ADK
entrez
132
canonical
uniprot
P55263
canonical
ensembl
ENSG00000156110
resolver
ensp
ENSP00000361819
resolver
ensp
ENSP00000443965
resolver
ensp
ENSP00000500056
resolver
ensp
ENSP00000500097
resolver
ensp
ENSP00000500201
resolver
ensp
ENSP00000500292
resolver
ensp
ENSP00000500390
resolver
ensp
ENSP00000774329
resolver
ensp
ENSP00000788008
resolver
enst
ENST00000672394
resolver
enst
ENST00000673310
resolver
enst
ENST00000673352
resolver
genesymbol
ADK
resolver
hgnc
HGNC:257
resolver
uniprot
A0A140VJE0
resolver
uniprot
A0A5F9ZH31
resolver
uniprot
A0A5F9ZH72
resolver
uniprot
A0A5F9ZHJ1
resolver
uniprot
B7Z783
resolver
uniprot
B7Z800
resolver
uniprot
O00741
resolver
uniprot
O00742
resolver
uniprot
Q16710
resolver
uniprot
Q5JQ10
resolver
uniprot
Q5JQ11
resolver
uniprot
Q9BTN2
resolver
uniprot_entry
A0A140VJE0_HUMAN
resolver
uniprot_entry
A0A5F9ZH31_HUMAN
resolver
uniprot_entry
A0A5F9ZH72_HUMAN
resolver
uniprot_entry
A0A5F9ZHJ1_HUMAN
resolver
uniprot_entry
ADK_HUMAN
resolver
uniprot_sec
B7Z783
resolver
uniprot_sec
B7Z800
resolver
uniprot_sec
O00741
resolver
uniprot_sec
O00742
resolver
uniprot_sec
Q16710
resolver
uniprot_sec
Q5JQ10
resolver
uniprot_sec
Q5JQ11
resolver
uniprot_sec
Q9BTN2
resolver
activity_regulation
ACTIVITY REGULATION: Activity is inhibited by 5-iodotubercidin and 5'-amino-5'-deoxyadenosine (PubMed:17154503, PubMed:9070863). Also inhibited by 5-(4-(Dimethylamino)phenyl)-6-(6-morpholin- 4-ylpyridin-3-ylethynyl)pyrimidin-4-ylamine, a alkynylpyrimidine class small-molecule (PubMed:17154503). {ECO:0000269|PubMed:17154503, ECO:0000269|PubMed:9070863}.
uniprot
proteins
amino_acid_sequence
MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPDFH
uniprot
proteins
disease_involvement
DISEASE: Hypermethioninemia due to adenosine kinase deficiency (HMAKD) [MIM:614300]: A metabolic disorder characterized by global developmental delay, early-onset seizures, mild dysmorphic features, and characteristic biochemical anomalies, including persistent hypermethioninemia with increased levels of S-adenosylmethionine and S-adenosylhomocysteine. Homocysteine levels are typically normal. {ECO:0000269|PubMed:21963049, ECO:0000269|PubMed:26642971, ECO:0000269|PubMed:27500280, ECO:0000269|PubMed:33309011, ECO:0000269|PubMed:39899686, ECO:0000269|PubMed:40840445}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.1.-
uniprot
proteins
ec_number
2.7.1.20
uniprot
proteins
function
FUNCTION: Adenosine kinase that mediates the phosphorylation of the purine nucleoside adenosine at the 5' position in an ATP-dependent manner: catalyzes phosphorylation of both unmodified and modified adenosines (PubMed:21963049, PubMed:40840445, PubMed:6246102, PubMed:8577746, PubMed:9070863). Plays a key role in the detoxification of modified adenosines containing N(6)-methylated adenine (m6A) post-transcriptional modification (PubMed:40840445). Modified nucleosides are derived from the degradation of RNAs (mRNAs, rRNAs and tRNAs) and possess intrinsic cytotoxicity and must be cleared to prevent metabolic dysfunction (PubMed:40840445). Catalyzes the phosphorylation of the free cytosolic methylated adenosine nucleotides N(6)-methyladenosine (m6A), N(6),N(6)-dimethyladenosine (m6,6A) and N(6)-isopentenyladenosine (i6A) into adenosine monophosphate (AMP) intermediates that are further detoxified by MAPDA/ADAL (PubMed:40840445). {ECO:0000269|PubMed:21963049, ECO:0000269|PubMed:40840445, ECO:0000269|PubMed:6246102, ECO:0000269|PubMed:8577746, ECO:0000269|PubMed:9070863}.
uniprot
proteins
mass_dalton
40545
uniprot
proteins
mutagenesis
MUTAGEN 11..12; /note="KK->AA,AD: Abolishes nuclear localization."; /evidence="ECO:0000269|PubMed:19635462"; MUTAGEN 33; /note="L->A: Abolished ability to mediate phosphorylation of unmodified and modified adenosines."; /evidence="ECO:0000269|PubMed:40840445"; MUTAGEN 35; /note="D->A: Abolished ability to mediate phosphorylation of unmodified and modified adenosines."; /evidence="ECO:0000269|PubMed:40840445"; MUTAGEN 57; /note="L->A: Abolished ability to mediate phosphorylation of unmodified and modified adenosines."; /evidence="ECO:0000269|PubMed:40840445"; MUTAGEN 153; /note="A->T: Increased ability to phosphorylate N(6)-methyladenosine (m6A), N(6),N(6)-dimethyladenosine (m6,6A), N(6)-isopentenyladenosine (i6A) and adenosine."; /evidence="ECO:0000269|PubMed:40840445"; MUTAGEN 155; /note="L->A: Decreased ability to phosphorylate N(6),N(6)-dimethyladenosine (m6,6A) and N(6)-isopentenyladenosine (i6A), but not N(6)-methyladenosine (m6A) or adenosine."; /evidence="ECO:0000269|PubMed:40840445"; MUTAGEN 187; /note="F->L: Abolished ability to mediate phosphorylation of unmodified and modified adenosines."; /evidence="ECO:0000269|PubMed:40840445"; MUTAGEN 218; /note="F->A: Decreased ability to phosphorylate N(6)-methyladenosine (m6A) and N(6),N(6)-dimethyladenosine (m6,6A)."; /evidence="ECO:0000269|PubMed:40840445"; MUTAGEN 313; /note="N->A: Decreased ability to phosphorylate N(6),N(6)-dimethyladenosine (m6,6A) and N(6)-isopentenyladenosine (i6A)."; /evidence="ECO:0000269|PubMed:40840445"; MUTAGEN 317; /note="D->A: Abolished ability to mediate phosphorylation of unmodified and modified adenosines."; /evidence="ECO:0000269|PubMed:40840445
uniprot
proteins
pathway_participation
PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1. {ECO:0000305|PubMed:9070863}.
uniprot
proteins
protein_family
Carbohydrate kinase PfkB family
uniprot
proteins
pubmed
12112843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17154503
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19635462
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21963049
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26642971
uniprot
proteins
pubmed
27500280
uniprot
proteins
pubmed
33309011
uniprot
proteins
pubmed
39899686
uniprot
proteins
pubmed
40840445
uniprot
proteins
pubmed
6246102
uniprot
proteins
pubmed
8577746
uniprot
proteins
pubmed
8917457
uniprot
proteins
pubmed
9070863
uniprot
proteins
pubmed
9843365
uniprot
proteins
sequence_length
362
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:8577746}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:19635462}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19635462}.
uniprot
proteins