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DNA (cytosine-5)-methyltransferase 3A (Dnmt3a) (EC 2.1.1.37) (DNA methyltransferase MmuIIIA) (DNA MTase MmuIIIA) (M.MmuIIIA)

 DNM3A_MOUSE             Reviewed;         908 AA.
O88508; Q3TZK8; Q3UH24; Q8CJ60; Q922J0; Q9CSE1;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 2.
22-NOV-2017, entry version 175.
RecName: Full=DNA (cytosine-5)-methyltransferase 3A;
Short=Dnmt3a;
EC=2.1.1.37;
AltName: Full=DNA methyltransferase MmuIIIA;
Short=DNA MTase MmuIIIA;
Short=M.MmuIIIA;
Name=Dnmt3a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9662389; DOI=10.1038/890;
Okano M., Xie S., Li E.;
"Cloning and characterization of a family of novel mammalian DNA
(cytosine-5) methyltransferases.";
Nat. Genet. 19:219-220(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary gland;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Brain, Embryo, and Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION,
ALTERNATIVE PROMOTER USAGE, AND TISSUE SPECIFICITY.
STRAIN=129/SvJ;
PubMed=12138111; DOI=10.1074/jbc.M205312200;
Chen T., Ueda Y., Xie S., Li E.;
"A novel Dnmt3a isoform produced from an alternative promoter
localizes to euchromatin and its expression correlates with active de
novo methylation.";
J. Biol. Chem. 277:38746-38754(2002).
[5]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=10555141; DOI=10.1016/S0092-8674(00)81656-6;
Okano M., Bell D.W., Haber D.A., Li E.;
"DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo
methylation and mammalian development.";
Cell 99:247-257(1999).
[6]
FUNCTION.
PubMed=11399089; DOI=10.1006/jmbi.2001.4710;
Gowher H., Jeltsch A.;
"Enzymatic properties of recombinant Dnmt3a DNA methyltransferase from
mouse: the enzyme modifies DNA in a non-processive manner and also
methylates non-CpG correction sites.";
J. Mol. Biol. 309:1201-1208(2001).
[7]
ERRATUM.
Gowher H., Jeltsch A.;
J. Mol. Biol. 310:951-951(2001).
[8]
FUNCTION, AND INTERACTION WITH ZBTB18 AND HDAC1.
PubMed=11350943; DOI=10.1093/emboj/20.10.2536;
Fuks F., Burgers W.A., Godin N., Kasai M., Kouzarides T.;
"Dnmt3a binds deacetylases and is recruited by a sequence-specific
repressor to silence transcription.";
EMBO J. 20:2536-2544(2001).
[9]
FUNCTION.
PubMed=11919202; DOI=10.1074/jbc.M202148200;
Gowher H., Jeltsch A.;
"Molecular enzymology of the catalytic domains of the Dnmt3a and
Dnmt3b DNA methyltransferases.";
J. Biol. Chem. 277:20409-20414(2002).
[10]
IDENTIFICATION IN A COMPLEX WITH HDAC1.
PubMed=12616525; DOI=10.1002/jcb.10457;
Datta J., Ghoshal K., Sharma S.M., Tajima S., Jacob S.T.;
"Biochemical fractionation reveals association of DNA
methyltransferase (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a
histone H3 methyltransferase and Hdac1.";
J. Cell. Biochem. 88:855-864(2003).
[11]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 302-VAL-PRO-303 AND
705-PRO-CYS-706.
PubMed=15456878; DOI=10.1128/MCB.24.20.9048-9058.2004;
Chen T., Tsujimoto N., Li E.;
"The PWWP domain of Dnmt3a and Dnmt3b is required for directing DNA
methylation to the major satellite repeats at pericentric
heterochromatin.";
Mol. Cell. Biol. 24:9048-9058(2004).
[12]
FUNCTION.
PubMed=15215868; DOI=10.1038/nature02633;
Kaneda M., Okano M., Hata K., Sado T., Tsujimoto N., Li E., Sasaki H.;
"Essential role for de novo DNA methyltransferase Dnmt3a in paternal
and maternal imprinting.";
Nature 429:900-903(2004).
[13]
SUMOYLATION, AND INTERACTION WITH UBC9; PIAS1 AND PIAS2.
PubMed=14752048; DOI=10.1093/nar/gkh195;
Ling Y., Sankpal U.T., Robertson A.K., McNally J.G., Karpova T.,
Robertson K.D.;
"Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1
modulates its interaction with histone deacetylases (HDACs) and its
capacity to repress transcription.";
Nucleic Acids Res. 32:598-610(2004).
[14]
ENZYME REGULATION.
PubMed=15671018; DOI=10.1074/jbc.M413412200;
Gowher H., Liebert K., Hermann A., Xu G., Jeltsch A.;
"Mechanism of stimulation of catalytic activity of Dnmt3A and Dnmt3B
DNA-(cytosine-C5)-methyltransferases by Dnmt3L.";
J. Biol. Chem. 280:13341-13348(2005).
[15]
FUNCTION.
PubMed=16567415; DOI=10.1093/jb/mvj044;
Takeshima H., Suetake I., Shimahara H., Ura K., Tate S., Tajima S.;
"Distinct DNA methylation activity of Dnmt3a and Dnmt3b towards naked
and nucleosomal DNA.";
J. Biochem. 139:503-515(2006).
[16]
MUTAGENESIS OF PHE-636; GLU-660; ASP-682; CYS-706; ASN-707; SER-710;
ARG-716; LYS-717; GLU-752; ASN-753; ARG-788; ARG-827; ARG-832;
ARG-878; ARG-881 AND ARG-883.
PubMed=16472822; DOI=10.1016/j.jmb.2006.01.035;
Gowher H., Loutchanwoot P., Vorobjeva O., Handa V., Jurkowska R.Z.,
Jurkowski T.P., Jeltsch A.;
"Mutational analysis of the catalytic domain of the murine Dnmt3a DNA-
(cytosine C5)-methyltransferase.";
J. Mol. Biol. 357:928-941(2006).
[17]
INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX.
PubMed=16357870; DOI=10.1038/nature04431;
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
Esteller M., Di Croce L., de Launoit Y., Fuks F.;
"The Polycomb group protein EZH2 directly controls DNA methylation.";
Nature 439:871-874(2006).
[18]
ERRATUM.
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
Esteller M., Di Croce L., de Launoit Y., Fuks F.;
Nature 446:824-824(2006).
[19]
FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF PHE-728.
PubMed=17713477; DOI=10.1038/nature06146;
Jia D., Jurkowska R.Z., Zhang X., Jeltsch A., Cheng X.;
"Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA
methylation.";
Nature 449:248-251(2007).
[20]
FUNCTION.
PubMed=18823905; DOI=10.1016/j.jmb.2008.03.001;
Takeshima H., Suetake I., Tajima S.;
"Mouse Dnmt3a preferentially methylates linker DNA and is inhibited by
histone H1.";
J. Mol. Biol. 383:810-821(2008).
[21]
INTERACTION WITH UHRF1.
PubMed=19798101; DOI=10.1038/embor.2009.201;
Meilinger D., Fellinger K., Bultmann S., Rothbauer U., Bonapace I.M.,
Klinkert W.E., Spada F., Leonhardt H.;
"Np95 interacts with de novo DNA methyltransferases, Dnmt3a and
Dnmt3b, and mediates epigenetic silencing of the viral CMV promoter in
embryonic stem cells.";
EMBO Rep. 10:1259-1264(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; THR-257; SER-386
AND SER-389, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Kidney, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[23]
SUBCELLULAR LOCATION.
PubMed=20547484; DOI=10.1074/jbc.M109.089433;
Dhayalan A., Rajavelu A., Rathert P., Tamas R., Jurkowska R.Z.,
Ragozin S., Jeltsch A.;
"The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and
guides DNA methylation.";
J. Biol. Chem. 285:26114-26120(2010).
[24]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-167, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Required for genome-wide de novo methylation and is
essential for the establishment of DNA methylation patterns during
development. DNA methylation is coordinated with methylation of
histones. It modifies DNA in a non-processive manner and also
methylates non-CpG sites. May preferentially methylate DNA linker
between 2 nucleosomal cores and is inhibited by histone H1. Plays
a role in paternal and maternal imprinting. Required for
methylation of most imprinted loci in germ cells. Acts as a
transcriptional corepressor for ZBTB18. Recruited to trimethylated
'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress
transcription through the recruitment of HDAC activity.
{ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:11350943,
ECO:0000269|PubMed:11399089, ECO:0000269|PubMed:11919202,
ECO:0000269|PubMed:15215868, ECO:0000269|PubMed:16567415,
ECO:0000269|PubMed:17713477, ECO:0000269|PubMed:18823905}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
homocysteine + DNA containing 5-methylcytosine.
{ECO:0000255|PROSITE-ProRule:PRU10018}.
-!- ENZYME REGULATION: Activated by binding to the regulatory factor
DNMT3L. {ECO:0000269|PubMed:15671018,
ECO:0000269|PubMed:17713477}.
-!- SUBUNIT: Heterotetramer composed of 1 DNMT3A homodimer and 2
DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L). Interacts with
DNMT1 and DNMT3B. Interacts with MPHOSPH8. Interacts with histone
H3 that is not methylated at 'Lys-4' (H3K4) (By similarity). Binds
the ZBTB18 transcriptional repressor. Interacts with SETDB1.
Associates with HDAC1 through its ADD domain. Interacts with the
PRC2/EED-EZH2 complex. Interacts with UBC9, PIAS1 and PIAS2.
{ECO:0000250, ECO:0000269|PubMed:11350943,
ECO:0000269|PubMed:12616525, ECO:0000269|PubMed:14752048,
ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:19798101}.
-!- INTERACTION:
Q9CWR8:Dnmt3l; NbExp=6; IntAct=EBI-995154, EBI-3043871;
Q9Z148-2:Ehmt2; NbExp=3; IntAct=EBI-15650457, EBI-15737169;
Q60848:Hells; NbExp=4; IntAct=EBI-995154, EBI-3043887;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12138111,
ECO:0000269|PubMed:15456878, ECO:0000269|PubMed:20547484}.
Cytoplasm {ECO:0000250}. Note=Accumulates in the major satellite
repeats at pericentric heterochromatin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=1;
IsoId=O88508-1; Sequence=Displayed;
Name=2;
IsoId=O88508-2; Sequence=VSP_009423;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed ubiquitously at low
levels. Expression of isoform 2 is restricted to tissues
containing cells which are undergoing active de novo methylation,
including spleen, testis and thymus.
{ECO:0000269|PubMed:12138111}.
-!- DEVELOPMENTAL STAGE: At E7.5, the protein is moderately expressed
in embryonic ectoderm and weakly in mesodermal cells. At E8.5 and
E9.5, the expression become ubiquitous with an increase in the
somites and in the ventral part of the embryo.
{ECO:0000269|PubMed:10555141}.
-!- DOMAIN: The PWWP domain is essential for targeting to pericentric
heterochromatin. It specifically recognizes and binds
trimethylated 'Lys-36' of histone H3 (H3K36me3) (PubMed:20547484).
{ECO:0000269|PubMed:20547484}.
-!- PTM: Sumoylated; sumoylation disrupts the ability to interact with
histone deacetylases (HDAC1 and HDAC2) and repress transcription.
{ECO:0000269|PubMed:14752048}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. C5-methyltransferase family.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
-!- SEQUENCE CAUTION:
Sequence=BAB28644.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF068625; AAC40177.2; -; mRNA.
EMBL; AF480164; AAN40038.1; -; mRNA.
EMBL; AK013096; BAB28644.2; ALT_INIT; mRNA.
EMBL; AK090132; BAC41110.1; -; mRNA.
EMBL; AK147263; BAE27806.1; -; mRNA.
EMBL; AK147627; BAE28033.1; -; mRNA.
EMBL; AK147642; BAE28043.1; -; mRNA.
EMBL; AK147676; BAE28067.1; -; mRNA.
EMBL; AK157792; BAE34200.1; -; mRNA.
EMBL; BC007466; AAH07466.1; -; mRNA.
CCDS; CCDS25784.1; -. [O88508-2]
CCDS; CCDS36397.1; -. [O88508-1]
RefSeq; NP_001258682.1; NM_001271753.1. [O88508-1]
RefSeq; NP_031898.1; NM_007872.4. [O88508-1]
RefSeq; NP_714965.1; NM_153743.4. [O88508-2]
RefSeq; XP_006515016.1; XM_006514953.3. [O88508-1]
RefSeq; XP_006515019.1; XM_006514956.3. [O88508-1]
UniGene; Mm.470389; -.
UniGene; Mm.5001; -.
PDB; 3SW9; X-ray; 3.05 A; P/Q=39-50.
PDB; 3SWC; X-ray; 2.33 A; P/Q=39-50.
PDBsum; 3SW9; -.
PDBsum; 3SWC; -.
ProteinModelPortal; O88508; -.
SMR; O88508; -.
BioGrid; 199261; 18.
DIP; DIP-38005N; -.
IntAct; O88508; 13.
MINT; MINT-2521021; -.
STRING; 10090.ENSMUSP00000020991; -.
ChEMBL; CHEMBL3108652; -.
REBASE; 3747; M.MmuDnmt3A.
iPTMnet; O88508; -.
PhosphoSitePlus; O88508; -.
EPD; O88508; -.
MaxQB; O88508; -.
PaxDb; O88508; -.
PeptideAtlas; O88508; -.
PRIDE; O88508; -.
Ensembl; ENSMUST00000020991; ENSMUSP00000020991; ENSMUSG00000020661. [O88508-1]
Ensembl; ENSMUST00000111186; ENSMUSP00000106817; ENSMUSG00000020661. [O88508-2]
Ensembl; ENSMUST00000172689; ENSMUSP00000133543; ENSMUSG00000020661. [O88508-2]
Ensembl; ENSMUST00000174817; ENSMUSP00000134009; ENSMUSG00000020661. [O88508-1]
GeneID; 13435; -.
KEGG; mmu:13435; -.
UCSC; uc007mxb.1; mouse. [O88508-1]
CTD; 1788; -.
MGI; MGI:1261827; Dnmt3a.
eggNOG; ENOG410IGHW; Eukaryota.
eggNOG; ENOG410XQ4Y; LUCA.
GeneTree; ENSGT00390000008341; -.
HOGENOM; HOG000230875; -.
HOVERGEN; HBG051381; -.
InParanoid; O88508; -.
KO; K17398; -.
OMA; FPVCHDS; -.
OrthoDB; EOG091G01TP; -.
PhylomeDB; O88508; -.
TreeFam; TF329039; -.
BRENDA; 2.1.1.37; 3474.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
ChiTaRS; Dnmt3a; mouse.
PRO; PR:O88508; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000020661; -.
CleanEx; MM_DNMT3A; -.
ExpressionAtlas; O88508; baseline and differential.
Genevisible; O88508; MM.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
GO; GO:0000792; C:heterochromatin; IDA:MGI.
GO; GO:0005720; C:nuclear heterochromatin; IDA:MGI.
GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001741; C:XY body; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:MGI.
GO; GO:0051719; F:DNA (cytosine-5-)-methyltransferase activity, acting on CpN substrates; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008168; F:methyltransferase activity; TAS:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0006306; P:DNA methylation; IDA:MGI.
GO; GO:0043045; P:DNA methylation involved in embryo development; IMP:UniProtKB.
GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
GO; GO:0032776; P:DNA methylation on cytosine; TAS:Reactome.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0044027; P:hypermethylation of CpG island; IDA:BHF-UCL.
GO; GO:0010216; P:maintenance of DNA methylation; TAS:BHF-UCL.
GO; GO:0006346; P:methylation-dependent chromatin silencing; IDA:MGI.
GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0010942; P:positive regulation of cell death; IEA:Ensembl.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IDA:BHF-UCL.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR025766; ADD.
InterPro; IPR018117; C5_DNA_meth_AS.
InterPro; IPR001525; C5_MeTfrase.
InterPro; IPR030487; DNMT3A.
InterPro; IPR000313; PWWP_dom.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR23068:SF10; PTHR23068:SF10; 2.
Pfam; PF00855; PWWP; 1.
SMART; SM00293; PWWP; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51533; ADD; 1.
PROSITE; PS00094; C5_MTASE_1; 1.
PROSITE; PS50812; PWWP; 1.
PROSITE; PS51679; SAM_MT_C5; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Chromatin regulator;
Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond;
Metal-binding; Methylation; Methyltransferase; Nucleus;
Phosphoprotein; Reference proteome; Repressor;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 908 DNA (cytosine-5)-methyltransferase 3A.
/FTId=PRO_0000088044.
DOMAIN 288 346 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
DOMAIN 478 610 ADD. {ECO:0000255|PROSITE-
ProRule:PRU00865}.
DOMAIN 630 908 SAM-dependent MTase C5-type.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
ZN_FING 489 519 GATA-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00865}.
ZN_FING 530 586 PHD-type; atypical. {ECO:0000255|PROSITE-
ProRule:PRU00865}.
REGION 195 399 Interaction with DNMT1 and DNMT3B.
{ECO:0000250}.
REGION 490 582 Interaction with the PRC2/EED-EZH2
complex.
REGION 637 641 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9Y6K1}.
REGION 682 684 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9Y6K1}.
REGION 887 889 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9Y6K1}.
ACT_SITE 706 706 {ECO:0000255|PROSITE-ProRule:PRU01016,
ECO:0000255|PROSITE-ProRule:PRU10018}.
BINDING 660 660 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9Y6K1}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 120 120 Phosphothreonine.
{ECO:0000250|UniProtKB:Q1LZ53}.
MOD_RES 167 167 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6K1}.
MOD_RES 251 251 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6K1}.
MOD_RES 257 257 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 386 386 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 158 158 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y6K1}.
VAR_SEQ 1 219 Missing (in isoform 2).
{ECO:0000303|PubMed:12138111,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_009423.
MUTAGEN 302 303 WP->ST: Prevents accumulation in
pericentric heterochromatin.
{ECO:0000269|PubMed:15456878}.
MUTAGEN 636 636 F->A: Reduces activity about 20-fold.
Loss of substrate binding.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 660 660 E->A: Reduces activity about 15-fold.
Loss of substrate binding.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 682 682 D->A: Strongly reduces substrate binding.
No effect on activity.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 705 706 PC->VD: No effect on localization.
{ECO:0000269|PubMed:15456878}.
MUTAGEN 706 706 C->A: Reduces activity about 5-fold.
Reduces DNA-binding capacity.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 707 707 N->Q: Reduces activity about 3-fold.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 710 710 S->A: No effect on activity.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 716 716 R->A: Reduces activity about 30-fold.
Reduces DNA-binding capacity.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 717 717 K->A: Reduces activity about 3-fold.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 728 728 F->A: Loss of activity du to the
incapacity to bind the regulatory subunit
DNMT3L. {ECO:0000269|PubMed:17713477}.
MUTAGEN 752 752 E->A: Reduces activity about 10-fold.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 753 753 N->A: Reduces activity about 10-fold.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 788 788 R->A: Reduces activity about 15-fold.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 827 827 R->A: Reduces activity about 2-fold.
Reduces DNA-binding capacity.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 832 832 R->A: Reduces DNA-binding capacity. No
effect on activity.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 878 878 R->A: Reduces activity about 6-fold.
Reduces DNA-binding capacity.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 881 881 R->A: Loss of activity. Strongly reduces
substrate binding.
{ECO:0000269|PubMed:16472822}.
MUTAGEN 883 883 R->A: Reduces activity about 3-fold.
Reduces DNA-binding capacity.
{ECO:0000269|PubMed:16472822}.
CONFLICT 151 151 Q -> P (in Ref. 4; AAH07466).
{ECO:0000305}.
CONFLICT 775 775 M -> T (in Ref. 3; BAB28644).
{ECO:0000305}.
CONFLICT 781 781 V -> G (in Ref. 3; BAB28644).
{ECO:0000305}.
CONFLICT 791 791 W -> R (in Ref. 3; BAB28644).
{ECO:0000305}.
CONFLICT 809 809 L -> P (in Ref. 3; BAB28644).
{ECO:0000305}.
CONFLICT 904 904 Y -> I (in Ref. 3; BAB28644).
{ECO:0000305}.
SEQUENCE 908 AA; 101672 MW; 5F98D5A8092C84A5 CRC64;
MPSSGPGDTS SSSLEREDDR KEGEEQEENR GKEERQEPSA TARKVGRPGR KRKHPPVESS
DTPKDPAVTT KSQPMAQDSG PSDLLPNGDL EKRSEPQPEE GSPAAGQKGG APAEGEGTET
PPEASRAVEN GCCVTKEGRG ASAGEGKEQK QTNIESMKME GSRGRLRGGL GWESSLRQRP
MPRLTFQAGD PYYISKRKRD EWLARWKREA EKKAKVIAVM NAVEENQASG ESQKVEEASP
PAVQQPTDPA SPTVATTPEP VGGDAGDKNA TKAADDEPEY EDGRGFGIGE LVWGKLRGFS
WWPGRIVSWW MTGRSRAAEG TRWVMWFGDG KFSVVCVEKL MPLSSFCSAF HQATYNKQPM
YRKAIYEVLQ VASSRAGKLF PACHDSDESD SGKAVEVQNK QMIEWALGGF QPSGPKGLEP
PEEEKNPYKE VYTDMWVEPE AAAYAPPPPA KKPRKSTTEK PKVKEIIDER TRERLVYEVR
QKCRNIEDIC ISCGSLNVTL EHPLFIGGMC QNCKNCFLEC AYQYDDDGYQ SYCTICCGGR
EVLMCGNNNC CRCFCVECVD LLVGPGAAQA AIKEDPWNCY MCGHKGTYGL LRRREDWPSR
LQMFFANNHD QEFDPPKVYP PVPAEKRKPI RVLSLFDGIA TGLLVLKDLG IQVDRYIASE
VCEDSITVGM VRHQGKIMYV GDVRSVTQKH IQEWGPFDLV IGGSPCNDLS IVNPARKGLY
EGTGRLFFEF YRLLHDARPK EGDDRPFFWL FENVVAMGVS DKRDISRFLE SNPVMIDAKE
VSAAHRARYF WGNLPGMNRP LASTVNDKLE LQECLEHGRI AKFSKVRTIT TRSNSIKQGK
DQHFPVFMNE KEDILWCTEM ERVFGFPVHY TDVSNMSRLA RQRLLGRSWS VPVIRHLFAP
LKEYFACV


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