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Protein

N6-adenosine-methyltransferase subunit METTL14

Gene

METTL14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

N6-methyltransferase that methylates adenosine residues of some mRNAs and acts as a regulator of the circadian clock and differentiation of embryonic stem cells. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in the efficiency of mRNA splicing, processing and mRNA stability (PubMed:24316715, PubMed:24407421, PubMed:25719671). M6A regulates the length of the circadian clock: acts as a early pace-setter in the circadian loop. M6A also acts as a regulator of mRNA stability: in embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization (By similarity).By similarity3 Publications

Catalytic activityi

S-adenosyl-L-methionine + m7G(5')pppAm = S-adenosyl-L-homocysteine + m7G(5')pppm6Am.1 Publication

GO - Molecular functioni

  • mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity Source: UniProtKB
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • gene expression Source: Reactome
  • mRNA destabilization Source: UniProtKB
  • mRNA methylation Source: UniProtKB
  • mRNA splicing, via spliceosome Source: UniProtKB
  • stem cell population maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
N6-adenosine-methyltransferase subunit METTL14 (EC:2.1.1.621 Publication)
Alternative name(s):
Methyltransferase-like protein 14
Gene namesi
Name:METTL14
Synonyms:KIAA1627
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:29330. METTL14.

Subcellular locationi

GO - Cellular componenti

  • MIS complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164722277.

Polymorphism and mutation databases

BioMutaiMETTL14.
DMDMi172045930.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456N6-adenosine-methyltransferase subunit METTL14PRO_0000325790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei399 – 3991PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9HCE5.
MaxQBiQ9HCE5.
PaxDbiQ9HCE5.
PRIDEiQ9HCE5.

PTM databases

iPTMnetiQ9HCE5.
PhosphoSiteiQ9HCE5.

Miscellaneous databases

PMAP-CutDBQ9HCE5.

Expressioni

Gene expression databases

BgeeiQ9HCE5.
ExpressionAtlasiQ9HCE5. baseline and differential.
GenevisibleiQ9HCE5. HS.

Organism-specific databases

HPAiHPA038002.

Interactioni

Subunit structurei

Component of the WMM complex, a N6-methyltransferase complex composed of WTAP, METTL3 and METTL14.3 Publications

Protein-protein interaction databases

BioGridi121744. 6 interactions.
DIPiDIP-60726N.
IntActiQ9HCE5. 4 interactions.
STRINGi9606.ENSP00000373474.

Structurei

3D structure databases

ProteinModelPortaliQ9HCE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili63 – 9331Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi409 – 45244Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the MT-A70-like family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2097. Eukaryota.
ENOG410XQ0H. LUCA.
GeneTreeiENSGT00550000075003.
HOGENOMiHOG000047862.
InParanoidiQ9HCE5.
KOiK05925.
OMAiFWNWDDI.
OrthoDBiEOG7XSTDT.
PhylomeDBiQ9HCE5.
TreeFamiTF323641.

Family and domain databases

InterProiIPR007757. MT-A70-like.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF05063. MT-A70. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51143. MT_A70. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HCE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSRLQEIRE RQKLRRQLLA QQLGAESADS IGAVLNSKDE QREIAETRET
60 70 80 90 100
CRASYDTSAP NAKRKYLDEG ETDEDKMEEY KDELEMQQDE ENLPYEEEIY
110 120 130 140 150
KDSSTFLKGT QSLNPHNDYC QHFVDTGHRP QNFIRDVGLA DRFEEYPKLR
160 170 180 190 200
ELIRLKDELI AKSNTPPMYL QADIEAFDIR ELTPKFDVIL LEPPLEEYYR
210 220 230 240 250
ETGITANEKC WTWDDIMKLE IDEIAAPRSF IFLWCGSGEG LDLGRVCLRK
260 270 280 290 300
WGYRRCEDIC WIKTNKNNPG KTKTLDPKAV FQRTKEHCLM GIKGTVKRST
310 320 330 340 350
DGDFIHANVD IDLIITEEPE IGNIEKPVEI FHIIEHFCLG RRRLHLFGRD
360 370 380 390 400
STIRPGWLTV GPTLTNSNYN AETYASYFSA PNSYLTGCTE EIERLRPKSP
410 420 430 440 450
PPKSKSDRGG GAPRGGGRGG TSAGRGRERN RSNFRGERGG FRGGRGGAHR

GGFPPR
Length:456
Mass (Da):52,150
Last modified:March 18, 2008 - v2
Checksum:i73A45B66BB76E241
GO

Sequence cautioni

The sequence BAB13453.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046847 mRNA. Translation: BAB13453.1. Different initiation.
AK055555 mRNA. Translation: BAB70954.1.
AC110079 Genomic DNA. No translation available.
CH471229 Genomic DNA. Translation: EAW73651.1.
BC006565 mRNA. Translation: AAH06565.1.
BC007449 mRNA. Translation: AAH07449.1.
CCDSiCCDS34053.1.
RefSeqiNP_066012.1. NM_020961.3.
UniGeneiHs.596872.
Hs.657806.

Genome annotation databases

EnsembliENST00000388822; ENSP00000373474; ENSG00000145388.
GeneIDi57721.
KEGGihsa:57721.
UCSCiuc003icf.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046847 mRNA. Translation: BAB13453.1. Different initiation.
AK055555 mRNA. Translation: BAB70954.1.
AC110079 Genomic DNA. No translation available.
CH471229 Genomic DNA. Translation: EAW73651.1.
BC006565 mRNA. Translation: AAH06565.1.
BC007449 mRNA. Translation: AAH07449.1.
CCDSiCCDS34053.1.
RefSeqiNP_066012.1. NM_020961.3.
UniGeneiHs.596872.
Hs.657806.

3D structure databases

ProteinModelPortaliQ9HCE5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121744. 6 interactions.
DIPiDIP-60726N.
IntActiQ9HCE5. 4 interactions.
STRINGi9606.ENSP00000373474.

PTM databases

iPTMnetiQ9HCE5.
PhosphoSiteiQ9HCE5.

Polymorphism and mutation databases

BioMutaiMETTL14.
DMDMi172045930.

Proteomic databases

EPDiQ9HCE5.
MaxQBiQ9HCE5.
PaxDbiQ9HCE5.
PRIDEiQ9HCE5.

Protocols and materials databases

DNASUi57721.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000388822; ENSP00000373474; ENSG00000145388.
GeneIDi57721.
KEGGihsa:57721.
UCSCiuc003icf.4. human.

Organism-specific databases

CTDi57721.
GeneCardsiMETTL14.
HGNCiHGNC:29330. METTL14.
HPAiHPA038002.
MIMi616504. gene.
neXtProtiNX_Q9HCE5.
PharmGKBiPA164722277.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2097. Eukaryota.
ENOG410XQ0H. LUCA.
GeneTreeiENSGT00550000075003.
HOGENOMiHOG000047862.
InParanoidiQ9HCE5.
KOiK05925.
OMAiFWNWDDI.
OrthoDBiEOG7XSTDT.
PhylomeDBiQ9HCE5.
TreeFamiTF323641.

Enzyme and pathway databases

ReactomeiR-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.

Miscellaneous databases

GenomeRNAii57721.
NextBioi64662.
PMAP-CutDBQ9HCE5.
PROiQ9HCE5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCE5.
ExpressionAtlasiQ9HCE5. baseline and differential.
GenevisibleiQ9HCE5. HS.

Family and domain databases

InterProiIPR007757. MT-A70-like.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF05063. MT-A70. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51143. MT_A70. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE WMM COMPLEX.
  9. Cited for: IDENTIFICATION IN THE WMM COMPLEX.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "A METTL3-METTL14 complex mediates mammalian nuclear RNA N-adenosine methylation."
    Liu J., Yue Y., Han D., Wang X., Fu Y., Zhang L., Jia G., Yu M., Lu Z., Deng X., Dai Q., Chen W., He C.
    Nat. Chem. Biol. 10:93-95(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE WMM COMPLEX.
  12. "N(6)-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions."
    Liu N., Dai Q., Zheng G., He C., Parisien M., Pan T.
    Nature 518:560-564(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Dynamic m(6)A mRNA methylation directs translational control of heat shock response."
    Zhou J., Wan J., Gao X., Zhang X., Jaffrey S.R., Qian S.B.
    Nature 526:591-594(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMET14_HUMAN
AccessioniPrimary (citable) accession number: Q9HCE5
Secondary accession number(s): A6NIG1, Q969V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: April 13, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.