{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9HCE5","secondaryAccessions":["A6NIG1","Q969V2"],"uniProtkbId":"MET14_HUMAN","entryAudit":{"firstPublicDate":"2008-03-18","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2008-03-18","entryVersion":156,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"N(6)-adenosine-methyltransferase non-catalytic subunit METTL14"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:29330"}],"value":"Methyltransferase-like protein 14"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27373337"}],"value":"hMETTL14"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:29330"}],"value":"METTL14"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10997877"}],"value":"KIAA1627"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q3UIK4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24316715"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24407421"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25719671"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27281194"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27373337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27627798"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29348140"}],"value":"The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some mRNAs and regulates the circadian clock, differentiation of embryonic stem cells and cortical neurogenesis (PubMed:24316715, PubMed:24407421, PubMed:25719671, PubMed:27281194, PubMed:27373337, PubMed:29348140). In the heterodimer formed with METTL3, METTL14 constitutes the RNA-binding scaffold that recognizes the substrate rather than the catalytic core (PubMed:27281194, PubMed:27373337, PubMed:27627798, PubMed:29348140). N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability and processing (PubMed:24316715, PubMed:24407421, PubMed:25719671). M6A acts as a key regulator of mRNA stability by promoting mRNA destabilization and degradation (By similarity). In embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization (By similarity). M6A regulates spermatogonial differentiation and meiosis and is essential for male fertility and spermatogenesis (By similarity). M6A also regulates cortical neurogenesis: m6A methylation of transcripts related to transcription factors, neural stem cells, the cell cycle and neuronal differentiation during brain development promotes their destabilization and decay, promoting differentiation of radial glial cells (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24316715"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24407421"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24981863"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27281194"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27373337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27627798"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29348140"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29507755"}],"value":"Heterodimer; heterodimerizes with METTL3 to form an antiparallel heterodimer that constitutes an active methyltransferase (PubMed:27281194, PubMed:27373337, PubMed:27627798). Component of the WMM complex, a N6-methyltransferase complex composed of a catalytic subcomplex, named MAC, and of an associated subcomplex, named MACOM (PubMed:24316715, PubMed:24407421, PubMed:24981863, PubMed:29348140, PubMed:29507755). The MAC subcomplex is composed of METTL3 and METTL14 (PubMed:24316715, PubMed:24407421, PubMed:24981863, PubMed:29507755). The MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29507755)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9HCE5","intActId":"EBI-6661081"},"interactantTwo":{"uniProtKBAccession":"Q86U44","geneName":"METTL3","intActId":"EBI-11105430"},"numberOfExperiments":23,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9HCE5","intActId":"EBI-6661081"},"interactantTwo":{"uniProtKBAccession":"Q86U44-1","geneName":"METTL3","intActId":"EBI-16084936"},"numberOfExperiments":10,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9HCE5","intActId":"EBI-6661081"},"interactantTwo":{"uniProtKBAccession":"Q15007-1","geneName":"WTAP","intActId":"EBI-16084961"},"numberOfExperiments":5,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24316715"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24407421"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26458103"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29348140"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00489"}],"value":"Belongs to the MT-A70-like family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27281194"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29348140"}],"value":"The effect of phosphorylation at Ser-399 is unclear. According to a report, phosphorylation at Ser-399 is important for interaction with METTL3: phosphorylated Ser-399 forms a salt bridge with 'Arg-471' of METTL3 (PubMed:27281194). According to another report, phosphorylation at Ser-399 does not affect interaction with METTL3 (PubMed:29348140)"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24316715"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27281194"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27373337"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27627798"}],"value":"The ability of METTL14 to have catalytic activity is unclear and a number of experimental evidence suggests that it has no methyltransferase activity by itself (PubMed:27281194, PubMed:27373337, PubMed:27627798). According to some reports, has some methyltransferase activity in vitro (PubMed:24316715). However, other studies showed that METTL14 constitutes the RNA-binding scaffold that recognizes the substrate rather than the catalytic core (PubMed:27281194, PubMed:27373337, PubMed:27627798). 3D-structure studies showed that METTL14 contains a degenerate active site that is unable to accommodate donor and acceptor substrates (PubMed:27627798)"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27627798"}],"value":"A disulfide bond between Cys-338 and Cys-388 is observed in a structure (PubMed:27627798). 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