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

 MTA70_HUMAN             Reviewed;         580 AA.
Q86U44; O14736; Q86V05; Q9HB32;
25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
25-JUL-2003, sequence version 2.
25-OCT-2017, entry version 129.
RecName: Full=N6-adenosine-methyltransferase 70 kDa subunit;
Short=MT-A70;
EC=2.1.1.62 {ECO:0000269|PubMed:27281194, ECO:0000269|PubMed:9409616};
AltName: Full=Methyltransferase-like protein 3;
Short=hMETTL3 {ECO:0000303|PubMed:27373337};
Name=METTL3; 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] {ECO:0000244|PDB:5K7M, ECO:0000244|PDB:5K7U, ECO:0000244|PDB:5K7W}
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).
[25] {ECO:0000244|PDB:5IL0, ECO:0000244|PDB:5IL1, ECO:0000244|PDB:5IL2}
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 of
some RNAs and regulates the circadian clock, differentiation of
embryonic stem cells and primary miRNA processing
(PubMed:22575960, PubMed:24284625, PubMed:25719671,
PubMed:25799998, PubMed:26321680, PubMed:26593424,
PubMed:27373337, PubMed:27281194, PubMed:9409616). In the
heterodimer formed with METTL14, METTL3 constitutes the catalytic
core (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 the efficiency of mRNA splicing,
processing, translation efficiency, editing and mRNA stability
(PubMed:22575960, PubMed:24284625, PubMed:25719671,
PubMed:25799998, PubMed:26321680, PubMed:26593424,
PubMed:9409616). 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 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, promoting
differentiation of ESCs (By similarity). M6A also takes place in
other RNA molecules, such as primary miRNA (pri-miRNAs)
(PubMed:25799998). METTL3 also 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:9409616}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + m(7)G(5')pppAm = S-
adenosyl-L-homocysteine + m(7)G(5')pppm(6)Am.
{ECO:0000269|PubMed:27281194, ECO:0000269|PubMed:27373337,
ECO:0000269|PubMed:9409616}.
-!- ENZYME REGULATION: Methyltransferase activity is regulated by
miRNAs via a sequence pairing mechanism.
{ECO:0000250|UniProtKB:Q8C3P7}.
-!- SUBUNIT: Heterodimer; heterodimerizes with METTL14 to form an
antiparallel heterodimer that constitutes an active
methyltransferase (PubMed:27373337, PubMed:27281194). Component of
the WMM complex, a N6-methyltransferase complex composed of WTAP,
METTL3 and METTL14 (PubMed:24407421, PubMed:24981863). 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}.
-!- INTERACTION:
Q9HCE5:METTL14; NbExp=10; IntAct=EBI-16084936, EBI-6661081;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26458103,
ECO:0000269|PubMed:27117702}. 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.
{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}.
-!- 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.
PDBsum; 5IL0; -.
PDBsum; 5IL1; -.
PDBsum; 5IL2; -.
PDBsum; 5K7M; -.
PDBsum; 5K7U; -.
PDBsum; 5K7W; -.
PDBsum; 5L6D; -.
PDBsum; 5L6E; -.
PDBsum; 5TEY; -.
ProteinModelPortal; Q86U44; -.
SMR; Q86U44; -.
BioGrid; 121139; 21.
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; -.
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.
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: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:0007623; P:circadian rhythm; 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: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:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0001510; P:RNA methylation; IMP: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; Direct protein sequencing;
Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 580 N6-adenosine-methyltransferase 70 kDa
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:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337}.
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:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337}.
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:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337}.
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.
{ECO:0000244|PubMed:19413330}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 348 348 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
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 294 294 C->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:27373337}.
MUTAGEN 326 326 C->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:27373337}.
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.
{ECO:0000269|PubMed:25799998,
ECO:0000269|PubMed:27117702}.
MUTAGEN 395 395 D->A: Abolishes methyltransferase
activity. {ECO:0000269|PubMed:27281194,
ECO:0000269|PubMed:27373337}.
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.
{ECO:0000269|PubMed:27281194}.
MUTAGEN 550 550 Q->A: Slight reduction in
methyltransferase activity.
{ECO:0000269|PubMed:27281194}.
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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