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

 MECP2_HUMAN             Reviewed;         486 AA.
P51608; O15233; Q6QHH9; Q7Z384;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 210.
RecName: Full=Methyl-CpG-binding protein 2;
Short=MeCp-2 protein;
Short=MeCp2;
Name=MECP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=9710633; DOI=10.1128/MCB.18.9.5492;
Kudo S.;
"Methyl-CpG-binding protein MeCP2 represses Sp1-activated
transcription of the human leukosialin gene when the promoter is
methylated.";
Mol. Cell. Biol. 18:5492-5499(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=8976388;
Vilain A., Apiou F., Vogt N., Dutrillaux B., Malfoy B.;
"Assignment of the gene for methyl-CpG-binding protein 2 (MECP2) to
human chromosome band Xq28 by in situ hybridization.";
Cytogenet. Cell Genet. 74:293-294(1996).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=10723722; DOI=10.1007/s003350010035;
Reichwald K., Thiesen J., Wiehe T., Weitzel J., Poustka W.A.,
Rosenthal A., Platzer M., Stratling W.H., Kioschis P.;
"Comparative sequence analysis of the MECP2-locus in human and mouse
reveals new transcribed regions.";
Mamm. Genome 11:182-190(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND INVOLVEMENT IN RTT.
PubMed=15034579; DOI=10.1038/ng1327;
Mnatzakanian G.N., Lohi H., Munteanu I., Alfred S.E., Yamada T.,
MacLeod P.J.M., Jones J.R., Scherer S.W., Schanen N.C., Friez M.J.,
Vincent J.B., Minassian B.A.;
"A previously unidentified MECP2 open reading frame defines a new
protein isoform relevant to Rett syndrome.";
Nat. Genet. 36:339-341(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Placenta;
Straetling W.H.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Colon endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Placenta;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-486 (ISOFORM A).
TISSUE=Skeletal muscle;
PubMed=8672133; DOI=10.1007/s003359900157;
D'Esposito M., Quaderi N.A., Ciccodicola A., Bruni P., Esposito T.,
D'Urso M., Brown S.D.M.;
"Isolation, physical mapping, and Northern analysis of the X-linked
human gene encoding methyl CpG-binding protein, MECP2.";
Mamm. Genome 7:533-535(1996).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-486 (ISOFORM A).
Reichwald K., Bauer D., Brenner V., Drescher B., Coy J.F.,
Kioschis P., Korn B., Nyakatura G., Platzer M., Poustka A.,
Sandoval N., Rosenthal A.;
"Genetic organization of human methyl-CpG-binding protein 2.";
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[12]
IDENTIFICATION (ISOFORM B).
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).
[13]
REVIEW ON VARIANTS.
PubMed=12872250; DOI=10.1002/humu.10243;
Miltenberger-Miltenyi G., Laccone F.;
"Mutations and polymorphisms in the human methyl CpG-binding protein
MECP2.";
Hum. Mutat. 22:107-115(2003).
[14]
INTERACTION WITH CDKL5.
PubMed=15917271; DOI=10.1093/hmg/ddi198;
Mari F., Azimonti S., Bertani I., Bolognese F., Colombo E.,
Caselli R., Scala E., Longo I., Grosso S., Pescucci C., Ariani F.,
Hayek G., Balestri P., Bergo A., Badaracco G., Zappella M.,
Broccoli V., Renieri A., Kilstrup-Nielsen C., Landsberger N.;
"CDKL5 belongs to the same molecular pathway of MeCP2 and it is
responsible for the early-onset seizure variant of Rett syndrome.";
Hum. Mol. Genet. 14:1935-1946(2005).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-116 AND SER-426,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-216, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-229, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
STRUCTURE BY NMR OF 77-166.
PubMed=10518942; DOI=10.1006/jmbi.1999.3023;
Wakefield R.I., Smith B.O., Nan X., Free A., Soteriou A., Uhrin D.,
Bird A.P., Barlow P.N.;
"The solution structure of the domain from MeCP2 that binds to
methylated DNA.";
J. Mol. Biol. 291:1055-1065(1999).
[26]
VARIANTS RTT TRP-106; CYS-133; SER-155; MET-158 AND CYS-306, AND
VARIANT LYS-397.
PubMed=10577905; DOI=10.1086/302690;
Wan M., Lee S.S.J., Zhang X., Houwink-Manville I., Song H.-R.,
Amir R.E., Budden S., Naidu S., Pereira J.L.P., Lo I.F.M.,
Zoghbi H.Y., Schanen N.C., Francke U.;
"Rett syndrome and beyond: recurrent spontaneous and familial MECP2
mutations at CpG hotspots.";
Am. J. Hum. Genet. 65:1520-1529(1999).
[27]
VARIANTS RTT TRP-106; CYS-133; SER-155 AND MET-158.
PubMed=10508514; DOI=10.1038/13810;
Amir R.E., Van den Veyver I.B., Wan M., Tran C.Q., Francke U.,
Zoghbi H.Y.;
"Rett syndrome is caused by mutations in X-linked MECP2, encoding
methyl-CpG-binding protein 2.";
Nat. Genet. 23:185-188(1999).
[28]
INVOLVEMENT IN MRXS13.
PubMed=10986043; DOI=10.1086/303078;
Meloni I., Bruttini M., Longo I., Mari F., Rizzolio F., D'Adamo P.,
Denvriendt K., Fryns J.-P., Toniolo D., Renieri A.;
"A mutation in the Rett syndrome gene, MECP2, causes X-linked mental
retardation and progressive spasticity in males.";
Am. J. Hum. Genet. 67:982-985(2000).
[29]
VARIANTS RTT VAL-100; GLN-106; TRP-106; CYS-133; ARG-152; SER-155;
MET-158; ARG-305; CYS-306 AND HIS-306, AND VARIANTS CYS-86; MET-203;
PRO-287; ALA-291; LYS-397; ILE-412 AND THR-444.
PubMed=11055898; DOI=10.1086/316913;
Buyse I.M., Fang P., Hoon K.T., Amir R.E., Zoghbi H.Y., Roa B.B.;
"Diagnostic testing for Rett syndrome by DHPLC and direct sequencing
analysis of the MECP2 gene: identification of several novel mutations
and polymorphisms.";
Am. J. Hum. Genet. 67:1428-1436(2000).
[30]
VARIANT MRXS13 VAL-140, AND VARIANT MET-203.
PubMed=11007980; DOI=10.1016/S0014-5793(00)01994-3;
Orrico A., Lam C., Galli L., Dotti M.T., Hayek G., Tong S.F.,
Poon P.M., Zappella M., Federico A., Sorrentino V.;
"MECP2 mutation in male patients with non-specific X-linked mental
retardation.";
FEBS Lett. 481:285-288(2000).
[31]
VARIANTS RTT LEU-101; HIS-101; THR-101; TRP-106; CYS-133; CYS-134;
ARG-152; MET-158; ARG-225; LEU-302; CYS-306 AND HIS-306, AND VARIANTS
LEU-229 AND THR-439.
PubMed=10767337; DOI=10.1093/hmg/9.7.1119;
Cheadle J.P., Gill H., Fleming N., Maynard J., Kerr A., Leonard H.,
Krawczak M., Cooper D.N., Lynch S., Thomas N., Hughes H., Hulten M.,
Ravine D., Sampson J.R., Clarke A.;
"Long-read sequence analysis of the MECP2 gene in Rett syndrome
patients: correlation of disease severity with mutation type and
location.";
Hum. Mol. Genet. 9:1119-1129(2000).
[32]
VARIANTS RTT GLN-106; MET-158; ARG-302; CYS-306 AND ALA-322.
PubMed=10814719; DOI=10.1093/hmg/9.9.1377;
Bienvenu T., Carrie A., de Roux N., Vinet M.-C., Jonveaux P.,
Couvert P., Villard L., Arzimanoglou A., Beldjord C., Fontes M.,
Tardieu M., Chelly J.;
"MECP2 mutations account for most cases of typical forms of Rett
syndrome.";
Hum. Mol. Genet. 9:1377-1384(2000).
[33]
VARIANTS RTT MET-158; HIS-302 AND CYS-306, AND VARIANTS VAL-201;
ALA-232; LEU-251 AND SER-376.
PubMed=10944854; DOI=10.1007/s100380070032;
Amano K., Nomura Y., Segawa M., Yamakawa K.;
"Mutational analysis of the MECP2 gene in Japanese patients with Rett
syndrome.";
J. Hum. Genet. 45:231-236(2000).
[34]
VARIANTS RTT GLU-97; TRP-106; CYS-133; ILE-155; MET-158 AND CYS-306.
PubMed=10745042; DOI=10.1136/jmg.37.4.250;
Xiang F., Buervenich S., Nicolao P., Bailey M.E., Zhang Z., Anvret M.;
"Mutation screening in Rett syndrome patients.";
J. Med. Genet. 37:250-255(2000).
[35]
VARIANTS RTT TRP-106; PHE-124; CYS-133; CYS-134; ARG-152; MET-158 AND
CYS-306.
PubMed=10991688; DOI=10.1136/jmg.37.8.608;
Obata K., Matsuishi T., Yamashita Y., Fukuda T., Kuwajima K.,
Horiuchi I., Nagamitsu S., Iwanaga R., Kimura A., Omori I., Endo S.,
Mori K., Kondo I.;
"Mutation analysis of the methyl-CpG binding protein 2 gene (MECP2) in
patients with Rett syndrome.";
J. Med. Genet. 37:608-610(2000).
[36]
VARIANTS RTT ARG-101; TRP-106; MET-158 AND CYS-306, AND VARIANT
LYS-397.
PubMed=10991689; DOI=10.1136/jmg.37.8.610;
Hampson K., Woods C.G., Latif F., Webb T.;
"Mutations in the MECP2 gene in a cohort of girls with Rett
syndrome.";
J. Med. Genet. 37:610-612(2000).
[37]
VARIANT RTT HIS-133.
PubMed=11706982; DOI=10.1002/ana.1272;
Armstrong J., Poo P., Pineda M., Aibar E., Gean E., Catala V.,
Monros E.;
"Classic Rett syndrome in a boy as a result of somatic mosaicism for a
MECP2 mutation.";
Ann. Neurol. 50:692-692(2001).
[38]
VARIANTS RTT ASP-120; CYS-133; MET-158 AND CYS-306.
PubMed=11376998; DOI=10.1016/S0387-7604(01)00197-8;
Inui K., Akagi M., Ono J., Tsukamoto H., Shimono K., Mano T., Imai K.,
Yamada M., Muramatsu T., Sakai N., Okada S.;
"Mutational analysis of MECP2 in Japanese patients with atypical Rett
syndrome.";
Brain Dev. 23:212-215(2001).
[39]
VARIANTS RTT TRP-106; CYS-134; ARG-152; MET-158; ALA-302; CYS-306 AND
ALA-322, AND VARIANTS VAL-201 AND LYS-397.
PubMed=11738883; DOI=10.1016/S0387-7604(01)00342-4;
Giunti L., Pelagatti S., Lazzerini V., Guarducci S., Lapi E.,
Coviello S., Cecconi A., Ombroni L., Andreucci E., Sani I.,
Brusaferri A., Lasagni A., Ricotti G., Giometto B., Nicolao P.,
Gasparini P., Granatiero M., Giovannucci Uzielli M.L.;
"Spectrum and distribution of MECP2 mutations in 64 Italian Rett
syndrome girls: tentative genotype/phenotype correlation.";
Brain Dev. 23:S242-S245(2001).
[40]
VARIANTS MRXS13 GLY-137; VAL-140; TRP-167; GLU-284; LEU-399 AND
GLN-453.
PubMed=11309367; DOI=10.1093/hmg/10.9.941;
Couvert P., Bienvenu T., Aquaviva C., Poirier K., Moraine C.,
Gendrot C., Verloes A., Andres C., Le Fevre A.C., Souville I.,
Steffann J., des Portes V., Ropers H.-H., Yntema H.G., Fryns J.-P.,
Briault S., Chelly J., Cherif B.;
"MECP2 is highly mutated in X-linked mental retardation.";
Hum. Mol. Genet. 10:941-946(2001).
[41]
VARIANTS RTT TRP-106; GLY-111; CYS-133; GLU-135; ARG-152; GLY-156;
MET-158; ILE-210; ARG-302 AND CYS-306.
PubMed=11241840; DOI=10.1002/humu.3;
Laccone F., Huppke P., Hanefeld F., Meins M.;
"Mutation spectrum in patients with Rett syndrome in the German
population: evidence of hot spot regions.";
Hum. Mutat. 17:183-190(2001).
[42]
VARIANT RTT ARG-101, AND INVOLVEMENT IN AS.
PubMed=11283202; DOI=10.1136/jmg.38.4.224;
Watson P., Black G., Ramsden S., Barrow M., Super M., Kerr B.,
Clayton-Smith J.;
"Angelman syndrome phenotype associated with mutations in MECP2, a
gene encoding a methyl CpG binding protein.";
J. Med. Genet. 38:224-228(2001).
[43]
VARIANT ENS-MECP2 SER-428.
PubMed=11238684; DOI=10.1136/jmg.38.3.171;
Imessaoudene B., Bonnefont J.-P., Royer G., Cormier-Daire V.,
Lyonnet S., Lyon G., Munnich A., Amiel J.;
"MECP2 mutation in non-fatal, non-progressive encephalopathy in a
male.";
J. Med. Genet. 38:171-174(2001).
[44]
VARIANTS RTT SER-101; TRP-106; CYS-133; CYS-134; ARG-152; ALA-158 AND
MET-158.
PubMed=11269512; DOI=10.1007/s001090000155;
Vacca M., Filippini F., Budillon A., Rossi V., Mercadante G.,
Manzati E., Gualandi F., Bigoni S., Trabanelli C., Pini G.,
Calzolari E., Ferlini A., Meloni I., Hayek G., Zappella M.,
Renieri A., D'Urso M., D'Esposito M., MacDonald F., Kerr A.,
Dhanjal S., Hulten M.;
"Mutation analysis of the MECP2 gene in British and Italian Rett
syndrome females.";
J. Mol. Med. 78:648-655(2001).
[45]
VARIANTS RTT TYR-97; TRP-106; HIS-133; CYS-133; ARG-152; MET-158;
ARG-305; CYS-306 AND LEU-322, AND VARIANT MET-197.
PubMed=11402105; DOI=10.1212/WNL.56.11.1486;
Hoffbuhr K., Devaney J.M., LaFleur B., Sirianni N., Scacheri C.,
Giron J., Schuette J., Innis J., Marino M., Philippart M.,
Narayanan V., Umansky R., Kronn D., Hoffman E.P., Naidu S.;
"MeCP2 mutations in children with and without the phenotype of Rett
syndrome.";
Neurology 56:1486-1495(2001).
[46]
VARIANT MRXS13 VAL-140.
PubMed=11885030; DOI=10.1086/339553;
Klauck S.M., Lindsay S., Beyer K.S., Splitt M., Burn J., Poustka A.;
"A mutation hot spot for nonspecific X-linked mental retardation in
the MECP2 gene causes the PPM-X syndrome.";
Am. J. Hum. Genet. 70:1034-1037(2002).
[47]
VARIANTS PRO-359 AND LYS-397.
PubMed=11896461; DOI=10.1038/sj.ejhg.5200761;
Moncla A., Kpebe A., Missirian C., Mancini J., Villard L.;
"Polymorphisms in the C-terminal domain of MECP2 in mentally
handicapped boys: implications for genetic counselling.";
Eur. J. Hum. Genet. 10:86-89(2002).
[48]
VARIANTS SER-196; SER-228; LYS-394 AND SER-480.
PubMed=12111644; DOI=10.1038/sj.ejhg.5200836;
Yntema H.G., Kleefstra T., Oudakker A.R., Romein T., de Vries B.B.A.,
Nillesen W., Sistermans E.A., Brunner H.G., Hamel B.C.J.,
van Bokhoven H.;
"Low frequency of MECP2 mutations in mentally retarded males.";
Eur. J. Hum. Genet. 10:487-490(2002).
[49]
VARIANTS VAL-181; SER-376; PRO-388 DEL AND LEU-402.
PubMed=12384770; DOI=10.1007/s00439-002-0786-3;
Beyer K.S., Blasi F., Bacchelli E., Klauck S.M., Maestrini E.,
Poustka A.;
"Mutation analysis of the coding sequence of the MECP2 gene in
infantile autism.";
Hum. Genet. 111:305-309(2002).
[50]
VARIANT MRXS13 VAL-140.
PubMed=12325019; DOI=10.1002/humu.10130;
Winnepenninckx B., Errijgers V., Hayez-Delatte F., Reyniers E.,
Kooy R.F.;
"Identification of a family with nonspecific mental retardation
(MRX79) with the A140V mutation in the MECP2 gene: is there a need for
routine screening?";
Hum. Mutat. 20:249-252(2002).
[51]
VARIANT MRXS13 VAL-140, VARIANT RTT TRP-344, VARIANTS MET-197;
SER-376; LEU-399 AND SER-428, AND DISCUSSION OF PATHOGENIC ROLE.
PubMed=12161600; DOI=10.1136/jmg.39.8.586;
Laccone F., Zoll B., Huppke P., Hanefeld F., Pepinski W., Trappe R.;
"MECP2 gene nucleotide changes and their pathogenicity in males:
proceed with caution.";
J. Med. Genet. 39:586-588(2002).
[52]
VARIANT MRXS13 VAL-140.
PubMed=11805248; DOI=10.1212/WNL.58.2.226;
Dotti M.T., Orrico A., De Stefano N., Battisti C., Sicurelli F.,
Severi S., Lam C.-W., Galli L., Sorrentino V., Federico A.;
"A Rett syndrome MECP2 mutation that causes mental retardation in
men.";
Neurology 58:226-230(2002).
[53]
VARIANTS RTT CYS-133; MET-158 AND CYS-306, AND VARIANTS SER-376 AND
SER-388.
PubMed=12567420; DOI=10.1002/ajmg.a.10898;
Conforti F.L., Mazzei R., Magariello A., Patitucci A.L.,
Gabriele A.L., Muglia M., Quattrone A., Fiumara A., Pavone L.,
Barone R., Nistico R., Mangone L.;
"Mutation analysis of the MECP2 gene in patients with Rett syndrome.";
Am. J. Med. Genet. A 117:184-187(2003).
[54]
VARIANT RTT VAL-100.
PubMed=12966522; DOI=10.1002/ajmg.a.20320;
Hammer S., Dorrani N., Hartiala J., Stein S., Schanen N.C.;
"Rett syndrome in a 47,XXX patient with a de novo MECP2 mutation.";
Am. J. Med. Genet. A 122:223-226(2003).
[55]
VARIANTS RTT GLN-10; PRO-128; CYS-133; ARG-152; MET-158 AND CYS-306.
PubMed=12966523; DOI=10.1002/ajmg.a.20321;
Smeets E., Schollen E., Moog U., Matthijs G., Herbergs J., Smeets H.,
Curfs L., Schrander-Stumpel C., Fryns J.-P.;
"Rett syndrome in adolescent and adult females: clinical and molecular
genetic findings.";
Am. J. Med. Genet. A 122:227-233(2003).
[56]
VARIANT MRXS13 LEU-225.
PubMed=12615169; DOI=10.1016/S1090-3798(02)00134-4;
Moog U., Smeets E.E.J., van Roozendaal K.E.P., Schoenmakers S.,
Herbergs J., Schoonbrood-Lenssen A.M.J., Schrander-Stumpel C.T.R.M.;
"Neurodevelopmental disorders in males related to the gene causing
Rett syndrome in females (MECP2).";
Eur. J. Paediatr. Neurol. 7:5-12(2003).
[57]
INVOLVEMENT IN AUTSX3.
PubMed=12770674; DOI=10.1016/S0887-8994(02)00624-0;
Carney R.M., Wolpert C.M., Ravan S.A., Shahbazian M., Ashley-Koch A.,
Cuccaro M.L., Vance J.M., Pericak-Vance M.A.;
"Identification of MeCP2 mutations in a series of females with
autistic disorder.";
Pediatr. Neurol. 28:205-211(2003).
[58]
VARIANTS RTT ARG-100; VAL-100; TRP-106; CYS-133; ARG-152; ALA-158;
MET-158; VAL-161; CYS-306 AND HIS-306.
PubMed=15057977; DOI=10.1002/ajmg.a.20571;
Schanen C., Houwink E.J.F., Dorrani N., Lane J., Everett R., Feng A.,
Cantor R.M., Percy A.;
"Phenotypic manifestations of MECP2 mutations in classical and
atypical Rett syndrome.";
Am. J. Med. Genet. A 126:129-140(2004).
[59]
INVOLVEMENT IN MRXSL.
PubMed=16080119; DOI=10.1086/444549;
Van Esch H., Bauters M., Ignatius J., Jansen M., Raynaud M.,
Hollanders K., Lugtenberg D., Bienvenu T., Jensen L.R., Gecz J.,
Moraine C., Marynen P., Fryns J.-P., Froyen G.;
"Duplication of the MECP2 region is a frequent cause of severe mental
retardation and progressive neurological symptoms in males.";
Am. J. Hum. Genet. 77:442-453(2005).
[60]
VARIANT MRXS13 SER-322.
PubMed=16966553; DOI=10.1212/01.wnl.0000233990.87889.15;
Ventura P., Galluzzi R., Bacca S.M., Giorda R., Massagli A.;
"A novel familial MECP2 mutation in a young boy: clinical and
molecular findings.";
Neurology 67:867-868(2006).
[61]
CHARACTERIZATION OF VARIANT RTT CYS-133, AND CHARACTERIZATION OF
VARIANT MRXS13 VAL-140.
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).
[62]
VARIANT RTT 270-ARG--SER-486 DEL.
PubMed=23662938; DOI=10.1111/epi.12203;
Kodera H., Kato M., Nord A.S., Walsh T., Lee M., Yamanaka G.,
Tohyama J., Nakamura K., Nakagawa E., Ikeda T., Ben-Zeev B., Lev D.,
Lerman-Sagie T., Straussberg R., Tanabe S., Ueda K., Amamoto M.,
Ohta S., Nonoda Y., Nishiyama K., Tsurusaki Y., Nakashima M.,
Miyake N., Hayasaka K., King M.C., Matsumoto N., Saitsu H.;
"Targeted capture and sequencing for detection of mutations causing
early onset epileptic encephalopathy.";
Epilepsia 54:1262-1269(2013).
[63]
VARIANT RTT CYS-133.
PubMed=25818041; DOI=10.1111/epi.12954;
Mercimek-Mahmutoglu S., Patel J., Cordeiro D., Hewson S., Callen D.,
Donner E.J., Hahn C.D., Kannu P., Kobayashi J., Minassian B.A.,
Moharir M., Siriwardena K., Weiss S.K., Weksberg R., Snead O.C. III;
"Diagnostic yield of genetic testing in epileptic encephalopathy in
childhood.";
Epilepsia 56:707-716(2015).
[64]
VARIANTS RTT 270-ARG--SER-486 DEL AND CYS-306.
PubMed=26993267; DOI=10.1136/jmedgenet-2015-103263;
Trump N., McTague A., Brittain H., Papandreou A., Meyer E., Ngoh A.,
Palmer R., Morrogh D., Boustred C., Hurst J.A., Jenkins L.,
Kurian M.A., Scott R.H.;
"Improving diagnosis and broadening the phenotypes in early-onset
seizure and severe developmental delay disorders through gene panel
analysis.";
J. Med. Genet. 53:310-317(2016).
[65]
VARIANT RTT CYS-133, AND VARIANT ASN-305.
PubMed=27864847; DOI=10.1002/humu.23149;
Clinical Study Group;
Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D.,
Bigoni S., Barba C., Mari F., Montomoli M., Pisano T., Rosati A.,
Guerrini R.;
"Diagnostic targeted resequencing in 349 patients with drug-resistant
pediatric epilepsies identifies causative mutations in 30 different
genes.";
Hum. Mutat. 38:216-225(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 SIN3A. Binds both 5-methylcytosine
(5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a
preference for 5-methylcytosine (5mC).
{ECO:0000250|UniProtKB:Q9Z2D6}.
-!- SUBUNIT: Interacts with FNBP3 (By similarity). Interacts with
CDKL5 (PubMed:15917271). Interacts with ATRX; MECP2 recruits ATRX
to pericentric heterochromatin in neuronal cells (By similarity).
Interacts with NCOR2 (By similarity).
{ECO:0000250|UniProtKB:Q9Z2D6, ECO:0000269|PubMed:15917271}.
-!- INTERACTION:
Q9H2X6:HIPK2; NbExp=2; IntAct=EBI-1189067, EBI-348345;
Q9QZR5:Hipk2 (xeno); NbExp=3; IntAct=EBI-1189067, EBI-366905;
P61244:MAX; NbExp=2; IntAct=EBI-1189067, EBI-751711;
P51531:SMARCA2; NbExp=4; IntAct=EBI-1189067, EBI-679562;
-!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalized with methyl-CpG in
the genome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A; Synonyms=Beta;
IsoId=P51608-1; Sequence=Displayed;
Name=B; Synonyms=Alpha;
IsoId=P51608-2; Sequence=VSP_022948;
Note=Ten times higher expression levels than isoform A in
brain.;
-!- TISSUE SPECIFICITY: Present in all adult somatic tissues tested.
-!- PTM: Phosphorylated on Ser-423 in brain upon synaptic activity,
which attenuates its repressor activity and seems to regulate
dendritic growth and spine maturation. {ECO:0000250}.
-!- DISEASE: Angelman syndrome (AS) [MIM:105830]: A neurodevelopmental
disorder characterized by severe motor and intellectual
retardation, ataxia, frequent jerky limb movements and flapping of
the arms and hands, hypotonia, seizures, absence of speech,
frequent smiling and episodes of paroxysmal laughter, open-mouthed
expression revealing the tongue. {ECO:0000269|PubMed:11283202}.
Note=The disease may be caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Mental retardation, X-linked, syndromic, 13 (MRXS13)
[MIM:300055]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. MRXS13 patients manifest mental retardation
associated with other variable features such as spasticity,
episodes of manic depressive psychosis, increased tone and
macroorchidism. {ECO:0000269|PubMed:10986043,
ECO:0000269|PubMed:11007980, ECO:0000269|PubMed:11309367,
ECO:0000269|PubMed:11805248, ECO:0000269|PubMed:11885030,
ECO:0000269|PubMed:12161600, ECO:0000269|PubMed:12325019,
ECO:0000269|PubMed:12615169, ECO:0000269|PubMed:16966553,
ECO:0000269|PubMed:17296936}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Rett syndrome (RTT) [MIM:312750]: An X-linked dominant
neurodevelopmental disorder, and one of the most common causes of
mental retardation in females. Patients appear to develop normally
until 6 to 18 months of age, then gradually lose speech and
purposeful hand movements, and develop microcephaly, seizures,
autism, ataxia, mental retardation and stereotypic hand movements.
After initial regression, the condition stabilizes and patients
usually survive into adulthood. {ECO:0000269|PubMed:10508514,
ECO:0000269|PubMed:10577905, ECO:0000269|PubMed:10745042,
ECO:0000269|PubMed:10767337, ECO:0000269|PubMed:10814719,
ECO:0000269|PubMed:10944854, ECO:0000269|PubMed:10991688,
ECO:0000269|PubMed:10991689, ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:11241840, ECO:0000269|PubMed:11269512,
ECO:0000269|PubMed:11283202, ECO:0000269|PubMed:11376998,
ECO:0000269|PubMed:11402105, ECO:0000269|PubMed:11706982,
ECO:0000269|PubMed:11738883, ECO:0000269|PubMed:12161600,
ECO:0000269|PubMed:12567420, ECO:0000269|PubMed:12966522,
ECO:0000269|PubMed:12966523, ECO:0000269|PubMed:15034579,
ECO:0000269|PubMed:15057977, ECO:0000269|PubMed:17296936,
ECO:0000269|PubMed:23662938, ECO:0000269|PubMed:25818041,
ECO:0000269|PubMed:26993267, ECO:0000269|PubMed:27864847}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Autism, X-linked 3 (AUTSX3) [MIM:300496]: A complex
multifactorial, pervasive developmental disorder characterized by
impairments in reciprocal social interaction and communication,
restricted and stereotyped patterns of interests and activities,
and the presence of developmental abnormalities by 3 years of age.
Most individuals with autism also manifest moderate mental
retardation. {ECO:0000269|PubMed:12770674}. Note=The disease may
be caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Encephalopathy, neonatal severe, due to MECP2 mutations
(ENS-MECP2) [MIM:300673]: A neurodevelopmental disorder
characterized by severe neonatal encephalopathy, developmental
delay, mental retardation, microcephaly, seizures. Additional
features include respiratory insufficiency and central
hypoventilation, gastroesophageal reflux, axial hypotonia,
hyperreflexia and dyskinetic movements.
{ECO:0000269|PubMed:11238684}. Note=The disease is caused by
mutations affecting the gene represented in this entry. The MECP2
gene is mutated in Rett syndrome, a severe neurodevelopmental
disorder that almost always occurs in females. Although it was
first thought that MECP2 mutations causing Rett syndrome were
lethal in males, later reports identified a severe neonatal
encephalopathy in surviving male sibs of patients with Rett
syndrome. Additional reports have confirmed a severe phenotype in
males with Rett syndrome-associated MECP2 mutations.
-!- DISEASE: Mental retardation, X-linked, syndromic, Lubs type
(MRXSL) [MIM:300260]: A disorder characterized by significantly
below average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. MRXSL patients manifest mental retardation
associated with variable features. They include swallowing
dysfunction and gastroesophageal reflux with secondary recurrent
respiratory infections, hypotonia, mild myopathy and
characteristic facies such as downslanting palpebral fissures,
hypertelorism and a short nose with a low nasal bridge.
{ECO:0000269|PubMed:16080119}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Increased
dosage of MECP2 due to gene duplication appears to be responsible
for the mental retardation phenotype.
-!- SEQUENCE CAUTION:
Sequence=CAD97991.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=RettBASE; Note=IRSA MECP2 variation database;
URL="http://mecp2.chw.edu.au/mecp2/";
-----------------------------------------------------------------------
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EMBL; L37298; AAC32737.1; -; mRNA.
EMBL; X99686; CAA68001.1; -; mRNA.
EMBL; AJ132917; CAB46446.1; -; mRNA.
EMBL; AF158180; AAF33023.1; -; mRNA.
EMBL; Y12643; CAA73190.1; -; mRNA.
EMBL; AY541280; AAS55455.1; -; mRNA.
EMBL; BX538060; CAD97991.1; ALT_INIT; mRNA.
EMBL; AF030876; AAC08757.1; -; Genomic_DNA.
EMBL; BC011612; AAH11612.1; -; mRNA.
EMBL; X89430; CAA61599.1; -; mRNA.
EMBL; X94628; CAA64331.1; -; Genomic_DNA.
CCDS; CCDS14741.1; -. [P51608-1]
CCDS; CCDS48193.1; -. [P51608-2]
RefSeq; NP_001104262.1; NM_001110792.1. [P51608-2]
RefSeq; NP_001303266.1; NM_001316337.1.
RefSeq; NP_004983.1; NM_004992.3. [P51608-1]
UniGene; Hs.200716; -.
UniGene; Hs.702514; -.
PDB; 1QK9; NMR; -; A=77-166.
PDB; 3C2I; X-ray; 2.50 A; A=77-167.
PDB; 5BT2; X-ray; 2.20 A; A=77-167.
PDBsum; 1QK9; -.
PDBsum; 3C2I; -.
PDBsum; 5BT2; -.
DisProt; DP00539; -.
ProteinModelPortal; P51608; -.
SMR; P51608; -.
BioGrid; 110368; 168.
CORUM; P51608; -.
DIP; DIP-39983N; -.
IntAct; P51608; 27.
MINT; MINT-3019066; -.
STRING; 9606.ENSP00000395535; -.
BindingDB; P51608; -.
ChEMBL; CHEMBL3638346; -.
iPTMnet; P51608; -.
PhosphoSitePlus; P51608; -.
BioMuta; MECP2; -.
DMDM; 1708973; -.
EPD; P51608; -.
MaxQB; P51608; -.
PaxDb; P51608; -.
PeptideAtlas; P51608; -.
PRIDE; P51608; -.
DNASU; 4204; -.
Ensembl; ENST00000303391; ENSP00000301948; ENSG00000169057. [P51608-1]
Ensembl; ENST00000453960; ENSP00000395535; ENSG00000169057. [P51608-2]
GeneID; 4204; -.
KEGG; hsa:4204; -.
UCSC; uc004fjv.3; human. [P51608-1]
CTD; 4204; -.
DisGeNET; 4204; -.
EuPathDB; HostDB:ENSG00000169057.19; -.
GeneCards; MECP2; -.
GeneReviews; MECP2; -.
HGNC; HGNC:6990; MECP2.
HPA; CAB037264; -.
HPA; HPA000593; -.
HPA; HPA001341; -.
MalaCards; MECP2; -.
MIM; 105830; phenotype.
MIM; 300005; gene.
MIM; 300055; phenotype.
MIM; 300260; phenotype.
MIM; 300496; phenotype.
MIM; 300673; phenotype.
MIM; 312750; phenotype.
neXtProt; NX_P51608; -.
OpenTargets; ENSG00000169057; -.
Orphanet; 3095; Atypical Rett syndrome.
Orphanet; 106; Autism.
Orphanet; 778; Rett syndrome.
Orphanet; 209370; Severe neonatal-onset encephalopathy with microcephaly.
Orphanet; 536; Systemic lupus erythematosus.
Orphanet; 1762; Trisomy Xq28.
Orphanet; 3077; X-linked intellectual disability - psychosis - macroorchidism.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA30729; -.
eggNOG; KOG4161; Eukaryota.
eggNOG; ENOG41126JX; LUCA.
GeneTree; ENSGT00530000063687; -.
HOGENOM; HOG000015809; -.
HOVERGEN; HBG052445; -.
InParanoid; P51608; -.
KO; K11588; -.
OMA; KMPRAGS; -.
PhylomeDB; P51608; -.
TreeFam; TF332974; -.
SignaLink; P51608; -.
ChiTaRS; MECP2; human.
EvolutionaryTrace; P51608; -.
GeneWiki; MECP2; -.
GenomeRNAi; 4204; -.
PRO; PR:P51608; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000169057; -.
CleanEx; HS_MECP2; -.
ExpressionAtlas; P51608; baseline and differential.
Genevisible; P51608; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0010385; F:double-stranded methylated DNA binding; IMP:MGI.
GO; GO:0008327; F:methyl-CpG binding; IBA:GO_Central.
GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0035197; F:siRNA binding; IEA:Ensembl.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0032048; P:cardiolipin metabolic process; IEA:Ensembl.
GO; GO:0050432; P:catecholamine secretion; IEA:Ensembl.
GO; GO:0006576; P:cellular biogenic amine metabolic process; IEA:Ensembl.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0006342; P:chromatin silencing; IEA:Ensembl.
GO; GO:0016358; P:dendrite development; IEA:Ensembl.
GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
GO; GO:0016573; P:histone acetylation; IEA:Ensembl.
GO; GO:0016571; P:histone methylation; IEA:Ensembl.
GO; GO:0006020; P:inositol metabolic process; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IBA:GO_Central.
GO; GO:0007616; P:long-term memory; IEA:Ensembl.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:Ensembl.
GO; GO:0007052; P:mitotic spindle organization; IMP:CAFA.
GO; GO:0035067; P:negative regulation of histone acetylation; IEA:Ensembl.
GO; GO:0031061; P:negative regulation of histone methylation; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:2000820; P:negative regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0001976; P:neurological system process involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
GO; GO:0009405; P:pathogenesis; IEA:Ensembl.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:CAFA.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:CAFA.
GO; GO:1900114; P:positive regulation of histone H3-K9 trimethylation; IEA:Ensembl.
GO; GO:0090063; P:positive regulation of microtubule nucleation; IMP:CAFA.
GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0019230; P:proprioception; IEA:Ensembl.
GO; GO:0008104; P:protein localization; IEA:Ensembl.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Ensembl.
GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IEA:Ensembl.
GO; GO:0007585; P:respiratory gaseous exchange; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IBA:GO_Central.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
GO; GO:0035176; P:social behavior; IEA:Ensembl.
GO; GO:0001964; P:startle response; IEA:Ensembl.
GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
InterPro; IPR016177; DNA-bd_dom.
InterPro; IPR017353; Me_CpG-bd_MeCP2.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
PANTHER; PTHR15074:SF7; PTHR15074:SF7; 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; Autism;
Autism spectrum disorder; Chromosomal rearrangement;
Complete proteome; Disease mutation; DNA-binding; Mental retardation;
Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation.
CHAIN 1 486 Methyl-CpG-binding protein 2.
/FTId=PRO_0000096345.
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:0000250|UniProtKB:Q9Z2D6}.
COMPBIAS 366 372 His-rich.
COMPBIAS 376 405 Pro-rich.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:Q00566}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 162 162 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9Z2D6}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 321 321 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z2D6}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2D6}.
MOD_RES 426 426 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 449 449 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 9 MVAGMLGLR -> MAAAAAAAPSGGGGGGEEERL (in
isoform B). {ECO:0000303|PubMed:15034579,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_022948.
VARIANT 10 10 E -> Q (in RTT; dbSNP:rs61754421).
{ECO:0000269|PubMed:12966523}.
/FTId=VAR_018180.
VARIANT 86 86 S -> C (in dbSNP:rs61754445).
{ECO:0000269|PubMed:11055898}.
/FTId=VAR_018181.
VARIANT 97 97 D -> E (in RTT; dbSNP:rs61754449).
{ECO:0000269|PubMed:10745042}.
/FTId=VAR_023552.
VARIANT 97 97 D -> Y (in RTT; dbSNP:rs61754448).
{ECO:0000269|PubMed:11402105}.
/FTId=VAR_018182.
VARIANT 100 100 L -> R (in RTT; dbSNP:rs61754451).
{ECO:0000269|PubMed:15057977}.
/FTId=VAR_023553.
VARIANT 100 100 L -> V (in RTT; dbSNP:rs28935168).
{ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:12966522,
ECO:0000269|PubMed:15057977}.
/FTId=VAR_017462.
VARIANT 101 101 P -> H (in RTT; dbSNP:rs61754453).
{ECO:0000269|PubMed:10767337}.
/FTId=VAR_018183.
VARIANT 101 101 P -> L (in RTT; dbSNP:rs61754453).
{ECO:0000269|PubMed:10767337}.
/FTId=VAR_018184.
VARIANT 101 101 P -> R (in RTT; also in a patient with
Angelman syndrome and some typical RTT
features; dbSNP:rs61754453).
{ECO:0000269|PubMed:10991689,
ECO:0000269|PubMed:11283202}.
/FTId=VAR_010276.
VARIANT 101 101 P -> S (in RTT; dbSNP:rs61754452).
{ECO:0000269|PubMed:11269512}.
/FTId=VAR_023554.
VARIANT 101 101 P -> T (in RTT).
{ECO:0000269|PubMed:10767337}.
/FTId=VAR_018185.
VARIANT 106 106 R -> Q (in RTT; dbSNP:rs61754457).
{ECO:0000269|PubMed:10814719,
ECO:0000269|PubMed:11055898}.
/FTId=VAR_018186.
VARIANT 106 106 R -> W (in RTT; dbSNP:rs28934907).
{ECO:0000269|PubMed:10508514,
ECO:0000269|PubMed:10577905,
ECO:0000269|PubMed:10745042,
ECO:0000269|PubMed:10767337,
ECO:0000269|PubMed:10991688,
ECO:0000269|PubMed:10991689,
ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:11241840,
ECO:0000269|PubMed:11269512,
ECO:0000269|PubMed:11402105,
ECO:0000269|PubMed:11738883,
ECO:0000269|PubMed:15057977}.
/FTId=VAR_010272.
VARIANT 111 111 R -> G (in RTT; dbSNP:rs61754459).
{ECO:0000269|PubMed:11241840}.
/FTId=VAR_018187.
VARIANT 120 120 Y -> D (in RTT; dbSNP:rs267608454).
{ECO:0000269|PubMed:11376998}.
/FTId=VAR_023555.
VARIANT 124 124 L -> F (in RTT; dbSNP:rs61755763).
{ECO:0000269|PubMed:10991688}.
/FTId=VAR_010277.
VARIANT 128 128 Q -> P (in RTT; dbSNP:rs61748383).
{ECO:0000269|PubMed:12966523}.
/FTId=VAR_018188.
VARIANT 133 133 R -> C (in RTT; impairs interaction with
ATRX and abolishes ATRX recruitment to
heterochromatin; dbSNP:rs28934904).
{ECO:0000269|PubMed:10508514,
ECO:0000269|PubMed:10577905,
ECO:0000269|PubMed:10745042,
ECO:0000269|PubMed:10767337,
ECO:0000269|PubMed:10991688,
ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:11241840,
ECO:0000269|PubMed:11269512,
ECO:0000269|PubMed:11376998,
ECO:0000269|PubMed:11402105,
ECO:0000269|PubMed:12567420,
ECO:0000269|PubMed:12966523,
ECO:0000269|PubMed:15057977,
ECO:0000269|PubMed:17296936,
ECO:0000269|PubMed:25818041,
ECO:0000269|PubMed:27864847}.
/FTId=VAR_010273.
VARIANT 133 133 R -> H (in RTT; dbSNP:rs61748389).
{ECO:0000269|PubMed:11402105,
ECO:0000269|PubMed:11706982}.
/FTId=VAR_018189.
VARIANT 134 134 S -> C (in RTT; dbSNP:rs61748390).
{ECO:0000269|PubMed:10767337,
ECO:0000269|PubMed:10991688,
ECO:0000269|PubMed:11269512,
ECO:0000269|PubMed:11738883}.
/FTId=VAR_010278.
VARIANT 135 135 K -> E (in RTT; dbSNP:rs61748391).
{ECO:0000269|PubMed:11241840}.
/FTId=VAR_018190.
VARIANT 137 137 E -> G (in MRXS13; dbSNP:rs61748392).
{ECO:0000269|PubMed:11309367}.
/FTId=VAR_017581.
VARIANT 140 140 A -> V (in MRXS13; impairs interaction
with ATRX and abolishes ATRX recruitment
to heterochromatin; dbSNP:rs28934908).
{ECO:0000269|PubMed:11007980,
ECO:0000269|PubMed:11309367,
ECO:0000269|PubMed:11805248,
ECO:0000269|PubMed:11885030,
ECO:0000269|PubMed:12161600,
ECO:0000269|PubMed:12325019,
ECO:0000269|PubMed:17296936}.
/FTId=VAR_010279.
VARIANT 152 152 P -> R (in RTT; dbSNP:rs61748404).
{ECO:0000269|PubMed:10767337,
ECO:0000269|PubMed:10991688,
ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:11241840,
ECO:0000269|PubMed:11269512,
ECO:0000269|PubMed:11402105,
ECO:0000269|PubMed:11738883,
ECO:0000269|PubMed:12966523,
ECO:0000269|PubMed:15057977}.
/FTId=VAR_010280.
VARIANT 155 155 F -> I (in RTT; dbSNP:rs61748406).
{ECO:0000269|PubMed:10745042}.
/FTId=VAR_023556.
VARIANT 155 155 F -> S (in RTT; dbSNP:rs28934905).
{ECO:0000269|PubMed:10508514,
ECO:0000269|PubMed:10577905,
ECO:0000269|PubMed:11055898}.
/FTId=VAR_010274.
VARIANT 156 156 D -> G (in RTT; dbSNP:rs61748407).
{ECO:0000269|PubMed:11241840}.
/FTId=VAR_018191.
VARIANT 158 158 T -> A (in RTT; dbSNP:rs61748411).
{ECO:0000269|PubMed:11269512,
ECO:0000269|PubMed:15057977}.
/FTId=VAR_023557.
VARIANT 158 158 T -> M (in RTT; dbSNP:rs28934906).
{ECO:0000269|PubMed:10508514,
ECO:0000269|PubMed:10577905,
ECO:0000269|PubMed:10745042,
ECO:0000269|PubMed:10767337,
ECO:0000269|PubMed:10814719,
ECO:0000269|PubMed:10944854,
ECO:0000269|PubMed:10991688,
ECO:0000269|PubMed:10991689,
ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:11241840,
ECO:0000269|PubMed:11269512,
ECO:0000269|PubMed:11376998,
ECO:0000269|PubMed:11402105,
ECO:0000269|PubMed:11738883,
ECO:0000269|PubMed:12567420,
ECO:0000269|PubMed:12966523,
ECO:0000269|PubMed:15057977}.
/FTId=VAR_010275.
VARIANT 161 161 G -> V (in RTT; dbSNP:rs61748417).
{ECO:0000269|PubMed:15057977}.
/FTId=VAR_023558.
VARIANT 167 167 R -> W (in MRXS13; dbSNP:rs61748420).
{ECO:0000269|PubMed:11309367}.
/FTId=VAR_018192.
VARIANT 181 181 A -> V (in dbSNP:rs61749705).
{ECO:0000269|PubMed:12384770}.
/FTId=VAR_018193.
VARIANT 196 196 T -> S (in dbSNP:rs61749713).
{ECO:0000269|PubMed:12111644}.
/FTId=VAR_018194.
VARIANT 197 197 T -> M (in dbSNP:rs61749714).
{ECO:0000269|PubMed:11402105,
ECO:0000269|PubMed:12161600}.
/FTId=VAR_018195.
VARIANT 201 201 A -> V (in dbSNP:rs61748381).
{ECO:0000269|PubMed:10944854,
ECO:0000269|PubMed:11738883}.
/FTId=VAR_010281.
VARIANT 203 203 T -> M (in dbSNP:rs61749720).
{ECO:0000269|PubMed:11007980,
ECO:0000269|PubMed:11055898}.
/FTId=VAR_018196.
VARIANT 210 210 K -> I (in RTT; dbSNP:rs61749730).
{ECO:0000269|PubMed:11241840}.
/FTId=VAR_018197.
VARIANT 225 225 P -> L (in MRXS13; dbSNP:rs61749715).
{ECO:0000269|PubMed:12615169}.
/FTId=VAR_037664.
VARIANT 225 225 P -> R (in RTT; dbSNP:rs61749715).
{ECO:0000269|PubMed:10767337}.
/FTId=VAR_018198.
VARIANT 228 228 T -> S (in dbSNP:rs61749738).
{ECO:0000269|PubMed:12111644}.
/FTId=VAR_018199.
VARIANT 229 229 S -> L (in dbSNP:rs61749739).
{ECO:0000269|PubMed:10767337}.
/FTId=VAR_018200.
VARIANT 232 232 G -> A (in dbSNP:rs61748422).
{ECO:0000269|PubMed:10944854}.
/FTId=VAR_018201.
VARIANT 251 251 P -> L (in dbSNP:rs61750229).
{ECO:0000269|PubMed:10944854}.
/FTId=VAR_018202.
VARIANT 270 486 Missing (in RTT).
{ECO:0000269|PubMed:23662938,
ECO:0000269|PubMed:26993267}.
/FTId=VAR_078720.
VARIANT 284 284 K -> E (in MRXS13; dbSNP:rs61750255).
{ECO:0000269|PubMed:11309367}.
/FTId=VAR_018203.
VARIANT 287 287 A -> P (in dbSNP:rs61750257).
{ECO:0000269|PubMed:11055898}.
/FTId=VAR_018204.
VARIANT 291 291 S -> A (in dbSNP:rs61751360).
{ECO:0000269|PubMed:11055898}.
/FTId=VAR_018205.
VARIANT 302 302 P -> A (in RTT; dbSNP:rs61751373).
{ECO:0000269|PubMed:11738883}.
/FTId=VAR_018206.
VARIANT 302 302 P -> H (in RTT; dbSNP:rs61749723).
{ECO:0000269|PubMed:10944854}.
/FTId=VAR_018207.
VARIANT 302 302 P -> L (in RTT; dbSNP:rs61749723).
{ECO:0000269|PubMed:10767337}.
/FTId=VAR_018208.
VARIANT 302 302 P -> R (in RTT; dbSNP:rs61749723).
{ECO:0000269|PubMed:10814719,
ECO:0000269|PubMed:11241840}.
/FTId=VAR_018209.
VARIANT 305 305 K -> N (probable disease-associated
mutation found in a patient with drug-
resistant epilepsy with intellectual
disability, parkinsonism and other
neurologic symptoms).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078221.
VARIANT 305 305 K -> R (in RTT; dbSNP:rs61751441).
{ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:11402105}.
/FTId=VAR_018210.
VARIANT 306 306 R -> C (in RTT; dbSNP:rs28935468).
{ECO:0000269|PubMed:10577905,
ECO:0000269|PubMed:10745042,
ECO:0000269|PubMed:10767337,
ECO:0000269|PubMed:10814719,
ECO:0000269|PubMed:10944854,
ECO:0000269|PubMed:10991688,
ECO:0000269|PubMed:10991689,
ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:11241840,
ECO:0000269|PubMed:11376998,
ECO:0000269|PubMed:11402105,
ECO:0000269|PubMed:11738883,
ECO:0000269|PubMed:12567420,
ECO:0000269|PubMed:12966523,
ECO:0000269|PubMed:15057977,
ECO:0000269|PubMed:26993267}.
/FTId=VAR_010282.
VARIANT 306 306 R -> H (in RTT; dbSNP:rs61751443).
{ECO:0000269|PubMed:10767337,
ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:15057977}.
/FTId=VAR_018211.
VARIANT 322 322 P -> A (in RTT; dbSNP:rs61751449).
{ECO:0000269|PubMed:10814719,
ECO:0000269|PubMed:11738883}.
/FTId=VAR_018212.
VARIANT 322 322 P -> L (in RTT; dbSNP:rs61751450).
{ECO:0000269|PubMed:11402105}.
/FTId=VAR_018213.
VARIANT 322 322 P -> S (in MRXS13; dbSNP:rs61751449).
{ECO:0000269|PubMed:16966553}.
/FTId=VAR_037665.
VARIANT 344 344 R -> W (in RTT; dbSNP:rs61752361).
{ECO:0000269|PubMed:12161600}.
/FTId=VAR_018214.
VARIANT 359 359 S -> P (in dbSNP:rs61752371).
{ECO:0000269|PubMed:11896461}.
/FTId=VAR_018215.
VARIANT 376 376 P -> S (in a RTT patient; unknown
pathological significance;
dbSNP:rs61752387).
{ECO:0000269|PubMed:10944854,
ECO:0000269|PubMed:12161600,
ECO:0000269|PubMed:12384770,
ECO:0000269|PubMed:12567420}.
/FTId=VAR_018216.
VARIANT 388 388 P -> L (in dbSNP:rs61753006).
/FTId=VAR_023559.
VARIANT 388 388 P -> S (in a RTT patient;
dbSNP:rs61753000).
{ECO:0000269|PubMed:12567420}.
/FTId=VAR_018218.
VARIANT 388 388 Missing. {ECO:0000269|PubMed:12384770}.
/FTId=VAR_018217.
VARIANT 394 394 E -> K (in dbSNP:rs63094662).
{ECO:0000269|PubMed:12111644}.
/FTId=VAR_018219.
VARIANT 397 397 E -> K (in dbSNP:rs56268439).
{ECO:0000269|PubMed:10577905,
ECO:0000269|PubMed:10991689,
ECO:0000269|PubMed:11055898,
ECO:0000269|PubMed:11738883,
ECO:0000269|PubMed:11896461}.
/FTId=VAR_010283.
VARIANT 399 399 P -> L (in MRXS13; unknown pathological
significance; dbSNP:rs62915962).
{ECO:0000269|PubMed:11309367,
ECO:0000269|PubMed:12161600}.
/FTId=VAR_018220.
VARIANT 402 402 P -> L (in dbSNP:rs61753014).
{ECO:0000269|PubMed:12384770}.
/FTId=VAR_018221.
VARIANT 412 412 V -> I (in dbSNP:rs61753966).
{ECO:0000269|PubMed:11055898}.
/FTId=VAR_018222.
VARIANT 428 428 G -> S (in ENS-MECP2; uncertain
pathological significance;
dbSNP:rs61753971).
{ECO:0000269|PubMed:11238684,
ECO:0000269|PubMed:12161600}.
/FTId=VAR_017463.
VARIANT 439 439 A -> T (in dbSNP:rs61753973).
{ECO:0000269|PubMed:10767337}.
/FTId=VAR_018223.
VARIANT 444 444 A -> T (in dbSNP:rs61753975).
{ECO:0000269|PubMed:11055898}.
/FTId=VAR_018224.
VARIANT 453 453 R -> Q (in MRXS13; dbSNP:rs61753980).
{ECO:0000269|PubMed:11309367}.
/FTId=VAR_018225.
VARIANT 480 480 P -> S (in dbSNP:rs267608636).
{ECO:0000269|PubMed:12111644}.
/FTId=VAR_018226.
CONFLICT 72 75 PAVP -> RLC (in Ref. 10; CAA61599).
{ECO:0000305}.
CONFLICT 290 290 E -> G (in Ref. 2; CAA68001).
{ECO:0000305}.
CONFLICT 466 466 M -> V (in Ref. 7; CAD97991).
{ECO:0000305}.
STRAND 95 97 {ECO:0000244|PDB:1QK9}.
STRAND 100 103 {ECO:0000244|PDB:1QK9}.
STRAND 105 110 {ECO:0000244|PDB:5BT2}.
TURN 115 118 {ECO:0000244|PDB:5BT2}.
STRAND 120 125 {ECO:0000244|PDB:5BT2}.
TURN 127 129 {ECO:0000244|PDB:1QK9}.
STRAND 130 134 {ECO:0000244|PDB:1QK9}.
HELIX 135 144 {ECO:0000244|PDB:5BT2}.
HELIX 152 154 {ECO:0000244|PDB:5BT2}.
SEQUENCE 486 AA; 52441 MW; EB6A33233AEDA566 CRC64;
MVAGMLGLRE EKSEDQDLQG LKDKPLKFKK VKKDKKEEKE GKHEPVQPSA HHSAEPAEAG
KAETSEGSGS APAVPEASAS PKQRRSIIRD RGPMYDDPTL PEGWTRKLKQ RKSGRSAGKY
DVYLINPQGK AFRSKVELIA YFEKVGDTSL DPNDFDFTVT GRGSPSRREQ KPPKKPKSPK
APGTGRGRGR PKGSGTTRPK AATSEGVQVK RVLEKSPGKL LVKMPFQTSP GGKAEGGGAT
TSTQVMVIKR PGRKRKAEAD PQAIPKKRGR KPGSVVAAAA AEAKKKAVKE SSIRSVQETV
LPIKKRKTRE TVSIEVKEVV KPLLVSTLGE KSGKGLKTCK SPGRKSKESS PKGRSSSASS
PPKKEHHHHH HHSESPKAPV PLLPPLPPPP PEPESSEDPT SPPEPQDLSS SVCKEEKMPR
GGSLESDGCP KEPAKTQPAV ATAATAAEKY KHRGEGERKD IVSSSMPRPN REEPVDSRTP
VTERVS


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CSB-EL013638RA Rat Methyl-CpG-binding protein 2(MECP2) ELISA kit 96T
pro-212 Recombinant Human Methyl CpG Binding Protein 2 MECP2 10
pro-212 Recombinant Human Methyl CpG Binding Protein 2 MECP2 0.1mg
CSB-E13524h Human Methyl CpG Binding Protein 2 (MECP2)ELISA Kit 96T
201-02-1284 Mouse Methyl CpG Binding Protein 2(MECP2)ELISA Kit 96T
CSB-EL013638RA Rat Methyl-CpG-binding protein 2(MECP2) ELISA kit SpeciesRat 96T
CSB-EL013638MO Mouse Methyl-CpG-binding protein 2(MECP2) ELISA kit 96T
P-Mecp2 Methyl CGP binding protein 2, Antigen blocking peptide 100ul


 

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