Alkbh1
entrez
211064
canonical
uniprot
P0CB42
canonical
ensembl
ENSMUSG00000079036
resolver
ensp
ENSMUSP00000124565
resolver
enst
ENSMUST00000162961
resolver
genesymbol
Alkbh1
resolver
genesymbol_syn
Abh
resolver
genesymbol_syn
Alkbh
resolver
uniprot_entry
ALKB1_MOUSE
resolver
amino_acid_sequence
MGKMAAAVASLATLAAEPREDAFRKLFRFYRQSRPGTADLGAVIDFSEAHLARSPKPGVPQVVRFPLNVSSVTERDAERVGLEPVSKWRAYGLEGYPGFIFIPNPFLPGCQRHWVKQCLKLYSQKPNVCNLDKHMTKEETQGLWEQSKEVLRSKEVTKRRPRSLLERLRWVTLGYHYNWDSKKYSADHYTPFPSDLAFLSEQVATACGFQGFQAEAGILNYYRLDSTLGIHVDRSELDHSKPLLSFSFGQSAIFLLGGLKRDEAPTAMFMHSGDIMVMSGFSRLLNHAVPRVLPHPDGECLPHCLETPLPAVLPSNSLVEPCSVEDWQVCATYLRTARVNMTVRQVLATGQDFPLEPVEETKRDIAADGLCHLHDPNSPVKRKRLNPNS
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:27027282, PubMed:27745969). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:27027282). 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 (By similarity). 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 (By similarity). 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 (By similarity). 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 (By similarity). Specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA (PubMed:27027282). N(6)-methyladenosine (m6A) DNA is present at some L1 elements in embryonic stem cells and probably promotes their silencing (PubMed:27027282). Demethylates mRNAs containing N(3)-methylcytidine modification (By similarity). Also able to repair alkylated single-stranded DNA by oxidative demethylation, but with low activity (By similarity). 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 (By similarity). 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 (By similarity). DNA lyase activity is not required during base excision repair and class switch recombination of the immunoglobulin heavy chain during B lymphocyte activation (PubMed:23825659). May play a role in placental trophoblast lineage differentiation (PubMed:18163532). {ECO:0000250|UniProtKB:Q13686, ECO:0000269|PubMed:18163532, ECO:0000269|PubMed:23825659, ECO:0000269|PubMed:27027282, ECO:0000269|PubMed:27745969}.
uniprot
proteins
mass_dalton
43746
uniprot
proteins
mutagenesis
MUTAGEN 233; /note="D->A: Loss of activity."; /evidence="ECO:0000269|PubMed:27027282
uniprot
proteins
pubmed
18163532
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21072209
uniprot
proteins
pubmed
22961808
uniprot
proteins
pubmed
23825659
uniprot
proteins
pubmed
27027282
uniprot
proteins
pubmed
27745969
uniprot
proteins
sequence_length
389
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18163532}. Note=Mainly localizes in euchromatin, largely excluded from heterochromatin and nucleoli. {ECO:0000269|PubMed:18163532}.
uniprot
proteins