MBD2_MOUSE
ID MBD2_MOUSE Reviewed; 414 AA.
AC Q9Z2E1; E9QMV9; Q811D9; Q9Z2D9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Methyl-CpG-binding domain protein 2 {ECO:0000305};
DE AltName: Full=Methyl-CpG-binding protein MBD2;
GN Name=Mbd2 {ECO:0000312|MGI:MGI:1333813};
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 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
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].
RC STRAIN=129;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14610093; DOI=10.1074/jbc.m309393200;
RA Ghoshal K., Majumder S., Datta J., Motiwala T., Bai S., Sharma S.M.,
RA Frankel W., Jacob S.T.;
RT "Role of human ribosomal RNA (rRNA) promoter methylation and of methyl-CpG-
RT binding protein MBD2 in the suppression of rRNA gene expression.";
RL J. Biol. Chem. 279:6783-6793(2004).
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 (By similarity). May enhance the
CC activation of some unmethylated cAMP-responsive promoters (By
CC similarity). Selectively represses transcription activity of methylated
CC rRNA promoters. {ECO:0000250|UniProtKB:Q9UBB5,
CC ECO:0000269|PubMed:14610093, 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 (By similarity). Interacts with DHX9 (By
CC similarity). Interacts with SPHK2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBB5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UBB5}.
CC Note=Nuclear, in discrete foci. Detected at replication foci in late S
CC phase. {ECO:0000250|UniProtKB:Q9UBB5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z2E1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z2E1-2; Sequence=VSP_011079, VSP_011080;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney, lung,
CC skeletal muscle, spleen and testis. Detected at lower levels in
CC embryonic stem cells. {ECO:0000269|PubMed:9774669}.
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DR EMBL; AF072243; AAC68872.1; -; mRNA.
DR EMBL; AF072245; AAC68874.1; -; mRNA.
DR EMBL; AF120986; AAD50372.1; -; Genomic_DNA.
DR EMBL; AF120983; AAD50372.1; JOINED; Genomic_DNA.
DR EMBL; AF120984; AAD50372.1; JOINED; Genomic_DNA.
DR EMBL; AF120985; AAD50372.1; JOINED; Genomic_DNA.
DR EMBL; AF120983; AAD50373.1; -; Genomic_DNA.
DR EMBL; AC134831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC170591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046607; AAH46607.2; -; mRNA.
DR CCDS; CCDS29335.1; -. [Q9Z2E1-1]
DR CCDS; CCDS79661.1; -. [Q9Z2E1-2]
DR RefSeq; NP_001298000.1; NM_001311071.1. [Q9Z2E1-2]
DR RefSeq; NP_034903.2; NM_010773.2. [Q9Z2E1-1]
DR AlphaFoldDB; Q9Z2E1; -.
DR BMRB; Q9Z2E1; -.
DR SMR; Q9Z2E1; -.
DR BioGRID; 201331; 28.
DR ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q9Z2E1; -.
DR IntAct; Q9Z2E1; 23.
DR MINT; Q9Z2E1; -.
DR STRING; 10090.ENSMUSP00000073701; -.
DR iPTMnet; Q9Z2E1; -.
DR PhosphoSitePlus; Q9Z2E1; -.
DR EPD; Q9Z2E1; -.
DR jPOST; Q9Z2E1; -.
DR MaxQB; Q9Z2E1; -.
DR PaxDb; Q9Z2E1; -.
DR PeptideAtlas; Q9Z2E1; -.
DR PRIDE; Q9Z2E1; -.
DR ProteomicsDB; 295968; -. [Q9Z2E1-1]
DR ProteomicsDB; 295969; -. [Q9Z2E1-2]
DR Antibodypedia; 9530; 399 antibodies from 38 providers.
DR DNASU; 17191; -.
DR Ensembl; ENSMUST00000074058; ENSMUSP00000073701; ENSMUSG00000024513. [Q9Z2E1-1]
DR Ensembl; ENSMUST00000114946; ENSMUSP00000110596; ENSMUSG00000024513. [Q9Z2E1-2]
DR GeneID; 17191; -.
DR KEGG; mmu:17191; -.
DR UCSC; uc008fom.2; mouse. [Q9Z2E1-2]
DR UCSC; uc008fon.2; mouse. [Q9Z2E1-1]
DR CTD; 8932; -.
DR MGI; MGI:1333813; Mbd2.
DR VEuPathDB; HostDB:ENSMUSG00000024513; -.
DR eggNOG; KOG4161; Eukaryota.
DR GeneTree; ENSGT00950000183005; -.
DR HOGENOM; CLU_055454_0_0_1; -.
DR InParanoid; Q9Z2E1; -.
DR OMA; NTMLLCK; -.
DR OrthoDB; 1431783at2759; -.
DR PhylomeDB; Q9Z2E1; -.
DR TreeFam; TF325032; -.
DR Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-MMU-73728; RNA Polymerase I Promoter Opening.
DR BioGRID-ORCS; 17191; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Mbd2; mouse.
DR PRO; PR:Q9Z2E1; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9Z2E1; protein.
DR Bgee; ENSMUSG00000024513; Expressed in epithelium of urethra and 276 other tissues.
DR ExpressionAtlas; Q9Z2E1; baseline and differential.
DR Genevisible; Q9Z2E1; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016581; C:NuRD complex; IC:ComplexPortal.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0035197; F:siRNA binding; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0042711; P:maternal behavior; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
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; IGI:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
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; IGI:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..414
FT /note="Methyl-CpG-binding domain protein 2"
FT /id="PRO_0000096261"
FT DOMAIN 148..216
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..244
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 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB5"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBB5"
FT VAR_SEQ 238..249
FT /note="GKPDLNTTLPIR -> FRLIKKQTLIGL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9774669"
FT /id="VSP_011079"
FT VAR_SEQ 250..414
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9774669"
FT /id="VSP_011080"
FT CONFLICT 117
FT /note="G -> V (in Ref. 1; AAC68872/AAC68874, 2; AAD50372/
FT AAD50373 and 4; AAH46607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 43501 MW; 1C658D4A6066602A CRC64;
MRAHPGGGRC CPEQEEGESA AGGSGAGGDS AIEQGGQGSA LAPSPVSGVR REGARGGGRG
RGRWKQAARG GGVCGRGRGR GRGRGRGRGR GRGRGRPQSG GSGLGGDGGG GAGGCGGGSG
GGVAPRRDPV PFPSGSSGPG PRGPRATESG KRMDCPALPP GWKKEEVIRK SGLSAGKSDV
YYFSPSGKKF RSKPQLARYL GNAVDLSSFD FRTGKMMPSK LQKNKQRLRN DPLNQNKGKP
DLNTTLPIRQ TASIFKQPVT KFTNHPSNKV KSDPQRMNEQ PRQLFWEKRL QGLSASDVTE
QIIKTMELPK GLQGVGPGSN DETLLSAVAS ALHTSSAPIT GQVSAAVEKN PAVWLNTSQP
LCKAFIVTDE DIRKQEERVQ QVRKKLEEAL MADILSRAAD TEEVDIDMDS GDEA
