MECP2_MOUSE
ID MECP2_MOUSE Reviewed; 484 AA.
AC Q9Z2D6; B1AUZ2; B1AUZ3; Q3TYG1;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Methyl-CpG-binding protein 2;
DE Short=MeCp-2 protein;
DE Short=MeCp2;
GN Name=Mecp2;
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] (ISOFORM A).
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 [MRNA] (ISOFORM A).
RX PubMed=10369871; DOI=10.1093/hmg/8.7.1253;
RA Coy J.F., Sedlacek Z., Baechner D., Delius H., Poustka A.;
RT "A complex pattern of evolutionary conservation and alternative
RT polyadenylation within the long 3'-untranslated region of the methyl-CpG-
RT binding protein 2 gene (MeCP2) suggests a regulatory role in gene
RT expression.";
RL Hum. Mol. Genet. 8:1253-1262(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RA Reichwald K., Thiessen J., Wiehe T., Kioschis P., Straetling W.H.,
RA Rosenthal A., Platzer M.;
RT "Comparative analysis of the methyl CpG binding protein 2 locus in man and
RT mouse reveals new untranslated sequences.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [7]
RP INTERACTION WITH FNBP3.
RX PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
RA Bedford M.T., Chan D.C., Leder P.;
RT "FBP WW domains and the Abl SH3 domain bind to a specific class of proline-
RT rich ligands.";
RL EMBO J. 16:2376-2383(1997).
RN [8]
RP IDENTIFICATION (ISOFORM B), AND SUBCELLULAR LOCATION.
RX PubMed=15034150; DOI=10.1093/nar/gkh349;
RA Kriaucionis S., Bird A.;
RT "The major form of MeCP2 has a novel N-terminus generated by alternative
RT splicing.";
RL Nucleic Acids Res. 32:1818-1823(2004).
RN [9]
RP PHOSPHORYLATION AT SER-421.
RX PubMed=17046689; DOI=10.1016/j.neuron.2006.09.037;
RA Zhou Z., Hong E.J., Cohen S., Zhao W.-N., Ho H.H., Schmidt L., Chen W.G.,
RA Lin Y., Savner E., Griffith E.C., Hu L., Steen J.A.J., Weitz C.J.,
RA Greenberg M.E.;
RT "Brain-specific phosphorylation of MeCP2 regulates activity-dependent Bdnf
RT transcription, dendritic growth, and spine maturation.";
RL Neuron 52:255-269(2006).
RN [10]
RP INTERACTION WITH ATRX, AND SUBCELLULAR LOCATION.
RX PubMed=17296936; DOI=10.1073/pnas.0608056104;
RA Nan X., Hou J., Maclean A., Nasir J., Lafuente M.J., Shu X.,
RA Kriaucionis S., Bird A.;
RT "Interaction between chromatin proteins MECP2 and ATRX is disrupted by
RT mutations that cause inherited mental retardation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2709-2714(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-229 AND SER-424, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [12]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=23434322; DOI=10.1016/j.cell.2013.02.004;
RA Spruijt C.G., Gnerlich F., Smits A.H., Pfaffeneder T., Jansen P.W.,
RA Bauer C., Munzel M., Wagner M., Muller M., Khan F., Eberl H.C.,
RA Mensinga A., Brinkman A.B., Lephikov K., Muller U., Walter J., Boelens R.,
RA van Ingen H., Leonhardt H., Carell T., Vermeulen M.;
RT "Dynamic readers for 5-(hydroxy)methylcytosine and its oxidized
RT derivatives.";
RL Cell 152:1146-1159(2013).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321 AND LYS-447, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [14]
RP INTERACTION WITH NCOR2, REGION, AND MUTAGENESIS OF THR-158; PRO-302;
RP LYS-304; LYS-305 AND ARG-306.
RX PubMed=23770565; DOI=10.1038/nn.3434;
RA Lyst M.J., Ekiert R., Ebert D.H., Merusi C., Nowak J., Selfridge J.,
RA Guy J., Kastan N.R., Robinson N.D., de Lima Alves F., Rappsilber J.,
RA Greenberg M.E., Bird A.;
RT "Rett syndrome mutations abolish the interaction of MeCP2 with the
RT NCoR/SMRT co-repressor.";
RL Nat. Neurosci. 16:898-902(2013).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-162, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16] {ECO:0007744|PDB:5NAF}
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 285-309 IN COMPLEX WITH TBL1XR1,
RP AND REGION.
RX PubMed=28348241; DOI=10.1073/pnas.1700731114;
RA Kruusvee V., Lyst M.J., Taylor C., Tarnauskaite Z., Bird A.P., Cook A.G.;
RT "Structure of the MeCP2-TBLR1 complex reveals a molecular basis for Rett
RT syndrome and related disorders.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E3243-E3250(2017).
CC -!- FUNCTION: Chromosomal protein that binds to methylated DNA. It can bind
CC specifically to a single methyl-CpG pair. It is not influenced by
CC sequences flanking the methyl-CpGs. Mediates transcriptional repression
CC through interaction with histone deacetylase and the corepressor SIN3.
CC Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-
CC containing DNA, with a preference for 5-methylcytosine (5mC).
CC {ECO:0000269|PubMed:23434322}.
CC -!- SUBUNIT: Interacts with FNBP3 (PubMed:9171351). Interacts with CDKL5
CC (By similarity). Interacts with ATRX; MECP2 recruits ATRX to
CC pericentric heterochromatin in neuronal cells (PubMed:17296936).
CC Interacts with NCOR2 (PubMed:23770565). Interacts with TBL1XR1; bridges
CC interaction between MECP2 and NCOR1 (PubMed:28348241). Interacts with
CC TBL1X; recruits TBL1X to the heterochromatin foci (By similarity).
CC {ECO:0000250|UniProtKB:P51608, ECO:0000269|PubMed:17296936,
CC ECO:0000269|PubMed:23770565, ECO:0000269|PubMed:28348241,
CC ECO:0000269|PubMed:9171351}.
CC -!- INTERACTION:
CC Q9Z2D6; Q61687: Atrx; NbExp=5; IntAct=EBI-1188816, EBI-2657527;
CC Q9Z2D6; Q9Z1T5: Deaf1; NbExp=2; IntAct=EBI-1188816, EBI-2364863;
CC Q9Z2D6; O88895: Hdac3; NbExp=5; IntAct=EBI-1188816, EBI-302263;
CC Q9Z2D6; Q60520: Sin3a; NbExp=5; IntAct=EBI-1188816, EBI-349034;
CC Q9Z2D6; O35846: Smarca2; NbExp=2; IntAct=EBI-1188816, EBI-371564;
CC Q9Z2D6; Q3TKT4: Smarca4; NbExp=2; IntAct=EBI-1188816, EBI-1210244;
CC Q9Z2D6; Q9CU62: Smc1a; NbExp=3; IntAct=EBI-1188816, EBI-2550016;
CC Q9Z2D6; Q9CW03: Smc3; NbExp=3; IntAct=EBI-1188816, EBI-2550068;
CC Q9Z2D6; O70494: Sp3; NbExp=2; IntAct=EBI-1188816, EBI-643514;
CC Q9Z2D6-1; Q60987: Foxg1; NbExp=4; IntAct=EBI-26609102, EBI-11166131;
CC Q9Z2D6-2; Q60987: Foxg1; NbExp=2; IntAct=EBI-26609115, EBI-11166131;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15034150,
CC ECO:0000269|PubMed:17296936}. Note=Colocalized with methyl-CpG in the
CC genome. Colocalized with TBL1X to the heterochromatin foci.
CC {ECO:0000250|UniProtKB:P51608}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=Beta;
CC IsoId=Q9Z2D6-1; Sequence=Displayed;
CC Name=B; Synonyms=Alpha;
CC IsoId=Q9Z2D6-2; Sequence=VSP_022949;
CC -!- PTM: Phosphorylated on Ser-421 by CaMK2 in brain upon synaptic
CC activity, which attenuates its repressor activity and seems to regulate
CC dendritic growth and spine maturation. Does not seem to be
CC phosphorylated on Ser-421 in other tissues.
CC {ECO:0000269|PubMed:17046689}.
CC -!- MISCELLANEOUS: [Isoform B]: Ten times higher expression levels than
CC isoform A in brain (at protein level). {ECO:0000305}.
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DR EMBL; AF072251; AAC68880.1; -; mRNA.
DR EMBL; AJ132922; CAB46495.1; -; mRNA.
DR EMBL; AF121351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF158181; AAF33024.1; -; mRNA.
DR EMBL; AK158664; BAE34602.1; -; mRNA.
DR EMBL; AL672002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027153; AAH27153.1; -; mRNA.
DR CCDS; CCDS41016.1; -. [Q9Z2D6-2]
DR CCDS; CCDS41017.1; -. [Q9Z2D6-1]
DR RefSeq; NP_001075448.1; NM_001081979.2. [Q9Z2D6-2]
DR RefSeq; NP_034918.1; NM_010788.4. [Q9Z2D6-1]
DR PDB; 5NAF; X-ray; 2.49 A; E/F=285-309.
DR PDBsum; 5NAF; -.
DR AlphaFoldDB; Q9Z2D6; -.
DR BMRB; Q9Z2D6; -.
DR SMR; Q9Z2D6; -.
DR BioGRID; 201380; 56.
DR CORUM; Q9Z2D6; -.
DR DIP; DIP-39984N; -.
DR IntAct; Q9Z2D6; 45.
DR MINT; Q9Z2D6; -.
DR STRING; 10090.ENSMUSP00000033770; -.
DR iPTMnet; Q9Z2D6; -.
DR PhosphoSitePlus; Q9Z2D6; -.
DR SwissPalm; Q9Z2D6; -.
DR EPD; Q9Z2D6; -.
DR jPOST; Q9Z2D6; -.
DR MaxQB; Q9Z2D6; -.
DR PaxDb; Q9Z2D6; -.
DR PeptideAtlas; Q9Z2D6; -.
DR PRIDE; Q9Z2D6; -.
DR ProteomicsDB; 295723; -. [Q9Z2D6-1]
DR ProteomicsDB; 295724; -. [Q9Z2D6-2]
DR ABCD; Q9Z2D6; 1 sequenced antibody.
DR Antibodypedia; 394; 875 antibodies from 48 providers.
DR DNASU; 17257; -.
DR Ensembl; ENSMUST00000033770; ENSMUSP00000033770; ENSMUSG00000031393. [Q9Z2D6-2]
DR Ensembl; ENSMUST00000100750; ENSMUSP00000098314; ENSMUSG00000031393. [Q9Z2D6-1]
DR Ensembl; ENSMUST00000170481; ENSMUSP00000127115; ENSMUSG00000031393. [Q9Z2D6-1]
DR GeneID; 17257; -.
DR KEGG; mmu:17257; -.
DR UCSC; uc009tnt.3; mouse. [Q9Z2D6-1]
DR UCSC; uc009tnu.3; mouse. [Q9Z2D6-2]
DR CTD; 4204; -.
DR MGI; MGI:99918; Mecp2.
DR VEuPathDB; HostDB:ENSMUSG00000031393; -.
DR eggNOG; KOG4161; Eukaryota.
DR GeneTree; ENSGT00530000063687; -.
DR HOGENOM; CLU_045066_0_0_1; -.
DR InParanoid; Q9Z2D6; -.
DR OMA; YDVYLIX; -.
DR OrthoDB; 1431783at2759; -.
DR PhylomeDB; Q9Z2D6; -.
DR TreeFam; TF332974; -.
DR Reactome; R-MMU-9022692; Regulation of MECP2 expression and activity. [Q9Z2D6-1]
DR BioGRID-ORCS; 17257; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Mecp2; mouse.
DR PRO; PR:Q9Z2D6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z2D6; protein.
DR Bgee; ENSMUSG00000031393; Expressed in substantia nigra and 291 other tissues.
DR ExpressionAtlas; Q9Z2D6; baseline and differential.
DR Genevisible; Q9Z2D6; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
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:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0035197; F:siRNA binding; IDA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:BHF-UCL.
DR GO; GO:0045322; F:unmethylated CpG binding; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0032048; P:cardiolipin metabolic process; IMP:MGI.
DR GO; GO:0050432; P:catecholamine secretion; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006576; P:cellular biogenic amine metabolic process; IMP:MGI.
DR GO; GO:0071317; P:cellular response to isoquinoline alkaloid; ISO:MGI.
DR GO; GO:0035865; P:cellular response to potassium ion; ISO:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0014009; P:glial cell proliferation; IMP:MGI.
DR GO; GO:0008211; P:glucocorticoid metabolic process; IMP:MGI.
DR GO; GO:0006541; P:glutamine metabolic process; IMP:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:MGI.
DR GO; GO:0016573; P:histone acetylation; IMP:MGI.
DR GO; GO:0016571; P:histone methylation; IMP:MGI.
DR GO; GO:0006020; P:inositol metabolic process; IMP:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007616; P:long-term memory; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:MGI.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:1903860; P:negative regulation of dendrite extension; ISO:MGI.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:2000635; P:negative regulation of primary miRNA processing; ISO:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:1903941; P:negative regulation of respiratory gaseous exchange; ISO:MGI.
DR GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:2000820; P:negative regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0001976; P:nervous system process involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IDA:MGI.
DR GO; GO:0042551; P:neuron maturation; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IMP:MGI.
DR GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; ISO:MGI.
DR GO; GO:1905492; P:positive regulation of branching morphogenesis of a nerve; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:1905643; P:positive regulation of DNA methylation; ISO:MGI.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:MGI.
DR GO; GO:1900114; P:positive regulation of histone H3-K9 trimethylation; IDA:BHF-UCL.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; ISO:MGI.
DR GO; GO:1901956; P:positive regulation of retrograde dense core granule transport; ISO:MGI.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0019230; P:proprioception; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0099611; P:regulation of action potential firing threshold; ISO:MGI.
DR GO; GO:0044030; P:regulation of DNA methylation; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:MGI.
DR GO; GO:0051570; P:regulation of histone H3-K9 methylation; IMP:MGI.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IMP:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IMP:MGI.
DR GO; GO:0042220; P:response to cocaine; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0051707; P:response to other organism; IMP:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR GO; GO:0001964; P:startle response; IMP:MGI.
DR GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR GO; GO:0099191; P:trans-synaptic signaling by BDNF; IMP:MGI.
DR GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR017353; Me_CpG-bd_MeCP2.
DR InterPro; IPR045138; MeCP2/MBD4.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR PANTHER; PTHR15074; PTHR15074; 1.
DR Pfam; PF01429; MBD; 1.
DR PIRSF; PIRSF038006; Methyl_CpG_bd_MeCP2; 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; Acetylation; Alternative splicing; DNA-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..484
FT /note="Methyl-CpG-binding protein 2"
FT /id="PRO_0000096347"
FT DOMAIN 90..162
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT DNA_BIND 185..197
FT /note="A.T hook 1"
FT DNA_BIND 265..277
FT /note="A.T hook 2"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..309
FT /note="Interaction with NCOR2"
FT /evidence="ECO:0000269|PubMed:23770565"
FT REGION 285..309
FT /note="Interaction with TBL1XR1"
FT /evidence="ECO:0000269|PubMed:28348241"
FT REGION 319..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00566"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51608"
FT MOD_RES 162
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51608"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 421
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000269|PubMed:17046689"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 447
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..9
FT /note="MVAGMLGLR -> MAAAAATAAAAAAPSGGGGGGEEERL (in isoform
FT B)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022949"
FT MUTAGEN 158
FT /note="T->M: Loss of localization to the nucleus.
FT Distributes diffusely in cells. Interacts normally with
FT NCOR2."
FT /evidence="ECO:0000269|PubMed:23770565"
FT MUTAGEN 302
FT /note="P->R: Abolishes interaction with NCOR2."
FT /evidence="ECO:0000269|PubMed:23770565"
FT MUTAGEN 304
FT /note="K->E: Abolishes interaction with NCOR2."
FT /evidence="ECO:0000269|PubMed:23770565"
FT MUTAGEN 305
FT /note="K->R: Abolishes interaction with NCOR2."
FT /evidence="ECO:0000269|PubMed:23770565"
FT MUTAGEN 306
FT /note="R->C: Abolishes interaction with NCOR2. Mice exhibit
FT a severe neurological Rett syndrome-like phenotype."
FT /evidence="ECO:0000269|PubMed:23770565"
FT CONFLICT 328
FT /note="L -> P (in Ref. 4; BAE34602)"
FT /evidence="ECO:0000305"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5NAF"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:5NAF"
SQ SEQUENCE 484 AA; 52307 MW; 62FD228F0118A49F CRC64;
MVAGMLGLRE EKSEDQDLQG LRDKPLKFKK AKKDKKEDKE GKHEPLQPSA HHSAEPAEAG
KAETSESSGS APAVPEASAS PKQRRSIIRD RGPMYDDPTL PEGWTRKLKQ RKSGRSAGKY
DVYLINPQGK AFRSKVELIA YFEKVGDTSL DPNDFDFTVT GRGSPSRREQ KPPKKPKSPK
APGTGRGRGR PKGSGTGRPK AAASEGVQVK RVLEKSPGKL VVKMPFQASP GGKGEGGGAT
TSAQVMVIKR PGRKRKAEAD PQAIPKKRGR KPGSVVAAAA AEAKKKAVKE SSIRSVHETV
LPIKKRKTRE TVSIEVKEVV KPLLVSTLGE KSGKGLKTCK SPGRKSKESS PKGRSSSASS
PPKKEHHHHH HHSESTKAPM PLLPSPPPPE PESSEDPISP PEPQDLSSSI CKEEKMPRGG
SLESDGCPKE PAKTQPMVAT TTTVAEKYKH RGEGERKDIV SSSMPRPNRE EPVDSRTPVT
ERVS
