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
//