METTL8
entrez
79828
canonical
uniprot
Q9H825
canonical
ensembl
ENSG00000123600
resolver
ensp
ENSP00000364407
resolver
ensp
ENSP00000376382
resolver
ensp
ENSP00000409025
resolver
ensp
ENSP00000480056
resolver
ensp
ENSP00000577481
resolver
ensp
ENSP00000577482
resolver
ensp
ENSP00000595900
resolver
ensp
ENSP00000633954
resolver
ensp
ENSP00000633955
resolver
enst
ENST00000375258
resolver
enst
ENST00000612742
resolver
enst
ENST00000907422
resolver
enst
ENST00000907423
resolver
enst
ENST00000925841
resolver
enst
ENST00000963895
resolver
enst
ENST00000963896
resolver
genesymbol
FLJ13984
resolver
genesymbol
METTL8
resolver
hgnc
HGNC:25856
resolver
uniprot
A0A087WW98
resolver
uniprot
A0A9K3Y8H4
resolver
uniprot
A8K7U3
resolver
uniprot
B3KW44
resolver
uniprot
B4DLT0
resolver
uniprot
D3DPD3
resolver
uniprot
E7ETE0
resolver
uniprot
Q53TM9
resolver
uniprot
Q53TQ0
resolver
uniprot_entry
A0A087WW98_HUMAN
resolver
uniprot_entry
A8K7U3_HUMAN
resolver
uniprot_entry
B3KW44_HUMAN
resolver
uniprot_entry
B4DLT0_HUMAN
resolver
uniprot_entry
METL8_HUMAN
resolver
uniprot_sec
A0A9K3Y8H4
resolver
uniprot_sec
D3DPD3
resolver
uniprot_sec
E7ETE0
resolver
uniprot_sec
Q53TM9
resolver
uniprot_sec
Q53TQ0
resolver
amino_acid_sequence
MNMIWRNSISCLRLGKVPHRYQSGYHPVAPLGSRILTDPAKVFEHNMWDHMQWSKEEEAAARKKVKENSAVRVLLEEQVKYEREASKYWDTFYKIHKNKFFKDRNWLLREFPEILPVDQKPEEKARESSWDHVKTSATNRFSRMHCPTVPDEKNHYEKSSGSSEGQSKTESDFSNLDSEKHKKGPMETGLFPGSNATFRILEVGCGAGNSVFPILNTLENSPESFLYCCDFASGAVELVKSHSSYRATQCFAFVHDVCDDGLPYPFPDGILDVILLVFVLSSIHPDRTLFI
uniprot
proteins
ec_number
2.1.1.-
uniprot
proteins
function
FUNCTION: Mitochondrial S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of mitochondrial tRNA(Ser)(UCN) and tRNA(Thr) (PubMed:34774131, PubMed:35017528). N(3)-methylcytidine methylation modification regulates mitochondrial translation efficiency and is required for activity of the respiratory chain (PubMed:34774131, PubMed:35017528). N(3)-methylcytidine methylation of mitochondrial tRNA(Ser)(UCN) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by TRIT1 as prerequisite (PubMed:34774131, PubMed:35017528). May also mediate N(3)-methylcytidine modification of mRNAs (PubMed:28655767). The existence of N(3)-methylcytidine modification on mRNAs is however unclear, and additional evidence is required to confirm the role of the N(3)-methylcytidine-specific mRNA methyltransferase activity of METTL8 in vivo (PubMed:33313824, PubMed:34774131). {ECO:0000269|PubMed:28655767, ECO:0000269|PubMed:33313824, ECO:0000269|PubMed:34774131, ECO:0000269|PubMed:35017528}.
uniprot
proteins
mass_dalton
33387
uniprot
proteins
mutagenesis
MUTAGEN 4; /note="I->Q: Partial relocalization to the cytoplasm; when associated with Q-9."; /evidence="ECO:0000269|PubMed:34774131"; MUTAGEN 9; /note="I->Q: Partial relocalization to the cytoplasm; when associated with Q-4."; /evidence="ECO:0000269|PubMed:34774131"; MUTAGEN 80; /note="K->R: Abolished SUMOylation."; /evidence="ECO:0000269|PubMed:32199293"; MUTAGEN 230; /note="D->A: Abolished N(3)-methylcytidine methyltransferase activity."; /evidence="ECO:0000269|PubMed:34774131, ECO:0000269|PubMed:35017528
uniprot
proteins
protein_family
METL family
uniprot
proteins
protein_family
Methyltransferase superfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
28655767
uniprot
proteins
pubmed
32199293
uniprot
proteins
pubmed
33313824
uniprot
proteins
pubmed
34774131
uniprot
proteins
pubmed
35017528
uniprot
proteins
sequence_length
291
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:34774131, ECO:0000269|PubMed:35017528}. Note=Mitochondrial protein: the cytoplasmic or nuclear localization observed by some groups is either the result of an incorrect localization caused by N-terminal tagging that interferes with mitochondrial targeting, or splice isoforms that lack the N-terminal mitochondrial transit sequence. {ECO:0000269|PubMed:34774131}.
uniprot
proteins