ID DNM3B_MOUSE Reviewed; 859 AA.
AC O88509; O88510; O88511;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 196.
DE RecName: Full=DNA (cytosine-5)-methyltransferase 3B;
DE Short=Dnmt3b;
DE EC=2.1.1.37;
DE AltName: Full=DNA methyltransferase MmuIIIB;
DE Short=DNA MTase MmuIIIB;
DE Short=M.MmuIIIB;
GN Name=Dnmt3b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=9662389; DOI=10.1038/890;
RA Okano M., Xie S., Li E.;
RT "Cloning and characterization of a family of novel mammalian DNA (cytosine-
RT 5) methyltransferases.";
RL Nat. Genet. 19:219-220(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=KM; TISSUE=Embryo;
RX PubMed=12567489;
RA Yin B., Chen Y., Zhu N., Wu G., Shen Y.;
RT "Cloning of full-length Dnmt3b cDNA and its alternative splicing isoforms
RT in mouse embryo.";
RL Zhongguo Yi Xue Ke Xue Yuan Xue Bao 21:431-438(1999).
RN [3]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10555141; DOI=10.1016/s0092-8674(00)81656-6;
RA Okano M., Bell D.W., Haber D.A., Li E.;
RT "DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo
RT methylation and mammalian development.";
RL Cell 99:247-257(1999).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF ALA-609; GLY-669; LEU-670; VAL-725; ASP-823
RP AND VAL-824.
RX PubMed=11919202; DOI=10.1074/jbc.m202148200;
RA Gowher H., Jeltsch A.;
RT "Molecular enzymology of the catalytic domains of the Dnmt3a and Dnmt3b DNA
RT methyltransferases.";
RL J. Biol. Chem. 277:20409-20414(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP CITRULLINATION AT ARG-415.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
RN [7]
RP INTERACTION WITH SUV39H1.
RX PubMed=12867029; DOI=10.1016/s0960-9822(03)00432-9;
RA Lehnertz B., Ueda Y., Derijck A.A.H.A., Braunschweig U., Perez-Burgos L.,
RA Kubicek S., Chen T., Li E., Jenuwein T., Peters A.H.F.M.;
RT "Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to
RT major satellite repeats at pericentric heterochromatin.";
RL Curr. Biol. 13:1192-1200(2003).
RN [8]
RP INTERACTION WITH BAZ2A.
RX PubMed=16085498; DOI=10.1016/j.cub.2005.06.057;
RA Zhou Y., Grummt I.;
RT "The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16
RT and is sufficient for rDNA silencing.";
RL Curr. Biol. 15:1434-1438(2005).
RN [9]
RP INTERACTION WITH EED AND EZH2.
RX PubMed=16357870; DOI=10.1038/nature04431;
RA Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RT "The Polycomb group protein EZH2 directly controls DNA methylation.";
RL Nature 439:871-874(2006).
RN [10]
RP ERRATUM OF PUBMED:16357870.
RA Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RL Nature 446:824-824(2006).
RN [11]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 236-VAL-TRP-237; SER-277 AND
RP 656-PRO-CYS-657.
RX PubMed=15456878; DOI=10.1128/mcb.24.20.9048-9058.2004;
RA Chen T., Tsujimoto N., Li E.;
RT "The PWWP domain of Dnmt3a and Dnmt3b is required for directing DNA
RT methylation to the major satellite repeats at pericentric
RT heterochromatin.";
RL Mol. Cell. Biol. 24:9048-9058(2004).
RN [12]
RP ACTIVITY REGULATION.
RX PubMed=15671018; DOI=10.1074/jbc.m413412200;
RA Gowher H., Liebert K., Hermann A., Xu G., Jeltsch A.;
RT "Mechanism of stimulation of catalytic activity of Dnmt3A and Dnmt3B DNA-
RT (cytosine-C5)-methyltransferases by Dnmt3L.";
RL J. Biol. Chem. 280:13341-13348(2005).
RN [13]
RP FUNCTION.
RX PubMed=16567415; DOI=10.1093/jb/mvj044;
RA Takeshima H., Suetake I., Shimahara H., Ura K., Tate S., Tajima S.;
RT "Distinct DNA methylation activity of Dnmt3a and Dnmt3b towards naked and
RT nucleosomal DNA.";
RL J. Biochem. 139:503-515(2006).
RN [14]
RP FUNCTION.
RX PubMed=18056424; DOI=10.1101/gad.1594007;
RA Linhart H.G., Lin H., Yamada Y., Moran E., Steine E.J., Gokhale S., Lo G.,
RA Cantu E., Ehrich M., He T., Meissner A., Jaenisch R.;
RT "Dnmt3b promotes tumorigenesis in vivo by gene-specific de novo methylation
RT and transcriptional silencing.";
RL Genes Dev. 21:3110-3122(2007).
RN [15]
RP FUNCTION, AND INTERACTION WITH CBX4.
RX PubMed=18567530; DOI=10.1016/j.biocel.2008.04.018;
RA Kim S.-H., Park J., Choi M.-C., Park J.-H., Kim H.-P., Lee J.-H., Oh D.-Y.,
RA Im S.-A., Bang Y.-J., Kim T.-Y.;
RT "DNA methyltransferase 3B acts as a co-repressor of the human polycomb
RT protein hPc2 to repress fibroblast growth factor receptor 3
RT transcription.";
RL Int. J. Biochem. Cell Biol. 40:2462-2471(2008).
RN [16]
RP INTERACTION WITH UHRF1.
RX PubMed=19798101; DOI=10.1038/embor.2009.201;
RA Meilinger D., Fellinger K., Bultmann S., Rothbauer U., Bonapace I.M.,
RA Klinkert W.E., Spada F., Leonhardt H.;
RT "Np95 interacts with de novo DNA methyltransferases, Dnmt3a and Dnmt3b, and
RT mediates epigenetic silencing of the viral CMV promoter in embryonic stem
RT cells.";
RL EMBO Rep. 10:1259-1264(2009).
RN [17]
RP DEVELOPMENTAL STAGE.
RX PubMed=18814855; DOI=10.1016/j.gep.2008.09.002;
RA Hirasawa R., Sasaki H.;
RT "Dynamic transition of Dnmt3b expression in mouse pre- and early post-
RT implantation embryos.";
RL Gene Expr. Patterns 9:27-30(2009).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 219-362, FUNCTION, AND INTERACTION
RP WITH DNA.
RX PubMed=11836534; DOI=10.1038/nsb759;
RA Qiu C., Sawada K., Zhang X., Cheng X.;
RT "The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new
RT family of DNA-binding folds.";
RL Nat. Struct. Biol. 9:217-224(2002).
CC -!- FUNCTION: Required for genome-wide de novo methylation and is essential
CC for the establishment of DNA methylation patterns during development.
CC DNA methylation is coordinated with methylation of histones. May
CC preferentially methylates nucleosomal DNA within the nucleosome core
CC region. May function as transcriptional co-repressor by associating
CC with CBX4 and independently of DNA methylation. Seems to be involved in
CC gene silencing. In association with DNMT1 and via the recruitment of
CC CTCFL/BORIS, involved in activation of BAG1 gene expression by
CC modulating dimethylation of promoter histone H3 at H3K4 and H3K9.
CC Functions as a transcriptional corepressor by associating with ZHX1 (By
CC similarity). Required for DUX4 silencing in somatic cells (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UBC3,
CC ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:11836534,
CC ECO:0000269|PubMed:11919202, ECO:0000269|PubMed:16567415,
CC ECO:0000269|PubMed:18056424, ECO:0000269|PubMed:18567530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC -!- ACTIVITY REGULATION: Activated by binding to the regulatory factor
CC DNMT3L. {ECO:0000269|PubMed:15671018}.
CC -!- SUBUNIT: Interacts with CBX4, DNMT1, DNMT3A, SETDB1, UBE2I9, UBL1 and
CC ZHX1 (By similarity). Interacts with SUV39H1 and BAZ2A/TIP5. Interacts
CC with the PRC2/EED-EZH2 complex. Interacts with UHRF1. {ECO:0000250,
CC ECO:0000269|PubMed:11836534, ECO:0000269|PubMed:12867029,
CC ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:16357870,
CC ECO:0000269|PubMed:18567530, ECO:0000269|PubMed:19798101}.
CC -!- INTERACTION:
CC O88509; P25916: Bmi1; NbExp=2; IntAct=EBI-7987547, EBI-927401;
CC O88509; Q9CWR8: Dnmt3l; NbExp=6; IntAct=EBI-7987547, EBI-3043871;
CC O88509; Q9Z148-2: Ehmt2; NbExp=3; IntAct=EBI-7987547, EBI-15737169;
CC O88509; Q60848: Hells; NbExp=4; IntAct=EBI-7987547, EBI-3043887;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15456878}.
CC Note=Accumulates in the major satellite repeats at pericentric
CC heterochromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=5;
CC IsoId=O88509-1; Sequence=Displayed;
CC Name=2; Synonyms=6;
CC IsoId=O88509-2; Sequence=VSP_005642;
CC Name=3; Synonyms=8;
CC IsoId=O88509-3; Sequence=VSP_005642, VSP_005643;
CC Name=4; Synonyms=7;
CC IsoId=O88509-4; Sequence=VSP_005643;
CC -!- DEVELOPMENTAL STAGE: Expressed in almost all blastocysts at 3.0 dpc.
CC Preferentially expressed in the trophectoderm (TE) in 3.5 dpc and polar
CC TE in 4.0 dpc blastocysts. In 4.5 dpc embryos, expressed in the polar
CC TE and some inner cell mass (ICM) embryonic lineage cells. In post-
CC implantation embryo at 5.5 dpc, expressed in the epiblast (embryonic
CC lineage) derived from the ICM. Highly expressed, at 7.5 dpc, in the
CC embryonic ectoderm, neural ectoderm, and chorionic ectoderm; a weak
CC expression is also detected in mesodermal and endodermal cells. At
CC later stages, the expression is detected predominantly in the forebrain
CC and eyes but weakly throughout the embryo.
CC {ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:18814855}.
CC -!- DOMAIN: The PWWP domain is essential for targeting to pericentric
CC heterochromatin.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; AF068626; AAC40178.2; -; mRNA.
DR EMBL; AF068627; AAC40179.2; -; mRNA.
DR EMBL; AF068628; AAC40180.2; -; mRNA.
DR EMBL; AF151969; AAF74515.1; -; mRNA.
DR EMBL; AF151970; AAF74516.1; -; mRNA.
DR EMBL; AF151971; AAF74517.1; -; mRNA.
DR EMBL; AF151972; AAF74518.1; -; mRNA.
DR EMBL; AF151973; AAF74519.1; -; mRNA.
DR EMBL; AF151974; AAF74520.1; -; mRNA.
DR EMBL; AF151975; AAF74521.1; -; mRNA.
DR EMBL; AF151976; AAF74522.1; -; mRNA.
DR CCDS; CCDS16913.1; -. [O88509-2]
DR CCDS; CCDS16914.1; -. [O88509-1]
DR CCDS; CCDS16915.1; -. [O88509-4]
DR CCDS; CCDS16916.1; -. [O88509-3]
DR RefSeq; NP_001003960.2; NM_001003960.4. [O88509-2]
DR RefSeq; NP_001003961.2; NM_001003961.4. [O88509-1]
DR RefSeq; NP_001258673.1; NM_001271744.1. [O88509-1]
DR RefSeq; NP_001258674.1; NM_001271745.1. [O88509-2]
DR RefSeq; NP_001258676.1; NM_001271747.1. [O88509-3]
DR RefSeq; NP_034198.3; NM_010068.5. [O88509-3]
DR PDB; 1KHC; X-ray; 1.80 A; A=219-362.
DR PDBsum; 1KHC; -.
DR AlphaFoldDB; O88509; -.
DR SMR; O88509; -.
DR BioGRID; 199262; 11.
DR CORUM; O88509; -.
DR DIP; DIP-43736N; -.
DR IntAct; O88509; 11.
DR MINT; O88509; -.
DR STRING; 10090.ENSMUSP00000051830; -.
DR BindingDB; O88509; -.
DR ChEMBL; CHEMBL2189115; -.
DR REBASE; 3748; M.MmuDnmt3B.
DR iPTMnet; O88509; -.
DR PhosphoSitePlus; O88509; -.
DR EPD; O88509; -.
DR jPOST; O88509; -.
DR MaxQB; O88509; -.
DR PaxDb; 10090-ENSMUSP00000105396; -.
DR PeptideAtlas; O88509; -.
DR ProteomicsDB; 277365; -. [O88509-1]
DR ProteomicsDB; 277366; -. [O88509-2]
DR ProteomicsDB; 277367; -. [O88509-3]
DR ProteomicsDB; 277368; -. [O88509-4]
DR DNASU; 13436; -.
DR Ensembl; ENSMUST00000072997.10; ENSMUSP00000072761.4; ENSMUSG00000027478.16. [O88509-1]
DR Ensembl; ENSMUST00000081628.13; ENSMUSP00000080334.7; ENSMUSG00000027478.16. [O88509-2]
DR Ensembl; ENSMUST00000088976.12; ENSMUSP00000086370.6; ENSMUSG00000027478.16. [O88509-4]
DR Ensembl; ENSMUST00000103150.10; ENSMUSP00000099439.4; ENSMUSG00000027478.16. [O88509-3]
DR Ensembl; ENSMUST00000103151.8; ENSMUSP00000099440.2; ENSMUSG00000027478.16. [O88509-3]
DR Ensembl; ENSMUST00000109772.8; ENSMUSP00000105394.2; ENSMUSG00000027478.16. [O88509-4]
DR Ensembl; ENSMUST00000109773.8; ENSMUSP00000105395.2; ENSMUSG00000027478.16. [O88509-2]
DR Ensembl; ENSMUST00000109774.9; ENSMUSP00000105396.3; ENSMUSG00000027478.16. [O88509-1]
DR GeneID; 13436; -.
DR KEGG; mmu:13436; -.
DR UCSC; uc008nib.3; mouse. [O88509-1]
DR UCSC; uc008nic.3; mouse. [O88509-2]
DR UCSC; uc008nie.3; mouse. [O88509-3]
DR AGR; MGI:1261819; -.
DR CTD; 1789; -.
DR MGI; MGI:1261819; Dnmt3b.
DR VEuPathDB; HostDB:ENSMUSG00000027478; -.
DR eggNOG; ENOG502QR6U; Eukaryota.
DR GeneTree; ENSGT00940000156928; -.
DR HOGENOM; CLU_006958_9_1_1; -.
DR InParanoid; O88509; -.
DR OMA; CLEYSRI; -.
DR OrthoDB; 2904336at2759; -.
DR TreeFam; TF329039; -.
DR BRENDA; 2.1.1.37; 3474.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR Reactome; R-MMU-4655427; SUMOylation of DNA methylation proteins.
DR BioGRID-ORCS; 13436; 2 hits in 81 CRISPR screens.
DR ChiTaRS; Dnmt3b; mouse.
DR EvolutionaryTrace; O88509; -.
DR PRO; PR:O88509; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88509; Protein.
DR Bgee; ENSMUSG00000027478; Expressed in epiblast (generic) and 203 other cell types or tissues.
DR ExpressionAtlas; O88509; baseline and differential.
DR Genevisible; O88509; MM.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:MGI.
DR GO; GO:0051718; F:DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates; IDA:MGI.
DR GO; GO:0051719; F:DNA (cytosine-5-)-methyltransferase activity, acting on CpN substrates; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0141068; P:autosome genomic imprinting; IMP:MGI.
DR GO; GO:0090116; P:C-5 methylation of cytosine; IDA:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin formation; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0043045; P:post-fertilization epigenetic regulation of gene expression; IGI:MGI.
DR GO; GO:0031503; P:protein-containing complex localization; IDA:MGI.
DR CDD; cd11728; ADDz_Dnmt3b; 1.
DR CDD; cd20155; PWWP_DNMT3B; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.10.720.50; PWWP, helical domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR IDEAL; IID50164; -.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR040552; DNMT3_ADD_GATA1-like.
DR InterPro; IPR049554; DNMT3_ADD_PHD.
DR InterPro; IPR030488; DNMT3B_ADD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR23068:SF9; DNA (CYTOSINE-5)-METHYLTRANSFERASE 3B; 1.
DR PANTHER; PTHR23068; DNA CYTOSINE-5- -METHYLTRANSFERASE 3-RELATED; 1.
DR Pfam; PF17980; ADD_DNMT3; 1.
DR Pfam; PF21255; ADDz_Dnmt3b; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Citrullination; DNA-binding;
KW Isopeptide bond; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transferase;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..859
FT /note="DNA (cytosine-5)-methyltransferase 3B"
FT /id="PRO_0000088046"
FT DOMAIN 232..290
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 428..560
FT /note="ADD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT DOMAIN 581..859
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ZN_FING 439..469
FT /note="GATA-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT ZN_FING 480..536
FT /note="PHD-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00865"
FT REGION 1..305
FT /note="Interaction with DNMT1 and DNMT3A"
FT /evidence="ECO:0000250"
FT REGION 25..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..532
FT /note="Interaction with the PRC2/EED-EZH2 complex"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
FT BINDING 588..592
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT BINDING 611
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT BINDING 633..635
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT BINDING 838..840
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6K1"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC3"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC3"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC3"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC3"
FT MOD_RES 415
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC3"
FT CROSSLNK 623
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBC3"
FT VAR_SEQ 363..382
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12567489,
FT ECO:0000303|PubMed:9662389"
FT /id="VSP_005642"
FT VAR_SEQ 750..812
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12567489,
FT ECO:0000303|PubMed:9662389"
FT /id="VSP_005643"
FT MUTAGEN 236..237
FT /note="VW->RR: Prevents accumulation in pericentric
FT heterochromatin."
FT /evidence="ECO:0000269|PubMed:15456878"
FT MUTAGEN 277
FT /note="S->P: Prevents accumulation in pericentric
FT heterochromatin."
FT /evidence="ECO:0000269|PubMed:15456878"
FT MUTAGEN 609
FT /note="A->T: Significantly reduces activity."
FT /evidence="ECO:0000269|PubMed:11919202"
FT MUTAGEN 656..657
FT /note="PC->GT: No effect on localization."
FT /evidence="ECO:0000269|PubMed:15456878"
FT MUTAGEN 669
FT /note="G->S: Significantly reduces activity."
FT /evidence="ECO:0000269|PubMed:11919202"
FT MUTAGEN 670
FT /note="L->T: Significantly reduces activity."
FT /evidence="ECO:0000269|PubMed:11919202"
FT MUTAGEN 725
FT /note="V->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11919202"
FT MUTAGEN 823
FT /note="D->G: Significantly reduces activity."
FT /evidence="ECO:0000269|PubMed:11919202"
FT MUTAGEN 824
FT /note="V->M: Significantly reduces activity."
FT /evidence="ECO:0000269|PubMed:11919202"
FT CONFLICT 217..218
FT /note="RD -> IY (in Ref. 2; AAF74515/AAF74516)"
FT /evidence="ECO:0000305"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:1KHC"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:1KHC"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:1KHC"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:1KHC"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1KHC"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:1KHC"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1KHC"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1KHC"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1KHC"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:1KHC"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:1KHC"
FT HELIX 303..320
FT /evidence="ECO:0007829|PDB:1KHC"
FT HELIX 332..344
FT /evidence="ECO:0007829|PDB:1KHC"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:1KHC"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:1KHC"
SQ SEQUENCE 859 AA; 97228 MW; 93E334D9FBCC590E CRC64;
MKGDSRHLNE EEGASGYEEC IIVNGNFSDQ SSDTKDAPSP PVLEAICTEP VCTPETRGRR
SSSRLSKREV SSLLNYTQDM TGDGDRDDEV DDGNGSDILM PKLTRETKDT RTRSESPAVR
TRHSNGTSSL ERQRASPRIT RGRQGRHHVQ EYPVEFPATR SRRRRASSSA STPWSSPASV
DFMEEVTPKS VSTPSVDLSQ DGDQEGMDTT QVDAESRDGD STEYQDDKEF GIGDLVWGKI
KGFSWWPAMV VSWKATSKRQ AMPGMRWVQW FGDGKFSEIS ADKLVALGLF SQHFNLATFN
KLVSYRKAMY HTLEKARVRA GKTFSSSPGE SLEDQLKPML EWAHGGFKPT GIEGLKPNKK
QPVVNKSKVR RSDSRNLEPR RRENKSRRRT TNDSAASESP PPKRLKTNSY GGKDRGEDEE
SRERMASEVT NNKGNLEDRC LSCGKKNPVS FHPLFEGGLC QSCRDRFLEL FYMYDEDGYQ
SYCTVCCEGR ELLLCSNTSC CRCFCVECLE VLVGAGTAED AKLQEPWSCY MCLPQRCHGV
LRRRKDWNMR LQDFFTTDPD LEEFEPPKLY PAIPAAKRRP IRVLSLFDGI ATGYLVLKEL
GIKVEKYIAS EVCAESIAVG TVKHEGQIKY VNDVRKITKK NIEEWGPFDL VIGGSPCNDL
SNVNPARKGL YEGTGRLFFE FYHLLNYTRP KEGDNRPFFW MFENVVAMKV NDKKDISRFL
ACNPVMIDAI KVSAAHRARY FWGNLPGMNR PVMASKNDKL ELQDCLEFSR TAKLKKVQTI
TTKSNSIRQG KNQLFPVVMN GKDDVLWCTE LERIFGFPAH YTDVSNMGRG ARQKLLGRSW
SVPVIRHLFA PLKDYFACE
//
