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N6-adenosine-methyltransferase catalytic subunit (EC 2.1.1.62) (Methyltransferase-like protein 3) (hMETTL3) (N6-adenosine-methyltransferase 70 kDa subunit) (MT-A70)

 MTA70_HUMAN             Reviewed;         580 AA.
Q86U44; O14736; Q86V05; Q9HB32;
25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
25-JUL-2003, sequence version 2.
20-JUN-2018, entry version 135.
RecName: Full=N6-adenosine-methyltransferase catalytic subunit {ECO:0000305};
EC=2.1.1.62 {ECO:0000269|PubMed:27281194, ECO:0000269|PubMed:27373337, ECO:0000269|PubMed:27627798, ECO:0000269|PubMed:29348140, ECO:0000269|PubMed:29506078, ECO:0000269|PubMed:9409616};
AltName: Full=Methyltransferase-like protein 3 {ECO:0000305};
Short=hMETTL3 {ECO:0000303|PubMed:27373337};
AltName: Full=N6-adenosine-methyltransferase 70 kDa subunit;
Short=MT-A70;
Name=METTL3 {ECO:0000312|HGNC:HGNC:17563}; Synonyms=MTA70;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), PROTEIN SEQUENCE OF
48-56; 134-149 AND 509-522, FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND CATALYTIC ACTIVITY.
PubMed=9409616;
Bokar J.A., Shambaugh M.E., Polayes D., Matera A.G., Rottman F.M.;
"Purification and cDNA cloning of the AdoMet-binding subunit of the
human mRNA (N6-adenosine)-methyltransferase.";
RNA 3:1233-1247(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-219 AND SER-243,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
FUNCTION.
PubMed=22575960; DOI=10.1038/nature11112;
Dominissini D., Moshitch-Moshkovitz S., Schwartz S., Salmon-Divon M.,
Ungar L., Osenberg S., Cesarkas K., Jacob-Hirsch J., Amariglio N.,
Kupiec M., Sorek R., Rechavi G.;
"Topology of the human and mouse m6A RNA methylomes revealed by m6A-
seq.";
Nature 485:201-206(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-219 AND THR-348,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
IDENTIFICATION IN THE WMM COMPLEX.
PubMed=24407421; DOI=10.1038/cr.2014.3;
Ping X.L., Sun B.F., Wang L., Xiao W., Yang X., Wang W.J.,
Adhikari S., Shi Y., Lv Y., Chen Y.S., Zhao X., Li A., Yang Y.,
Dahal U., Lou X.M., Liu X., Huang J., Yuan W.P., Zhu X.F., Cheng T.,
Zhao Y.L., Wang X., Danielsen J.M., Liu F., Yang Y.G.;
"Mammalian WTAP is a regulatory subunit of the RNA N6-methyladenosine
methyltransferase.";
Cell Res. 24:177-189(2014).
[15]
IDENTIFICATION IN THE WMM COMPLEX.
PubMed=24981863; DOI=10.1016/j.celrep.2014.05.048;
Schwartz S., Mumbach M.R., Jovanovic M., Wang T., Maciag K.,
Bushkin G.G., Mertins P., Ter-Ovanesyan D., Habib N., Cacchiarelli D.,
Sanjana N.E., Freinkman E., Pacold M.E., Satija R., Mikkelsen T.S.,
Hacohen N., Zhang F., Carr S.A., Lander E.S., Regev A.;
"Perturbation of m6A writers reveals two distinct classes of mRNA
methylation at internal and 5' sites.";
Cell Rep. 8:284-296(2014).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
FUNCTION.
PubMed=24284625; DOI=10.1038/nature12730;
Wang X., Lu Z., Gomez A., Hon G.C., Yue Y., Han D., Fu Y.,
Parisien M., Dai Q., Jia G., Ren B., Pan T., He C.;
"N-methyladenosine-dependent regulation of messenger RNA stability.";
Nature 505:117-120(2014).
[18]
FUNCTION.
PubMed=25719671; DOI=10.1038/nature14234;
Liu N., Dai Q., Zheng G., He C., Parisien M., Pan T.;
"N(6)-methyladenosine-dependent RNA structural switches regulate RNA-
protein interactions.";
Nature 518:560-564(2015).
[19]
FUNCTION, AND MUTAGENESIS OF 395-ASP--TRP-398.
PubMed=25799998; DOI=10.1038/nature14281;
Alarcon C.R., Lee H., Goodarzi H., Halberg N., Tavazoie S.F.;
"N6-methyladenosine marks primary microRNAs for processing.";
Nature 519:482-485(2015).
[20]
FUNCTION.
PubMed=26321680; DOI=10.1016/j.cell.2015.08.011;
Alarcon C.R., Goodarzi H., Lee H., Liu X., Tavazoie S., Tavazoie S.F.;
"HNRNPA2B1 is a mediator of m(6)A-dependent nuclear RNA processing
events.";
Cell 162:1299-1308(2015).
[21]
FUNCTION.
PubMed=26593424; DOI=10.1016/j.cell.2015.10.012;
Meyer K.D., Patil D.P., Zhou J., Zinoviev A., Skabkin M.A.,
Elemento O., Pestova T.V., Qian S.B., Jaffrey S.R.;
"5' UTR m(6)A promotes cap-independent translation.";
Cell 163:999-1010(2015).
[22]
SUBCELLULAR LOCATION.
PubMed=26458103; DOI=10.1038/nature15377;
Zhou J., Wan J., Gao X., Zhang X., Jaffrey S.R., Qian S.B.;
"Dynamic m(6)A mRNA methylation directs translational control of heat
shock response.";
Nature 526:591-594(2015).
[23]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH NCBP1;
EIF4E AND EIF3B, AND MUTAGENESIS OF 395-ASP--TRP-398.
PubMed=27117702; DOI=10.1016/j.molcel.2016.03.021;
Lin S., Choe J., Du P., Triboulet R., Gregory R.I.;
"The m(6)A methyltransferase METTL3 promotes translation in human
cancer cells.";
Mol. Cell 62:335-345(2016).
[24]
FUNCTION, AND IDENTIFICATION IN THE WMM COMPLEX.
PubMed=27602518; DOI=10.1038/nature19342;
Patil D.P., Chen C.K., Pickering B.F., Chow A., Jackson C.,
Guttman M., Jaffrey S.R.;
"m(6)A RNA methylation promotes XIST-mediated transcriptional
repression.";
Nature 537:369-373(2016).
[25]
FUNCTION.
PubMed=28637692; DOI=10.1101/gad.301036.117;
Ke S., Pandya-Jones A., Saito Y., Fak J.J., Vaagboe C.B., Geula S.,
Hanna J.H., Black D.L., Darnell J.E. Jr., Darnell R.B.;
"m(6)A mRNA modifications are deposited in nascent pre-mRNA and are
not required for splicing but do specify cytoplasmic turnover.";
Genes Dev. 31:990-1006(2017).
[26]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 395-ASP--TRP-398.
PubMed=28297716; DOI=10.1038/nature21671;
Xiang Y., Laurent B., Hsu C.H., Nachtergaele S., Lu Z., Sheng W.,
Xu C., Chen H., Ouyang J., Wang S., Ling D., Hsu P.H., Zou L.,
Jambhekar A., He C., Shi Y.;
"RNA m(6)A methylation regulates the ultraviolet-induced DNA damage
response.";
Nature 543:573-576(2017).
[27]
IDENTIFICATION IN THE WMM COMPLEX.
PubMed=29507755; DOI=10.1038/s41421-018-0019-0;
Yue Y., Liu J., Cui X., Cao J., Luo G., Zhang Z., Cheng T., Gao M.,
Shu X., Ma H., Wang F., Wang X., Shen B., Wang Y., Feng X., He C.,
Liu J.;
"VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near
stop codon and associates with alternative polyadenylation.";
Cell Discov. 4:10-10(2018).
[28]
FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ENZYME REGULATION,
IDENTIFICATION IN THE WMM COMPLEX, SUMOYLATION AT LYS-177; LYS-211;
LYS-212 AND LYS-215, AND MUTAGENESIS OF LYS-177 AND 211-LYS--LYS-215.
PubMed=29506078; DOI=10.1093/nar/gky156;
Du Y., Hou G., Zhang H., Dou J., He J., Guo Y., Li L., Chen R.,
Wang Y., Deng R., Huang J., Jiang B., Xu M., Cheng J., Chen G.Q.,
Zhao X., Yu J.;
"SUMOylation of the m6A-RNA methyltransferase METTL3 modulates its
function.";
Nucleic Acids Res. 0:0-0(2018).
[29]
FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE WMM COMPLEX,
PHOSPHORYLATION AT SER-2; SER-43; SER-48; SER-50; SER-219; SER-243;
THR-348 AND SER-350, AND MUTAGENESIS OF SER-2; SER-43; SER-48; SER-50;
SER-219; SER-243; 211-LYS--LYS-215 AND 348-THR--SER-350.
PubMed=29348140; DOI=10.1261/rna.064063.117;
Schoeller E., Weichmann F., Treiber T., Ringle S., Treiber N.,
Flatley A., Feederle R., Bruckmann A., Meister G.;
"Interactions, localization, and phosphorylation of the m6A generating
METTL3-METTL14-WTAP complex.";
RNA 24:499-512(2018).
[30]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 354-580 IN COMPLEX WITH
METTL14 AND S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY,
SUBUNIT, AND MUTAGENESIS OF ASP-395; TYR-406; ASN-549 AND GLN-550.
PubMed=27627798; DOI=10.7554/eLife.18434;
Sledz P., Jinek M.;
"Structural insights into the molecular mechanism of the m(6)A writer
complex.";
Elife 5:E18434-E18434(2016).
[31]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 357-580 IN COMPLEX WITH
METTL14 AND S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY,
SUBUNIT, MUTAGENESIS OF CYS-294; CYS-326; ASP-395; TRP-475 AND
ASN-477, VARIANT CYS-406, AND CHARACTERIZATION OF VARIANT CYS-406.
PubMed=27373337; DOI=10.1016/j.molcel.2016.05.041;
Wang P., Doxtader K.A., Nam Y.;
"Structural basis for cooperative function of Mettl3 and Mettl14
methyltransferases.";
Mol. Cell 63:306-317(2016).
[32]
X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 369-580 IN COMPLEX WITH
METTL14 AND S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY,
SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-377; ASP-395;
462-GLN--GLY-479; GLU-532; ARG-536; HIS-538; ASN-539; ASN-549 AND
GLN-550.
PubMed=27281194; DOI=10.1038/nature18298;
Wang X., Feng J., Xue Y., Guan Z., Zhang D., Liu Z., Gong Z., Wang Q.,
Huang J., Tang C., Zou T., Yin P.;
"Structural basis of N(6)-adenosine methylation by the METTL3-METTL14
complex.";
Nature 534:575-578(2016).
-!- FUNCTION: The METTL3-METTL14 heterodimer forms a N6-
methyltransferase complex that methylates adenosine residues at
the N(6) position of some RNAs and regulates various processes
such as the circadian clock, differentiation of embryonic and
haematopoietic stem cells, cortical neurogenesis, response to DNA
damage, differentiation of T-cells and primary miRNA processing
(PubMed:22575960, PubMed:24284625, PubMed:25719671,
PubMed:25799998, PubMed:26321680, PubMed:26593424,
PubMed:27627798, PubMed:27373337, PubMed:27281194,
PubMed:28297716, PubMed:29506078, PubMed:29348140,
PubMed:9409616). In the heterodimer formed with METTL14, METTL3
constitutes the catalytic core (PubMed:27627798, PubMed:27373337,
PubMed:27281194). N6-methyladenosine (m6A), which takes place at
the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in
mRNA stability, processing, translation efficiency and editing
(PubMed:22575960, PubMed:24284625, PubMed:25719671,
PubMed:25799998, PubMed:26321680, PubMed:26593424,
PubMed:28297716, PubMed:9409616). M6A acts as a key regulator of
mRNA stability: methylation is completed upon the release of mRNA
into the nucleoplasm and promotes mRNA destabilization and
degradation (PubMed:28637692). In embryonic stem cells (ESCs), m6A
methylation of mRNAs encoding key naive pluripotency-promoting
transcripts results in transcript destabilization, promoting
differentiation of ESCs (By similarity). M6A regulates the length
of the circadian clock: acts as an early pace-setter in the
circadian loop by putting mRNA production on a fast-track for
facilitating nuclear processing, thereby providing an early point
of control in setting the dynamics of the feedback loop (By
similarity). M6A regulates spermatogonial differentiation and
meiosis and is essential for male fertility and spermatogenesis
(By similarity). Involved in the response to DNA damage: in
response to ultraviolet irradiation, METTL3 rapidly catalyzes the
formation of m6A on poly(A) transcripts at DNA damage sites,
leading to the recruitment of POLK to DNA damage sites
(PubMed:28297716). M6A is also required for T-cell homeostasis and
differentiation: m6A methylation of transcripts of SOCS family
members (SOCS1, SOCS3 and CISH) in naive T-cells promotes mRNA
destabilization and degradation, promoting T-cell differentiation
(By similarity). M6A also takes place in other RNA molecules, such
as primary miRNA (pri-miRNAs) (PubMed:25799998). Mediates m6A
methylation of Xist RNA, thereby participating in random X
inactivation: m6A methylation of Xist leads to target YTHDC1
reader on Xist and promote transcription repression activity of
Xist (PubMed:27602518). 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).
METTL3 mediates methylation of pri-miRNAs, marking them for
recognition and processing by DGCR8 (PubMed:25799998). Acts as a
positive regulator of mRNA translation independently of the
methyltransferase activity: promotes translation by interacting
with the translation initiation machinery in the cytoplasm
(PubMed:27117702). Its overexpression in a number of cancer cells
suggests that it may participate to cancer cell proliferation by
promoting mRNA translation (PubMed:27117702).
{ECO:0000250|UniProtKB:Q8C3P7, ECO:0000269|PubMed:22575960,
ECO:0000269|PubMed:24284625, ECO:0000269|PubMed:25719671,
ECO:0000269|PubMed:25799998, ECO:0000269|PubMed:26321680,
ECO:0000269|PubMed:26593424, ECO:0000269|PubMed:27117702,
ECO:0000269|PubMed:27281194, ECO:0000269|PubMed:27373337,
ECO:0000269|PubMed:27602518, ECO:0000269|PubMed:27627798,
ECO:0000269|PubMed:28297716, ECO:0000269|PubMed:28637692,
ECO:0000269|PubMed:29348140, ECO:0000269|PubMed:29506078,
ECO:0000269|PubMed:9409616}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a 5-(N(7)-methyl 5-
triphosphoguanosine)-2'-O-methyladenosine-[mRNA] = S-adenosyl-L-
homocysteine + a 5-(N(7)-methyl 5-triphosphoguanosine)-N(6),2'-O-
dimethyladenosine-[mRNA]. {ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337, ECO:0000269|PubMed:27627798,
ECO:0000269|PubMed:29348140, ECO:0000269|PubMed:29506078,
ECO:0000269|PubMed:9409616}.
-!- ENZYME REGULATION: Methyltransferase activity is regulated by
miRNAs via a sequence pairing mechanism (By similarity).
Methyltransferase activity is inhibited by sumoylation
(PubMed:29506078). {ECO:0000250|UniProtKB:Q8C3P7,
ECO:0000269|PubMed:29506078}.
-!- SUBUNIT: Heterodimer; heterodimerizes with METTL14 to form an
antiparallel heterodimer that constitutes an active
methyltransferase (PubMed:27627798, PubMed:27373337,
PubMed:27281194). Component of the WMM complex, a N6-
methyltransferase complex composed of a catalytic subcomplex,
named MAC, and of an associated subcomplex, named MACOM
(PubMed:24407421, PubMed:24981863, PubMed:27602518,
PubMed:29507755, PubMed:29506078, PubMed:29348140). The MAC
subcomplex is composed of METTL3 and METTL14 (PubMed:24407421,
PubMed:24981863, PubMed:27602518, PubMed:29507755). The MACOM
subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and,
in some cases of RBM15 (RBM15 or RBM15B) (PubMed:27602518,
PubMed:29507755). Interacts with NCBP1/CBP80 (PubMed:27117702).
Interacts with EIF4E (PubMed:27117702). Interacts with EIF3B
(PubMed:27117702). {ECO:0000269|PubMed:24407421,
ECO:0000269|PubMed:24981863, ECO:0000269|PubMed:27117702,
ECO:0000269|PubMed:27281194, ECO:0000269|PubMed:27373337,
ECO:0000269|PubMed:27602518, ECO:0000269|PubMed:27627798,
ECO:0000269|PubMed:29348140, ECO:0000269|PubMed:29506078,
ECO:0000269|PubMed:29507755}.
-!- INTERACTION:
Q9HCE5:METTL14; NbExp=10; IntAct=EBI-16084936, EBI-6661081;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25719671,
ECO:0000269|PubMed:26458103, ECO:0000269|PubMed:27117702,
ECO:0000269|PubMed:29348140, ECO:0000269|PubMed:29506078}. Nucleus
speckle {ECO:0000269|PubMed:9409616}. Cytoplasm
{ECO:0000269|PubMed:27117702}. Note=Colocalizes with speckles in
interphase nuclei, suggesting that it may be associated with
nuclear pre-mRNA splicing components (PubMed:9409616). In response
to ultraviolet irradiation, colocalizes to DNA damage sites
however, it probably does not bind DNA but localizes in the
vicinity of DNA damage sites (PubMed:28297716).
{ECO:0000269|PubMed:28297716, ECO:0000269|PubMed:9409616}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q86U44-1; Sequence=Displayed;
Name=2;
IsoId=Q86U44-2; Sequence=VSP_007864, VSP_007865, VSP_007866;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed at low level. Expressed in
spleen, thymus, prostate, testis, ovary, small intestine, colon
and peripheral blood leukocytes. {ECO:0000269|PubMed:9409616}.
-!- INDUCTION: Overexpressed in a number of cancer tissues, such as
lung adenocarcinoma and colon adenocarcinoma (PubMed:27117702).
{ECO:0000269|PubMed:27117702}.
-!- DOMAIN: Gate loop 1 and gate loop 2 regions are adjacent to the S-
adenosyl-L-homocysteine-binding site and display large
conformational changes upon ligand-binding. They may play an
important role in adenosine recognition. The interface loop
contributes to the heterodimer interaction.
{ECO:0000269|PubMed:27281194}.
-!- PTM: Sumoylation inhibits the N6-adenosine-methyltransferase
activity. Sumoylation does not affect subcellular location or
interaction with METTL14. Desumoylated by SENP1.
{ECO:0000269|PubMed:29506078}.
-!- SIMILARITY: Belongs to the MT-A70-like family.
{ECO:0000255|PROSITE-ProRule:PRU00489}.
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EMBL; AF014837; AAB71850.1; -; Genomic_DNA.
EMBL; AF283991; AAG13956.1; -; Genomic_DNA.
EMBL; AE000658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX247964; CAD62303.1; -; mRNA.
EMBL; BC003031; AAH03031.1; -; mRNA.
EMBL; BC001650; AAH01650.1; -; mRNA.
EMBL; BC052244; AAH52244.1; -; mRNA.
CCDS; CCDS32044.1; -. [Q86U44-1]
RefSeq; NP_062826.2; NM_019852.4. [Q86U44-1]
UniGene; Hs.168799; -.
PDB; 5IL0; X-ray; 1.88 A; A=369-580.
PDB; 5IL1; X-ray; 1.71 A; A=369-580.
PDB; 5IL2; X-ray; 1.61 A; A=369-580.
PDB; 5K7M; X-ray; 1.65 A; A=357-580.
PDB; 5K7U; X-ray; 1.70 A; A=357-580.
PDB; 5K7W; X-ray; 1.65 A; A=357-580.
PDB; 5L6D; X-ray; 1.85 A; A=354-580.
PDB; 5L6E; X-ray; 1.90 A; A=354-580.
PDB; 5TEY; X-ray; 1.80 A; A=1-580.
PDB; 5YZ9; Other; -; A=259-357.
PDBsum; 5IL0; -.
PDBsum; 5IL1; -.
PDBsum; 5IL2; -.
PDBsum; 5K7M; -.
PDBsum; 5K7U; -.
PDBsum; 5K7W; -.
PDBsum; 5L6D; -.
PDBsum; 5L6E; -.
PDBsum; 5TEY; -.
PDBsum; 5YZ9; -.
ProteinModelPortal; Q86U44; -.
SMR; Q86U44; -.
BioGrid; 121139; 21.
ComplexPortal; CPX-1605; WMM N6-adenosine-methyltransferase complex.
DIP; DIP-60727N; -.
IntAct; Q86U44; 10.
STRING; 9606.ENSP00000298717; -.
iPTMnet; Q86U44; -.
PhosphoSitePlus; Q86U44; -.
BioMuta; METTL3; -.
DMDM; 33301371; -.
EPD; Q86U44; -.
MaxQB; Q86U44; -.
PaxDb; Q86U44; -.
PeptideAtlas; Q86U44; -.
PRIDE; Q86U44; -.
ProteomicsDB; 69768; -.
ProteomicsDB; 69769; -. [Q86U44-2]
DNASU; 56339; -.
Ensembl; ENST00000298717; ENSP00000298717; ENSG00000165819. [Q86U44-1]
GeneID; 56339; -.
KEGG; hsa:56339; -.
UCSC; uc001wbc.4; human. [Q86U44-1]
CTD; 56339; -.
DisGeNET; 56339; -.
EuPathDB; HostDB:ENSG00000165819.11; -.
GeneCards; METTL3; -.
HGNC; HGNC:17563; METTL3.
MIM; 612472; gene.
neXtProt; NX_Q86U44; -.
OpenTargets; ENSG00000165819; -.
PharmGKB; PA134955499; -.
eggNOG; KOG2098; Eukaryota.
eggNOG; COG4725; LUCA.
GeneTree; ENSGT00550000075058; -.
HOGENOM; HOG000012669; -.
HOVERGEN; HBG052521; -.
InParanoid; Q86U44; -.
KO; K05925; -.
OMA; HTKLWAM; -.
OrthoDB; EOG091G07WA; -.
PhylomeDB; Q86U44; -.
TreeFam; TF323854; -.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
ChiTaRS; METTL3; human.
GeneWiki; METTL3; -.
GenomeRNAi; 56339; -.
PRO; PR:Q86U44; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000165819; -.
CleanEx; HS_METTL3; -.
ExpressionAtlas; Q86U44; baseline and differential.
Genevisible; Q86U44; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
GO; GO:0016422; F:mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0008173; F:RNA methyltransferase activity; IDA:UniProtKB.
GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
GO; GO:0006382; P:adenosine to inosine editing; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0098508; P:endothelial to hematopoietic transition; ISS:UniProtKB.
GO; GO:0021861; P:forebrain radial glial cell differentiation; ISS:UniProtKB.
GO; GO:0042063; P:gliogenesis; ISS:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
GO; GO:0080009; P:mRNA methylation; IDA:UniProtKB.
GO; GO:0006397; P:mRNA processing; ISS:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
GO; GO:1903679; P:positive regulation of cap-independent translational initiation; IMP:UniProtKB.
GO; GO:1990744; P:primary miRNA methylation; IDA:UniProtKB.
GO; GO:0031053; P:primary miRNA processing; IDA:UniProtKB.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
GO; GO:0051445; P:regulation of meiotic cell cycle; ISS:UniProtKB.
GO; GO:0045580; P:regulation of T cell differentiation; ISS:UniProtKB.
GO; GO:0001510; P:RNA methylation; IMP:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
InterPro; IPR025848; MT-A70.
InterPro; IPR007757; MT-A70-like.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF05063; MT-A70; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51143; MT_A70; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Biological rhythms;
Complete proteome; Cytoplasm; Differentiation;
Direct protein sequencing; DNA damage; Isopeptide bond;
Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; RNA-binding; S-adenosyl-L-methionine;
Spermatogenesis; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 580 N6-adenosine-methyltransferase catalytic
subunit.
/FTId=PRO_0000207630.
REGION 377 378 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:5IL1,
ECO:0000244|PDB:5IL2,
ECO:0000244|PDB:5K7U,
ECO:0000244|PDB:5K7W,
ECO:0000244|PDB:5L6D,
ECO:0000244|PDB:5L6E,
ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337,
ECO:0000269|PubMed:27627798}.
REGION 396 410 Gate loop 1.
{ECO:0000303|PubMed:27281194}.
REGION 450 454 Interaction with METTL14.
{ECO:0000244|PDB:5IL0,
ECO:0000244|PDB:5IL1,
ECO:0000244|PDB:5IL2,
ECO:0000269|PubMed:27281194}.
REGION 462 479 Interphase loop.
{ECO:0000303|PubMed:27281194}.
REGION 464 480 Interaction with METTL14.
{ECO:0000244|PDB:5IL0,
ECO:0000244|PDB:5IL1,
ECO:0000244|PDB:5IL2,
ECO:0000269|PubMed:27281194}.
REGION 465 478 Positively charged region required for
RNA-binding.
{ECO:0000269|PubMed:27281194}.
REGION 507 515 Gate loop 2.
{ECO:0000303|PubMed:27281194}.
REGION 536 539 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:5IL1,
ECO:0000244|PDB:5IL2,
ECO:0000244|PDB:5K7U,
ECO:0000244|PDB:5K7W,
ECO:0000244|PDB:5L6D,
ECO:0000244|PDB:5L6E,
ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337,
ECO:0000269|PubMed:27627798}.
REGION 549 550 S-adenosyl-L-methionine binding.
{ECO:0000244|PDB:5IL1,
ECO:0000244|PDB:5IL2,
ECO:0000244|PDB:5K7U,
ECO:0000244|PDB:5K7W,
ECO:0000244|PDB:5L6D,
ECO:0000244|PDB:5L6E,
ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337,
ECO:0000269|PubMed:27627798}.
MOTIF 210 215 Nuclear localization signal.
{ECO:0000269|PubMed:29348140}.
BINDING 395 395 S-adenosyl-L-methionine.
{ECO:0000244|PDB:5IL1,
ECO:0000244|PDB:5IL2,
ECO:0000244|PDB:5K7U,
ECO:0000244|PDB:5K7W,
ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337}.
BINDING 438 438 Interaction with METTL14.
{ECO:0000244|PDB:5IL1,
ECO:0000244|PDB:5IL2,
ECO:0000269|PubMed:27281194}.
BINDING 441 441 Interaction with METTL14.
{ECO:0000244|PDB:5IL1,
ECO:0000244|PDB:5IL2,
ECO:0000269|PubMed:27281194}.
BINDING 513 513 S-adenosyl-L-methionine.
{ECO:0000244|PDB:5IL1,
ECO:0000244|PDB:5IL2,
ECO:0000244|PDB:5K7U,
ECO:0000244|PDB:5K7W,
ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337}.
MOD_RES 2 2 N-acetylserine; alternate.
{ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 Phosphoserine; alternate.
{ECO:0000269|PubMed:29348140}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:29348140}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000269|PubMed:29348140}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000269|PubMed:29348140}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:29348140}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:29348140}.
MOD_RES 348 348 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:29348140}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000269|PubMed:29348140}.
CROSSLNK 177 177 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:29506078}.
CROSSLNK 211 211 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:29506078}.
CROSSLNK 212 212 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:29506078}.
CROSSLNK 215 215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:29506078}.
VAR_SEQ 1 284 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_007864.
VAR_SEQ 486 505 GVKGNPQGFNQGLDCDVIVA -> SSSGAQFNRWSTKKNHL
ISY (in isoform 2). {ECO:0000303|Ref.2}.
/FTId=VSP_007865.
VAR_SEQ 506 580 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_007866.
VARIANT 406 406 Y -> C (found in patients with large
intestine cancer; unknown pathological
significance; does not affect interaction
with METTL14; abolished RNA
methyltransferase activity in vitro).
{ECO:0000269|PubMed:27373337}.
/FTId=VAR_076859.
MUTAGEN 2 2 S->A: Does not affect nuclear
localization, interaction with METTL14 or
WTAP or catalytic activity; when
associated with A-43; A-48 and A-50.
{ECO:0000269|PubMed:29348140}.
MUTAGEN 43 43 S->A: Does not affect nuclear
localization, interaction with METTL14 or
WTAP or catalytic activity; when
associated with A-2; A-48 and A-50.
{ECO:0000269|PubMed:29348140}.
MUTAGEN 48 48 S->A: Does not affect nuclear
localization, interaction with METTL14 or
WTAP or catalytic activity; when
associated with A-2; A-43 and A-50.
{ECO:0000269|PubMed:29348140}.
MUTAGEN 50 50 S->A: Does not affect nuclear
localization, interaction with METTL14 or
WTAP or catalytic activity; when
associated with A-2; A-43 and A-48.
{ECO:0000269|PubMed:29348140}.
MUTAGEN 177 177 K->R: In 4KR; strongly decreased
sumoylation; when associated with 211-R--
R-215. {ECO:0000269|PubMed:29506078}.
MUTAGEN 211 215 KKSRK->GGSGG: Abolishes localization to
the nucleus.
{ECO:0000269|PubMed:29348140}.
MUTAGEN 211 215 KKSRK->RRSRR: In 3KR; decreased
sumoylation. In 4KR; strongly decreased
sumoylation; when associated with R-177.
{ECO:0000269|PubMed:29506078}.
MUTAGEN 219 219 S->A: Does not affect nuclear
localization, interaction with METTL14 or
WTAP or catalytic activity; when
associated with A-243 and 348-A--A-350.
{ECO:0000269|PubMed:29348140}.
MUTAGEN 243 243 S->A: Does not affect nuclear
localization, interaction with METTL14 or
WTAP or catalytic activity; when
associated with A-219 and 348-A--A-350.
{ECO:0000269|PubMed:29348140}.
MUTAGEN 294 294 C->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:27373337}.
MUTAGEN 326 326 C->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:27373337}.
MUTAGEN 348 350 TPS->APA: Does not affect nuclear
localization, interaction with METTL14 or
WTAP or catalytic activity; when
associated with A-219 and A-243.
{ECO:0000269|PubMed:29348140}.
MUTAGEN 377 377 D->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:27281194}.
MUTAGEN 395 398 DPPW->APPA: Loss of function. Abolishes
ability to regulate primary miRNA
processing. Does not affect ability to
promote mRNA translation. Abolishes
formation of m6A at DNA damage sites.
{ECO:0000269|PubMed:25799998,
ECO:0000269|PubMed:27117702,
ECO:0000269|PubMed:27627798,
ECO:0000269|PubMed:28297716}.
MUTAGEN 395 395 D->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337}.
MUTAGEN 406 406 Y->A: Strong reduction in
methyltransferase activity.
{ECO:0000269|PubMed:27627798}.
MUTAGEN 462 479 QLQRIIRTGRTGHWLNHG->AAAAAA: Impaired RNA-
binding and methyltransferase activities.
{ECO:0000269|PubMed:27281194}.
MUTAGEN 475 475 W->A: Decreased methyltransferase
activity. {ECO:0000269|PubMed:27373337}.
MUTAGEN 477 477 N->A: Decreased methyltransferase
activity. {ECO:0000269|PubMed:27373337}.
MUTAGEN 532 532 E->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:27281194}.
MUTAGEN 536 536 R->A: Slight reduction in
methyltransferase activity.
{ECO:0000269|PubMed:27281194}.
MUTAGEN 538 538 H->A: Slight reduction in
methyltransferase activity.
{ECO:0000269|PubMed:27281194}.
MUTAGEN 539 539 N->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:27281194}.
MUTAGEN 549 549 N->A: Slight reduction in
methyltransferase activity. Strong
reduction in methyltransferase activity;
when associated with A-550.
{ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27627798}.
MUTAGEN 550 550 Q->A: Slight reduction in
methyltransferase activity. Strong
reduction in methyltransferase activity;
when associated with A-549.
{ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27627798}.
CONFLICT 251 251 N -> I (in Ref. 1; AAB71850).
{ECO:0000305}.
CONFLICT 263 264 KF -> I (in Ref. 1; AAB71850).
{ECO:0000305}.
CONFLICT 382 382 D -> V (in Ref. 1; AAB71850).
{ECO:0000305}.
CONFLICT 568 568 R -> K (in Ref. 4; AAH52244).
{ECO:0000305}.
STRAND 372 376 {ECO:0000244|PDB:5IL2}.
TURN 378 380 {ECO:0000244|PDB:5IL2}.
HELIX 383 386 {ECO:0000244|PDB:5IL2}.
STRAND 390 394 {ECO:0000244|PDB:5IL2}.
HELIX 411 416 {ECO:0000244|PDB:5IL2}.
HELIX 419 422 {ECO:0000244|PDB:5IL2}.
STRAND 424 432 {ECO:0000244|PDB:5IL2}.
HELIX 436 446 {ECO:0000244|PDB:5IL2}.
STRAND 450 460 {ECO:0000244|PDB:5IL2}.
STRAND 464 466 {ECO:0000244|PDB:5IL2}.
STRAND 473 477 {ECO:0000244|PDB:5IL2}.
STRAND 480 489 {ECO:0000244|PDB:5IL2}.
STRAND 498 506 {ECO:0000244|PDB:5IL2}.
STRAND 510 512 {ECO:0000244|PDB:5IL2}.
HELIX 516 524 {ECO:0000244|PDB:5IL2}.
STRAND 530 534 {ECO:0000244|PDB:5IL2}.
HELIX 537 539 {ECO:0000244|PDB:5IL2}.
STRAND 544 548 {ECO:0000244|PDB:5IL2}.
STRAND 553 555 {ECO:0000244|PDB:5IL2}.
HELIX 559 568 {ECO:0000244|PDB:5IL2}.
SEQUENCE 580 AA; 64474 MW; 63A7F10195A3C6AC CRC64;
MSDTWSSIQA HKKQLDSLRE RLQRRRKQDS GHLDLRNPEA ALSPTFRSDS PVPTAPTSGG
PKPSTASAVP ELATDPELEK KLLHHLSDLA LTLPTDAVSI CLAISTPDAP ATQDGVESLL
QKFAAQELIE VKRGLLQDDA HPTLVTYADH SKLSAMMGAV AEKKGPGEVA GTVTGQKRRA
EQDSTTVAAF ASSLVSGLNS SASEPAKEPA KKSRKHAASD VDLEIESLLN QQSTKEQQSK
KVSQEILELL NTTTAKEQSI VEKFRSRGRA QVQEFCDYGT KEECMKASDA DRPCRKLHFR
RIINKHTDES LGDCSFLNTC FHMDTCKYVH YEIDACMDSE APGSKDHTPS QELALTQSVG
GDSSADRLFP PQWICCDIRY LDVSILGKFA VVMADPPWDI HMELPYGTLT DDEMRRLNIP
VLQDDGFLFL WVTGRAMELG RECLNLWGYE RVDEIIWVKT NQLQRIIRTG RTGHWLNHGK
EHCLVGVKGN PQGFNQGLDC DVIVAEVRST SHKPDEIYGM IERLSPGTRK IELFGRPHNV
QPNWITLGNQ LDGIHLLDPD VVARFKQRYP DGIISKPKNL


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E2223m ELISA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt 96T
E2223Rb ELISA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT,Oryctolagus cuniculus,Rabb 96T
U2223m CLIA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Temt 96T
E2223h ELISA Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Homo sapiens,Human,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,INMT 96T
E0518p Mouse ELISA Kit FOR N6-adenosine-methyltransferase subunit METTL14 96T
PLCG2_RAT Mouse ELISA Kit FOR N6-adenosine-methyltransferase subunit METTL14 96T
CSB-EL013732HU Human N6-adenosine-methyltransferase 70 kDa subunit(METTL3) ELISA kit 96T


 

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