MBD2_HUMAN
ID MBD2_HUMAN Reviewed; 411 AA.
AC Q9UBB5; O95242; Q9UIS8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Methyl-CpG-binding domain protein 2 {ECO:0000305};
DE AltName: Full=Demethylase;
DE Short=DMTase;
DE AltName: Full=Methyl-CpG-binding protein MBD2;
GN Name=MBD2 {ECO:0000312|HGNC:HGNC:6917};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 157-411 (ISOFORM 3), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=9774669; DOI=10.1128/mcb.18.11.6538;
RA Hendrich B., Bird A.;
RT "Identification and characterization of a family of mammalian methyl-CpG
RT binding proteins.";
RL Mol. Cell. Biol. 18:6538-6547(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10441743; DOI=10.1007/s003359901112;
RA Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.;
RT "Genomic structure and chromosomal mapping of the murine and human mbd1,
RT mbd2, mbd3, and mbd4 genes.";
RL Mamm. Genome 10:906-912(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10050851; DOI=10.1038/17533;
RA Bhattacharya S.K., Ramchandani S., Cervoni N., Szyf M.;
RT "A mammalian protein with specific demethylase activity for mCpG DNA.";
RL Nature 397:579-583(1999).
RN [5]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH MECP1
RP AND HDAC1.
RX PubMed=10471499; DOI=10.1038/12659;
RA Ng H.-H., Zhang Y., Hendrich B., Johnson C.A., Turner B.M.,
RA Erdjument-Bromage H., Tempst P., Reinberg D., Bird A.;
RT "MBD2 is a transcriptional repressor belonging to the MeCP1 histone
RT deacetylase complex.";
RL Nat. Genet. 23:58-61(1999).
RN [6]
RP FUNCTION, HETERODIMERIZATION WITH MBD3, AND INTERACTION WITH DNMT1.
RX PubMed=10947852; DOI=10.1046/j.1365-2443.2000.00359.x;
RA Tatematsu K., Yamazaki T., Ishikawa F.;
RT "MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex
RT containing DNMT1 at the replication foci in late S phase.";
RL Genes Cells 5:677-688(2000).
RN [7]
RP FUNCTION (ISOFORM 1), AND INTERACTION WITH SIN3A.
RX PubMed=10950960; DOI=10.1074/jbc.m005929200;
RA Boeke J., Ammerpohl O., Kegel S., Moehren U., Renkawitz R.;
RT "The minimal repression domain of MBD2b overlaps with the methyl-CpG-
RT binding domain and binds directly to Sin3A.";
RL J. Biol. Chem. 275:34963-34967(2000).
RN [8]
RP INTERACTION WITH HDAC1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11102443; DOI=10.1074/jbc.m007372200;
RA Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
RA Howard B.H.;
RT "Stable histone deacetylase complexes distinguished by the presence of SANT
RT domain proteins CoREST/kiaa0071 and Mta-L1.";
RL J. Biol. Chem. 276:6817-6824(2001).
RN [9]
RP INTERACTION WITH MIZF.
RX PubMed=11553631; DOI=10.1074/jbc.m107048200;
RA Sekimata M., Takahashi A., Murakami-Sekimata A., Homma Y.;
RT "Involvement of a novel zinc finger protein, MIZF, in transcriptional
RT repression by interacting with a methyl-CpG-binding protein, MBD2.";
RL J. Biol. Chem. 276:42632-42638(2001).
RN [10]
RP INTERACTION WITH P66ALPHA AND P66BETA, AND SUBCELLULAR LOCATION.
RX PubMed=12183469; DOI=10.1074/jbc.m207467200;
RA Brackertz M., Boeke J., Zhang R., Renkawitz R.;
RT "Two highly related p66 proteins comprise a new family of potent
RT transcriptional repressors interacting with MBD2 and MBD3.";
RL J. Biol. Chem. 277:40958-40966(2002).
RN [11]
RP INTERACTION WITH GPN1.
RX PubMed=12588985; DOI=10.1128/mcb.23.5.1656-1665.2003;
RA Lembo F., Pero R., Angrisano T., Vitiello C., Iuliano R., Bruni C.B.,
RA Chiariotti L.;
RT "MBDin, a novel MBD2-interacting protein, relieves MBD2 repression
RT potential and reactivates transcription from methylated promoters.";
RL Mol. Cell. Biol. 23:1656-1665(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH DHX9.
RX PubMed=12665568; DOI=10.1128/mcb.23.8.2645-2657.2003;
RA Fujita H., Fujii R., Aratani S., Amano T., Fukamizu A., Nakajima T.;
RT "Antithetic effects of MBD2a on gene regulation.";
RL Mol. Cell. Biol. 23:2645-2657(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP FUNCTION, AND INTERACTION WITH GATAD2A AND GATAD2B.
RX PubMed=16415179; DOI=10.1093/nar/gkj437;
RA Brackertz M., Gong Z., Leers J., Renkawitz R.;
RT "p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone
RT interaction.";
RL Nucleic Acids Res. 34:397-406(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-407, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP INTERACTION WITH SPHK2.
RX PubMed=19729656; DOI=10.1126/science.1176709;
RA Hait N.C., Allegood J., Maceyka M., Strub G.M., Harikumar K.B., Singh S.K.,
RA Luo C., Marmorstein R., Kordula T., Milstien S., Spiegel S.;
RT "Regulation of histone acetylation in the nucleus by sphingosine-1-
RT phosphate.";
RL Science 325:1254-1257(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-407, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=24307175; DOI=10.1074/jbc.m113.512236;
RA Cramer J.M., Scarsdale J.N., Walavalkar N.M., Buchwald W.A., Ginder G.D.,
RA Williams D.C. Jr.;
RT "Probing the dynamic distribution of bound states for methylcytosine-
RT binding domains on DNA.";
RL J. Biol. Chem. 289:1294-1302(2014).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24]
RP STRUCTURE BY NMR OF 360-393 IN COMPLEX WITH GATAD2A, SUBUNIT, AND
RP INTERACTION WITH GATAD2A.
RX PubMed=21490301; DOI=10.1073/pnas.1015341108;
RA Gnanapragasam M.N., Scarsdale J.N., Amaya M.L., Webb H.D., Desai M.A.,
RA Walavalkar N.M., Wang S.Z., Zu Zhu S., Ginder G.D., Williams D.C. Jr.;
RT "p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical
RT for globin gene silencing by the MBD2-NuRD complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7487-7492(2011).
CC -!- FUNCTION: Binds CpG islands in promoters where the DNA is methylated at
CC position 5 of cytosine within CpG dinucleotides. Binds hemimethylated
CC DNA as well. Recruits histone deacetylases and DNA methyltransferases.
CC Acts as transcriptional repressor and plays a role in gene silencing.
CC Functions as a scaffold protein, targeting GATAD2A and GATAD2B to
CC chromatin to promote repression. May enhance the activation of some
CC unmethylated cAMP-responsive promoters. {ECO:0000269|PubMed:10471499,
CC ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:12665568,
CC ECO:0000269|PubMed:16415179, ECO:0000269|PubMed:24307175,
CC ECO:0000269|PubMed:9774669}.
CC -!- SUBUNIT: Heterodimer with MBD3. Component of the MeCP1 complex that
CC contains HDAC1 and HDAC2. Binds DNMT1, MIZF, GPN1, SIN3A, GATAD2A/p66-
CC alpha and GATAD2B/p66-beta. Interacts with DHX9. Interacts with SPHK2
CC (PubMed:19729656). {ECO:0000269|PubMed:10471499,
CC ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:10950960,
CC ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:11553631,
CC ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:12588985,
CC ECO:0000269|PubMed:12665568, ECO:0000269|PubMed:16415179,
CC ECO:0000269|PubMed:19729656, ECO:0000269|PubMed:21490301}.
CC -!- INTERACTION:
CC Q9UBB5; Q86YP4: GATAD2A; NbExp=8; IntAct=EBI-923391, EBI-726224;
CC Q9UBB5; Q96QR8: PURB; NbExp=3; IntAct=EBI-923391, EBI-2880222;
CC Q9UBB5; Q16637: SMN2; NbExp=2; IntAct=EBI-923391, EBI-395421;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12183469,
CC ECO:0000269|PubMed:9774669}. Note=Nuclear, in discrete foci. Detected
CC at replication foci in late S phase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=MBD2a, MBD2b;
CC IsoId=Q9UBB5-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9UBB5-3; Sequence=VSP_011077, VSP_011078;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, stomach,
CC testis and placenta. {ECO:0000269|PubMed:10050851}.
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305}.
CC -!- CAUTION: Functional studies (PubMed:10050851, PubMed:10950960 and
CC PubMed:12665568) have used a C-terminal fragment of isoform 1 which has
CC been described originally as isoform MBD2b but cannot however be proven
CC by supporting cDNA sequences. {ECO:0000305|PubMed:9774669}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MBD2ID41309ch18q21.html";
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DR EMBL; AF072242; AAC68871.1; -; mRNA.
DR EMBL; AF072246; AAC68875.1; -; mRNA.
DR EMBL; AF120989; AAD56596.1; -; Genomic_DNA.
DR EMBL; AF120988; AAD56596.1; JOINED; Genomic_DNA.
DR EMBL; AF120993; AAD56597.1; -; Genomic_DNA.
DR EMBL; AF120988; AAD56597.1; JOINED; Genomic_DNA.
DR EMBL; AF120989; AAD56597.1; JOINED; Genomic_DNA.
DR EMBL; AF120990; AAD56597.1; JOINED; Genomic_DNA.
DR EMBL; AF120991; AAD56597.1; JOINED; Genomic_DNA.
DR EMBL; AF120992; AAD56597.1; JOINED; Genomic_DNA.
DR EMBL; BC032638; AAH32638.1; -; mRNA.
DR CCDS; CCDS11953.1; -. [Q9UBB5-1]
DR CCDS; CCDS45871.1; -. [Q9UBB5-3]
DR RefSeq; NP_003918.1; NM_003927.4. [Q9UBB5-1]
DR RefSeq; NP_056647.1; NM_015832.4. [Q9UBB5-3]
DR PDB; 2L2L; NMR; -; B=360-393.
DR PDB; 6C1A; X-ray; 2.05 A; A/B/E/F=143-220.
DR PDB; 6C1T; X-ray; 1.84 A; A/D=143-220.
DR PDB; 6C1U; X-ray; 2.30 A; A/B/E/F=143-220.
DR PDB; 6C1V; X-ray; 2.30 A; A/B/E/F=143-220.
DR PDB; 6C2F; X-ray; 2.65 A; A/D/G/J/M/P=143-220.
DR PDB; 6CNP; X-ray; 2.10 A; A/B=143-220.
DR PDB; 6CNQ; X-ray; 2.15 A; A/B=143-220.
DR PDB; 7AO8; EM; 4.50 A; C=1-411.
DR PDB; 7AO9; EM; 6.10 A; C=1-411.
DR PDB; 7AOA; EM; 19.40 A; C=1-411.
DR PDB; 7MWK; X-ray; 2.45 A; A/B=143-220.
DR PDB; 7MWM; X-ray; 1.60 A; A/B=143-220.
DR PDB; 7RAY; X-ray; 1.78 A; A=143-220.
DR PDBsum; 2L2L; -.
DR PDBsum; 6C1A; -.
DR PDBsum; 6C1T; -.
DR PDBsum; 6C1U; -.
DR PDBsum; 6C1V; -.
DR PDBsum; 6C2F; -.
DR PDBsum; 6CNP; -.
DR PDBsum; 6CNQ; -.
DR PDBsum; 7AO8; -.
DR PDBsum; 7AO9; -.
DR PDBsum; 7AOA; -.
DR PDBsum; 7MWK; -.
DR PDBsum; 7MWM; -.
DR PDBsum; 7RAY; -.
DR AlphaFoldDB; Q9UBB5; -.
DR BMRB; Q9UBB5; -.
DR SMR; Q9UBB5; -.
DR BioGRID; 114445; 133.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q9UBB5; -.
DR IntAct; Q9UBB5; 38.
DR MINT; Q9UBB5; -.
DR STRING; 9606.ENSP00000256429; -.
DR BindingDB; Q9UBB5; -.
DR ChEMBL; CHEMBL3707462; -.
DR iPTMnet; Q9UBB5; -.
DR PhosphoSitePlus; Q9UBB5; -.
DR BioMuta; MBD2; -.
DR DMDM; 50401198; -.
DR EPD; Q9UBB5; -.
DR jPOST; Q9UBB5; -.
DR MassIVE; Q9UBB5; -.
DR MaxQB; Q9UBB5; -.
DR PaxDb; Q9UBB5; -.
DR PeptideAtlas; Q9UBB5; -.
DR PRIDE; Q9UBB5; -.
DR ProteomicsDB; 83923; -. [Q9UBB5-1]
DR ProteomicsDB; 83924; -. [Q9UBB5-3]
DR Antibodypedia; 9530; 399 antibodies from 38 providers.
DR DNASU; 8932; -.
DR Ensembl; ENST00000256429.8; ENSP00000256429.3; ENSG00000134046.12. [Q9UBB5-1]
DR Ensembl; ENST00000583046.1; ENSP00000464554.1; ENSG00000134046.12. [Q9UBB5-3]
DR GeneID; 8932; -.
DR KEGG; hsa:8932; -.
DR MANE-Select; ENST00000256429.8; ENSP00000256429.3; NM_003927.5; NP_003918.1.
DR UCSC; uc002lfg.2; human. [Q9UBB5-1]
DR CTD; 8932; -.
DR DisGeNET; 8932; -.
DR GeneCards; MBD2; -.
DR HGNC; HGNC:6917; MBD2.
DR HPA; ENSG00000134046; Low tissue specificity.
DR MIM; 603547; gene.
DR neXtProt; NX_Q9UBB5; -.
DR OpenTargets; ENSG00000134046; -.
DR PharmGKB; PA30660; -.
DR VEuPathDB; HostDB:ENSG00000134046; -.
DR eggNOG; KOG4161; Eukaryota.
DR GeneTree; ENSGT00950000183005; -.
DR HOGENOM; CLU_055454_0_0_1; -.
DR InParanoid; Q9UBB5; -.
DR OMA; NTMLLCK; -.
DR OrthoDB; 1431783at2759; -.
DR PhylomeDB; Q9UBB5; -.
DR TreeFam; TF325032; -.
DR PathwayCommons; Q9UBB5; -.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR SignaLink; Q9UBB5; -.
DR SIGNOR; Q9UBB5; -.
DR BioGRID-ORCS; 8932; 37 hits in 1104 CRISPR screens.
DR ChiTaRS; MBD2; human.
DR GeneWiki; Methyl-CpG-binding_domain_protein_2; -.
DR GenomeRNAi; 8932; -.
DR Pharos; Q9UBB5; Tchem.
DR PRO; PR:Q9UBB5; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9UBB5; protein.
DR Bgee; ENSG00000134046; Expressed in gingival epithelium and 210 other tissues.
DR ExpressionAtlas; Q9UBB5; baseline and differential.
DR Genevisible; Q9UBB5; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IC:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; HDA:UniProtKB.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003696; F:satellite DNA binding; TAS:ProtInc.
DR GO; GO:0035197; F:siRNA binding; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; IGI:BHF-UCL.
DR GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
DR DisProt; DP01068; -.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR032343; MBD2/MBD3_p55-bd.
DR InterPro; IPR025884; MeCpG-bd_2/3_C_dom.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF14048; MBD_C; 1.
DR Pfam; PF16564; MBDa; 1.
DR SMART; SM00391; MBD; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR PROSITE; PS50982; MBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..411
FT /note="Methyl-CpG-binding domain protein 2"
FT /id="PRO_0000096260"
FT DOMAIN 145..213
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..149
FT /note="Necessary for interaction with DHX9"
FT /evidence="ECO:0000269|PubMed:12665568"
FT REGION 214..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 235..302
FT /note="GKPDLNTTLPIRQTASIFKQPVTKVTNHPSNKVKSDPQRMNEQPRQLFWEKR
FT LQGLSASDVTEQIIKT -> LRWNTHRPAPWHALSRLCLLIRCLLCLECAYPLPLHLVN
FT SYSSKTQLHCLHLWEACPAYSRQNQSFPP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9774669"
FT /id="VSP_011077"
FT VAR_SEQ 303..411
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9774669"
FT /id="VSP_011078"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:7MWM"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:7MWM"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:7MWM"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:7MWM"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:7MWM"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6C2F"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:7MWM"
FT HELIX 366..388
FT /evidence="ECO:0007829|PDB:2L2L"
FT TURN 389..392
FT /evidence="ECO:0007829|PDB:2L2L"
SQ SEQUENCE 411 AA; 43255 MW; FC4E5E0CF9BA0FFA CRC64;
MRAHPGGGRC CPEQEEGESA AGGSGAGGDS AIEQGGQGSA LAPSPVSGVR REGARGGGRG
RGRWKQAGRG GGVCGRGRGR GRGRGRGRGR GRGRGRPPSG GSGLGGDGGG CGGGGSGGGG
APRREPVPFP SGSAGPGPRG PRATESGKRM DCPALPPGWK KEEVIRKSGL SAGKSDVYYF
SPSGKKFRSK PQLARYLGNT VDLSSFDFRT GKMMPSKLQK NKQRLRNDPL NQNKGKPDLN
TTLPIRQTAS IFKQPVTKVT NHPSNKVKSD PQRMNEQPRQ LFWEKRLQGL SASDVTEQII
KTMELPKGLQ GVGPGSNDET LLSAVASALH TSSAPITGQV SAAVEKNPAV WLNTSQPLCK
AFIVTDEDIR KQEERVQQVR KKLEEALMAD ILSRAADTEE MDIEMDSGDE A
