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Methyl-CpG-binding domain protein 2 (Methyl-CpG-binding protein MBD2)

 MBD2_MOUSE              Reviewed;         414 AA.
Q9Z2E1; E9QMV9; Q811D9; Q9Z2D9;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 149.
RecName: Full=Methyl-CpG-binding domain protein 2;
AltName: Full=Methyl-CpG-binding protein MBD2;
Name=Mbd2;
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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
STRAIN=C57BL/6J;
PubMed=9774669; DOI=10.1128/MCB.18.11.6538;
Hendrich B., Bird A.;
"Identification and characterization of a family of mammalian methyl-
CpG binding proteins.";
Mol. Cell. Biol. 18:6538-6547(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129;
PubMed=10441743; DOI=10.1007/s003359901112;
Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.;
"Genomic structure and chromosomal mapping of the murine and human
mbd1, mbd2, mbd3, and mbd4 genes.";
Mamm. Genome 10:906-912(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Colon;
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).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14610093; DOI=10.1074/jbc.M309393200;
Ghoshal K., Majumder S., Datta J., Motiwala T., Bai S., Sharma S.M.,
Frankel W., Jacob S.T.;
"Role of human ribosomal RNA (rRNA) promoter methylation and of
methyl-CpG-binding protein MBD2 in the suppression of rRNA gene
expression.";
J. Biol. Chem. 279:6783-6793(2004).
-!- FUNCTION: Binds CpG islands in promoters where the DNA is
methylated at position 5 of cytosine within CpG dinucleotides.
Binds hemimethylated DNA as well. Recruits histone deacetylases
and DNA methyltransferases. Acts as transcriptional repressor and
plays a role in gene silencing. Functions as a scaffold protein,
targeting GATAD2A and GATAD2B to chromatin to promote repression
(By similarity). May enhance the activation of some unmethylated
cAMP-responsive promoters (By similarity). Selectively represses
transcription activity of methylated rRNA promoters. {ECO:0000250,
ECO:0000269|PubMed:14610093, ECO:0000269|PubMed:9774669}.
-!- SUBUNIT: Heterodimer with MBD3. Component of the MeCP1 complex
that contains HDAC1 and HDAC2. Binds DNMT1, MIZF, GPN1, SIN3A,
GATAD2A/p66-alpha and GATAD2B/p66-beta (By similarity). Interacts
with DHX9 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Nuclear, in
discrete foci. Detected at replication foci in late S phase (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Z2E1-1; Sequence=Displayed;
Name=2;
IsoId=Q9Z2E1-2; Sequence=VSP_011079, VSP_011080;
-!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney,
lung, skeletal muscle, spleen and testis. Detected at lower levels
in embryonic stem cells. {ECO:0000269|PubMed:9774669}.
-----------------------------------------------------------------------
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EMBL; AF072243; AAC68872.1; -; mRNA.
EMBL; AF072245; AAC68874.1; -; mRNA.
EMBL; AF120986; AAD50372.1; -; Genomic_DNA.
EMBL; AF120983; AAD50372.1; JOINED; Genomic_DNA.
EMBL; AF120984; AAD50372.1; JOINED; Genomic_DNA.
EMBL; AF120985; AAD50372.1; JOINED; Genomic_DNA.
EMBL; AF120983; AAD50373.1; -; Genomic_DNA.
EMBL; AC134831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC166815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC170591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC046607; AAH46607.2; -; mRNA.
CCDS; CCDS29335.1; -. [Q9Z2E1-1]
CCDS; CCDS79661.1; -. [Q9Z2E1-2]
RefSeq; NP_001298000.1; NM_001311071.1. [Q9Z2E1-2]
RefSeq; NP_034903.2; NM_010773.2. [Q9Z2E1-1]
UniGene; Mm.322; -.
ProteinModelPortal; Q9Z2E1; -.
SMR; Q9Z2E1; -.
BioGrid; 201331; 25.
ComplexPortal; CPX-953; MBD2/NuRD nucleosome remodeling and deacetylase complex.
CORUM; Q9Z2E1; -.
IntAct; Q9Z2E1; 24.
MINT; Q9Z2E1; -.
STRING; 10090.ENSMUSP00000073701; -.
iPTMnet; Q9Z2E1; -.
PhosphoSitePlus; Q9Z2E1; -.
EPD; Q9Z2E1; -.
PaxDb; Q9Z2E1; -.
PeptideAtlas; Q9Z2E1; -.
PRIDE; Q9Z2E1; -.
Ensembl; ENSMUST00000074058; ENSMUSP00000073701; ENSMUSG00000024513. [Q9Z2E1-1]
Ensembl; ENSMUST00000114946; ENSMUSP00000110596; ENSMUSG00000024513. [Q9Z2E1-2]
GeneID; 17191; -.
KEGG; mmu:17191; -.
UCSC; uc008fom.2; mouse. [Q9Z2E1-2]
UCSC; uc008fon.2; mouse. [Q9Z2E1-1]
CTD; 8932; -.
MGI; MGI:1333813; Mbd2.
eggNOG; ENOG410INB9; Eukaryota.
eggNOG; ENOG410ZPAZ; LUCA.
GeneTree; ENSGT00410000025376; -.
HOGENOM; HOG000013073; -.
HOVERGEN; HBG052417; -.
InParanoid; Q9Z2E1; -.
KO; K11590; -.
OMA; PAIWLNT; -.
OrthoDB; EOG091G0I05; -.
TreeFam; TF325032; -.
Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
Reactome; R-MMU-73728; RNA Polymerase I Promoter Opening.
ChiTaRS; Mbd2; mouse.
PRO; PR:Q9Z2E1; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024513; Expressed in 328 organ(s), highest expression level in blood.
CleanEx; MM_MBD2; -.
ExpressionAtlas; Q9Z2E1; baseline and differential.
Genevisible; Q9Z2E1; MM.
GO; GO:0000785; C:chromatin; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000792; C:heterochromatin; IDA:MGI.
GO; GO:0000118; C:histone deacetylase complex; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0070742; F:C2H2 zinc finger domain binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0008327; F:methyl-CpG binding; IDA:MGI.
GO; GO:0003729; F:mRNA binding; IDA:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0035197; F:siRNA binding; IDA:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0034622; P:cellular protein-containing complex assembly; IMP:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0042711; P:maternal behavior; IMP:MGI.
GO; GO:0006346; P:methylation-dependent chromatin silencing; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0035563; P:positive regulation of chromatin binding; ISO:MGI.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IGI:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR032343; MBD2/MBD3_p55-bd.
InterPro; IPR025884; MeCpG-bd_2/3_C_dom.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
Pfam; PF01429; MBD; 1.
Pfam; PF14048; MBD_C; 1.
Pfam; PF16564; MBDa; 1.
SMART; SM00391; MBD; 1.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS50982; MBD; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 414 Methyl-CpG-binding domain protein 2.
/FTId=PRO_0000096261.
DOMAIN 148 216 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
COMPBIAS 6 143 Gly-rich.
COMPBIAS 50 96 Arg-rich.
MOD_RES 184 184 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBB5}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UBB5}.
VAR_SEQ 238 249 GKPDLNTTLPIR -> FRLIKKQTLIGL (in isoform
2). {ECO:0000303|PubMed:9774669}.
/FTId=VSP_011079.
VAR_SEQ 250 414 Missing (in isoform 2).
{ECO:0000303|PubMed:9774669}.
/FTId=VSP_011080.
CONFLICT 117 117 G -> V (in Ref. 1; AAC68872/AAC68874, 2;
AAD50372/AAD50373 and 4; AAH46607).
{ECO:0000305}.
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


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