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DNA (cytosine-5)-methyltransferase 3B (Dnmt3b) (EC 2.1.1.37) (DNA methyltransferase HsaIIIB) (DNA MTase HsaIIIB) (M.HsaIIIB)

 DNM3B_HUMAN             Reviewed;         853 AA.
Q9UBC3; A2A2E2; B4DSM8; B4DSU1; E1P5M6; E1P5M7; E7EN63; E9PBF2;
Q9UBD4; Q9UJQ5; Q9UKA6; Q9UNE5; Q9Y5R9; Q9Y5S0;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
10-OCT-2018, entry version 188.
RecName: Full=DNA (cytosine-5)-methyltransferase 3B;
Short=Dnmt3b;
EC=2.1.1.37;
AltName: Full=DNA methyltransferase HsaIIIB;
Short=DNA MTase HsaIIIB;
Short=M.HsaIIIB;
Name=DNMT3B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Fetal testis, and Small intestine;
PubMed=10433969; DOI=10.1016/S0378-1119(99)00252-8;
Xie S., Wang Z., Okano M., Nogami M., Li Y., He W.-W., Okumura K.,
Li E.;
"Cloning, expression and chromosome locations of the human DNMT3 gene
family.";
Gene 236:87-95(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), AND VARIANTS ICF1 SER-663;
GLY-726; GLY-817 AND MET-818.
TISSUE=Testis;
PubMed=10647011; DOI=10.1038/46052;
Xu G.-L., Bestor T.H., Bourc'his D., Hsieh C.-L., Tommerup N.,
Bugge M., Hulten M., Qu X., Russo J.J., Viegas-Pequignot E.;
"Chromosome instability and immunodeficiency syndrome caused by
mutations in a DNA methyltransferase gene.";
Nature 402:187-191(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Ni J., Pradhan S., Roberts R.J.;
"Cloning, expression and characterization of human DNMT3 genes.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 636-853 (ISOFORMS 1; 4 AND 5).
TISSUE=Testis;
PubMed=10325416; DOI=10.1093/nar/27.11.2291;
Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J.,
Gonzales F.A., Jones P.A.;
"The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate
mRNA expression in normal tissues and overexpression in tumors.";
Nucleic Acids Res. 27:2291-2298(1999).
[8]
INTERACTION WITH UBL1 AND UBE2I9, SUMOYLATION, AND SUBCELLULAR
LOCATION.
PubMed=11735126; DOI=10.1006/bbrc.2001.6057;
Kang E.S., Park C.W., Chung J.H.;
"Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9
through its N-terminal region and is subject to modification by SUMO-
1.";
Biochem. Biophys. Res. Commun. 289:862-868(2001).
[9]
INTERACTION WITH DNMT1 AND DNMT3A, AND SUBCELLULAR LOCATION.
PubMed=12145218; DOI=10.1093/emboj/cdf401;
Kim G.-D., Ni J., Kelesoglu N., Roberts R.J., Pradhan S.;
"Co-operation and communication between the human maintenance and de
novo DNA (cytosine-5) methyltransferases.";
EMBO J. 21:4183-4195(2002).
[10]
INTERACTION WITH SETDB1.
PubMed=16682412; DOI=10.1074/jbc.M513249200;
Li H., Rauch T., Chen Z.-X., Szabo P.E., Riggs A.D., Pfeifer G.P.;
"The histone methyltransferase SETDB1 and the DNA methyltransferase
DNMT3A interact directly and localize to promoters silenced in cancer
cells.";
J. Biol. Chem. 281:19489-19500(2006).
[11]
FUNCTION, AND 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).
[12]
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).
[13]
FUNCTION, AND INTERACTION WITH ZHX1.
PubMed=17303076; DOI=10.1016/j.bbrc.2007.01.187;
Kim S.H., Park J., Choi M.C., Kim H.P., Park J.H., Jung Y., Lee J.H.,
Oh D.Y., Im S.A., Bang Y.J., Kim T.Y.;
"Zinc-fingers and homeoboxes 1 (ZHX1) binds DNA methyltransferase
(DNMT) 3B to enhance DNMT3B-mediated transcriptional repression.";
Biochem. Biophys. Res. Commun. 355:318-323(2007).
[14]
DE NOVO DNA METHYLATION OF TARGET GENES.
PubMed=17200670; DOI=10.1038/ng1950;
Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M.,
Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E.,
Bergman Y., Simon I., Cedar H.;
"Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes
for de novo methylation in cancer.";
Nat. Genet. 39:232-236(2007).
[15]
FUNCTION.
PubMed=18413740; DOI=10.1158/0008-5472.CAN-07-6654;
Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S.,
Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P.,
Gius D.;
"DNA methyltransferase 1 and 3B activate BAG-1 expression via
recruitment of CTCFL/BORIS and modulation of promoter histone
methylation.";
Cancer Res. 68:2726-2735(2008).
[16]
FUNCTION.
PubMed=18567530; DOI=10.1016/j.biocel.2008.04.018;
Kim S.-H., Park J., Choi M.-C., Park J.-H., Kim H.-P., Lee J.-H.,
Oh D.-Y., Im S.-A., Bang Y.-J., Kim T.-Y.;
"DNA methyltransferase 3B acts as a co-repressor of the human polycomb
protein hPc2 to repress fibroblast growth factor receptor 3
transcription.";
Int. J. Biochem. Cell Biol. 40:2462-2471(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; THR-96; SER-100;
SER-110; SER-136; SER-195; SER-202 AND SER-209, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-209, 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).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-89 AND LYS-617, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[21]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 206-355.
Structural genomics consortium (SGC);
"Crystal structure of the PWWP domain of human DNA (cytosine-5-)-
methyltransferase 3 beta.";
Submitted (MAR-2009) to the PDB data bank.
[22]
X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 380-509.
PubMed=21720545; DOI=10.1371/journal.pone.0018919;
Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L.,
Qiu W., Wang Y., Min J.;
"Structural and histone binding ability characterizations of human
PWWP domains.";
PLoS ONE 6:E18919-E18919(2011).
[23]
VARIANTS ICF1 THR-603 AND SER-THR-PRO-806 INS.
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).
[24]
VARIANTS ICF1 THR-603; GLY-726 AND SER-THR-PRO-806 INS.
PubMed=10588719; DOI=10.1073/pnas.96.25.14412;
Hansen R.S., Wijmenga C., Luo P., Stanek A.M., Canfield T.K.,
Weemaes C.M.R., Gartler S.M.;
"The DNMT3B DNA methyltransferase gene is mutated in the ICF
immunodeficiency syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 96:14412-14417(1999).
[25]
VARIANTS ICF1 VAL-585; THR-603; ALA-606; GLY-699; GLY-726; PRO-766;
ARG-814 AND MET-818.
PubMed=11102980;
DOI=10.1002/1098-1004(200012)16:6<509::AID-HUMU8>3.0.CO;2-V;
Wijmenga C., Hansen R.S., Gimelli G., Bjoerck E.J., Davies E.G.,
Valentine D., Belohradsky B.H., van Dongen J.J., Smeets D.F.C.M.,
van den Heuvel L.P.W.J., Luyten J.A.F.M., Strengman E.,
Weemaes C.M.R., Pearson P.L.;
"Genetic variation in ICF syndrome: evidence for genetic
heterogeneity.";
Hum. Mutat. 16:509-517(2000).
[26]
VARIANTS ICF1 PRO-270; VAL-585; THR-603; ALA-606; SER-663; PRO-664;
GLY-699; GLY-726; PRO-766; ARG-814; GLY-817; MET-818 AND GLN-840.
PubMed=15580563; DOI=10.1002/humu.20113;
Jiang Y.L., Rigolet M., Bourc'his D., Nigon F., Bokesoy I.,
Fryns J.-P., Hulten M., Jonveaux P., Maraschio P., Megarbane A.,
Moncla A., Viegas-Pequignot E.;
"DNMT3B mutations and DNA methylation defect define two types of ICF
syndrome.";
Hum. Mutat. 25:56-63(2005).
[27]
VARIANT ICF1 MET-836.
PubMed=21120685; DOI=10.1007/s10875-010-9488-0;
Kaya N., Al-Muhsen S., Al-Saud B., Al-Bakheet A., Colak D.,
Al-Ghonaium A., Al-Dhekri H., Al-Mousa H., Arnaout R., Al-Owain M.,
Iqbal M.;
"ICF syndrome in Saudi Arabia: immunological, cytogenetic and
molecular analysis.";
J. Clin. Immunol. 31:245-252(2011).
[28]
VARIANTS FSHD2 ARG-527 AND LEU-691, AND FUNCTION.
PubMed=27153398; DOI=10.1016/j.ajhg.2016.03.013;
van den Boogaard M.L., Lemmers R.J., Balog J., Wohlgemuth M.,
Auranen M., Mitsuhashi S., van der Vliet P.J., Straasheijm K.R.,
van den Akker R.F., Kriek M., Laurense-Bik M.E., Raz V.,
van Ostaijen-Ten Dam M.M., Hansson K.B., van der Kooi E.L.,
Kiuru-Enari S., Udd B., van Tol M.J., Nishino I., Tawil R.,
Tapscott S.J., van Engelen B.G., van der Maarel S.M.;
"Mutations in DNMT3B modify epigenetic repression of the D4Z4 repeat
and the penetrance of facioscapulohumeral dystrophy.";
Am. J. Hum. Genet. 98:1020-1029(2016).
[29]
VARIANT ICF1 THR-585.
PubMed=27734333; DOI=10.1007/s10875-016-0340-z;
Rechavi E., Lev A., Eyal E., Barel O., Kol N., Barhom S.F.,
Pode-Shakked B., Anikster Y., Somech R., Simon A.J.;
"A novel mutation in a critical region for the methyl donor binding in
DNMT3B causes immunodeficiency, centromeric instability, and facial
anomalies syndrome (ICF).";
J. Clin. Immunol. 36:801-809(2016).
-!- 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. May preferentially methylates nucleosomal DNA within the
nucleosome core region. May function as transcriptional co-
repressor by associating with CBX4 and independently of DNA
methylation. Seems to be involved in gene silencing (By
similarity). In association with DNMT1 and via the recruitment of
CTCFL/BORIS, involved in activation of BAG1 gene expression by
modulating dimethylation of promoter histone H3 at H3K4 and H3K9.
Isoforms 4 and 5 are probably not functional due to the deletion
of two conserved methyltransferase motifs. Function as
transcriptional corepressor by associating with ZHX1. Required for
DUX4 silencing in somatic cells (PubMed:27153398). {ECO:0000250,
ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:17303076,
ECO:0000269|PubMed:18413740, ECO:0000269|PubMed:18567530,
ECO:0000269|PubMed:27153398}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
homocysteine + DNA containing 5-methylcytosine.
{ECO:0000255|PROSITE-ProRule:PRU10018}.
-!- ACTIVITY REGULATION: Activated by binding to the regulatory factor
DNMT3L. {ECO:0000250}.
-!- SUBUNIT: Interacts with BAZ2A/TIP5, SUV39H1 and CBX4. Interacts
with UHRF1 (By similarity). Interacts with DNMT1 and DNMT3A,
SETDB1, UBL1, UBE2I9 and ZHX1. Interacts with the PRC2/EED-EZH2
complex. {ECO:0000250, ECO:0000269|PubMed:11735126,
ECO:0000269|PubMed:12145218, ECO:0000269|PubMed:16357870,
ECO:0000269|PubMed:16682412, ECO:0000269|PubMed:17303076}.
-!- INTERACTION:
O75530:EED; NbExp=4; IntAct=EBI-80125, EBI-923794;
Q96KQ7:EHMT2; NbExp=2; IntAct=EBI-80125, EBI-744366;
Q15910:EZH2; NbExp=14; IntAct=EBI-80125, EBI-530054;
Q9QR71:LANA1 (xeno); NbExp=2; IntAct=EBI-80125, EBI-15602554;
P63165:SUMO1; NbExp=4; IntAct=EBI-80125, EBI-80140;
P63279:UBE2I; NbExp=3; IntAct=EBI-80125, EBI-80168;
Q96T88:UHRF1; NbExp=7; IntAct=EBI-80125, EBI-1548946;
Q9UKY1:ZHX1; NbExp=6; IntAct=EBI-6083193, EBI-347767;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11735126,
ECO:0000269|PubMed:12145218}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1;
IsoId=Q9UBC3-1; Sequence=Displayed;
Name=2;
IsoId=Q9UBC3-2; Sequence=VSP_005637;
Name=3;
IsoId=Q9UBC3-3; Sequence=VSP_005637, VSP_005638;
Name=4;
IsoId=Q9UBC3-4; Sequence=VSP_005637, VSP_005639, VSP_005640;
Name=5;
IsoId=Q9UBC3-5; Sequence=VSP_005637, VSP_005641;
Name=6;
IsoId=Q9UBC3-6; Sequence=VSP_005636, VSP_005637;
Name=7;
IsoId=Q9UBC3-7; Sequence=VSP_045874, VSP_005637, VSP_045876;
Note=No experimental confirmation available.;
Name=8;
IsoId=Q9UBC3-8; Sequence=VSP_045875, VSP_005637, VSP_045876;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous; highly expressed in fetal liver,
heart, kidney, placenta, and at lower levels in spleen, colon,
brain, liver, small intestine, lung, peripheral blood mononuclear
cells, and skeletal muscle. Isoform 1 is expressed in all tissues
except brain, skeletal muscle and PBMC, 3 is ubiquitous, 4 is
expressed in all tissues except brain, skeletal muscle, lung and
prostate and 5 is detectable only in testis and at very low level
in brain and prostate.
-!- DOMAIN: The PWWP domain is essential for targeting to pericentric
heterochromatin.
-!- PTM: Sumoylated. {ECO:0000269|PubMed:11735126}.
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- DISEASE: Immunodeficiency-centromeric instability-facial anomalies
syndrome 1 (ICF1) [MIM:242860]: A rare disorder characterized by a
variable immunodeficiency resulting in recurrent infections,
facial anomalies, and branching of chromosomes 1, 9, and 16. Other
variable symptoms include growth retardation, failure to thrive,
and psychomotor retardation. Laboratory studies show limited
hypomethylation of DNA in a small fraction of the genome in some,
but not all, patients. {ECO:0000269|PubMed:10555141,
ECO:0000269|PubMed:10588719, ECO:0000269|PubMed:10647011,
ECO:0000269|PubMed:11102980, ECO:0000269|PubMed:15580563,
ECO:0000269|PubMed:21120685, ECO:0000269|PubMed:27734333}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Facioscapulohumeral muscular dystrophy 2 (FSHD2)
[MIM:158901]: A degenerative muscle disease characterized by
slowly progressive weakness of the muscles of the face, upper-arm,
and shoulder girdle. The onset of symptoms usually occurs in the
first or second decade of life. Affected individuals usually
present with impairment of upper extremity elevation. This tends
to be followed by facial weakness, primarily involving the
orbicularis oris and orbicularis oculi muscles.
{ECO:0000269|PubMed:27153398}. Note=The gene represented in this
entry may act as a disease modifier. DNMT3B mutations lead to DUX4
expression in somatic tissues, including muscle cells, when an
haplotype on chromosome 4 is permissive for DUX4 expression.
Ectopic expression of DUX4 in skeletal muscle activates the
expression of stem cell and germline genes, and, when
overexpressed in somatic cells, DUX4 can ultimately lead to cell
death.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. C5-methyltransferase family.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
-!- WEB RESOURCE: Name=DNMT3Bbase; Note=DNMT3B mutation db;
URL="http://structure.bmc.lu.se/idbase/DNMT3Bbase/";
-----------------------------------------------------------------------
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EMBL; AF156487; AAD53062.1; -; mRNA.
EMBL; AF156488; AAD53063.1; -; mRNA.
EMBL; AF176228; AAF04015.1; -; mRNA.
EMBL; AF331857; AAL57040.1; -; mRNA.
EMBL; AK299821; BAG61690.1; -; mRNA.
EMBL; AK299915; BAG61753.1; -; mRNA.
EMBL; AL035071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW76351.1; -; Genomic_DNA.
EMBL; CH471077; EAW76352.1; -; Genomic_DNA.
EMBL; CH471077; EAW76353.1; -; Genomic_DNA.
EMBL; CH471077; EAW76354.1; -; Genomic_DNA.
EMBL; CH471077; EAW76356.1; -; Genomic_DNA.
EMBL; AF129267; AAD31432.1; -; mRNA.
EMBL; AF129268; AAD31433.1; -; mRNA.
EMBL; AF129269; AAD31434.1; -; mRNA.
CCDS; CCDS13204.1; -. [Q9UBC3-6]
CCDS; CCDS13205.1; -. [Q9UBC3-1]
CCDS; CCDS13206.1; -. [Q9UBC3-2]
CCDS; CCDS13207.1; -. [Q9UBC3-3]
CCDS; CCDS56183.1; -. [Q9UBC3-8]
CCDS; CCDS56184.1; -. [Q9UBC3-7]
RefSeq; NP_001193984.1; NM_001207055.1. [Q9UBC3-8]
RefSeq; NP_001193985.1; NM_001207056.1. [Q9UBC3-7]
RefSeq; NP_008823.1; NM_006892.3. [Q9UBC3-1]
RefSeq; NP_787044.1; NM_175848.1. [Q9UBC3-2]
RefSeq; NP_787045.1; NM_175849.1. [Q9UBC3-3]
RefSeq; NP_787046.1; NM_175850.2. [Q9UBC3-6]
UniGene; Hs.643024; -.
UniGene; Hs.713611; -.
PDB; 3FLG; X-ray; 1.80 A; A=206-355.
PDB; 3QKJ; X-ray; 2.04 A; A/B/C/D=206-355.
PDB; 5CIU; X-ray; 2.24 A; A/B=206-355.
PDB; 5NR3; X-ray; 2.30 A; A/B=206-355.
PDB; 5NRR; X-ray; 1.70 A; A/B=206-355.
PDB; 5NRS; X-ray; 2.30 A; A/B=206-355.
PDB; 5NRV; X-ray; 2.08 A; A/D=206-355.
PDB; 5NV0; X-ray; 2.40 A; A/B=206-355.
PDB; 5NV2; X-ray; 2.03 A; A/B=206-355.
PDB; 5NV7; X-ray; 2.57 A; A/B=206-355.
PDB; 5NVO; X-ray; 2.40 A; A/B=206-355.
PDBsum; 3FLG; -.
PDBsum; 3QKJ; -.
PDBsum; 5CIU; -.
PDBsum; 5NR3; -.
PDBsum; 5NRR; -.
PDBsum; 5NRS; -.
PDBsum; 5NRV; -.
PDBsum; 5NV0; -.
PDBsum; 5NV2; -.
PDBsum; 5NV7; -.
PDBsum; 5NVO; -.
ProteinModelPortal; Q9UBC3; -.
SMR; Q9UBC3; -.
BioGrid; 108126; 73.
CORUM; Q9UBC3; -.
DIP; DIP-30000N; -.
IntAct; Q9UBC3; 29.
MINT; Q9UBC3; -.
STRING; 9606.ENSP00000328547; -.
BindingDB; Q9UBC3; -.
ChEMBL; CHEMBL6095; -.
REBASE; 4120; M.HsaDnmt3B.
iPTMnet; Q9UBC3; -.
PhosphoSitePlus; Q9UBC3; -.
BioMuta; DNMT3B; -.
DMDM; 17375667; -.
EPD; Q9UBC3; -.
MaxQB; Q9UBC3; -.
PaxDb; Q9UBC3; -.
PeptideAtlas; Q9UBC3; -.
PRIDE; Q9UBC3; -.
ProteomicsDB; 83935; -.
ProteomicsDB; 83936; -. [Q9UBC3-2]
ProteomicsDB; 83937; -. [Q9UBC3-3]
ProteomicsDB; 83938; -. [Q9UBC3-4]
ProteomicsDB; 83939; -. [Q9UBC3-5]
ProteomicsDB; 83940; -. [Q9UBC3-6]
DNASU; 1789; -.
Ensembl; ENST00000201963; ENSP00000201963; ENSG00000088305. [Q9UBC3-6]
Ensembl; ENST00000328111; ENSP00000328547; ENSG00000088305. [Q9UBC3-1]
Ensembl; ENST00000348286; ENSP00000337764; ENSG00000088305. [Q9UBC3-3]
Ensembl; ENST00000353855; ENSP00000313397; ENSG00000088305. [Q9UBC3-2]
Ensembl; ENST00000443239; ENSP00000403169; ENSG00000088305. [Q9UBC3-8]
Ensembl; ENST00000456297; ENSP00000412305; ENSG00000088305. [Q9UBC3-7]
GeneID; 1789; -.
KEGG; hsa:1789; -.
UCSC; uc002wyc.3; human. [Q9UBC3-1]
CTD; 1789; -.
DisGeNET; 1789; -.
EuPathDB; HostDB:ENSG00000088305.18; -.
GeneCards; DNMT3B; -.
HGNC; HGNC:2979; DNMT3B.
HPA; CAB069896; -.
HPA; HPA001595; -.
MalaCards; DNMT3B; -.
MIM; 158901; phenotype.
MIM; 242860; phenotype.
MIM; 602900; gene.
neXtProt; NX_Q9UBC3; -.
OpenTargets; ENSG00000088305; -.
Orphanet; 2268; ICF syndrome.
PharmGKB; PA27446; -.
eggNOG; ENOG410IGHW; Eukaryota.
eggNOG; ENOG410XQ4Y; LUCA.
GeneTree; ENSGT00390000008341; -.
HOGENOM; HOG000230875; -.
HOVERGEN; HBG051381; -.
InParanoid; Q9UBC3; -.
KO; K17399; -.
OMA; RRKDWNV; -.
OrthoDB; EOG091G01TP; -.
PhylomeDB; Q9UBC3; -.
TreeFam; TF329039; -.
BRENDA; 2.1.1.37; 2681.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins.
Reactome; R-HSA-5334118; DNA methylation.
SIGNOR; Q9UBC3; -.
ChiTaRS; DNMT3B; human.
EvolutionaryTrace; Q9UBC3; -.
GeneWiki; DNMT3B; -.
GenomeRNAi; 1789; -.
PRO; PR:Q9UBC3; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000088305; Expressed in 137 organ(s), highest expression level in secondary oocyte.
CleanEx; HS_DNMT3B; -.
Genevisible; Q9UBC3; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0009008; F:DNA-methyltransferase activity; TAS:Reactome.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071455; P:cellular response to hyperoxia; IEA:Ensembl.
GO; GO:0006306; P:DNA methylation; TAS:UniProtKB.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
CDD; cd11728; ADDz_Dnmt3b; 1.
InterPro; IPR025766; ADD.
InterPro; IPR018117; C5_DNA_meth_AS.
InterPro; IPR001525; C5_MeTfrase.
InterPro; IPR030488; DNMT3B_ADD.
InterPro; IPR000313; PWWP_dom.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR011011; Znf_FYVE_PHD.
Pfam; PF00145; DNA_methylase; 1.
Pfam; PF00855; PWWP; 1.
SMART; SM00293; PWWP; 1.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF57903; SSF57903; 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; Activator; Alternative splicing; Citrullination;
Complete proteome; Disease mutation; DNA-binding; Isopeptide bond;
Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repressor; S-adenosyl-L-methionine;
Transferase; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 853 DNA (cytosine-5)-methyltransferase 3B.
/FTId=PRO_0000088045.
DOMAIN 225 283 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
DOMAIN 423 555 ADD. {ECO:0000255|PROSITE-
ProRule:PRU00865}.
DOMAIN 575 853 SAM-dependent MTase C5-type.
{ECO:0000255|PROSITE-ProRule:PRU01016}.
ZN_FING 434 464 GATA-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00865}.
ZN_FING 475 531 PHD-type; atypical. {ECO:0000255|PROSITE-
ProRule:PRU00865}.
REGION 1 298 Interaction with DNMT1 and DNMT3A.
{ECO:0000269|PubMed:12145218}.
REGION 435 527 Interaction with the PRC2/EED-EZH2
complex. {ECO:0000250}.
REGION 582 586 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9Y6K1}.
REGION 627 629 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9Y6K1}.
REGION 832 834 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:Q9Y6K1}.
ACT_SITE 651 651 {ECO:0000255|PROSITE-ProRule:PRU01016,
ECO:0000255|PROSITE-ProRule:PRU10018}.
BINDING 605 605 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9Y6K1}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 96 96 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 202 202 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 209 209 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 410 410 Citrulline. {ECO:0000250}.
CROSSLNK 89 89 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 617 617 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MEPSPEPPSLESM (in isoform 6).
{ECO:0000303|PubMed:10647011}.
/FTId=VSP_005636.
VAR_SEQ 69 144 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045874.
VAR_SEQ 103 144 Missing (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045875.
VAR_SEQ 356 375 Missing (in isoform 2, isoform 3, isoform
4, isoform 5, isoform 6, isoform 7 and
isoform 8). {ECO:0000303|PubMed:10325416,
ECO:0000303|PubMed:10433969,
ECO:0000303|PubMed:10647011,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_005637.
VAR_SEQ 744 806 Missing (in isoform 7 and isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045876.
VAR_SEQ 744 744 R -> S (in isoform 4).
{ECO:0000303|PubMed:10325416}.
/FTId=VSP_005639.
VAR_SEQ 745 853 Missing (in isoform 4).
{ECO:0000303|PubMed:10325416}.
/FTId=VSP_005640.
VAR_SEQ 745 807 Missing (in isoform 3).
{ECO:0000303|PubMed:10433969}.
/FTId=VSP_005638.
VAR_SEQ 768 853 LKKVQTITTKSNSIKQGKNQLFPVVMNGKEDVLWCTELERI
FGFPVHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDY
FACE -> DLWLSCALHRRVQHGPWCPPEAAGKVLERACHP
TPLRPSEGLLCM (in isoform 5).
{ECO:0000303|PubMed:10325416}.
/FTId=VSP_005641.
VARIANT 54 54 R -> P (in dbSNP:rs17123590).
/FTId=VAR_033885.
VARIANT 270 270 S -> P (in ICF1; dbSNP:rs121908947).
{ECO:0000269|PubMed:15580563}.
/FTId=VAR_022579.
VARIANT 527 527 C -> R (in FSHD2).
{ECO:0000269|PubMed:27153398}.
/FTId=VAR_077527.
VARIANT 585 585 A -> T (in ICF1; dbSNP:rs750849178).
{ECO:0000269|PubMed:27734333}.
/FTId=VAR_077528.
VARIANT 585 585 A -> V (in ICF1).
{ECO:0000269|PubMed:11102980,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011506.
VARIANT 603 603 A -> T (in ICF1; dbSNP:rs121908943).
{ECO:0000269|PubMed:10555141,
ECO:0000269|PubMed:10588719,
ECO:0000269|PubMed:11102980,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011499.
VARIANT 606 606 V -> A (in ICF1; dbSNP:rs867732105).
{ECO:0000269|PubMed:11102980,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011507.
VARIANT 663 663 G -> S (in ICF1; dbSNP:rs121908942).
{ECO:0000269|PubMed:10647011,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011500.
VARIANT 664 664 L -> P (in ICF1).
{ECO:0000269|PubMed:15580563}.
/FTId=VAR_022580.
VARIANT 691 691 P -> L (in FSHD2; dbSNP:rs889145646).
{ECO:0000269|PubMed:27153398}.
/FTId=VAR_077529.
VARIANT 699 699 V -> G (in ICF1).
{ECO:0000269|PubMed:11102980,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011508.
VARIANT 726 726 V -> G (in ICF1; dbSNP:rs121908941).
{ECO:0000269|PubMed:10588719,
ECO:0000269|PubMed:10647011,
ECO:0000269|PubMed:11102980,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011501.
VARIANT 766 766 A -> P (in ICF1; dbSNP:rs1191203668).
{ECO:0000269|PubMed:11102980,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011509.
VARIANT 806 806 E -> ESTP (in ICF1).
/FTId=VAR_011502.
VARIANT 814 814 H -> R (in ICF1; dbSNP:rs1219696128).
{ECO:0000269|PubMed:11102980,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011510.
VARIANT 817 817 D -> G (in ICF1; dbSNP:rs121908939).
{ECO:0000269|PubMed:10647011,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011503.
VARIANT 818 818 V -> M (in ICF1; dbSNP:rs121908940).
{ECO:0000269|PubMed:10647011,
ECO:0000269|PubMed:11102980,
ECO:0000269|PubMed:15580563}.
/FTId=VAR_011504.
VARIANT 836 836 V -> M (in ICF1; unknown pathological
significance; dbSNP:rs866792483).
{ECO:0000269|PubMed:21120685}.
/FTId=VAR_077530.
VARIANT 840 840 R -> Q (in ICF1; dbSNP:rs121908946).
{ECO:0000269|PubMed:15580563}.
/FTId=VAR_022581.
CONFLICT 575 575 I -> T (in Ref. 4; BAG61690).
{ECO:0000305}.
CONFLICT 583 583 G -> D (in Ref. 4; BAG61753).
{ECO:0000305}.
CONFLICT 655 655 S -> P (in Ref. 4; BAG61690).
{ECO:0000305}.
STRAND 219 222 {ECO:0000244|PDB:5CIU}.
STRAND 228 231 {ECO:0000244|PDB:5NRR}.
STRAND 239 244 {ECO:0000244|PDB:5NRR}.
HELIX 246 248 {ECO:0000244|PDB:5NRR}.
STRAND 258 263 {ECO:0000244|PDB:5NRR}.
TURN 264 266 {ECO:0000244|PDB:5NRR}.
STRAND 269 273 {ECO:0000244|PDB:5NRR}.
HELIX 274 276 {ECO:0000244|PDB:5NRR}.
STRAND 277 279 {ECO:0000244|PDB:5NRR}.
HELIX 283 286 {ECO:0000244|PDB:5NRR}.
HELIX 289 294 {ECO:0000244|PDB:5NRR}.
HELIX 296 313 {ECO:0000244|PDB:5NRR}.
HELIX 325 337 {ECO:0000244|PDB:5NRR}.
TURN 341 343 {ECO:0000244|PDB:5NRR}.
HELIX 344 348 {ECO:0000244|PDB:5NRR}.
SEQUENCE 853 AA; 95751 MW; F20A67CF78951532 CRC64;
MKGDTRHLNG EEDAGGREDS ILVNGACSDQ SSDSPPILEA IRTPEIRGRR SSSRLSKREV
SSLLSYTQDL TGDGDGEDGD GSDTPVMPKL FRETRTRSES PAVRTRNNNS VSSRERHRPS
PRSTRGRQGR NHVDESPVEF PATRSLRRRA TASAGTPWPS PPSSYLTIDL TDDTEDTHGT
PQSSSTPYAR LAQDSQQGGM ESPQVEADSG DGDSSEYQDG KEFGIGDLVW GKIKGFSWWP
AMVVSWKATS KRQAMSGMRW VQWFGDGKFS EVSADKLVAL GLFSQHFNLA TFNKLVSYRK
AMYHALEKAR VRAGKTFPSS PGDSLEDQLK PMLEWAHGGF KPTGIEGLKP NNTQPVVNKS
KVRRAGSRKL ESRKYENKTR RRTADDSATS DYCPAPKRLK TNCYNNGKDR GDEDQSREQM
ASDVANNKSS LEDGCLSCGR KNPVSFHPLF EGGLCQTCRD RFLELFYMYD DDGYQSYCTV
CCEGRELLLC SNTSCCRCFC VECLEVLVGT GTAAEAKLQE PWSCYMCLPQ RCHGVLRRRK
DWNVRLQAFF TSDTGLEYEA PKLYPAIPAA RRRPIRVLSL FDGIATGYLV LKELGIKVGK
YVASEVCEES IAVGTVKHEG NIKYVNDVRN ITKKNIEEWG PFDLVIGGSP CNDLSNVNPA
RKGLYEGTGR LFFEFYHLLN YSRPKEGDDR PFFWMFENVV AMKVGDKRDI SRFLECNPVM
IDAIKVSAAH RARYFWGNLP GMNRPVIASK NDKLELQDCL EYNRIAKLKK VQTITTKSNS
IKQGKNQLFP VVMNGKEDVL WCTELERIFG FPVHYTDVSN MGRGARQKLL GRSWSVPVIR
HLFAPLKDYF ACE


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EIAAB08638 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase,3-demethylubiquinone-9 3-methyltransferase,Coq3,DHHB methyltransferase,DHHB-MT,DHHB-MTase,Dihydroxyhexaprenylbenzoate methyltransferase,Hexaprenyld
EIAAB11605 DNA (cytosine-5)-methyltransferase 3A,DNA methyltransferase HsaIIIA,DNA MTase HsaIIIA,Dnmt3a,DNMT3A,Homo sapiens,Human,M.HsaIIIA
EIAAB11602 DNA (cytosine-5)-methyltransferase 3A,DNA methyltransferase MmuIIIA,DNA MTase MmuIIIA,Dnmt3a,Dnmt3a,M.MmuIIIA,Mouse,Mus musculus
DNMT3B DNMT1 Gene DNA (cytosine-5-)-methyltransferase 1
DNPEP DNMT3B Gene DNA (cytosine-5-)-methyltransferase 3 beta
CSB-EL007085HU Human DNA (cytosine-5)-methyltransferase 3B (DNMT3B) ELISA kit 96T
CSB-EL007085MO Mouse DNA (cytosine-5)-methyltransferase 3B (DNMT3B) ELISA kit 96T
EIAAB08635 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase,3-demethylubiquinone-n 3-methyltransferase,Bos taurus,Bovine,COQ3,DHHB methyltransferase,DHHB-MT,DHHB-MTase,Dihydroxyhexaprenylbenzoate methyltrans
EIAAB11616 AIM,Chicken,DNA (cytosine-5)-methyltransferase 1,DNA methyltransferase GgaI,DNA MTase GgaI,DNMT,Dnmt1,DNMT1,Gallus gallus,M.GgaI,MCMT
DNM3B_MOUSE ELISA Kit FOR DNA (cytosine-5)-methyltransferase 3B; organism: Mouse; gene name: Dnmt3b 96T
DNM3B_HUMAN ELISA Kit FOR DNA (cytosine-5)-methyltransferase 3B; organism: Human; gene name: DNMT3B 96T
EIAAB43808 Bos taurus,Bovine,DNA (cytosine-5)-methyltransferase-like protein 2,Dnmt2,DNMT2,TRDMT1,tRNA (cytosine-5-)-methyltransferase
EIAAB43810 DNA (cytosine-5)-methyltransferase-like protein 2,Dnmt2,Dnmt2,Rat,Rattus norvegicus,Trdmt1,tRNA (cytosine(38)-C(5))-methyltransferase
PY-10202 Oxidative stress, DNA damage, and apoptosis: Anti- DNA (cytosine-5-)-methyltransferase 3 beta (DNMT3b),Chicken-Poly 1mg


 

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