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HMDB Protein ID HMDBP00562
Secondary Accession Numbers
  • 5834
Name Adenylate kinase isoenzyme 1
  1. AK 1
  2. ATP-AMP transphosphorylase 1
  3. Myokinase
Gene Name AK1
Protein Type Enzyme
Biological Properties
General Function Involved in ATP binding
Specific Function Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth.
  • Adefovir Dipivoxil Metabolism Pathway
  • Adenine phosphoribosyltransferase deficiency (APRT)
  • Adenosine Deaminase Deficiency
  • Adenylosuccinate Lyase Deficiency
  • AICA-Ribosiduria
  • Azathioprine Action Pathway
  • Gout or Kelley-Seegmiller Syndrome
  • Lesch-Nyhan Syndrome (LNS)
  • Mercaptopurine Action Pathway
  • Mitochondrial DNA depletion syndrome
  • Molybdenum Cofactor Deficiency
  • Myoadenylate deaminase deficiency
  • Purine metabolism
  • Purine metabolism
  • Purine Nucleoside Phosphorylase Deficiency
  • Tenofovir Metabolism Pathway
  • Thioguanine Action Pathway
  • Xanthine Dehydrogenase Deficiency (Xanthinuria)
  • Xanthinuria type I
  • Xanthinuria type II
Adenosine triphosphate + Adenosine monophosphate → ADP details
Adenosine triphosphate + Deoxyadenosine monophosphate → ADP + dADP details
GO Classification
Biological Process
cell cycle arrest
nucleobase-containing small molecule interconversion
ATP metabolic process
Cellular Component
plasma membrane
cell part
intracellular part
catalytic activity
phosphotransferase activity, phosphate group as acceptor
transferase activity
adenylate kinase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleobase, nucleoside, nucleotide kinase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
Molecular Function
ATP binding
adenylate kinase activity
purine nucleotide metabolic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside triphosphate metabolic process
purine ribonucleoside triphosphate metabolic process
atp metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 9
Locus 9q34.1
Gene Sequence
>585 bp
Protein Properties
Number of Residues 194
Molecular Weight 21634.725
Theoretical pI 8.627
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Adenylate kinase isoenzyme 1
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P00568
UniProtKB/Swiss-Prot Entry Name KAD1_HUMAN
GenBank Gene ID AB021871
GeneCard ID AK1
GenAtlas ID AK1
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Von Zabern I, Wittmann-Liebold B, Untucht-Grau R, Schirmer RH, Pai EF: Primary and tertiary structure of the principal human adenylate kinase. Eur J Biochem. 1976 Sep;68(1):281-90. [PubMed:183954 ]
  3. Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A: Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 1989 Jun 15;264(17):10148-55. [PubMed:2542324 ]
  4. Qualtieri A, Pedace V, Bisconte MG, Bria M, Gulino B, Andreoli V, Brancati C: Severe erythrocyte adenylate kinase deficiency due to homozygous A-->G substitution at codon 164 of human AK1 gene associated with chronic haemolytic anaemia. Br J Haematol. 1997 Dec;99(4):770-6. [PubMed:9432020 ]
  5. Corrons JL, Garcia E, Tusell JJ, Varughese KI, West C, Beutler E: Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic anemia. Blood. 2003 Jul 1;102(1):353-6. Epub 2003 Mar 20. [PubMed:12649162 ]