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P51608 (MECP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 176. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methyl-CpG-binding protein 2

Short name=MeCp-2 protein
Short name=MeCp2
Gene names
Name:MECP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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) By similarity.

Subunit structure

Interacts with FNBP3 By similarity. Interacts with CDKL5. Ref.14

Subcellular location

Nucleus. Note: Colocalized with methyl-CpG in the genome.

Tissue specificity

Present in all adult somatic tissues tested.

Post-translational modification

Phosphorylated on Ser-423 in brain upon synaptic activity, which attenuates its repressor activity and seems to regulate dendritic growth and spine maturation By similarity.

Involvement in 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.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.36 Ref.40

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26 Ref.28 Ref.38 Ref.44 Ref.48 Ref.49 Ref.50 Ref.54 Ref.58

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.24 Ref.25 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.39 Ref.40 Ref.42 Ref.43 Ref.49 Ref.51 Ref.52 Ref.53 Ref.56

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.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.55

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.
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. Ref.41

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.
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. Ref.57

Sequence similarities

Contains 2 A.T hook DNA-binding domains.

Contains 1 MBD (methyl-CpG-binding) domain.

Sequence caution

The sequence CAD97991.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainRepeat
   LigandDNA-binding
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

behavioral fear response

Inferred from electronic annotation. Source: Ensembl

cardiolipin metabolic process

Inferred from electronic annotation. Source: Ensembl

catecholamine secretion

Inferred from electronic annotation. Source: Ensembl

cerebellum development

Inferred from electronic annotation. Source: Ensembl

chromatin silencing

Inferred from electronic annotation. Source: Ensembl

dendrite development

Inferred from electronic annotation. Source: Ensembl

embryo development

Inferred from electronic annotation. Source: Ensembl

glucocorticoid metabolic process

Inferred from electronic annotation. Source: Ensembl

glutamine metabolic process

Inferred from electronic annotation. Source: Ensembl

histone acetylation

Inferred from electronic annotation. Source: Ensembl

histone methylation

Inferred from electronic annotation. Source: Ensembl

inositol metabolic process

Inferred from electronic annotation. Source: Ensembl

long-term memory

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

mitochondrial electron transport, ubiquinol to cytochrome c

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone acetylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone methylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 9620804. Source: ProtInc

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11441023. Source: UniProtKB

neurological system process involved in regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

neuron maturation

Inferred from electronic annotation. Source: Ensembl

pathogenesis

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of synapse assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

proprioception

Inferred from electronic annotation. Source: Ensembl

protein localization

Inferred from electronic annotation. Source: Ensembl

regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression by genetic imprinting

Inferred from electronic annotation. Source: Ensembl

regulation of respiratory gaseous exchange by neurological system process

Inferred from electronic annotation. Source: Ensembl

respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

social behavior

Inferred from electronic annotation. Source: Ensembl

startle response

Inferred from electronic annotation. Source: Ensembl

synapse assembly

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ventricular system development

Inferred from electronic annotation. Source: Ensembl

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

heterochromatin

Inferred from direct assay PubMed 11441023. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11441023. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement PubMed 9620804. Source: ProtInc

chromatin binding

Inferred from electronic annotation. Source: Ensembl

double-stranded methylated DNA binding

Inferred from mutant phenotype PubMed 17296936. Source: MGI

mRNA binding

Inferred from electronic annotation. Source: Ensembl

methyl-CpG binding

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 11441023. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 11441023. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

siRNA binding

Inferred from electronic annotation. Source: Ensembl

transcription corepressor activity

Traceable author statement PubMed 10773092. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIPK2Q9H2X62EBI-1189067,EBI-348345
Hipk2Q9QZR53EBI-1189067,EBI-366905From a different organism.
SMARCA2P515314EBI-1189067,EBI-679562

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P51608-1)

Also known as: Beta;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P51608-2)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MVAGMLGLR → MAAAAAAAPSGGGGGGEEERL
Note: Ten times higher expression levels than isoform A in brain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Methyl-CpG-binding protein 2
PRO_0000096345

Regions

Domain90 – 16273MBD
DNA binding185 – 19713A.T hook 1
DNA binding265 – 27713A.T hook 2
Compositional bias366 – 3727His-rich
Compositional bias376 – 40530Pro-rich

Amino acid modifications

Modified residue801Phosphoserine Ref.17 Ref.19 Ref.21 Ref.22
Modified residue1161Phosphoserine Ref.17
Modified residue2161Phosphoserine Ref.21
Modified residue2291Phosphoserine By similarity
Modified residue3211N6-acetyllysine By similarity
Modified residue4231Phosphoserine By similarity
Modified residue4261Phosphoserine Ref.17
Modified residue4491N6-acetyllysine Ref.20

Natural variations

Alternative sequence1 – 99MVAGMLGLR → MAAAAAAAPSGGGGGGEEER L in isoform B.
VSP_022948
Natural variant101E → Q in RTT. Ref.53
VAR_018180
Natural variant861S → C. Ref.27
VAR_018181
Natural variant971D → E in RTT. Ref.32
VAR_023552
Natural variant971D → Y in RTT. Ref.43
VAR_018182
Natural variant1001L → R in RTT. Ref.56
VAR_023553
Natural variant1001L → V in RTT; dbSBP:rs28935168. Ref.27 Ref.52 Ref.56
Corresponds to variant rs28935168 [ dbSNP | Ensembl ].
VAR_017462
Natural variant1011P → H in RTT. Ref.29
VAR_018183
Natural variant1011P → L in RTT. Ref.29
VAR_018184
Natural variant1011P → R in RTT; also in a patient with Angelman syndrome and some typical RTT features. Ref.34 Ref.40
VAR_010276
Natural variant1011P → S in RTT. Ref.42
VAR_023554
Natural variant1011P → T in RTT. Ref.29
VAR_018185
Natural variant1061R → Q in RTT. Ref.27 Ref.30
VAR_018186
Natural variant1061R → W in RTT. Ref.24 Ref.25 Ref.27 Ref.29 Ref.32 Ref.33 Ref.34 Ref.37 Ref.39 Ref.42 Ref.43 Ref.56
Corresponds to variant rs28934907 [ dbSNP | Ensembl ].
VAR_010272
Natural variant1111R → G in RTT. Ref.39
VAR_018187
Natural variant1201Y → D in RTT. Ref.36
VAR_023555
Natural variant1241L → F in RTT. Ref.33
VAR_010277
Natural variant1281Q → P in RTT. Ref.53
VAR_018188
Natural variant1331R → C in RTT. Ref.24 Ref.25 Ref.27 Ref.29 Ref.32 Ref.33 Ref.36 Ref.39 Ref.42 Ref.43 Ref.51 Ref.53 Ref.56
Corresponds to variant rs28934904 [ dbSNP | Ensembl ].
VAR_010273
Natural variant1331R → H in RTT. Ref.35 Ref.43
VAR_018189
Natural variant1341S → C in RTT. Ref.29 Ref.33 Ref.37 Ref.42
VAR_010278
Natural variant1351K → E in RTT. Ref.39
VAR_018190
Natural variant1371E → G in MRXS13. Ref.38
VAR_017581
Natural variant1401A → V in MRXS13. Ref.28 Ref.38 Ref.44 Ref.48 Ref.49 Ref.50
Corresponds to variant rs28934908 [ dbSNP | Ensembl ].
VAR_010279
Natural variant1521P → R in RTT. Ref.27 Ref.29 Ref.33 Ref.37 Ref.39 Ref.42 Ref.43 Ref.53 Ref.56
VAR_010280
Natural variant1551F → I in RTT. Ref.32
VAR_023556
Natural variant1551F → S in RTT. Ref.24 Ref.25 Ref.27
Corresponds to variant rs28934905 [ dbSNP | Ensembl ].
VAR_010274
Natural variant1561D → G in RTT. Ref.39
VAR_018191
Natural variant1581T → A in RTT. Ref.42 Ref.56
VAR_023557
Natural variant1581T → M in RTT. Ref.24 Ref.25 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37 Ref.39 Ref.42 Ref.43 Ref.51 Ref.53 Ref.56
Corresponds to variant rs28934906 [ dbSNP | Ensembl ].
VAR_010275
Natural variant1611G → V in RTT. Ref.56
VAR_023558
Natural variant1671R → W in MRXS13. Ref.38
VAR_018192
Natural variant1811A → V. Ref.47
VAR_018193
Natural variant1961T → S. Ref.46
VAR_018194
Natural variant1971T → M. Ref.43 Ref.49
VAR_018195
Natural variant2011A → V. Ref.31 Ref.37
Corresponds to variant rs61748381 [ dbSNP | Ensembl ].
VAR_010281
Natural variant2031T → M. Ref.27 Ref.28
VAR_018196
Natural variant2101K → I in RTT. Ref.39
VAR_018197
Natural variant2251P → L in MRXS13. Ref.54
VAR_037664
Natural variant2251P → R in RTT. Ref.29
VAR_018198
Natural variant2281T → S. Ref.46
Corresponds to variant rs61749738 [ dbSNP | Ensembl ].
VAR_018199
Natural variant2291S → L. Ref.29
VAR_018200
Natural variant2321G → A. Ref.31
Corresponds to variant rs61748422 [ dbSNP | Ensembl ].
VAR_018201
Natural variant2511P → L. Ref.31
VAR_018202
Natural variant2841K → E in MRXS13. Ref.38
VAR_018203
Natural variant2871A → P. Ref.27
VAR_018204
Natural variant2911S → A. Ref.27
VAR_018205
Natural variant3021P → A in RTT. Ref.37
VAR_018206
Natural variant3021P → H in RTT. Ref.31
VAR_018207
Natural variant3021P → L in RTT. Ref.29
VAR_018208
Natural variant3021P → R in RTT. Ref.30 Ref.39
VAR_018209
Natural variant3051K → R in RTT. Ref.27 Ref.43
VAR_018210
Natural variant3061R → C in RTT. Ref.24 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37 Ref.39 Ref.43 Ref.51 Ref.53 Ref.56
Corresponds to variant rs28935468 [ dbSNP | Ensembl ].
VAR_010282
Natural variant3061R → H in RTT. Ref.27 Ref.29 Ref.56
VAR_018211
Natural variant3221P → A in RTT. Ref.30 Ref.37
VAR_018212
Natural variant3221P → L in RTT. Ref.43
VAR_018213
Natural variant3221P → S in MRXS13. Ref.58
VAR_037665
Natural variant3441R → W in RTT. Ref.49
VAR_018214
Natural variant3591S → P. Ref.45
VAR_018215
Natural variant3761P → S in a RTT patient; unknown pathological significance. Ref.31 Ref.47 Ref.49 Ref.51
VAR_018216
Natural variant3881P → L.
VAR_023559
Natural variant3881P → S in a RTT patient. Ref.51
VAR_018218
Natural variant3881Missing. Ref.47
VAR_018217
Natural variant3941E → K. Ref.46
VAR_018219
Natural variant3971E → K. Ref.24 Ref.27 Ref.34 Ref.37 Ref.45
Corresponds to variant rs56268439 [ dbSNP | Ensembl ].
VAR_010283
Natural variant3991P → L in MRXS13; unknown pathological significance. Ref.38 Ref.49
VAR_018220
Natural variant4021P → L. Ref.47
VAR_018221
Natural variant4121V → I. Ref.27
Corresponds to variant rs61753966 [ dbSNP | Ensembl ].
VAR_018222
Natural variant4281G → S in ENS-MECP2; uncertain pathological significance. Ref.41 Ref.49
VAR_017463
Natural variant4391A → T. Ref.29
VAR_018223
Natural variant4441A → T. Ref.27
Corresponds to variant rs61753975 [ dbSNP | Ensembl ].
VAR_018224
Natural variant4531R → Q in MRXS13. Ref.38
VAR_018225
Natural variant4801P → S. Ref.46
VAR_018226

Experimental info

Sequence conflict72 – 754PAVP → RLC Ref.10
Sequence conflict2901E → G in CAA68001. Ref.2
Sequence conflict4661M → V in CAD97991. Ref.7

Secondary structure

................. 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (Beta) [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EB6A33233AEDA566

FASTA48652,441
        10         20         30         40         50         60 
MVAGMLGLRE EKSEDQDLQG LKDKPLKFKK VKKDKKEEKE GKHEPVQPSA HHSAEPAEAG 

        70         80         90        100        110        120 
KAETSEGSGS APAVPEASAS PKQRRSIIRD RGPMYDDPTL PEGWTRKLKQ RKSGRSAGKY 

       130        140        150        160        170        180 
DVYLINPQGK AFRSKVELIA YFEKVGDTSL DPNDFDFTVT GRGSPSRREQ KPPKKPKSPK 

       190        200        210        220        230        240 
APGTGRGRGR PKGSGTTRPK AATSEGVQVK RVLEKSPGKL LVKMPFQTSP GGKAEGGGAT 

       250        260        270        280        290        300 
TSTQVMVIKR PGRKRKAEAD PQAIPKKRGR KPGSVVAAAA AEAKKKAVKE SSIRSVQETV 

       310        320        330        340        350        360 
LPIKKRKTRE TVSIEVKEVV KPLLVSTLGE KSGKGLKTCK SPGRKSKESS PKGRSSSASS 

       370        380        390        400        410        420 
PPKKEHHHHH HHSESPKAPV PLLPPLPPPP PEPESSEDPT SPPEPQDLSS SVCKEEKMPR 

       430        440        450        460        470        480 
GGSLESDGCP KEPAKTQPAV ATAATAAEKY KHRGEGERKD IVSSSMPRPN REEPVDSRTP 


VTERVS 

« Hide

Isoform B (Alpha) [UniParc].

Checksum: 443ECB3D5EA4DAB8
Show »

FASTA49853,323

References

« Hide 'large scale' references
[1]"Methyl-CpG-binding protein MeCP2 represses Sp1-activated transcription of the human leukosialin gene when the promoter is methylated."
Kudo S.
Mol. Cell. Biol. 18:5492-5499(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"Assignment of the gene for methyl-CpG-binding protein 2 (MECP2) to human chromosome band Xq28 by in situ hybridization."
Vilain A., Apiou F., Vogt N., Dutrillaux B., Malfoy B.
Cytogenet. Cell Genet. 74:293-294(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[3]"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."
Coy J.F., Sedlacek Z., Baechner D., Delius H., Poustka A.
Hum. Mol. Genet. 8:1253-1262(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[4]"Comparative sequence analysis of the MECP2-locus in human and mouse reveals new transcribed regions."
Reichwald K., Thiesen J., Wiehe T., Weitzel J., Poustka W.A., Rosenthal A., Platzer M., Stratling W.H., Kioschis P.
Mamm. Genome 11:182-190(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[5]"A previously unidentified MECP2 open reading frame defines a new protein isoform relevant to Rett syndrome."
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.
Nat. Genet. 36:339-341(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), INVOLVEMENT IN RTT.
[6]Straetling W.H.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Placenta.
[7]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Tissue: Colon endothelium.
[8]"The DNA sequence of the human X chromosome."
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. expand/collapse author list , 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.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Placenta.
[10]"Isolation, physical mapping, and Northern analysis of the X-linked human gene encoding methyl CpG-binding protein, MECP2."
D'Esposito M., Quaderi N.A., Ciccodicola A., Bruni P., Esposito T., D'Urso M., Brown S.D.M.
Mamm. Genome 7:533-535(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-486 (ISOFORM A).
Tissue: Skeletal muscle.
[11]"Genetic organization of human methyl-CpG-binding protein 2."
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.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-486 (ISOFORM A).
[12]"The major form of MeCP2 has a novel N-terminus generated by alternative splicing."
Kriaucionis S., Bird A.
Nucleic Acids Res. 32:1818-1823(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORM B).
[13]"Mutations and polymorphisms in the human methyl CpG-binding protein MECP2."
Miltenberger-Miltenyi G., Laccone F.
Hum. Mutat. 22:107-115(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[14]"CDKL5 belongs to the same molecular pathway of MeCP2 and it is responsible for the early-onset seizure variant of Rett syndrome."
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.
Hum. Mol. Genet. 14:1935-1946(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDKL5.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-116 AND SER-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[20]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"The solution structure of the domain from MeCP2 that binds to methylated DNA."
Wakefield R.I., Smith B.O., Nan X., Free A., Soteriou A., Uhrin D., Bird A.P., Barlow P.N.
J. Mol. Biol. 291:1055-1065(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 77-166.
[24]"Rett syndrome and beyond: recurrent spontaneous and familial MECP2 mutations at CpG hotspots."
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.
Am. J. Hum. Genet. 65:1520-1529(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT TRP-106; CYS-133; SER-155; MET-158 AND CYS-306, VARIANT LYS-397.
[25]"Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2."
Amir R.E., Van den Veyver I.B., Wan M., Tran C.Q., Francke U., Zoghbi H.Y.
Nat. Genet. 23:185-188(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT TRP-106; CYS-133; SER-155 AND MET-158.
[26]"A mutation in the Rett syndrome gene, MECP2, causes X-linked mental retardation and progressive spasticity in males."
Meloni I., Bruttini M., Longo I., Mari F., Rizzolio F., D'Adamo P., Denvriendt K., Fryns J.-P., Toniolo D., Renieri A.
Am. J. Hum. Genet. 67:982-985(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRXS13.
[27]"Diagnostic testing for Rett syndrome by DHPLC and direct sequencing analysis of the MECP2 gene: identification of several novel mutations and polymorphisms."
Buyse I.M., Fang P., Hoon K.T., Amir R.E., Zoghbi H.Y., Roa B.B.
Am. J. Hum. Genet. 67:1428-1436(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT VAL-100; GLN-106; TRP-106; CYS-133; ARG-152; SER-155; MET-158; ARG-305; CYS-306 AND HIS-306, VARIANTS CYS-86; MET-203; PRO-287; ALA-291; LYS-397; ILE-412 AND THR-444.
[28]"MECP2 mutation in male patients with non-specific X-linked mental retardation."
Orrico A., Lam C., Galli L., Dotti M.T., Hayek G., Tong S.F., Poon P.M., Zappella M., Federico A., Sorrentino V.
FEBS Lett. 481:285-288(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRXS13 VAL-140, VARIANT MET-203.
[29]"Long-read sequence analysis of the MECP2 gene in Rett syndrome patients: correlation of disease severity with mutation type and location."
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.
Hum. Mol. Genet. 9:1119-1129(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, VARIANTS LEU-229 AND THR-439.
[30]"MECP2 mutations account for most cases of typical forms of Rett syndrome."
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.
Hum. Mol. Genet. 9:1377-1384(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT GLN-106; MET-158; ARG-302; CYS-306 AND ALA-322.
[31]"Mutational analysis of the MECP2 gene in Japanese patients with Rett syndrome."
Amano K., Nomura Y., Segawa M., Yamakawa K.
J. Hum. Genet. 45:231-236(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT MET-158; HIS-302 AND CYS-306, VARIANTS VAL-201; ALA-232; LEU-251 AND SER-376.
[32]"Mutation screening in Rett syndrome patients."
Xiang F., Buervenich S., Nicolao P., Bailey M.E., Zhang Z., Anvret M.
J. Med. Genet. 37:250-255(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT GLU-97; TRP-106; CYS-133; ILE-155; MET-158 AND CYS-306.
[33]"Mutation analysis of the methyl-CpG binding protein 2 gene (MECP2) in patients with Rett syndrome."
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.
J. Med. Genet. 37:608-610(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT TRP-106; PHE-124; CYS-133; CYS-134; ARG-152; MET-158 AND CYS-306.
[34]"Mutations in the MECP2 gene in a cohort of girls with Rett syndrome."
Hampson K., Woods C.G., Latif F., Webb T.
J. Med. Genet. 37:610-612(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT ARG-101; TRP-106; MET-158 AND CYS-306, VARIANT LYS-397.
[35]"Classic Rett syndrome in a boy as a result of somatic mosaicism for a MECP2 mutation."
Armstrong J., Poo P., Pineda M., Aibar E., Gean E., Catala V., Monros E.
Ann. Neurol. 50:692-692(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RTT HIS-133.
[36]"Mutational analysis of MECP2 in Japanese patients with atypical Rett syndrome."
Inui K., Akagi M., Ono J., Tsukamoto H., Shimono K., Mano T., Imai K., Yamada M., Muramatsu T., Sakai N., Okada S.
Brain Dev. 23:212-215(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT ASP-120; CYS-133; MET-158 AND CYS-306.
[37]"Spectrum and distribution of MECP2 mutations in 64 Italian Rett syndrome girls: tentative genotype/phenotype correlation."
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.
Brain Dev. 23:S242-S245(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT TRP-106; CYS-134; ARG-152; MET-158; ALA-302; CYS-306 AND ALA-322, VARIANTS VAL-201 AND LYS-397.
[38]"MECP2 is highly mutated in X-linked mental retardation."
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.
Hum. Mol. Genet. 10:941-946(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MRXS13 GLY-137; VAL-140; TRP-167; GLU-284; LEU-399 AND GLN-453.
[39]"Mutation spectrum in patients with Rett syndrome in the German population: evidence of hot spot regions."
Laccone F., Huppke P., Hanefeld F., Meins M.
Hum. Mutat. 17:183-190(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT TRP-106; GLY-111; CYS-133; GLU-135; ARG-152; GLY-156; MET-158; ILE-210; ARG-302 AND CYS-306.
[40]"Angelman syndrome phenotype associated with mutations in MECP2, a gene encoding a methyl CpG binding protein."
Watson P., Black G., Ramsden S., Barrow M., Super M., Kerr B., Clayton-Smith J.
J. Med. Genet. 38:224-228(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RTT ARG-101, INVOLVEMENT IN AS.
[41]"MECP2 mutation in non-fatal, non-progressive encephalopathy in a male."
Imessaoudene B., Bonnefont J.-P., Royer G., Cormier-Daire V., Lyonnet S., Lyon G., Munnich A., Amiel J.
J. Med. Genet. 38:171-174(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ENS-MECP2 SER-428.
[42]"Mutation analysis of the MECP2 gene in British and Italian Rett syndrome females."
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. expand/collapse author list , MacDonald F., Kerr A., Dhanjal S., Hulten M.
J. Mol. Med. 78:648-655(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT SER-101; TRP-106; CYS-133; CYS-134; ARG-152; ALA-158 AND MET-158.
[43]"MeCP2 mutations in children with and without the phenotype of Rett syndrome."
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.
Neurology 56:1486-1495(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT TYR-97; TRP-106; HIS-133; CYS-133; ARG-152; MET-158; ARG-305; CYS-306 AND LEU-322, VARIANT MET-197.
[44]"A mutation hot spot for nonspecific X-linked mental retardation in the MECP2 gene causes the PPM-X syndrome."
Klauck S.M., Lindsay S., Beyer K.S., Splitt M., Burn J., Poustka A.
Am. J. Hum. Genet. 70:1034-1037(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRXS13 VAL-140.
[45]"Polymorphisms in the C-terminal domain of MECP2 in mentally handicapped boys: implications for genetic counselling."
Moncla A., Kpebe A., Missirian C., Mancini J., Villard L.
Eur. J. Hum. Genet. 10:86-89(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PRO-359 AND LYS-397.
[46]"Low frequency of MECP2 mutations in mentally retarded males."
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.
Eur. J. Hum. Genet. 10:487-490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-196; SER-228; LYS-394 AND SER-480.
[47]"Mutation analysis of the coding sequence of the MECP2 gene in infantile autism."
Beyer K.S., Blasi F., Bacchelli E., Klauck S.M., Maestrini E., Poustka A.
Hum. Genet. 111:305-309(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-181; SER-376; PRO-388 DEL AND LEU-402.
[48]"Identification of a family with nonspecific mental retardation (MRX79) with the A140V mutation in the MECP2 gene: is there a need for routine screening?"
Winnepenninckx B., Errijgers V., Hayez-Delatte F., Reyniers E., Kooy R.F.
Hum. Mutat. 20:249-252(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRXS13 VAL-140.
[49]"MECP2 gene nucleotide changes and their pathogenicity in males: proceed with caution."
Laccone F., Zoll B., Huppke P., Hanefeld F., Pepinski W., Trappe R.
J. Med. Genet. 39:586-588(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRXS13 VAL-140, VARIANT RTT TRP-344, VARIANTS MET-197; SER-376; LEU-399 AND SER-428, DISCUSSION OF PATHOGENIC ROLE.
[50]"A Rett syndrome MECP2 mutation that causes mental retardation in men."
Dotti M.T., Orrico A., De Stefano N., Battisti C., Sicurelli F., Severi S., Lam C.-W., Galli L., Sorrentino V., Federico A.
Neurology 58:226-230(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRXS13 VAL-140.
[51]"Mutation analysis of the MECP2 gene in patients with Rett syndrome."
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.
Am. J. Med. Genet. A 117:184-187(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT CYS-133; MET-158 AND CYS-306, VARIANTS SER-376 AND SER-388.
[52]"Rett syndrome in a 47,XXX patient with a de novo MECP2 mutation."
Hammer S., Dorrani N., Hartiala J., Stein S., Schanen N.C.
Am. J. Med. Genet. A 122:223-226(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RTT VAL-100.
[53]"Rett syndrome in adolescent and adult females: clinical and molecular genetic findings."
Smeets E., Schollen E., Moog U., Matthijs G., Herbergs J., Smeets H., Curfs L., Schrander-Stumpel C., Fryns J.-P.
Am. J. Med. Genet. A 122:227-233(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT GLN-10; PRO-128; CYS-133; ARG-152; MET-158 AND CYS-306.
[54]"Neurodevelopmental disorders in males related to the gene causing Rett syndrome in females (MECP2)."
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.
Eur. J. Paediatr. Neurol. 7:5-12(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRXS13 LEU-225.
[55]"Identification of MeCP2 mutations in a series of females with autistic disorder."
Carney R.M., Wolpert C.M., Ravan S.A., Shahbazian M., Ashley-Koch A., Cuccaro M.L., Vance J.M., Pericak-Vance M.A.
Pediatr. Neurol. 28:205-211(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AUTSX3.
[56]"Phenotypic manifestations of MECP2 mutations in classical and atypical Rett syndrome."
Schanen C., Houwink E.J.F., Dorrani N., Lane J., Everett R., Feng A., Cantor R.M., Percy A.
Am. J. Med. Genet. A 126:129-140(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RTT ARG-100; VAL-100; TRP-106; CYS-133; ARG-152; ALA-158; MET-158; VAL-161; CYS-306 AND HIS-306.
[57]"Duplication of the MECP2 region is a frequent cause of severe mental retardation and progressive neurological symptoms in males."
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.
Am. J. Hum. Genet. 77:442-453(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRXSL.
[58]"A novel familial MECP2 mutation in a young boy: clinical and molecular findings."
Ventura P., Galluzzi R., Bacca S.M., Giorda R., Massagli A.
Neurology 67:867-868(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MRXS13 SER-322.
+Additional computationally mapped references.

Web resources

RettBASE

IRSA MECP2 variation database

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L37298 mRNA. Translation: AAC32737.1.
X99686 mRNA. Translation: CAA68001.1.
AJ132917 mRNA. Translation: CAB46446.1.
AF158180 mRNA. Translation: AAF33023.1.
Y12643 mRNA. Translation: CAA73190.1.
AY541280 mRNA. Translation: AAS55455.1.
BX538060 mRNA. Translation: CAD97991.1. Different initiation.
AF030876 Genomic DNA. Translation: AAC08757.1.
BC011612 mRNA. Translation: AAH11612.1.
X89430 mRNA. Translation: CAA61599.1.
X94628 Genomic DNA. Translation: CAA64331.1.
RefSeqNP_001104262.1. NM_001110792.1.
NP_004983.1. NM_004992.3.
XP_005274738.1. XM_005274681.2.
UniGeneHs.200716.
Hs.702514.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QK9NMR-A77-164[»]
3C2IX-ray2.50A77-167[»]
DisProtDP00539.
ProteinModelPortalP51608.
SMRP51608. Positions 71-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110368. 50 interactions.
IntActP51608. 5 interactions.
MINTMINT-3019066.
STRING9606.ENSP00000395535.

PTM databases

PhosphoSiteP51608.

Polymorphism databases

DMDM1708973.

Proteomic databases

PaxDbP51608.
PRIDEP51608.

Protocols and materials databases

DNASU4204.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303391; ENSP00000301948; ENSG00000169057. [P51608-1]
ENST00000453960; ENSP00000395535; ENSG00000169057. [P51608-2]
ENST00000598049; ENSP00000472559; ENSG00000268563. [P51608-2]
ENST00000601699; ENSP00000470011; ENSG00000268563. [P51608-1]
GeneID4204.
KEGGhsa:4204.
UCSCuc004fjv.2. human. [P51608-1]
uc004fjw.2. human. [P51608-2]

Organism-specific databases

CTD4204.
GeneCardsGC0XM153287.
HGNCHGNC:6990. MECP2.
HPAHPA000593.
HPA001341.
MIM105830. phenotype.
300005. gene.
300055. phenotype.
300260. phenotype.
300496. phenotype.
300673. phenotype.
312750. phenotype.
neXtProtNX_P51608.
Orphanet3095. Atypical Rett syndrome.
106. Autism.
3077. Intellectual deficit, X-linked - psychosis - macroorchidism.
778. Rett syndrome.
209370. Severe neonatal-onset encephalopathy with microcephaly.
536. Systemic lupus erythematosus.
1762. Trisomy Xq28.
777. X-linked non-syndromic intellectual deficit.
PharmGKBPA30729.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237320.
HOGENOMHOG000015809.
HOVERGENHBG052445.
KOK11588.
OMAHETVLPI.
PhylomeDBP51608.
TreeFamTF332974.

Enzyme and pathway databases

SignaLinkP51608.

Gene expression databases

ArrayExpressP51608.
BgeeP51608.
CleanExHS_MECP2.
GenevestigatorP51608.

Family and domain databases

Gene3D3.30.890.10. 1 hit.
InterProIPR017956. AT_hook_DNA-bd_motif.
IPR016177. DNA-bd_dom.
IPR017353. Me_CpG-bd_MeCP2.
IPR001739. Methyl_CpG_DNA-bd.
[Graphical view]
PfamPF01429. MBD. 1 hit.
[Graphical view]
PIRSFPIRSF038006. Methyl_CpG_bd_MeCP2. 1 hit.
SMARTSM00384. AT_hook. 2 hits.
SM00391. MBD. 1 hit.
[Graphical view]
SUPFAMSSF54171. SSF54171. 1 hit.
PROSITEPS50982. MBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMECP2. human.
EvolutionaryTraceP51608.
GeneWikiMECP2.
GenomeRNAi4204.
NextBio16564.
PROP51608.
SOURCESearch...

Entry information

Entry nameMECP2_HUMAN
AccessionPrimary (citable) accession number: P51608
Secondary accession number(s): O15233, Q6QHH9, Q7Z384
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM