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Methyl-CpG-binding domain protein 3 (Methyl-CpG-binding protein MBD3)

 MBD3_MOUSE              Reviewed;         285 AA.
Q9Z2D8; Q792D3; Q8CFJ1;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
22-NOV-2017, entry version 138.
RecName: Full=Methyl-CpG-binding domain protein 3;
AltName: Full=Methyl-CpG-binding protein MBD3;
Name=Mbd3;
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 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
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.
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 MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Mammary tumor;
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).
[4]
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Acts as transcriptional repressor and plays a role in
gene silencing. Does not bind DNA by itself. Binds to DNA with a
preference for sites containing methylated CpG dinucleotides (in
vitro). Binds to a lesser degree DNA containing unmethylated CpG
dinucleotides (By similarity). Recruits histone deacetylases and
DNA methyltransferases. {ECO:0000250, ECO:0000269|PubMed:9774669}.
-!- SUBUNIT: Heterodimer with MBD2. Part of the NuRD and the MeCP1
complex. Interacts with BCL6, HDAC1, MTA2, DNMT1, p66-alpha and
p66-beta (By similarity). {ECO:0000250}.
-!- INTERACTION:
P14404:Mecom; NbExp=5; IntAct=EBI-1994598, EBI-1994523;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14610093,
ECO:0000269|PubMed:9774669}. Chromosome {ECO:0000250}.
Note=Detected on chromatin, at promoter regions of active genes
(By similarity). Nuclear, in discrete foci. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Z2D8-1; Sequence=Displayed;
Name=2;
IsoId=Q9Z2D8-2; Sequence=VSP_011082;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney,
liver, lung, skeletal muscle, spleen and testis. Detected at lower
levels in embryonic stem cells. {ECO:0000269|PubMed:9774669}.
-----------------------------------------------------------------------
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EMBL; AF072248; AAC68877.1; -; mRNA.
EMBL; AF120995; AAD48909.1; -; Genomic_DNA.
EMBL; BC038264; AAH38264.1; -; mRNA.
CCDS; CCDS24020.1; -. [Q9Z2D8-1]
CCDS; CCDS78860.1; -. [Q9Z2D8-2]
RefSeq; NP_001293072.1; NM_001306143.1. [Q9Z2D8-2]
RefSeq; NP_038623.1; NM_013595.3. [Q9Z2D8-1]
UniGene; Mm.7142; -.
ProteinModelPortal; Q9Z2D8; -.
SMR; Q9Z2D8; -.
BioGrid; 201332; 15.
CORUM; Q9Z2D8; -.
DIP; DIP-46518N; -.
IntAct; Q9Z2D8; 12.
MINT; MINT-4101368; -.
STRING; 10090.ENSMUSP00000089948; -.
iPTMnet; Q9Z2D8; -.
PhosphoSitePlus; Q9Z2D8; -.
PaxDb; Q9Z2D8; -.
PeptideAtlas; Q9Z2D8; -.
PRIDE; Q9Z2D8; -.
Ensembl; ENSMUST00000092295; ENSMUSP00000089948; ENSMUSG00000035478. [Q9Z2D8-1]
Ensembl; ENSMUST00000105349; ENSMUSP00000100986; ENSMUSG00000035478. [Q9Z2D8-2]
GeneID; 17192; -.
KEGG; mmu:17192; -.
UCSC; uc007gda.1; mouse. [Q9Z2D8-2]
UCSC; uc007gdb.1; mouse. [Q9Z2D8-1]
CTD; 53615; -.
MGI; MGI:1333812; Mbd3.
eggNOG; KOG4161; Eukaryota.
eggNOG; ENOG4111HPQ; LUCA.
GeneTree; ENSGT00410000025376; -.
HOGENOM; HOG000013073; -.
HOVERGEN; HBG052417; -.
InParanoid; Q9Z2D8; -.
KO; K11591; -.
OMA; LMHAVII; -.
OrthoDB; EOG091G0I05; -.
PhylomeDB; Q9Z2D8; -.
TreeFam; TF325032; -.
Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-MMU-8943724; Regulation of PTEN gene transcription.
ChiTaRS; Mbd3; mouse.
PRO; PR:Q9Z2D8; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000035478; -.
CleanEx; MM_MBD3; -.
ExpressionAtlas; Q9Z2D8; baseline and differential.
Genevisible; Q9Z2D8; MM.
GO; GO:0000785; C:chromatin; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0000792; C:heterochromatin; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0016581; C:NuRD complex; IPI:MGI.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB.
GO; GO:0031492; F:nucleosomal DNA binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; ISO:MGI.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0016573; P:histone acetylation; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0006346; P:methylation-dependent chromatin silencing; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0009888; P:tissue development; IMP:MGI.
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.
1: Evidence at protein level;
Alternative splicing; Chromosome; Coiled coil; Complete proteome;
DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 285 Methyl-CpG-binding domain protein 3.
/FTId=PRO_0000096263.
DOMAIN 1 69 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
COILED 221 279 {ECO:0000255}.
COMPBIAS 229 283 Glu-rich.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000250|UniProtKB:O95983}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000250|UniProtKB:O95983}.
CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95983}.
CROSSLNK 90 90 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95983}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:O95983}.
VAR_SEQ 5 36 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011082.
SEQUENCE 285 AA; 32168 MW; E4E57BD48463643F CRC64;
MERKRWECPA LPQGWEREEV PRRSGLSAGH RDVFYYSPSG KKFRSKPQLA RYLGGSMDLS
TFDFRTGKML MNKMNKSRQR VRYDSSNQVK GKPDLNTALP VRQTASIFKQ PVTKITNHPS
NKVKSDPQKA VDQPRQLFWE KKLSGLSAFD IAEELVRTMD LPKGLQGVGP GCTDETLLSA
IASALHTSTL PITGQLSAAV EKNPGVWLNT AQPLCKAFMV TDDDIRKQEE LVQQVRKRLE
EALMADMLAH VEELARDGEA PLDKACAEEE EEEEEEEEEP EPERV


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