayed; CC Name=Short; CC IsoId=P55263-2; Sequence=VSP_004668; CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level in placenta, CC liver, muscle and kidney. CC -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family. CC -!- CAUTION: Ref.2 sequence differs from that shown due to a CC frameshift in position 17. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U50196; AAA97893.1; -. DR EMBL; U33936; AAB01689.1; ALT_FRAME. DR EMBL; U90338; AAB50234.1; -. DR EMBL; U90339; AAB50235.1; -. DR EMBL; BC003568; AAH03568.1; -. DR PIR; JC5363; JC5363. DR PIR; JC5364; JC5364. DR PDB; 1BX4; 13-OCT-99. DR Genew; HGNC:257; ADK. DR GK; P55263; -. DR MIM; 102750; -. DR GO; GO:0004001; F:adenosine kinase activity; TAS. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthesis; TAS. DR InterPro; IPR001805; Adenokinase. DR InterPro; IPR002173; PfkB. DR Pfam; PF00294; pfkB; 1. DR PRINTS; PR00989; ADENOKINASE. DR PROSITE; PS00583; PFKB_KINASES_1; FALSE_NEG. DR PROSITE; PS00584; PFKB_KINASES_2; 1. KW Transferase; Kinase; Purine salvage; Magnesium; Alternative splicing; KW Phosphorylation; 3D-structure. FT ACT_SITE 317 317 FT MOD_RES 77 77 PHOSPHORYLATION. FT VARSPLIC 1 21 MAAAEEEPKPKKLKVEAPQAL -> MTSV (in isoform FT Short). FT /FTId=VSP_004668. FT CONFLICT 21 21 L -> V (in Ref. 2). FT CONFLICT 98 98 H -> A (IN REF. 1; AA SEQUENCE). FT CONFLICT 133 133 N -> D (in Ref. 2). FT CONFLICT 171 171 K -> R (in Ref. 2). FT CONFLICT 190 190 T -> H (in Ref. 1). FT CONFLICT 219 219 I -> F (in Ref. 4). FT CONFLICT 273 273 S -> V (IN REF. 1; AA SEQUENCE). FT CONFLICT 289 289 I -> N (IN REF. 1; AA SEQUENCE). FT CONFLICT 307 307 K -> R (in Ref. 2). FT TURN 23 24 FT STRAND 26 29 FT STRAND 33 39 FT HELIX 42 47 FT TURN 48 49 FT STRAND 54 57 FT HELIX 60 62 FT HELIX 63 72 FT STRAND 76 80 FT HELIX 82 94 FT TURN 98 99 FT STRAND 101 108 FT HELIX 111 122 FT TURN 123 124 FT STRAND 126 132 FT STRAND 139 145 FT TURN 146 147 FT STRAND 148 154 FT HELIX 156 160 FT HELIX 163 165 FT TURN 166 168 FT HELIX 170 178 FT STRAND 181 185 FT HELIX 186 190 FT TURN 191 191 FT HELIX 193 205 FT TURN 206 207 FT STRAND 209 213 FT HELIX 217 222 FT TURN 223 223 FT HELIX 224 230 FT HELIX 231 233 FT STRAND 236 240 FT HELIX 241 250 FT TURN 251 252 FT HELIX 258 266 FT TURN 267 267 FT TURN 273 274 FT STRAND 278 283 FT TURN 284 285 FT STRAND 286 291 FT STRAND 296 299 FT TURN 307 308 FT HELIX 312 327 FT TURN 328 330 FT HELIX 333 347 FT TURN 348 349 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 //