MECP2_HUMAN
ID MECP2_HUMAN Reviewed; 486 AA.
AC P51608; O15233; Q6QHH9; Q7Z384;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 246.
DE RecName: Full=Methyl-CpG-binding protein 2;
DE Short=MeCp-2 protein;
DE Short=MeCp2;
GN Name=MECP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=9710633; DOI=10.1128/mcb.18.9.5492;
RA Kudo S.;
RT "Methyl-CpG-binding protein MeCP2 represses Sp1-activated transcription of
RT the human leukosialin gene when the promoter is methylated.";
RL Mol. Cell. Biol. 18:5492-5499(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=8976388; DOI=10.1159/000134438;
RA Vilain A., Apiou F., Vogt N., Dutrillaux B., Malfoy B.;
RT "Assignment of the gene for methyl-CpG-binding protein 2 (MECP2) to human
RT chromosome band Xq28 by in situ hybridization.";
RL Cytogenet. Cell Genet. 74:293-294(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=10723722; DOI=10.1007/s003350010035;
RA Reichwald K., Thiesen J., Wiehe T., Weitzel J., Poustka W.A., Rosenthal A.,
RA Platzer M., Stratling W.H., Kioschis P.;
RT "Comparative sequence analysis of the MECP2-locus in human and mouse
RT reveals new transcribed regions.";
RL Mamm. Genome 11:182-190(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND INVOLVEMENT IN RTT.
RX PubMed=15034579; DOI=10.1038/ng1327;
RA Mnatzakanian G.N., Lohi H., Munteanu I., Alfred S.E., Yamada T.,
RA MacLeod P.J.M., Jones J.R., Scherer S.W., Schanen N.C., Friez M.J.,
RA Vincent J.B., Minassian B.A.;
RT "A previously unidentified MECP2 open reading frame defines a new protein
RT isoform relevant to Rett syndrome.";
RL Nat. Genet. 36:339-341(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Placenta;
RA Straetling W.H.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Placenta;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-486 (ISOFORM A).
RC TISSUE=Skeletal muscle;
RX PubMed=8672133; DOI=10.1007/s003359900157;
RA D'Esposito M., Quaderi N.A., Ciccodicola A., Bruni P., Esposito T.,
RA D'Urso M., Brown S.D.M.;
RT "Isolation, physical mapping, and Northern analysis of the X-linked human
RT gene encoding methyl CpG-binding protein, MECP2.";
RL Mamm. Genome 7:533-535(1996).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-486 (ISOFORM A).
RA Reichwald K., Bauer D., Brenner V., Drescher B., Coy J.F., Kioschis P.,
RA Korn B., Nyakatura G., Platzer M., Poustka A., Sandoval N., Rosenthal A.;
RT "Genetic organization of human methyl-CpG-binding protein 2.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP IDENTIFICATION (ISOFORM B).
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 [13]
RP REVIEW ON VARIANTS.
RX PubMed=12872250; DOI=10.1002/humu.10243;
RA Miltenberger-Miltenyi G., Laccone F.;
RT "Mutations and polymorphisms in the human methyl CpG-binding protein
RT MECP2.";
RL Hum. Mutat. 22:107-115(2003).
RN [14]
RP INTERACTION WITH CDKL5.
RX PubMed=15917271; DOI=10.1093/hmg/ddi198;
RA Mari F., Azimonti S., Bertani I., Bolognese F., Colombo E., Caselli R.,
RA Scala E., Longo I., Grosso S., Pescucci C., Ariani F., Hayek G.,
RA Balestri P., Bergo A., Badaracco G., Zappella M., Broccoli V., Renieri A.,
RA Kilstrup-Nielsen C., Landsberger N.;
RT "CDKL5 belongs to the same molecular pathway of MeCP2 and it is responsible
RT for the early-onset seizure variant of Rett syndrome.";
RL Hum. Mol. Genet. 14:1935-1946(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-116 AND SER-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-229, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [25]
RP STRUCTURE BY NMR OF 77-166.
RX PubMed=10518942; DOI=10.1006/jmbi.1999.3023;
RA Wakefield R.I., Smith B.O., Nan X., Free A., Soteriou A., Uhrin D.,
RA Bird A.P., Barlow P.N.;
RT "The solution structure of the domain from MeCP2 that binds to methylated
RT DNA.";
RL J. Mol. Biol. 291:1055-1065(1999).
RN [26]
RP VARIANTS RTT TRP-106; CYS-133; SER-155; MET-158 AND CYS-306, AND VARIANT
RP LYS-397.
RX PubMed=10577905; DOI=10.1086/302690;
RA Wan M., Lee S.S.J., Zhang X., Houwink-Manville I., Song H.-R., Amir R.E.,
RA Budden S., Naidu S., Pereira J.L.P., Lo I.F.M., Zoghbi H.Y., Schanen N.C.,
RA Francke U.;
RT "Rett syndrome and beyond: recurrent spontaneous and familial MECP2
RT mutations at CpG hotspots.";
RL Am. J. Hum. Genet. 65:1520-1529(1999).
RN [27]
RP VARIANTS RTT TRP-106; CYS-133; SER-155 AND MET-158.
RX PubMed=10508514; DOI=10.1038/13810;
RA Amir R.E., Van den Veyver I.B., Wan M., Tran C.Q., Francke U., Zoghbi H.Y.;
RT "Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-
RT CpG-binding protein 2.";
RL Nat. Genet. 23:185-188(1999).
RN [28]
RP INVOLVEMENT IN MRXS13.
RX PubMed=10986043; DOI=10.1086/303078;
RA Meloni I., Bruttini M., Longo I., Mari F., Rizzolio F., D'Adamo P.,
RA Denvriendt K., Fryns J.-P., Toniolo D., Renieri A.;
RT "A mutation in the Rett syndrome gene, MECP2, causes X-linked mental
RT retardation and progressive spasticity in males.";
RL Am. J. Hum. Genet. 67:982-985(2000).
RN [29]
RP VARIANTS RTT VAL-100; GLN-106; TRP-106; CYS-133; ARG-152; SER-155; MET-158;
RP ARG-305; CYS-306 AND HIS-306, AND VARIANTS CYS-86; MET-203; PRO-287;
RP ALA-291; LYS-397; ILE-412 AND THR-444.
RX PubMed=11055898; DOI=10.1086/316913;
RA Buyse I.M., Fang P., Hoon K.T., Amir R.E., Zoghbi H.Y., Roa B.B.;
RT "Diagnostic testing for Rett syndrome by DHPLC and direct sequencing
RT analysis of the MECP2 gene: identification of several novel mutations and
RT polymorphisms.";
RL Am. J. Hum. Genet. 67:1428-1436(2000).
RN [30]
RP VARIANT MRXS13 VAL-140, AND VARIANT MET-203.
RX PubMed=11007980; DOI=10.1016/s0014-5793(00)01994-3;
RA Orrico A., Lam C., Galli L., Dotti M.T., Hayek G., Tong S.F., Poon P.M.,
RA Zappella M., Federico A., Sorrentino V.;
RT "MECP2 mutation in male patients with non-specific X-linked mental
RT retardation.";
RL FEBS Lett. 481:285-288(2000).
RN [31]
RP VARIANTS RTT LEU-101; HIS-101; THR-101; TRP-106; CYS-133; CYS-134; ARG-152;
RP MET-158; ARG-225; LEU-302; CYS-306 AND HIS-306, AND VARIANTS LEU-229 AND
RP THR-439.
RX PubMed=10767337; DOI=10.1093/hmg/9.7.1119;
RA Cheadle J.P., Gill H., Fleming N., Maynard J., Kerr A., Leonard H.,
RA Krawczak M., Cooper D.N., Lynch S., Thomas N., Hughes H., Hulten M.,
RA Ravine D., Sampson J.R., Clarke A.;
RT "Long-read sequence analysis of the MECP2 gene in Rett syndrome patients:
RT correlation of disease severity with mutation type and location.";
RL Hum. Mol. Genet. 9:1119-1129(2000).
RN [32]
RP VARIANTS RTT GLN-106; MET-158; ARG-302; CYS-306 AND ALA-322.
RX PubMed=10814719; DOI=10.1093/hmg/9.9.1377;
RA Bienvenu T., Carrie A., de Roux N., Vinet M.-C., Jonveaux P., Couvert P.,
RA Villard L., Arzimanoglou A., Beldjord C., Fontes M., Tardieu M., Chelly J.;
RT "MECP2 mutations account for most cases of typical forms of Rett
RT syndrome.";
RL Hum. Mol. Genet. 9:1377-1384(2000).
RN [33]
RP VARIANTS RTT MET-158; HIS-302 AND CYS-306, AND VARIANTS VAL-201; ALA-232;
RP LEU-251 AND SER-376.
RX PubMed=10944854; DOI=10.1007/s100380070032;
RA Amano K., Nomura Y., Segawa M., Yamakawa K.;
RT "Mutational analysis of the MECP2 gene in Japanese patients with Rett
RT syndrome.";
RL J. Hum. Genet. 45:231-236(2000).
RN [34]
RP VARIANTS RTT GLU-97; TRP-106; CYS-133; ILE-155; MET-158 AND CYS-306.
RX PubMed=10745042; DOI=10.1136/jmg.37.4.250;
RA Xiang F., Buervenich S., Nicolao P., Bailey M.E., Zhang Z., Anvret M.;
RT "Mutation screening in Rett syndrome patients.";
RL J. Med. Genet. 37:250-255(2000).
RN [35]
RP VARIANTS RTT TRP-106; PHE-124; CYS-133; CYS-134; ARG-152; MET-158 AND
RP CYS-306.
RX PubMed=10991688; DOI=10.1136/jmg.37.8.608;
RA Obata K., Matsuishi T., Yamashita Y., Fukuda T., Kuwajima K., Horiuchi I.,
RA Nagamitsu S., Iwanaga R., Kimura A., Omori I., Endo S., Mori K., Kondo I.;
RT "Mutation analysis of the methyl-CpG binding protein 2 gene (MECP2) in
RT patients with Rett syndrome.";
RL J. Med. Genet. 37:608-610(2000).
RN [36]
RP VARIANTS RTT ARG-101; TRP-106; MET-158 AND CYS-306, AND VARIANT LYS-397.
RX PubMed=10991689; DOI=10.1136/jmg.37.8.610;
RA Hampson K., Woods C.G., Latif F., Webb T.;
RT "Mutations in the MECP2 gene in a cohort of girls with Rett syndrome.";
RL J. Med. Genet. 37:610-612(2000).
RN [37]
RP VARIANT RTT HIS-133.
RX PubMed=11706982; DOI=10.1002/ana.1272;
RA Armstrong J., Poo P., Pineda M., Aibar E., Gean E., Catala V., Monros E.;
RT "Classic Rett syndrome in a boy as a result of somatic mosaicism for a
RT MECP2 mutation.";
RL Ann. Neurol. 50:692-692(2001).
RN [38]
RP VARIANTS RTT ASP-120; CYS-133; MET-158 AND CYS-306.
RX PubMed=11376998; DOI=10.1016/s0387-7604(01)00197-8;
RA Inui K., Akagi M., Ono J., Tsukamoto H., Shimono K., Mano T., Imai K.,
RA Yamada M., Muramatsu T., Sakai N., Okada S.;
RT "Mutational analysis of MECP2 in Japanese patients with atypical Rett
RT syndrome.";
RL Brain Dev. 23:212-215(2001).
RN [39]
RP VARIANTS RTT TRP-106; CYS-134; ARG-152; MET-158; ALA-302; CYS-306 AND
RP ALA-322, AND VARIANTS VAL-201 AND LYS-397.
RX PubMed=11738883; DOI=10.1016/s0387-7604(01)00342-4;
RA Giunti L., Pelagatti S., Lazzerini V., Guarducci S., Lapi E., Coviello S.,
RA Cecconi A., Ombroni L., Andreucci E., Sani I., Brusaferri A., Lasagni A.,
RA Ricotti G., Giometto B., Nicolao P., Gasparini P., Granatiero M.,
RA Giovannucci Uzielli M.L.;
RT "Spectrum and distribution of MECP2 mutations in 64 Italian Rett syndrome
RT girls: tentative genotype/phenotype correlation.";
RL Brain Dev. 23:S242-S245(2001).
RN [40]
RP VARIANTS MRXS13 GLY-137; VAL-140; TRP-167; GLU-284; LEU-399 AND GLN-453.
RX PubMed=11309367; DOI=10.1093/hmg/10.9.941;
RA Couvert P., Bienvenu T., Aquaviva C., Poirier K., Moraine C., Gendrot C.,
RA Verloes A., Andres C., Le Fevre A.C., Souville I., Steffann J.,
RA des Portes V., Ropers H.-H., Yntema H.G., Fryns J.-P., Briault S.,
RA Chelly J., Cherif B.;
RT "MECP2 is highly mutated in X-linked mental retardation.";
RL Hum. Mol. Genet. 10:941-946(2001).
RN [41]
RP VARIANTS RTT TRP-106; GLY-111; CYS-133; GLU-135; ARG-152; GLY-156; MET-158;
RP ILE-210; ARG-302 AND CYS-306.
RX PubMed=11241840; DOI=10.1002/humu.3;
RA Laccone F., Huppke P., Hanefeld F., Meins M.;
RT "Mutation spectrum in patients with Rett syndrome in the German population:
RT evidence of hot spot regions.";
RL Hum. Mutat. 17:183-190(2001).
RN [42]
RP VARIANT RTT ARG-101, AND INVOLVEMENT IN AS.
RX PubMed=11283202; DOI=10.1136/jmg.38.4.224;
RA Watson P., Black G., Ramsden S., Barrow M., Super M., Kerr B.,
RA Clayton-Smith J.;
RT "Angelman syndrome phenotype associated with mutations in MECP2, a gene
RT encoding a methyl CpG binding protein.";
RL J. Med. Genet. 38:224-228(2001).
RN [43]
RP VARIANT ENS-MECP2 SER-428.
RX PubMed=11238684; DOI=10.1136/jmg.38.3.171;
RA Imessaoudene B., Bonnefont J.-P., Royer G., Cormier-Daire V., Lyonnet S.,
RA Lyon G., Munnich A., Amiel J.;
RT "MECP2 mutation in non-fatal, non-progressive encephalopathy in a male.";
RL J. Med. Genet. 38:171-174(2001).
RN [44]
RP VARIANTS RTT SER-101; TRP-106; CYS-133; CYS-134; ARG-152; ALA-158 AND
RP MET-158.
RX PubMed=11269512; DOI=10.1007/s001090000155;
RA Vacca M., Filippini F., Budillon A., Rossi V., Mercadante G., Manzati E.,
RA Gualandi F., Bigoni S., Trabanelli C., Pini G., Calzolari E., Ferlini A.,
RA Meloni I., Hayek G., Zappella M., Renieri A., D'Urso M., D'Esposito M.,
RA MacDonald F., Kerr A., Dhanjal S., Hulten M.;
RT "Mutation analysis of the MECP2 gene in British and Italian Rett syndrome
RT females.";
RL J. Mol. Med. 78:648-655(2001).
RN [45]
RP VARIANTS RTT TYR-97; TRP-106; HIS-133; CYS-133; ARG-152; MET-158; ARG-305;
RP CYS-306 AND LEU-322, AND VARIANT MET-197.
RX PubMed=11402105; DOI=10.1212/wnl.56.11.1486;
RA Hoffbuhr K., Devaney J.M., LaFleur B., Sirianni N., Scacheri C., Giron J.,
RA Schuette J., Innis J., Marino M., Philippart M., Narayanan V., Umansky R.,
RA Kronn D., Hoffman E.P., Naidu S.;
RT "MeCP2 mutations in children with and without the phenotype of Rett
RT syndrome.";
RL Neurology 56:1486-1495(2001).
RN [46]
RP VARIANT MRXS13 VAL-140.
RX PubMed=11885030; DOI=10.1086/339553;
RA Klauck S.M., Lindsay S., Beyer K.S., Splitt M., Burn J., Poustka A.;
RT "A mutation hot spot for nonspecific X-linked mental retardation in the
RT MECP2 gene causes the PPM-X syndrome.";
RL Am. J. Hum. Genet. 70:1034-1037(2002).
RN [47]
RP VARIANTS PRO-359 AND LYS-397.
RX PubMed=11896461; DOI=10.1038/sj.ejhg.5200761;
RA Moncla A., Kpebe A., Missirian C., Mancini J., Villard L.;
RT "Polymorphisms in the C-terminal domain of MECP2 in mentally handicapped
RT boys: implications for genetic counselling.";
RL Eur. J. Hum. Genet. 10:86-89(2002).
RN [48]
RP VARIANTS SER-196; SER-228; LYS-394 AND SER-480.
RX PubMed=12111644; DOI=10.1038/sj.ejhg.5200836;
RA Yntema H.G., Kleefstra T., Oudakker A.R., Romein T., de Vries B.B.A.,
RA Nillesen W., Sistermans E.A., Brunner H.G., Hamel B.C.J., van Bokhoven H.;
RT "Low frequency of MECP2 mutations in mentally retarded males.";
RL Eur. J. Hum. Genet. 10:487-490(2002).
RN [49]
RP VARIANTS VAL-181; SER-376; PRO-388 DEL AND LEU-402.
RX PubMed=12384770; DOI=10.1007/s00439-002-0786-3;
RA Beyer K.S., Blasi F., Bacchelli E., Klauck S.M., Maestrini E., Poustka A.;
RT "Mutation analysis of the coding sequence of the MECP2 gene in infantile
RT autism.";
RL Hum. Genet. 111:305-309(2002).
RN [50]
RP VARIANT MRXS13 VAL-140.
RX PubMed=12325019; DOI=10.1002/humu.10130;
RA Winnepenninckx B., Errijgers V., Hayez-Delatte F., Reyniers E., Kooy R.F.;
RT "Identification of a family with nonspecific mental retardation (MRX79)
RT with the A140V mutation in the MECP2 gene: is there a need for routine
RT screening?";
RL Hum. Mutat. 20:249-252(2002).
RN [51]
RP VARIANT MRXS13 VAL-140, VARIANT RTT TRP-344, VARIANTS MET-197; SER-376;
RP LEU-399 AND SER-428, AND DISCUSSION OF PATHOGENIC ROLE.
RX PubMed=12161600; DOI=10.1136/jmg.39.8.586;
RA Laccone F., Zoll B., Huppke P., Hanefeld F., Pepinski W., Trappe R.;
RT "MECP2 gene nucleotide changes and their pathogenicity in males: proceed
RT with caution.";
RL J. Med. Genet. 39:586-588(2002).
RN [52]
RP VARIANT MRXS13 VAL-140.
RX PubMed=11805248; DOI=10.1212/wnl.58.2.226;
RA Dotti M.T., Orrico A., De Stefano N., Battisti C., Sicurelli F., Severi S.,
RA Lam C.-W., Galli L., Sorrentino V., Federico A.;
RT "A Rett syndrome MECP2 mutation that causes mental retardation in men.";
RL Neurology 58:226-230(2002).
RN [53]
RP VARIANTS RTT CYS-133; MET-158; CYS-306 AND SER-388, AND VARIANT SER-376.
RX PubMed=12567420; DOI=10.1002/ajmg.a.10898;
RA Conforti F.L., Mazzei R., Magariello A., Patitucci A.L., Gabriele A.L.,
RA Muglia M., Quattrone A., Fiumara A., Pavone L., Barone R., Nistico R.,
RA Mangone L.;
RT "Mutation analysis of the MECP2 gene in patients with Rett syndrome.";
RL Am. J. Med. Genet. A 117:184-187(2003).
RN [54]
RP VARIANT RTT VAL-100.
RX PubMed=12966522; DOI=10.1002/ajmg.a.20320;
RA Hammer S., Dorrani N., Hartiala J., Stein S., Schanen N.C.;
RT "Rett syndrome in a 47,XXX patient with a de novo MECP2 mutation.";
RL Am. J. Med. Genet. A 122:223-226(2003).
RN [55]
RP VARIANTS RTT GLN-10; PRO-128; CYS-133; ARG-152; MET-158 AND CYS-306.
RX PubMed=12966523; DOI=10.1002/ajmg.a.20321;
RA Smeets E., Schollen E., Moog U., Matthijs G., Herbergs J., Smeets H.,
RA Curfs L., Schrander-Stumpel C., Fryns J.-P.;
RT "Rett syndrome in adolescent and adult females: clinical and molecular
RT genetic findings.";
RL Am. J. Med. Genet. A 122:227-233(2003).
RN [56]
RP VARIANT MRXS13 LEU-225.
RX PubMed=12615169; DOI=10.1016/s1090-3798(02)00134-4;
RA Moog U., Smeets E.E.J., van Roozendaal K.E.P., Schoenmakers S.,
RA Herbergs J., Schoonbrood-Lenssen A.M.J., Schrander-Stumpel C.T.R.M.;
RT "Neurodevelopmental disorders in males related to the gene causing Rett
RT syndrome in females (MECP2).";
RL Eur. J. Paediatr. Neurol. 7:5-12(2003).
RN [57]
RP INVOLVEMENT IN AUTSX3.
RX PubMed=12770674; DOI=10.1016/s0887-8994(02)00624-0;
RA Carney R.M., Wolpert C.M., Ravan S.A., Shahbazian M., Ashley-Koch A.,
RA Cuccaro M.L., Vance J.M., Pericak-Vance M.A.;
RT "Identification of MeCP2 mutations in a series of females with autistic
RT disorder.";
RL Pediatr. Neurol. 28:205-211(2003).
RN [58]
RP VARIANTS RTT ARG-100; VAL-100; TRP-106; CYS-133; ARG-152; ALA-158; MET-158;
RP VAL-161; CYS-306 AND HIS-306.
RX PubMed=15057977; DOI=10.1002/ajmg.a.20571;
RA Schanen C., Houwink E.J.F., Dorrani N., Lane J., Everett R., Feng A.,
RA Cantor R.M., Percy A.;
RT "Phenotypic manifestations of MECP2 mutations in classical and atypical
RT Rett syndrome.";
RL Am. J. Med. Genet. A 126:129-140(2004).
RN [59]
RP INVOLVEMENT IN MRXSL.
RX PubMed=16080119; DOI=10.1086/444549;
RA Van Esch H., Bauters M., Ignatius J., Jansen M., Raynaud M., Hollanders K.,
RA Lugtenberg D., Bienvenu T., Jensen L.R., Gecz J., Moraine C., Marynen P.,
RA Fryns J.-P., Froyen G.;
RT "Duplication of the MECP2 region is a frequent cause of severe mental
RT retardation and progressive neurological symptoms in males.";
RL Am. J. Hum. Genet. 77:442-453(2005).
RN [60]
RP VARIANT MRXS13 SER-322.
RX PubMed=16966553; DOI=10.1212/01.wnl.0000233990.87889.15;
RA Ventura P., Galluzzi R., Bacca S.M., Giorda R., Massagli A.;
RT "A novel familial MECP2 mutation in a young boy: clinical and molecular
RT findings.";
RL Neurology 67:867-868(2006).
RN [61]
RP CHARACTERIZATION OF VARIANT RTT CYS-133, AND CHARACTERIZATION OF VARIANT
RP MRXS13 VAL-140.
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 [62]
RP VARIANT RTT 270-ARG--SER-486 DEL.
RX PubMed=23662938; DOI=10.1111/epi.12203;
RA Kodera H., Kato M., Nord A.S., Walsh T., Lee M., Yamanaka G., Tohyama J.,
RA Nakamura K., Nakagawa E., Ikeda T., Ben-Zeev B., Lev D., Lerman-Sagie T.,
RA Straussberg R., Tanabe S., Ueda K., Amamoto M., Ohta S., Nonoda Y.,
RA Nishiyama K., Tsurusaki Y., Nakashima M., Miyake N., Hayasaka K.,
RA King M.C., Matsumoto N., Saitsu H.;
RT "Targeted capture and sequencing for detection of mutations causing early
RT onset epileptic encephalopathy.";
RL Epilepsia 54:1262-1269(2013).
RN [63]
RP VARIANT RTT CYS-133.
RX PubMed=25818041; DOI=10.1111/epi.12954;
RA Mercimek-Mahmutoglu S., Patel J., Cordeiro D., Hewson S., Callen D.,
RA Donner E.J., Hahn C.D., Kannu P., Kobayashi J., Minassian B.A., Moharir M.,
RA Siriwardena K., Weiss S.K., Weksberg R., Snead O.C. III;
RT "Diagnostic yield of genetic testing in epileptic encephalopathy in
RT childhood.";
RL Epilepsia 56:707-716(2015).
RN [64]
RP VARIANTS RTT 270-ARG--SER-486 DEL AND CYS-306.
RX PubMed=26993267; DOI=10.1136/jmedgenet-2015-103263;
RA Trump N., McTague A., Brittain H., Papandreou A., Meyer E., Ngoh A.,
RA Palmer R., Morrogh D., Boustred C., Hurst J.A., Jenkins L., Kurian M.A.,
RA Scott R.H.;
RT "Improving diagnosis and broadening the phenotypes in early-onset seizure
RT and severe developmental delay disorders through gene panel analysis.";
RL J. Med. Genet. 53:310-317(2016).
RN [65]
RP VARIANT RTT TRP-344.
RX PubMed=28709814; DOI=10.1016/j.braindev.2017.06.003;
RA Liang J.S., Lin L.J., Yang M.T., Wang J.S., Lu J.F.;
RT "The therapeutic implication of a novel SCN2A mutation associated early-
RT onset epileptic encephalopathy with Rett-like features.";
RL Brain Dev. 39:877-881(2017).
RN [66]
RP VARIANT RTT CYS-133, AND VARIANT ASN-305.
RX PubMed=27864847; DOI=10.1002/humu.23149;
RG Clinical Study Group;
RA Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
RA Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D., Bigoni S.,
RA Barba C., Mari F., Montomoli M., Pisano T., Rosati A., Guerrini R.;
RT "Diagnostic targeted resequencing in 349 patients with drug-resistant
RT pediatric epilepsies identifies causative mutations in 30 different
RT genes.";
RL Hum. Mutat. 38:216-225(2017).
RN [67]
RP VARIANTS RTT ARG-305 AND CYS-306, CHARACTERIZATION OF VARIANTS RTT ARG-305
RP AND CYS-306, SUBCELLULAR LOCATION, AND INTERACTION WITH TBL1XR1 AND TBL1X.
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 SIN3A.
CC Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-
CC containing DNA, with a preference for 5-methylcytosine (5mC).
CC {ECO:0000250|UniProtKB:Q9Z2D6}.
CC -!- SUBUNIT: Interacts with FNBP3 (By similarity). Interacts with CDKL5
CC (PubMed:15917271). Interacts with ATRX; MECP2 recruits ATRX to
CC pericentric heterochromatin in neuronal cells (By similarity).
CC Interacts with NCOR2 (By similarity). Interacts with TBL1XR1; bridges
CC interaction between MECP2 and NCOR1 (PubMed:28348241). Interacts with
CC TBL1X; recruits TBL1X to the heterochromatin foci (PubMed:28348241).
CC {ECO:0000250|UniProtKB:Q9Z2D6, ECO:0000269|PubMed:15917271,
CC ECO:0000269|PubMed:28348241}.
CC -!- INTERACTION:
CC P51608; Q6PCB6: ABHD17C; NbExp=3; IntAct=EBI-1189067, EBI-22011868;
CC P51608; P63010-2: AP2B1; NbExp=3; IntAct=EBI-1189067, EBI-11529439;
CC P51608; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-1189067, EBI-14199987;
CC P51608; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-1189067, EBI-718459;
CC P51608; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-1189067, EBI-2837444;
CC P51608; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-1189067, EBI-350590;
CC P51608; P35222: CTNNB1; NbExp=3; IntAct=EBI-1189067, EBI-491549;
CC P51608; Q7L576: CYFIP1; NbExp=3; IntAct=EBI-1189067, EBI-1048143;
CC P51608; Q9UHI6: DDX20; NbExp=3; IntAct=EBI-1189067, EBI-347658;
CC P51608; O75398: DEAF1; NbExp=3; IntAct=EBI-1189067, EBI-718185;
CC P51608; Q99504: EYA3; NbExp=3; IntAct=EBI-1189067, EBI-9089567;
CC P51608; Q6PIV2: FOXR1; NbExp=3; IntAct=EBI-1189067, EBI-10253815;
CC P51608; Q9H2X6: HIPK2; NbExp=2; IntAct=EBI-1189067, EBI-348345;
CC P51608; P04792: HSPB1; NbExp=3; IntAct=EBI-1189067, EBI-352682;
CC P51608; P42858: HTT; NbExp=18; IntAct=EBI-1189067, EBI-466029;
CC P51608; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-1189067, EBI-21911304;
CC P51608; Q92993-2: KAT5; NbExp=3; IntAct=EBI-1189067, EBI-20795332;
CC P51608; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-1189067, EBI-714379;
CC P51608; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-1189067, EBI-10261141;
CC P51608; P07948: LYN; NbExp=3; IntAct=EBI-1189067, EBI-79452;
CC P51608; P61244: MAX; NbExp=2; IntAct=EBI-1189067, EBI-751711;
CC P51608; Q8TDB4: MGARP; NbExp=3; IntAct=EBI-1189067, EBI-4397720;
CC P51608; O43196-2: MSH5; NbExp=3; IntAct=EBI-1189067, EBI-25844576;
CC P51608; Q99457: NAP1L3; NbExp=3; IntAct=EBI-1189067, EBI-8645631;
CC P51608; P07196: NEFL; NbExp=3; IntAct=EBI-1189067, EBI-475646;
CC P51608; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1189067, EBI-748974;
CC P51608; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-1189067, EBI-1058491;
CC P51608; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-1189067, EBI-25830200;
CC P51608; O75925: PIAS1; NbExp=3; IntAct=EBI-1189067, EBI-629434;
CC P51608; P60891: PRPS1; NbExp=3; IntAct=EBI-1189067, EBI-749195;
CC P51608; P57729: RAB38; NbExp=3; IntAct=EBI-1189067, EBI-6552718;
CC P51608; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-1189067, EBI-438710;
CC P51608; Q8WWW0-2: RASSF5; NbExp=3; IntAct=EBI-1189067, EBI-960502;
CC P51608; Q9ULX5: RNF112; NbExp=3; IntAct=EBI-1189067, EBI-25829984;
CC P51608; Q96D59: RNF183; NbExp=3; IntAct=EBI-1189067, EBI-743938;
CC P51608; Q96ST3: SIN3A; NbExp=2; IntAct=EBI-1189067, EBI-347218;
CC P51608; P51531: SMARCA2; NbExp=4; IntAct=EBI-1189067, EBI-679562;
CC P51608; Q12824: SMARCB1; NbExp=3; IntAct=EBI-1189067, EBI-358419;
CC P51608; Q16637-3: SMN2; NbExp=3; IntAct=EBI-1189067, EBI-395447;
CC P51608; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-1189067, EBI-10696971;
CC P51608; O75558: STX11; NbExp=3; IntAct=EBI-1189067, EBI-714135;
CC P51608; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-1189067, EBI-11525489;
CC P51608; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-1189067, EBI-10259086;
CC P51608; P10599: TXN; NbExp=3; IntAct=EBI-1189067, EBI-594644;
CC P51608; O76024: WFS1; NbExp=3; IntAct=EBI-1189067, EBI-720609;
CC P51608; Q9QZR5: Hipk2; Xeno; NbExp=3; IntAct=EBI-1189067, EBI-366905;
CC P51608; Q60974: Ncor1; Xeno; NbExp=4; IntAct=EBI-1189067, EBI-349004;
CC P51608; Q9WU42: Ncor2; Xeno; NbExp=4; IntAct=EBI-1189067, EBI-6673326;
CC P51608; Q9QXE7: Tbl1x; Xeno; NbExp=3; IntAct=EBI-1189067, EBI-8821270;
CC P51608; Q8BHJ5: Tbl1xr1; Xeno; NbExp=4; IntAct=EBI-1189067, EBI-1216384;
CC P51608-1; O88508: Dnmt3a; Xeno; NbExp=10; IntAct=EBI-26687319, EBI-995154;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Z2D6}.
CC Note=Colocalized with methyl-CpG in the genome. Colocalized with TBL1X
CC to the heterochromatin foci. {ECO:0000269|PubMed:28348241}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=Beta;
CC IsoId=P51608-1; Sequence=Displayed;
CC Name=B; Synonyms=Alpha;
CC IsoId=P51608-2; Sequence=VSP_022948;
CC -!- TISSUE SPECIFICITY: Present in all adult somatic tissues tested.
CC -!- PTM: Phosphorylated on Ser-423 in brain upon synaptic activity, which
CC attenuates its repressor activity and seems to regulate dendritic
CC growth and spine maturation. {ECO:0000250}.
CC -!- DISEASE: Angelman syndrome (AS) [MIM:105830]: A neurodevelopmental
CC disorder characterized by severe motor and intellectual retardation,
CC ataxia, frequent jerky limb movements and flapping of the arms and
CC hands, hypotonia, seizures, absence of speech, frequent smiling and
CC episodes of paroxysmal laughter, open-mouthed expression revealing the
CC tongue. {ECO:0000269|PubMed:11283202}. Note=The disease may be caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic 13
CC (MRXS13) [MIM:300055]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC MRXS13 patients manifest intellectual disability associated with other
CC variable features such as spasticity, episodes of manic depressive
CC psychosis, increased tone and macroorchidism.
CC {ECO:0000269|PubMed:10986043, ECO:0000269|PubMed:11007980,
CC ECO:0000269|PubMed:11309367, ECO:0000269|PubMed:11805248,
CC ECO:0000269|PubMed:11885030, ECO:0000269|PubMed:12161600,
CC ECO:0000269|PubMed:12325019, ECO:0000269|PubMed:12615169,
CC ECO:0000269|PubMed:16966553, ECO:0000269|PubMed:17296936}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Rett syndrome (RTT) [MIM:312750]: An X-linked dominant
CC neurodevelopmental disorder, and one of the most common causes of
CC intellectual disability in females. Patients appear to develop normally
CC until 6 to 18 months of age, then gradually lose speech and purposeful
CC hand movements, and develop microcephaly, seizures, autism, ataxia,
CC intellectual disability and stereotypic hand movements. After initial
CC regression, the condition stabilizes and patients usually survive into
CC adulthood. {ECO:0000269|PubMed:10508514, ECO:0000269|PubMed:10577905,
CC ECO:0000269|PubMed:10745042, ECO:0000269|PubMed:10767337,
CC ECO:0000269|PubMed:10814719, ECO:0000269|PubMed:10944854,
CC ECO:0000269|PubMed:10991688, ECO:0000269|PubMed:10991689,
CC ECO:0000269|PubMed:11055898, ECO:0000269|PubMed:11241840,
CC ECO:0000269|PubMed:11269512, ECO:0000269|PubMed:11283202,
CC ECO:0000269|PubMed:11376998, ECO:0000269|PubMed:11402105,
CC ECO:0000269|PubMed:11706982, ECO:0000269|PubMed:11738883,
CC ECO:0000269|PubMed:12161600, ECO:0000269|PubMed:12567420,
CC ECO:0000269|PubMed:12966522, ECO:0000269|PubMed:12966523,
CC ECO:0000269|PubMed:15034579, ECO:0000269|PubMed:15057977,
CC ECO:0000269|PubMed:17296936, ECO:0000269|PubMed:23662938,
CC ECO:0000269|PubMed:25818041, ECO:0000269|PubMed:26993267,
CC ECO:0000269|PubMed:27864847, ECO:0000269|PubMed:28348241,
CC ECO:0000269|PubMed:28709814}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Autism, X-linked 3 (AUTSX3) [MIM:300496]: A complex
CC multifactorial, pervasive developmental disorder characterized by
CC impairments in reciprocal social interaction and communication,
CC restricted and stereotyped patterns of interests and activities, and
CC the presence of developmental abnormalities by 3 years of age. Most
CC individuals with autism also manifest moderate intellectual disability.
CC {ECO:0000269|PubMed:12770674}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Encephalopathy, neonatal severe, due to MECP2 mutations (ENS-
CC MECP2) [MIM:300673]: A neurodevelopmental disorder characterized by
CC severe neonatal encephalopathy, developmental delay, intellectual
CC disability, microcephaly, seizures. Additional features include
CC respiratory insufficiency and central hypoventilation, gastroesophageal
CC reflux, axial hypotonia, hyperreflexia and dyskinetic movements.
CC {ECO:0000269|PubMed:11238684}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. The MECP2 gene is mutated
CC in Rett syndrome, a severe neurodevelopmental disorder that almost
CC always occurs in females. Although it was first thought that MECP2
CC mutations causing Rett syndrome were lethal in males, later reports
CC identified a severe neonatal encephalopathy in surviving male sibs of
CC patients with Rett syndrome. Additional reports have confirmed a severe
CC phenotype in males with Rett syndrome-associated MECP2 mutations.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic, Lubs
CC type (MRXSL) [MIM:300260]: A disorder characterized by significantly
CC below average general intellectual functioning associated with
CC impairments in adaptive behavior and manifested during the
CC developmental period. MRXSL patients manifest intellectual disability
CC associated with variable features. They include swallowing dysfunction
CC and gastroesophageal reflux with secondary recurrent respiratory
CC infections, hypotonia, mild myopathy and characteristic facies such as
CC downslanting palpebral fissures, hypertelorism and a short nose with a
CC low nasal bridge. {ECO:0000269|PubMed:16080119}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC Increased dosage of MECP2 due to gene duplication appears to be
CC responsible for the intellectual disability phenotype.
CC -!- MISCELLANEOUS: [Isoform B]: Ten times higher expression levels than
CC isoform A in brain. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97991.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=RettBASE; Note=IRSA MECP2 variation database;
CC URL="http://mecp2.chw.edu.au/";
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DR EMBL; L37298; AAC32737.1; -; mRNA.
DR EMBL; X99686; CAA68001.1; -; mRNA.
DR EMBL; AJ132917; CAB46446.1; -; mRNA.
DR EMBL; AF158180; AAF33023.1; -; mRNA.
DR EMBL; Y12643; CAA73190.1; -; mRNA.
DR EMBL; AY541280; AAS55455.1; -; mRNA.
DR EMBL; BX538060; CAD97991.1; ALT_INIT; mRNA.
DR EMBL; AF030876; AAC08757.1; -; Genomic_DNA.
DR EMBL; BC011612; AAH11612.1; -; mRNA.
DR EMBL; X89430; CAA61599.1; -; mRNA.
DR EMBL; X94628; CAA64331.1; -; Genomic_DNA.
DR CCDS; CCDS14741.1; -. [P51608-1]
DR CCDS; CCDS48193.1; -. [P51608-2]
DR RefSeq; NP_001104262.1; NM_001110792.1. [P51608-2]
DR RefSeq; NP_001303266.1; NM_001316337.1.
DR RefSeq; NP_004983.1; NM_004992.3. [P51608-1]
DR PDB; 1QK9; NMR; -; A=77-166.
DR PDB; 3C2I; X-ray; 2.50 A; A=77-167.
DR PDB; 5BT2; X-ray; 2.20 A; A=77-167.
DR PDB; 6C1Y; X-ray; 2.30 A; A/B=80-164.
DR PDB; 6OGJ; X-ray; 1.80 A; A/B=77-166.
DR PDB; 6OGK; X-ray; 1.65 A; A=77-167.
DR PDB; 6YWW; X-ray; 2.10 A; A=77-161.
DR PDBsum; 1QK9; -.
DR PDBsum; 3C2I; -.
DR PDBsum; 5BT2; -.
DR PDBsum; 6C1Y; -.
DR PDBsum; 6OGJ; -.
DR PDBsum; 6OGK; -.
DR PDBsum; 6YWW; -.
DR AlphaFoldDB; P51608; -.
DR BMRB; P51608; -.
DR SMR; P51608; -.
DR BioGRID; 110368; 239.
DR CORUM; P51608; -.
DR DIP; DIP-39983N; -.
DR IntAct; P51608; 189.
DR MINT; P51608; -.
DR STRING; 9606.ENSP00000395535; -.
DR BindingDB; P51608; -.
DR ChEMBL; CHEMBL3638346; -.
DR GlyGen; P51608; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P51608; -.
DR MetOSite; P51608; -.
DR PhosphoSitePlus; P51608; -.
DR BioMuta; MECP2; -.
DR DMDM; 1708973; -.
DR EPD; P51608; -.
DR jPOST; P51608; -.
DR MassIVE; P51608; -.
DR MaxQB; P51608; -.
DR PaxDb; P51608; -.
DR PeptideAtlas; P51608; -.
DR PRIDE; P51608; -.
DR ProteomicsDB; 56344; -. [P51608-1]
DR ProteomicsDB; 56345; -. [P51608-2]
DR ABCD; P51608; 1 sequenced antibody.
DR Antibodypedia; 394; 875 antibodies from 48 providers.
DR DNASU; 4204; -.
DR Ensembl; ENST00000303391.11; ENSP00000301948.6; ENSG00000169057.24. [P51608-1]
DR Ensembl; ENST00000453960.7; ENSP00000395535.2; ENSG00000169057.24. [P51608-2]
DR GeneID; 4204; -.
DR KEGG; hsa:4204; -.
DR MANE-Select; ENST00000453960.7; ENSP00000395535.2; NM_001110792.2; NP_001104262.1. [P51608-2]
DR UCSC; uc004fjv.3; human. [P51608-1]
DR CTD; 4204; -.
DR DisGeNET; 4204; -.
DR GeneCards; MECP2; -.
DR GeneReviews; MECP2; -.
DR HGNC; HGNC:6990; MECP2.
DR HPA; ENSG00000169057; Low tissue specificity.
DR MalaCards; MECP2; -.
DR MIM; 105830; phenotype.
DR MIM; 300005; gene.
DR MIM; 300055; phenotype.
DR MIM; 300260; phenotype.
DR MIM; 300496; phenotype.
DR MIM; 300673; phenotype.
DR MIM; 312750; phenotype.
DR neXtProt; NX_P51608; -.
DR OpenTargets; ENSG00000169057; -.
DR Orphanet; 3095; Atypical Rett syndrome.
DR Orphanet; 106; NON RARE IN EUROPE: Autism.
DR Orphanet; 1762; Proximal Xq28 duplication syndrome.
DR Orphanet; 778; Rett syndrome.
DR Orphanet; 209370; Severe neonatal-onset encephalopathy with microcephaly.
DR Orphanet; 536; Systemic lupus erythematosus.
DR Orphanet; 3077; X-linked intellectual disability-psychosis-macroorchidism syndrome.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA30729; -.
DR VEuPathDB; HostDB:ENSG00000169057; -.
DR eggNOG; KOG4161; Eukaryota.
DR GeneTree; ENSGT00530000063687; -.
DR HOGENOM; CLU_045066_0_0_1; -.
DR InParanoid; P51608; -.
DR OMA; YDVYLIX; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; P51608; -.
DR TreeFam; TF332974; -.
DR PathwayCommons; P51608; -.
DR Reactome; R-HSA-8986944; Transcriptional Regulation by MECP2.
DR Reactome; R-HSA-9022534; Loss of MECP2 binding ability to 5hmC-DNA.
DR Reactome; R-HSA-9022535; Loss of phosphorylation of MECP2 at T308.
DR Reactome; R-HSA-9022537; Loss of MECP2 binding ability to the NCoR/SMRT complex.
DR Reactome; R-HSA-9022538; Loss of MECP2 binding ability to 5mC-DNA.
DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR Reactome; R-HSA-9022702; MECP2 regulates transcription of neuronal ligands.
DR Reactome; R-HSA-9022707; MECP2 regulates transcription factors.
DR Reactome; R-HSA-9022927; MECP2 regulates transcription of genes involved in GABA signaling.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR SignaLink; P51608; -.
DR SIGNOR; P51608; -.
DR BioGRID-ORCS; 4204; 7 hits in 721 CRISPR screens.
DR ChiTaRS; MECP2; human.
DR EvolutionaryTrace; P51608; -.
DR GeneWiki; MECP2; -.
DR GenomeRNAi; 4204; -.
DR Pharos; P51608; Tchem.
DR PRO; PR:P51608; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51608; protein.
DR Bgee; ENSG00000169057; Expressed in paraflocculus and 184 other tissues.
DR ExpressionAtlas; P51608; baseline and differential.
DR Genevisible; P51608; HS.
DR GO; GO:0005813; C:centrosome; IMP:CAFA.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IMP:MGI.
DR GO; GO:0008327; F:methyl-CpG binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0035197; F:siRNA binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:ARUK-UCL.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
DR GO; GO:0032048; P:cardiolipin metabolic process; IEA:Ensembl.
DR GO; GO:0050432; P:catecholamine secretion; IEA:Ensembl.
DR GO; GO:0006576; P:cellular biogenic amine metabolic process; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
DR GO; GO:0031507; P:heterochromatin assembly; IEA:Ensembl.
DR GO; GO:0016573; P:histone acetylation; IEA:Ensembl.
DR GO; GO:0016571; P:histone methylation; IEA:Ensembl.
DR GO; GO:0006020; P:inositol metabolic process; IEA:Ensembl.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:CAFA.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:2000820; P:negative regulation of transcription from RNA polymerase II promoter involved in smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0001976; P:nervous system process involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:CAFA.
DR GO; GO:1905643; P:positive regulation of DNA methylation; IDA:BHF-UCL.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:CAFA.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR GO; GO:1900114; P:positive regulation of histone H3-K9 trimethylation; IEA:Ensembl.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; IMP:CAFA.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0019230; P:proprioception; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:MGI.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IEA:Ensembl.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0051707; P:response to other organism; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR GO; GO:0001964; P:startle response; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR GO; GO:0099191; P:trans-synaptic signaling by BDNF; IEA:Ensembl.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR DisProt; DP00539; -.
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; Autism;
KW Autism spectrum disorder; Chromosomal rearrangement; Disease variant;
KW DNA-binding; Intellectual disability; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..486
FT /note="Methyl-CpG-binding protein 2"
FT /id="PRO_0000096345"
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..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..309
FT /note="Interaction with NCOR2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT REGION 285..309
FT /note="Interaction with TBL1XR1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT REGION 324..486
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 378..400
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..486
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:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 162
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..9
FT /note="MVAGMLGLR -> MAAAAAAAPSGGGGGGEEERL (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15034579,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_022948"
FT VARIANT 10
FT /note="E -> Q (in RTT; dbSNP:rs61754421)"
FT /evidence="ECO:0000269|PubMed:12966523"
FT /id="VAR_018180"
FT VARIANT 86
FT /note="S -> C (in dbSNP:rs61754445)"
FT /evidence="ECO:0000269|PubMed:11055898"
FT /id="VAR_018181"
FT VARIANT 97
FT /note="D -> E (in RTT; dbSNP:rs61754449)"
FT /evidence="ECO:0000269|PubMed:10745042"
FT /id="VAR_023552"
FT VARIANT 97
FT /note="D -> Y (in RTT; dbSNP:rs61754448)"
FT /evidence="ECO:0000269|PubMed:11402105"
FT /id="VAR_018182"
FT VARIANT 100
FT /note="L -> R (in RTT; dbSNP:rs61754451)"
FT /evidence="ECO:0000269|PubMed:15057977"
FT /id="VAR_023553"
FT VARIANT 100
FT /note="L -> V (in RTT; dbSNP:rs28935168)"
FT /evidence="ECO:0000269|PubMed:11055898,
FT ECO:0000269|PubMed:12966522, ECO:0000269|PubMed:15057977"
FT /id="VAR_017462"
FT VARIANT 101
FT /note="P -> H (in RTT; dbSNP:rs61754453)"
FT /evidence="ECO:0000269|PubMed:10767337"
FT /id="VAR_018183"
FT VARIANT 101
FT /note="P -> L (in RTT; dbSNP:rs61754453)"
FT /evidence="ECO:0000269|PubMed:10767337"
FT /id="VAR_018184"
FT VARIANT 101
FT /note="P -> R (in RTT; also in a patient with Angelman
FT syndrome and some typical RTT features; dbSNP:rs61754453)"
FT /evidence="ECO:0000269|PubMed:10991689,
FT ECO:0000269|PubMed:11283202"
FT /id="VAR_010276"
FT VARIANT 101
FT /note="P -> S (in RTT; dbSNP:rs61754452)"
FT /evidence="ECO:0000269|PubMed:11269512"
FT /id="VAR_023554"
FT VARIANT 101
FT /note="P -> T (in RTT)"
FT /evidence="ECO:0000269|PubMed:10767337"
FT /id="VAR_018185"
FT VARIANT 106
FT /note="R -> Q (in RTT; dbSNP:rs61754457)"
FT /evidence="ECO:0000269|PubMed:10814719,
FT ECO:0000269|PubMed:11055898"
FT /id="VAR_018186"
FT VARIANT 106
FT /note="R -> W (in RTT; dbSNP:rs28934907)"
FT /evidence="ECO:0000269|PubMed:10508514,
FT ECO:0000269|PubMed:10577905, ECO:0000269|PubMed:10745042,
FT ECO:0000269|PubMed:10767337, ECO:0000269|PubMed:10991688,
FT ECO:0000269|PubMed:10991689, ECO:0000269|PubMed:11055898,
FT ECO:0000269|PubMed:11241840, ECO:0000269|PubMed:11269512,
FT ECO:0000269|PubMed:11402105, ECO:0000269|PubMed:11738883,
FT ECO:0000269|PubMed:15057977"
FT /id="VAR_010272"
FT VARIANT 111
FT /note="R -> G (in RTT; dbSNP:rs61754459)"
FT /evidence="ECO:0000269|PubMed:11241840"
FT /id="VAR_018187"
FT VARIANT 120
FT /note="Y -> D (in RTT; dbSNP:rs267608454)"
FT /evidence="ECO:0000269|PubMed:11376998"
FT /id="VAR_023555"
FT VARIANT 124
FT /note="L -> F (in RTT; dbSNP:rs61755763)"
FT /evidence="ECO:0000269|PubMed:10991688"
FT /id="VAR_010277"
FT VARIANT 128
FT /note="Q -> P (in RTT; dbSNP:rs61748383)"
FT /evidence="ECO:0000269|PubMed:12966523"
FT /id="VAR_018188"
FT VARIANT 133
FT /note="R -> C (in RTT; impairs interaction with ATRX and
FT abolishes ATRX recruitment to heterochromatin;
FT dbSNP:rs28934904)"
FT /evidence="ECO:0000269|PubMed:10508514,
FT ECO:0000269|PubMed:10577905, ECO:0000269|PubMed:10745042,
FT ECO:0000269|PubMed:10767337, ECO:0000269|PubMed:10991688,
FT ECO:0000269|PubMed:11055898, ECO:0000269|PubMed:11241840,
FT ECO:0000269|PubMed:11269512, ECO:0000269|PubMed:11376998,
FT ECO:0000269|PubMed:11402105, ECO:0000269|PubMed:12567420,
FT ECO:0000269|PubMed:12966523, ECO:0000269|PubMed:15057977,
FT ECO:0000269|PubMed:17296936, ECO:0000269|PubMed:25818041,
FT ECO:0000269|PubMed:27864847"
FT /id="VAR_010273"
FT VARIANT 133
FT /note="R -> H (in RTT; dbSNP:rs61748389)"
FT /evidence="ECO:0000269|PubMed:11402105,
FT ECO:0000269|PubMed:11706982"
FT /id="VAR_018189"
FT VARIANT 134
FT /note="S -> C (in RTT; dbSNP:rs61748390)"
FT /evidence="ECO:0000269|PubMed:10767337,
FT ECO:0000269|PubMed:10991688, ECO:0000269|PubMed:11269512,
FT ECO:0000269|PubMed:11738883"
FT /id="VAR_010278"
FT VARIANT 135
FT /note="K -> E (in RTT; dbSNP:rs61748391)"
FT /evidence="ECO:0000269|PubMed:11241840"
FT /id="VAR_018190"
FT VARIANT 137
FT /note="E -> G (in MRXS13; dbSNP:rs61748392)"
FT /evidence="ECO:0000269|PubMed:11309367"
FT /id="VAR_017581"
FT VARIANT 140
FT /note="A -> V (in MRXS13; impairs interaction with ATRX and
FT abolishes ATRX recruitment to heterochromatin;
FT dbSNP:rs28934908)"
FT /evidence="ECO:0000269|PubMed:11007980,
FT ECO:0000269|PubMed:11309367, ECO:0000269|PubMed:11805248,
FT ECO:0000269|PubMed:11885030, ECO:0000269|PubMed:12161600,
FT ECO:0000269|PubMed:12325019, ECO:0000269|PubMed:17296936"
FT /id="VAR_010279"
FT VARIANT 152
FT /note="P -> R (in RTT; dbSNP:rs61748404)"
FT /evidence="ECO:0000269|PubMed:10767337,
FT ECO:0000269|PubMed:10991688, ECO:0000269|PubMed:11055898,
FT ECO:0000269|PubMed:11241840, ECO:0000269|PubMed:11269512,
FT ECO:0000269|PubMed:11402105, ECO:0000269|PubMed:11738883,
FT ECO:0000269|PubMed:12966523, ECO:0000269|PubMed:15057977"
FT /id="VAR_010280"
FT VARIANT 155
FT /note="F -> I (in RTT; dbSNP:rs61748406)"
FT /evidence="ECO:0000269|PubMed:10745042"
FT /id="VAR_023556"
FT VARIANT 155
FT /note="F -> S (in RTT; dbSNP:rs28934905)"
FT /evidence="ECO:0000269|PubMed:10508514,
FT ECO:0000269|PubMed:10577905, ECO:0000269|PubMed:11055898"
FT /id="VAR_010274"
FT VARIANT 156
FT /note="D -> G (in RTT; dbSNP:rs61748407)"
FT /evidence="ECO:0000269|PubMed:11241840"
FT /id="VAR_018191"
FT VARIANT 158
FT /note="T -> A (in RTT; dbSNP:rs61748411)"
FT /evidence="ECO:0000269|PubMed:11269512,
FT ECO:0000269|PubMed:15057977"
FT /id="VAR_023557"
FT VARIANT 158
FT /note="T -> M (in RTT; dbSNP:rs28934906)"
FT /evidence="ECO:0000269|PubMed:10508514,
FT ECO:0000269|PubMed:10577905, ECO:0000269|PubMed:10745042,
FT ECO:0000269|PubMed:10767337, ECO:0000269|PubMed:10814719,
FT ECO:0000269|PubMed:10944854, ECO:0000269|PubMed:10991688,
FT ECO:0000269|PubMed:10991689, ECO:0000269|PubMed:11055898,
FT ECO:0000269|PubMed:11241840, ECO:0000269|PubMed:11269512,
FT ECO:0000269|PubMed:11376998, ECO:0000269|PubMed:11402105,
FT ECO:0000269|PubMed:11738883, ECO:0000269|PubMed:12567420,
FT ECO:0000269|PubMed:12966523, ECO:0000269|PubMed:15057977"
FT /id="VAR_010275"
FT VARIANT 161
FT /note="G -> V (in RTT; dbSNP:rs61748417)"
FT /evidence="ECO:0000269|PubMed:15057977"
FT /id="VAR_023558"
FT VARIANT 167
FT /note="R -> W (in MRXS13; dbSNP:rs61748420)"
FT /evidence="ECO:0000269|PubMed:11309367"
FT /id="VAR_018192"
FT VARIANT 181
FT /note="A -> V (in dbSNP:rs61749705)"
FT /evidence="ECO:0000269|PubMed:12384770"
FT /id="VAR_018193"
FT VARIANT 196
FT /note="T -> S (in dbSNP:rs61749713)"
FT /evidence="ECO:0000269|PubMed:12111644"
FT /id="VAR_018194"
FT VARIANT 197
FT /note="T -> M (in dbSNP:rs61749714)"
FT /evidence="ECO:0000269|PubMed:11402105,
FT ECO:0000269|PubMed:12161600"
FT /id="VAR_018195"
FT VARIANT 201
FT /note="A -> V (in dbSNP:rs61748381)"
FT /evidence="ECO:0000269|PubMed:10944854,
FT ECO:0000269|PubMed:11738883"
FT /id="VAR_010281"
FT VARIANT 203
FT /note="T -> M (in dbSNP:rs61749720)"
FT /evidence="ECO:0000269|PubMed:11007980,
FT ECO:0000269|PubMed:11055898"
FT /id="VAR_018196"
FT VARIANT 210
FT /note="K -> I (in RTT; dbSNP:rs61749730)"
FT /evidence="ECO:0000269|PubMed:11241840"
FT /id="VAR_018197"
FT VARIANT 225
FT /note="P -> L (in MRXS13; dbSNP:rs61749715)"
FT /evidence="ECO:0000269|PubMed:12615169"
FT /id="VAR_037664"
FT VARIANT 225
FT /note="P -> R (in RTT; dbSNP:rs61749715)"
FT /evidence="ECO:0000269|PubMed:10767337"
FT /id="VAR_018198"
FT VARIANT 228
FT /note="T -> S (in dbSNP:rs61749738)"
FT /evidence="ECO:0000269|PubMed:12111644"
FT /id="VAR_018199"
FT VARIANT 229
FT /note="S -> L (in dbSNP:rs61749739)"
FT /evidence="ECO:0000269|PubMed:10767337"
FT /id="VAR_018200"
FT VARIANT 232
FT /note="G -> A (in dbSNP:rs61748422)"
FT /evidence="ECO:0000269|PubMed:10944854"
FT /id="VAR_018201"
FT VARIANT 251
FT /note="P -> L (in dbSNP:rs61750229)"
FT /evidence="ECO:0000269|PubMed:10944854"
FT /id="VAR_018202"
FT VARIANT 270..486
FT /note="Missing (in RTT)"
FT /evidence="ECO:0000269|PubMed:23662938,
FT ECO:0000269|PubMed:26993267"
FT /id="VAR_078720"
FT VARIANT 284
FT /note="K -> E (in MRXS13; dbSNP:rs61750255)"
FT /evidence="ECO:0000269|PubMed:11309367"
FT /id="VAR_018203"
FT VARIANT 287
FT /note="A -> P (in dbSNP:rs61750257)"
FT /evidence="ECO:0000269|PubMed:11055898"
FT /id="VAR_018204"
FT VARIANT 291
FT /note="S -> A (in dbSNP:rs61751360)"
FT /evidence="ECO:0000269|PubMed:11055898"
FT /id="VAR_018205"
FT VARIANT 302
FT /note="P -> A (in RTT; dbSNP:rs61751373)"
FT /evidence="ECO:0000269|PubMed:11738883"
FT /id="VAR_018206"
FT VARIANT 302
FT /note="P -> H (in RTT; dbSNP:rs61749723)"
FT /evidence="ECO:0000269|PubMed:10944854"
FT /id="VAR_018207"
FT VARIANT 302
FT /note="P -> L (in RTT; dbSNP:rs61749723)"
FT /evidence="ECO:0000269|PubMed:10767337"
FT /id="VAR_018208"
FT VARIANT 302
FT /note="P -> R (in RTT; dbSNP:rs61749723)"
FT /evidence="ECO:0000269|PubMed:10814719,
FT ECO:0000269|PubMed:11241840"
FT /id="VAR_018209"
FT VARIANT 305
FT /note="K -> N (probable disease-associated variant found in
FT a patient with drug-resistant epilepsy with intellectual
FT disability, parkinsonism and other neurologic symptoms;
FT dbSNP:rs1057519543)"
FT /evidence="ECO:0000269|PubMed:27864847"
FT /id="VAR_078221"
FT VARIANT 305
FT /note="K -> R (in RTT; abolishes interaction with TBL1X;
FT dbSNP:rs61751441)"
FT /evidence="ECO:0000269|PubMed:11055898,
FT ECO:0000269|PubMed:11402105, ECO:0000269|PubMed:28348241"
FT /id="VAR_018210"
FT VARIANT 306
FT /note="R -> C (in RTT; abolishes interaction with TBL1X and
FT TBL1XR1; dbSNP:rs28935468)"
FT /evidence="ECO:0000269|PubMed:10577905,
FT ECO:0000269|PubMed:10745042, ECO:0000269|PubMed:10767337,
FT ECO:0000269|PubMed:10814719, ECO:0000269|PubMed:10944854,
FT ECO:0000269|PubMed:10991688, ECO:0000269|PubMed:10991689,
FT ECO:0000269|PubMed:11055898, ECO:0000269|PubMed:11241840,
FT ECO:0000269|PubMed:11376998, ECO:0000269|PubMed:11402105,
FT ECO:0000269|PubMed:11738883, ECO:0000269|PubMed:12567420,
FT ECO:0000269|PubMed:12966523, ECO:0000269|PubMed:15057977,
FT ECO:0000269|PubMed:26993267, ECO:0000269|PubMed:28348241"
FT /id="VAR_010282"
FT VARIANT 306
FT /note="R -> H (in RTT; dbSNP:rs61751443)"
FT /evidence="ECO:0000269|PubMed:10767337,
FT ECO:0000269|PubMed:11055898, ECO:0000269|PubMed:15057977"
FT /id="VAR_018211"
FT VARIANT 322
FT /note="P -> A (in RTT; dbSNP:rs61751449)"
FT /evidence="ECO:0000269|PubMed:10814719,
FT ECO:0000269|PubMed:11738883"
FT /id="VAR_018212"
FT VARIANT 322
FT /note="P -> L (in RTT; dbSNP:rs61751450)"
FT /evidence="ECO:0000269|PubMed:11402105"
FT /id="VAR_018213"
FT VARIANT 322
FT /note="P -> S (in MRXS13; dbSNP:rs61751449)"
FT /evidence="ECO:0000269|PubMed:16966553"
FT /id="VAR_037665"
FT VARIANT 344
FT /note="R -> W (in RTT; dbSNP:rs61752361)"
FT /evidence="ECO:0000269|PubMed:12161600,
FT ECO:0000269|PubMed:28709814"
FT /id="VAR_018214"
FT VARIANT 359
FT /note="S -> P (in dbSNP:rs61752371)"
FT /evidence="ECO:0000269|PubMed:11896461"
FT /id="VAR_018215"
FT VARIANT 376
FT /note="P -> S (in dbSNP:rs61752387)"
FT /evidence="ECO:0000269|PubMed:10944854,
FT ECO:0000269|PubMed:12161600, ECO:0000269|PubMed:12384770,
FT ECO:0000269|PubMed:12567420"
FT /id="VAR_018216"
FT VARIANT 388
FT /note="P -> L (in dbSNP:rs61753006)"
FT /id="VAR_023559"
FT VARIANT 388
FT /note="P -> S (in RTT; unknown pathological significance;
FT dbSNP:rs61753000)"
FT /evidence="ECO:0000269|PubMed:12567420"
FT /id="VAR_018218"
FT VARIANT 388
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:12384770"
FT /id="VAR_018217"
FT VARIANT 394
FT /note="E -> K (in dbSNP:rs63094662)"
FT /evidence="ECO:0000269|PubMed:12111644"
FT /id="VAR_018219"
FT VARIANT 397
FT /note="E -> K (in dbSNP:rs56268439)"
FT /evidence="ECO:0000269|PubMed:10577905,
FT ECO:0000269|PubMed:10991689, ECO:0000269|PubMed:11055898,
FT ECO:0000269|PubMed:11738883, ECO:0000269|PubMed:11896461"
FT /id="VAR_010283"
FT VARIANT 399
FT /note="P -> L (in MRXS13; unknown pathological
FT significance; dbSNP:rs62915962)"
FT /evidence="ECO:0000269|PubMed:11309367,
FT ECO:0000269|PubMed:12161600"
FT /id="VAR_018220"
FT VARIANT 402
FT /note="P -> L (in dbSNP:rs61753014)"
FT /evidence="ECO:0000269|PubMed:12384770"
FT /id="VAR_018221"
FT VARIANT 412
FT /note="V -> I (in dbSNP:rs61753966)"
FT /evidence="ECO:0000269|PubMed:11055898"
FT /id="VAR_018222"
FT VARIANT 428
FT /note="G -> S (in ENS-MECP2; uncertain pathological
FT significance; dbSNP:rs61753971)"
FT /evidence="ECO:0000269|PubMed:11238684,
FT ECO:0000269|PubMed:12161600"
FT /id="VAR_017463"
FT VARIANT 439
FT /note="A -> T (in dbSNP:rs61753973)"
FT /evidence="ECO:0000269|PubMed:10767337"
FT /id="VAR_018223"
FT VARIANT 444
FT /note="A -> T (in dbSNP:rs61753975)"
FT /evidence="ECO:0000269|PubMed:11055898"
FT /id="VAR_018224"
FT VARIANT 453
FT /note="R -> Q (in MRXS13; dbSNP:rs61753980)"
FT /evidence="ECO:0000269|PubMed:11309367"
FT /id="VAR_018225"
FT VARIANT 480
FT /note="P -> S (in dbSNP:rs267608636)"
FT /evidence="ECO:0000269|PubMed:12111644"
FT /id="VAR_018226"
FT CONFLICT 72..75
FT /note="PAVP -> RLC (in Ref. 10; CAA61599)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="E -> G (in Ref. 2; CAA68001)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="M -> V (in Ref. 7; CAD97991)"
FT /evidence="ECO:0000305"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:6OGJ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1QK9"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1QK9"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:6OGK"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:6OGK"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:6OGK"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1QK9"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1QK9"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:6OGK"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:6OGK"
SQ 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
