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Methyl-CpG-binding protein 2 (MeCp-2 protein) (MeCp2)

 MECP2_MOUSE             Reviewed;         484 AA.
Q9Z2D6; B1AUZ2; B1AUZ3; Q3TYG1;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
18-JUL-2018, entry version 176.
RecName: Full=Methyl-CpG-binding protein 2;
Short=MeCp-2 protein;
Short=MeCp2;
Name=Mecp2;
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] (ISOFORM A).
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 [MRNA] (ISOFORM A).
PubMed=10369871; DOI=10.1093/hmg/8.7.1253;
Coy J.F., Sedlacek Z., Baechner D., Delius H., Poustka A.;
"A complex pattern of evolutionary conservation and alternative
polyadenylation within the long 3'-untranslated region of the methyl-
CpG-binding protein 2 gene (MeCP2) suggests a regulatory role in gene
expression.";
Hum. Mol. Genet. 8:1253-1262(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
Reichwald K., Thiessen J., Wiehe T., Kioschis P., Straetling W.H.,
Rosenthal A., Platzer M.;
"Comparative analysis of the methyl CpG binding protein 2 locus in man
and mouse reveals new untranslated sequences.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
STRAIN=C57BL/6J; TISSUE=Visual cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[7]
INTERACTION WITH FNBP3.
PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
Bedford M.T., Chan D.C., Leder P.;
"FBP WW domains and the Abl SH3 domain bind to a specific class of
proline-rich ligands.";
EMBO J. 16:2376-2383(1997).
[8]
IDENTIFICATION (ISOFORM B), AND SUBCELLULAR LOCATION.
PubMed=15034150; DOI=10.1093/nar/gkh349;
Kriaucionis S., Bird A.;
"The major form of MeCP2 has a novel N-terminus generated by
alternative splicing.";
Nucleic Acids Res. 32:1818-1823(2004).
[9]
PHOSPHORYLATION AT SER-421.
PubMed=17046689; DOI=10.1016/j.neuron.2006.09.037;
Zhou Z., Hong E.J., Cohen S., Zhao W.-N., Ho H.H., Schmidt L.,
Chen W.G., Lin Y., Savner E., Griffith E.C., Hu L., Steen J.A.J.,
Weitz C.J., Greenberg M.E.;
"Brain-specific phosphorylation of MeCP2 regulates activity-dependent
Bdnf transcription, dendritic growth, and spine maturation.";
Neuron 52:255-269(2006).
[10]
INTERACTION WITH ATRX, AND SUBCELLULAR LOCATION.
PubMed=17296936; DOI=10.1073/pnas.0608056104;
Nan X., Hou J., Maclean A., Nasir J., Lafuente M.J., Shu X.,
Kriaucionis S., Bird A.;
"Interaction between chromatin proteins MECP2 and ATRX is disrupted by
mutations that cause inherited mental retardation.";
Proc. Natl. Acad. Sci. U.S.A. 104:2709-2714(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-229 AND SER-424,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[12]
FUNCTION, AND DNA-BINDING.
PubMed=23434322; DOI=10.1016/j.cell.2013.02.004;
Spruijt C.G., Gnerlich F., Smits A.H., Pfaffeneder T., Jansen P.W.,
Bauer C., Munzel M., Wagner M., Muller M., Khan F., Eberl H.C.,
Mensinga A., Brinkman A.B., Lephikov K., Muller U., Walter J.,
Boelens R., van Ingen H., Leonhardt H., Carell T., Vermeulen M.;
"Dynamic readers for 5-(hydroxy)methylcytosine and its oxidized
derivatives.";
Cell 152:1146-1159(2013).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321 AND LYS-447, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[14]
INTERACTION WITH NCOR2, REGION, AND MUTAGENESIS OF THR-158; PRO-302;
LYS-304; LYS-305 AND ARG-306.
PubMed=23770565; DOI=10.1038/nn.3434;
Lyst M.J., Ekiert R., Ebert D.H., Merusi C., Nowak J., Selfridge J.,
Guy J., Kastan N.R., Robinson N.D., de Lima Alves F., Rappsilber J.,
Greenberg M.E., Bird A.;
"Rett syndrome mutations abolish the interaction of MeCP2 with the
NCoR/SMRT co-repressor.";
Nat. Neurosci. 16:898-902(2013).
[15]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-162, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[16] {ECO:0000244|PDB:5NAF}
X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 285-309 IN COMPLEX WITH
TBL1XR1, AND REGION.
PubMed=28348241; DOI=10.1073/pnas.1700731114;
Kruusvee V., Lyst M.J., Taylor C., Tarnauskaite Z., Bird A.P.,
Cook A.G.;
"Structure of the MeCP2-TBLR1 complex reveals a molecular basis for
Rett syndrome and related disorders.";
Proc. Natl. Acad. Sci. U.S.A. 114:E3243-E3250(2017).
-!- FUNCTION: Chromosomal protein that binds to methylated DNA. It can
bind specifically to a single methyl-CpG pair. It is not
influenced by sequences flanking the methyl-CpGs. Mediates
transcriptional repression through interaction with histone
deacetylase and the corepressor SIN3. Binds both 5-methylcytosine
(5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a
preference for 5-methylcytosine (5mC).
{ECO:0000269|PubMed:23434322}.
-!- SUBUNIT: Interacts with FNBP3 (PubMed:9171351). Interacts with
CDKL5 (By similarity). Interacts with ATRX; MECP2 recruits ATRX to
pericentric heterochromatin in neuronal cells (PubMed:17296936).
Interacts with NCOR2 (PubMed:23770565). Interacts with TBL1XR1;
bridges interaction between MECP2 and NCOR1 (PubMed:28348241).
Interacts with TBL1X; recuits TBL1X to the heterochromatin foci
(By similarity). {ECO:0000250|UniProtKB:P51608,
ECO:0000269|PubMed:17296936, ECO:0000269|PubMed:23770565,
ECO:0000269|PubMed:28348241, ECO:0000269|PubMed:9171351}.
-!- INTERACTION:
Q61687:Atrx; NbExp=4; IntAct=EBI-1188816, EBI-2657527;
O88895:Hdac3; NbExp=5; IntAct=EBI-1188816, EBI-302263;
P63158:Hmgb1; NbExp=2; IntAct=EBI-1188816, EBI-6665811;
Q60520:Sin3a; NbExp=4; IntAct=EBI-1188816, EBI-349034;
O35846:Smarca2; NbExp=2; IntAct=EBI-1188816, EBI-371564;
Q9CU62:Smc1a; NbExp=3; IntAct=EBI-1188816, EBI-2550016;
Q9CW03:Smc3; NbExp=3; IntAct=EBI-1188816, EBI-2550068;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15034150,
ECO:0000269|PubMed:17296936}. Note=Colocalized with methyl-CpG in
the genome. Colocalized with TBL1X to the heterochromatin foci.
{ECO:0000250|UniProtKB:P51608}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A; Synonyms=Beta;
IsoId=Q9Z2D6-1; Sequence=Displayed;
Name=B; Synonyms=Alpha;
IsoId=Q9Z2D6-2; Sequence=VSP_022949;
Note=Ten times higher expression levels than isoform A in brain
(at protein level).;
-!- PTM: Phosphorylated on Ser-421 by CaMK2 in brain upon synaptic
activity, which attenuates its repressor activity and seems to
regulate dendritic growth and spine maturation. Does not seem to
be phosphorylated on Ser-421 in other tissues.
{ECO:0000269|PubMed:17046689}.
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EMBL; AF072251; AAC68880.1; -; mRNA.
EMBL; AJ132922; CAB46495.1; -; mRNA.
EMBL; AF121351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF158181; AAF33024.1; -; mRNA.
EMBL; AK158664; BAE34602.1; -; mRNA.
EMBL; AL672002; CAM18741.1; -; Genomic_DNA.
EMBL; AL672002; CAM18742.1; -; Genomic_DNA.
EMBL; BC027153; AAH27153.1; -; mRNA.
CCDS; CCDS41016.1; -. [Q9Z2D6-2]
CCDS; CCDS41017.1; -. [Q9Z2D6-1]
RefSeq; NP_001075448.1; NM_001081979.2. [Q9Z2D6-2]
RefSeq; NP_034918.1; NM_010788.4. [Q9Z2D6-1]
UniGene; Mm.131408; -.
UniGene; Mm.414303; -.
PDB; 5NAF; X-ray; 2.49 A; E/F=285-309.
PDBsum; 5NAF; -.
ProteinModelPortal; Q9Z2D6; -.
SMR; Q9Z2D6; -.
BioGrid; 201380; 10.
CORUM; Q9Z2D6; -.
DIP; DIP-39984N; -.
IntAct; Q9Z2D6; 13.
MINT; Q9Z2D6; -.
STRING; 10090.ENSMUSP00000033770; -.
iPTMnet; Q9Z2D6; -.
PhosphoSitePlus; Q9Z2D6; -.
EPD; Q9Z2D6; -.
PaxDb; Q9Z2D6; -.
PeptideAtlas; Q9Z2D6; -.
PRIDE; Q9Z2D6; -.
Ensembl; ENSMUST00000033770; ENSMUSP00000033770; ENSMUSG00000031393. [Q9Z2D6-2]
Ensembl; ENSMUST00000100750; ENSMUSP00000098314; ENSMUSG00000031393. [Q9Z2D6-1]
Ensembl; ENSMUST00000170481; ENSMUSP00000127115; ENSMUSG00000031393. [Q9Z2D6-1]
GeneID; 17257; -.
KEGG; mmu:17257; -.
UCSC; uc009tnt.3; mouse. [Q9Z2D6-1]
UCSC; uc009tnu.3; mouse. [Q9Z2D6-2]
CTD; 4204; -.
MGI; MGI:99918; Mecp2.
eggNOG; KOG4161; Eukaryota.
eggNOG; ENOG41126JX; LUCA.
GeneTree; ENSGT00530000063687; -.
HOGENOM; HOG000015809; -.
HOVERGEN; HBG052445; -.
InParanoid; Q9Z2D6; -.
KO; K11588; -.
OMA; KMPRAGS; -.
OrthoDB; EOG091G05HO; -.
PhylomeDB; Q9Z2D6; -.
TreeFam; TF332974; -.
PRO; PR:Q9Z2D6; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031393; -.
CleanEx; MM_MECP2; -.
ExpressionAtlas; Q9Z2D6; baseline and differential.
Genevisible; Q9Z2D6; MM.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0000930; C:gamma-tubulin complex; IEA:Ensembl.
GO; GO:0000792; C:heterochromatin; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:MGI.
GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0000400; F:four-way junction DNA binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0008327; F:methyl-CpG binding; IDA:MGI.
GO; GO:0003729; F:mRNA binding; IDA:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0035197; F:siRNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:MGI.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0045322; F:unmethylated CpG binding; ISO:MGI.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0001662; P:behavioral fear response; IMP:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0032048; P:cardiolipin metabolic process; IMP:MGI.
GO; GO:0050432; P:catecholamine secretion; IMP:MGI.
GO; GO:0006576; P:cellular biogenic amine metabolic process; IMP:MGI.
GO; GO:0071317; P:cellular response to isoquinoline alkaloid; ISO:MGI.
GO; GO:0035865; P:cellular response to potassium ion; ISO:MGI.
GO; GO:0021549; P:cerebellum development; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:0006342; P:chromatin silencing; IMP:MGI.
GO; GO:0016358; P:dendrite development; IMP:MGI.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
GO; GO:0008211; P:glucocorticoid metabolic process; IMP:MGI.
GO; GO:0006541; P:glutamine metabolic process; IMP:MGI.
GO; GO:0016573; P:histone acetylation; IMP:MGI.
GO; GO:0016571; P:histone methylation; IMP:MGI.
GO; GO:0006020; P:inositol metabolic process; IMP:MGI.
GO; GO:0007612; P:learning; IMP:MGI.
GO; GO:0007616; P:long-term memory; IMP:MGI.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
GO; GO:0007613; P:memory; IMP:MGI.
GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IMP:MGI.
GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI.
GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:MGI.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
GO; GO:1903860; P:negative regulation of dendrite extension; ISO:MGI.
GO; GO:0061000; P:negative regulation of dendritic spine development; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0035067; P:negative regulation of histone acetylation; IMP:MGI.
GO; GO:0031061; P:negative regulation of histone methylation; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:2000635; P:negative regulation of primary miRNA processing; ISO:MGI.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:2000820; P:negative regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0001976; P:neurological system process involved in regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:0050905; P:neuromuscular process; IMP:MGI.
GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0042551; P:neuron maturation; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IMP:MGI.
GO; GO:0009405; P:pathogenesis; IMP:MGI.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IMP:MGI.
GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; ISO:MGI.
GO; GO:1905492; P:positive regulation of branching morphogenesis of a nerve; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
GO; GO:1905643; P:positive regulation of DNA methylation; ISO:MGI.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:1900114; P:positive regulation of histone H3-K9 trimethylation; IDA:BHF-UCL.
GO; GO:0090063; P:positive regulation of microtubule nucleation; ISO:MGI.
GO; GO:1901956; P:positive regulation of retrograde dense core granule transport; ISO:MGI.
GO; GO:0051965; P:positive regulation of synapse assembly; IMP:MGI.
GO; GO:0031915; P:positive regulation of synaptic plasticity; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0019230; P:proprioception; IMP:MGI.
GO; GO:0008104; P:protein localization; IMP:MGI.
GO; GO:0044030; P:regulation of DNA methylation; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:MGI.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:MGI.
GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IMP:MGI.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
GO; GO:0007585; P:respiratory gaseous exchange; IMP:MGI.
GO; GO:0042220; P:response to cocaine; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; IMP:MGI.
GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
GO; GO:0035176; P:social behavior; IMP:MGI.
GO; GO:0001964; P:startle response; IMP:MGI.
GO; GO:0007416; P:synapse assembly; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0021591; P:ventricular system development; IMP:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR017353; Me_CpG-bd_MeCP2.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
PANTHER; PTHR15074:SF4; PTHR15074:SF4; 1.
Pfam; PF01429; MBD; 1.
PIRSF; PIRSF038006; Methyl_CpG_bd_MeCP2; 1.
SMART; SM00391; MBD; 1.
SUPFAM; SSF54171; SSF54171; 1.
PROSITE; PS50982; MBD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
DNA-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Repressor; Transcription; Transcription regulation.
CHAIN 1 484 Methyl-CpG-binding protein 2.
/FTId=PRO_0000096347.
DOMAIN 90 162 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
DNA_BIND 185 197 A.T hook 1.
DNA_BIND 265 277 A.T hook 2.
REGION 269 309 Interaction with NCOR2.
{ECO:0000269|PubMed:23770565}.
REGION 285 309 Interaction with TBL1XR1.
{ECO:0000269|PubMed:28348241}.
COMPBIAS 366 372 His-rich.
COMPBIAS 379 403 Pro-rich.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:Q00566}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000250|UniProtKB:P51608}.
MOD_RES 162 162 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000250|UniProtKB:P51608}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 321 321 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 421 421 Phosphoserine; by CaMK2.
{ECO:0000269|PubMed:17046689}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 447 447 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
VAR_SEQ 1 9 MVAGMLGLR -> MAAAAATAAAAAAPSGGGGGGEEERL
(in isoform B).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_022949.
MUTAGEN 158 158 T->M: Loss of localization to the
nucleus. Distributes diffusely in cells.
Interacts normally with NCOR2.
{ECO:0000269|PubMed:23770565}.
MUTAGEN 302 302 P->R: Abolishes interaction with NCOR2.
{ECO:0000269|PubMed:23770565}.
MUTAGEN 304 304 K->E: Abolishes interaction with NCOR2.
{ECO:0000269|PubMed:23770565}.
MUTAGEN 305 305 K->R: Abolishes interaction with NCOR2.
{ECO:0000269|PubMed:23770565}.
MUTAGEN 306 306 R->C: Abolishes interaction with NCOR2.
Mice exhibit a severe neurological Rett
syndrome-like phenotype.
{ECO:0000269|PubMed:23770565}.
CONFLICT 328 328 L -> P (in Ref. 4; BAE34602).
{ECO:0000305}.
HELIX 298 300 {ECO:0000244|PDB:5NAF}.
HELIX 303 305 {ECO:0000244|PDB:5NAF}.
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


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