ALKBH1
entrez
8846
canonical
uniprot
Q13686
canonical
ensembl
ENSG00000100601
resolver
ensp
ENSP00000216489
resolver
ensp
ENSP00000689212
resolver
enst
ENST00000216489
resolver
genesymbol
ALKBH1
resolver
genesymbol_syn
ABH
resolver
genesymbol_syn
ABH1
resolver
genesymbol_syn
ALKBH
resolver
hgnc
HGNC:17911
resolver
uniprot
Q5XKL0
resolver
uniprot
Q8TAU1
resolver
uniprot
Q9ULA7
resolver
uniprot_entry
ALKB1_HUMAN
resolver
uniprot_entry
Q5XKL0_HUMAN
resolver
uniprot_sec
Q8TAU1
resolver
uniprot_sec
Q9ULA7
resolver
amino_acid_sequence
MGKMAAAVGSVATLATEPGEDAFRKLFRFYRQSRPGTADLEGVIDFSAAHAARGKGPGAQKVIKSQLNVSSVSEQNAYRAGLQPVSKWQAYGLKGYPGFIFIPNPFLPGYQWHWVKQCLKLYSQKPNVCNLDKHMSKEETQDLWEQSKEFLRYKEATKRRPRSLLEKLRWVTVGYHYNWDSKKYSADHYTPFPSDLGFLSEQVAAACGFEDFRAEAGILNYYRLDSTLGIHVDRSELDHSKPLLSFSFGQSAIFLLGGLQRDEAPTAMFMHSGDIMIMSGFSRLLNHAVPRVLPNPEGEGLPHCLEAPLPAVLPRDSMVEPCSMEDWQVCASYLKTARVNMTVRQVLATDQNFPLEPIEDEKRDISTEGFCHLDDQNSEVKRARINPDS
uniprot
proteins
ec_number
1.14.11.-
uniprot
proteins
ec_number
1.14.11.33
uniprot
proteins
ec_number
1.14.11.51
uniprot
proteins
ec_number
4.2.99.18
uniprot
proteins
function
FUNCTION: Dioxygenase that acts on nucleic acids, such as DNA and tRNA (PubMed:18603530, PubMed:27497299, PubMed:27745969). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:18603530, PubMed:27497299). A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts on tRNAs and mediates their demethylation or oxidation depending on the context and subcellular compartment (PubMed:27497299, PubMed:27745969). Mainly acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs, with a preference for N(1)-methyladenine at position 58 (m1A58) present on a stem loop structure of tRNAs (PubMed:27745969). Acts as a regulator of translation initiation and elongation in response to glucose deprivation: regulates both translation initiation, by mediating demethylation of tRNA(Met), and translation elongation, N(1)-methyladenine-containing tRNAs being preferentially recruited to polysomes to promote translation elongation (PubMed:27745969). In mitochondrion, specifically interacts with mt-tRNA(Met) and mediates oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c) at this position (PubMed:27497299). mt-tRNA(Met) containing the f(5)c modification at the wobble position enables recognition of the AUA codon in addition to the AUG codon, expanding codon recognition in mitochondrial translation (PubMed:27497299). Specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA (PubMed:30017583, PubMed:30392959). N(6)-methyladenosine (m6A) DNA is present at some L1 elements in embryonic stem cells and probably promotes their silencing (By similarity). Demethylates mRNAs containing N(3)-methylcytidine modification (PubMed:31188562). Also able to repair alkylated single-stranded DNA by oxidative demethylation, but with low activity (PubMed:18603530). Also has DNA lyase activity and introduces double-stranded breaks at abasic sites: cleaves both single-stranded DNA and double-stranded DNA at abasic sites, with the greatest activity towards double-stranded DNA with two abasic sites (PubMed:19959401). DNA lyase activity does not require alpha-ketoglutarate and iron and leads to the formation of an irreversible covalent protein-DNA adduct with the 5' DNA product (PubMed:19959401, PubMed:23577621). DNA lyase activity is not required during base excision repair and class switch recombination of the immunoglobulin heavy chain during B lymphocyte activation. May play a role in placental trophoblast lineage differentiation (By similarity). {ECO:0000250|UniProtKB:P0CB42, ECO:0000269|PubMed:18603530, ECO:0000269|PubMed:19959401, ECO:0000269|PubMed:23577621, ECO:0000269|PubMed:27497299, ECO:0000269|PubMed:27745969, ECO:0000269|PubMed:30017583, ECO:0000269|PubMed:30392959, ECO:0000269|PubMed:31188562}.
uniprot
proteins
mass_dalton
43832
uniprot
proteins
mutagenesis
MUTAGEN 3; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 25; /note="K->A: Moderate decrease in DNA lyase activity. Reduced DNA lyase activity; when associated with A-133."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 55; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 61; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 64; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 87; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 94; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 113; /note="H->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:25459764"; MUTAGEN 116; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 118; /note="C->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:25459764"; MUTAGEN 120; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 125; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 129; /note="C->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:25459764"; MUTAGEN 133; /note="K->A: Reduced DNA lyase activity. Slightly more reduced DNA lyase activity; when associated with A-25. Strongly reduced activity; when associated with A-154."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 134; /note="H->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:25459764"; MUTAGEN 137; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 148; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 154; /note="K->A: Does not affect DNA lyase activity. Strongly reduced activity; when associated with A-133."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 158; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 167; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 182; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 183; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 218; /note="I->L: Reduces Fe2OG dioxygenase activity by 50%."; /evidence="ECO:0000269|PubMed:18603530"; MUTAGEN 231..233; /note="HVD->AVA: Loss of catalytic activity. Abolishes ability to regulate translation in respose to glucose deprivation."; /evidence="ECO:0000269|PubMed:27745969"; MUTAGEN 231; /note="H->A: Near loss of Fe2OG dioxygenase activity. No effect on DNA lyase activity."; /evidence="ECO:0000269|PubMed:18603530, ECO:0000269|PubMed:19959401"; MUTAGEN 233; /note="D->A: Loss of Fe2OG dioxygenase activity. No effect on DNA lyase activity. Abolishes ability to mediate oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c). Abolished DNAN6-methyl adenine demethylase activity."; /evidence="ECO:0000269|PubMed:18603530, ECO:0000269|PubMed:19959401, ECO:0000269|PubMed:27497299, ECO:0000269|PubMed:30017583, ECO:0000269|PubMed:31188562"; MUTAGEN 241; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 287; /note="H->A: Loss of Fe2OG dioxygenase activity. No effect on DNA lyase activity."; /evidence="ECO:0000269|PubMed:18603530, ECO:0000269|PubMed:19959401"; MUTAGEN 303; /note="H->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:25459764"; MUTAGEN 304; /note="C->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:25459764"; MUTAGEN 335; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 338; /note="R->A: Reduced Fe2OG dioxygenase activity. Abolishes ability to mediate oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c)."; /evidence="ECO:0000269|PubMed:18603530, ECO:0000269|PubMed:27497299"; MUTAGEN 344; /note="R->A: Reduced Fe2OG dioxygenase activity."; /evidence="ECO:0000269|PubMed:18603530"; MUTAGEN 362; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621"; MUTAGEN 371; /note="C->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:25459764"; MUTAGEN 372; /note="H->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:25459764"; MUTAGEN 381; /note="K->A: Does not affect DNA lyase activity."; /evidence="ECO:0000269|PubMed:23577621
uniprot
proteins
protein_family
AlkB family
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17979886
uniprot
proteins
pubmed
18603530
uniprot
proteins
pubmed
19959401
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22961808
uniprot
proteins
pubmed
23577621
uniprot
proteins
pubmed
25459764
uniprot
proteins
pubmed
27497299
uniprot
proteins
pubmed
27745969
uniprot
proteins
pubmed
30017583
uniprot
proteins
pubmed
30392959
uniprot
proteins
pubmed
31188562
uniprot
proteins
pubmed
8600462
uniprot
proteins
sequence_length
389
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22961808}. Mitochondrion {ECO:0000269|PubMed:17979886, ECO:0000269|PubMed:18603530, ECO:0000269|PubMed:27497299}. Note=Mainly localizes in euchromatin, largely excluded from heterochromatin and nucleoli (By similarity). {ECO:0000250|UniProtKB:P0CB42}.
uniprot
proteins