P51608 (MECP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methyl-CpG-binding protein 2
Short name=MeCp-2 protein
Short name=MeCp2

Gene names

Name:

MECP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.35 Ref.39 Mental retardation, X-linked, syndromic, 13 (MRXS13) [MIM:300055]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative 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.25 Ref.27 Ref.37 Ref.43 Ref.47 Ref.48 Ref.49 Ref.53 Ref.57 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.23 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.41 Ref.42 Ref.48 Ref.50 Ref.51 Ref.52 Ref.55 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.54 Encephalopathy, neonatal severe, due to MECP2 mutations (ENS-MECP2) [MIM:300673]: A neurodevelopmental disorder characterized by severe neonatal encephalopythy, 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.40 Mental retardation, X-linked, syndromic, Lubs type (MRXSL) [MIM:300260]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative 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.56
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Disease mutation Mental retardation
Domain	Repeat
Ligand	DNA-binding
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult locomotory behavior Inferred from electronic annotation. Source: Compara behavioral fear response Inferred from electronic annotation. Source: Compara cardiolipin metabolic process Inferred from electronic annotation. Source: Compara catecholamine secretion Inferred from electronic annotation. Source: Compara cerebellum development Inferred from electronic annotation. Source: Compara chromatin silencing Inferred from electronic annotation. Source: Compara dendrite development Inferred from electronic annotation. Source: Compara embryo development Inferred from electronic annotation. Source: Compara glucocorticoid metabolic process Inferred from electronic annotation. Source: Compara glutamine metabolic process Inferred from electronic annotation. Source: Compara histone acetylation Inferred from electronic annotation. Source: Compara histone methylation Inferred from electronic annotation. Source: Compara inositol metabolic process Inferred from electronic annotation. Source: Compara long-term memory Inferred from electronic annotation. Source: Compara long-term synaptic potentiation Inferred from electronic annotation. Source: Compara mitochondrial electron transport, ubiquinol to cytochrome c Inferred from electronic annotation. Source: Compara negative regulation of histone acetylation Inferred from electronic annotation. Source: Compara negative regulation of histone methylation Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Traceable author statement PubMed 9620804. Source: ProtInc neurological system process involved in regulation of systemic arterial blood pressure Inferred from electronic annotation. Source: Compara neuron maturation Inferred from electronic annotation. Source: Compara pathogenesis Inferred from electronic annotation. Source: Compara phosphatidylcholine metabolic process Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of synapse assembly Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara proprioception Inferred from electronic annotation. Source: Compara protein localization Inferred from electronic annotation. Source: Compara regulation of excitatory postsynaptic membrane potential Inferred from electronic annotation. Source: Compara regulation of gene expression by genetic imprinting Inferred from electronic annotation. Source: Compara regulation of respiratory gaseous exchange by neurological system process Inferred from electronic annotation. Source: Compara respiratory gaseous exchange Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from electronic annotation. Source: Compara social behavior Inferred from electronic annotation. Source: Compara startle response Inferred from electronic annotation. Source: Compara synapse assembly Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW ventricular system development Inferred from electronic annotation. Source: Compara visual learning Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara heterochromatin Inferred from direct assay PubMed 11441023. Source: UniProtKB nucleus Inferred from direct assay PubMed 11441023. Source: UniProtKB
Molecular_function	chromatin binding Inferred from electronic annotation. Source: Compara double-stranded methylated DNA binding Inferred from mutant phenotype PubMed 17296936. Source: MGI mRNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara siRNA binding Inferred from electronic annotation. Source: Compara transcription corepressor activity Traceable author statement PubMed 10773092. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMARCA2	P51531	4	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 486

486

Methyl-CpG-binding protein 2

PRO_0000096345

Regions

Domain

90 – 162

73

MBD

DNA binding

185 – 197

13

A.T hook 1

DNA binding

265 – 277

13

A.T hook 2

Compositional bias

366 – 372

7

His-rich

Compositional bias

376 – 405

30

Pro-rich

Amino acid modifications

Modified residue

80

1

Phosphoserine Ref.17 Ref.18 Ref.20 Ref.21

Modified residue

116

1

Phosphoserine Ref.17

Modified residue

216

1

Phosphoserine Ref.20

Modified residue

229

1

Phosphoserine By similarity

Modified residue

423

1

Phosphoserine By similarity

Modified residue

426

1

Phosphoserine Ref.17

Modified residue

449

1

N6-acetyllysine Ref.19

Natural variations

Alternative sequence

1 – 9

9

MVAGMLGLR → MAAAAAAAPSGGGGGGEEER L in isoform B.

VSP_022948

Natural variant

10

1

E → Q in RTT. Ref.52

VAR_018180

Natural variant

86

1

S → C. Ref.26

VAR_018181

Natural variant

97

1

D → E in RTT. Ref.31

VAR_023552

Natural variant

97

1

D → Y in RTT. Ref.42

VAR_018182

Natural variant

100

1

L → R in RTT. Ref.55

VAR_023553

Natural variant

100

1

L → V in RTT; dbSBP:rs28935168. Ref.26 Ref.51 Ref.55
Corresponds to variant rs28935168 [ dbSNP | Ensembl ].

VAR_017462

Natural variant

101

1

P → H in RTT. Ref.28

VAR_018183

Natural variant

101

1

P → L in RTT. Ref.28

VAR_018184

Natural variant

101

1

P → R in RTT; also in a patient with Angelman syndrome and some typical RTT features. Ref.33 Ref.39

VAR_010276

Natural variant

101

1

P → S in RTT. Ref.41

VAR_023554

Natural variant

101

1

P → T in RTT. Ref.28

VAR_018185

Natural variant

106

1

R → Q in RTT. Ref.26 Ref.29

VAR_018186

Natural variant

106

1

R → W in RTT. Ref.23 Ref.24 Ref.26 Ref.28 Ref.31 Ref.32 Ref.33 Ref.36 Ref.38 Ref.41 Ref.42 Ref.55
Corresponds to variant rs28934907 [ dbSNP | Ensembl ].

VAR_010272

Natural variant

111

1

R → G in RTT. Ref.38

VAR_018187

Natural variant

120

1

Y → D in RTT. Ref.35

VAR_023555

Natural variant

124

1

L → F in RTT. Ref.32

VAR_010277

Natural variant

128

1

Q → P in RTT. Ref.52

VAR_018188

Natural variant

133

1

R → C in RTT. Ref.23 Ref.24 Ref.26 Ref.28 Ref.31 Ref.32 Ref.35 Ref.38 Ref.41 Ref.42 Ref.50 Ref.52 Ref.55
Corresponds to variant rs28934904 [ dbSNP | Ensembl ].

VAR_010273

Natural variant

133

1

R → H in RTT. Ref.34 Ref.42

VAR_018189

Natural variant

134

1

S → C in RTT. Ref.28 Ref.32 Ref.36 Ref.41

VAR_010278

Natural variant

135

1

K → E in RTT. Ref.38

VAR_018190

Natural variant

137

1

E → G in MRXS13. Ref.37

VAR_017581

Natural variant

140

1

A → V in MRXS13. Ref.27 Ref.37 Ref.43 Ref.47 Ref.48 Ref.49
Corresponds to variant rs28934908 [ dbSNP | Ensembl ].

VAR_010279

Natural variant

152

1

P → R in RTT. Ref.26 Ref.28 Ref.32 Ref.36 Ref.38 Ref.41 Ref.42 Ref.52 Ref.55

VAR_010280

Natural variant

155

1

F → I in RTT. Ref.31

VAR_023556

Natural variant

155

1

F → S in RTT. Ref.23 Ref.24 Ref.26
Corresponds to variant rs28934905 [ dbSNP | Ensembl ].

VAR_010274

Natural variant

156

1

D → G in RTT. Ref.38

VAR_018191

Natural variant

158

1

T → A in RTT. Ref.41 Ref.55

VAR_023557

Natural variant

158

1

T → M in RTT. Ref.23 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36 Ref.38 Ref.41 Ref.42 Ref.50 Ref.52 Ref.55
Corresponds to variant rs28934906 [ dbSNP | Ensembl ].

VAR_010275

Natural variant

161

1

G → V in RTT. Ref.55

VAR_023558

Natural variant

167

1

R → W in MRXS13. Ref.37

VAR_018192

Natural variant

181

1

A → V. Ref.46

VAR_018193

Natural variant

196

1

T → S. Ref.45

VAR_018194

Natural variant

197

1

T → M. Ref.42 Ref.48

VAR_018195

Natural variant

201

1

A → V. Ref.30 Ref.36

VAR_010281

Natural variant

203

1

T → M. Ref.26 Ref.27

VAR_018196

Natural variant

210

1

K → I in RTT. Ref.38

VAR_018197

Natural variant

225

1

P → L in MRXS13. Ref.53

VAR_037664

Natural variant

225

1

P → R in RTT. Ref.28

VAR_018198

Natural variant

228

1

T → S. Ref.45

VAR_018199

Natural variant

229

1

S → L. Ref.28

VAR_018200

Natural variant

232

1

G → A. Ref.30

VAR_018201

Natural variant

251

1

P → L. Ref.30

VAR_018202

Natural variant

284

1

K → E in MRXS13. Ref.37

VAR_018203

Natural variant

287

1

A → P. Ref.26

VAR_018204

Natural variant

291

1

S → A. Ref.26

VAR_018205

Natural variant

302

1

P → A in RTT. Ref.36

VAR_018206

Natural variant

302

1

P → H in RTT. Ref.30

VAR_018207

Natural variant

302

1

P → L in RTT. Ref.28

VAR_018208

Natural variant

302

1

P → R in RTT. Ref.29 Ref.38

VAR_018209

Natural variant

305

1

K → R in RTT. Ref.26 Ref.42

VAR_018210

Natural variant

306

1

R → C in RTT. Ref.23 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36 Ref.38 Ref.42 Ref.50 Ref.52 Ref.55
Corresponds to variant rs28935468 [ dbSNP | Ensembl ].

VAR_010282

Natural variant

306

1

R → H in RTT. Ref.26 Ref.28 Ref.55

VAR_018211

Natural variant

322

1

P → A in RTT. Ref.29 Ref.36

VAR_018212

Natural variant

322

1

P → L in RTT. Ref.42

VAR_018213

Natural variant

322

1

P → S in MRXS13. Ref.57

VAR_037665

Natural variant

344

1

R → W in RTT. Ref.48

VAR_018214

Natural variant

359

1

S → P. Ref.44

VAR_018215

Natural variant

376

1

P → S in a RTT patient; unknown pathological significance. Ref.30 Ref.46 Ref.48 Ref.50

VAR_018216

Natural variant

388

1

P → L.

VAR_023559

Natural variant

388

1

P → S in a RTT patient. Ref.50

VAR_018218

Natural variant

388

1

Missing. Ref.46

VAR_018217

Natural variant

394

1

E → K. Ref.45

VAR_018219

Natural variant

397

1

E → K. Ref.23 Ref.26 Ref.33 Ref.36 Ref.44
Corresponds to variant rs56268439 [ dbSNP | Ensembl ].

VAR_010283

Natural variant

399

1

P → L in MRXS13; unknown pathological significance. Ref.37 Ref.48

VAR_018220

Natural variant

402

1

P → L. Ref.46

VAR_018221

Natural variant

412

1

V → I. Ref.26

VAR_018222

Natural variant

428

1

G → S in ENS-MECP2; uncertain pathological significance. Ref.40 Ref.48

VAR_017463

Natural variant

439

1

A → T. Ref.28

VAR_018223

Natural variant

444

1

A → T. Ref.26

VAR_018224

Natural variant

453

1

R → Q in MRXS13. Ref.37

VAR_018225

Natural variant

480

1

P → S. Ref.45

VAR_018226

Experimental info

Sequence conflict

72 – 75

4

PAVP → RLC Ref.10

Sequence conflict

290

1

E → G in CAA68001. Ref.2

Sequence conflict

466

1

M → V in CAD97991. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

486

Helix Strand Turn

Details...

Beta strand

95 – 97

3

Beta strand

100 – 103

4

Beta strand

105 – 110

6

Turn

115 – 118

4

Beta strand

120 – 125

6

Turn

127 – 129

3

Beta strand

130 – 134

5

Helix

135 – 145

11

Turn

152 – 154

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (Beta) [UniParc]. Last modified October 1, 1996. Version 1. Checksum: EB6A33233AEDA566	FASTA	486	52,441
	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
	Isoform B (Alpha) [UniParc]. Checksum: 443ECB3D5EA4DAB8	FASTA	498	53,323
	10 20 30 40 50 60 MAAAAAAAPS GGGGGGEEER LEEKSEDQDL QGLKDKPLKF KKVKKDKKEE KEGKHEPVQP 70 80 90 100 110 120 SAHHSAEPAE AGKAETSEGS GSAPAVPEAS ASPKQRRSII RDRGPMYDDP TLPEGWTRKL 130 140 150 160 170 180 KQRKSGRSAG KYDVYLINPQ GKAFRSKVEL IAYFEKVGDT SLDPNDFDFT VTGRGSPSRR 190 200 210 220 230 240 EQKPPKKPKS PKAPGTGRGR GRPKGSGTTR PKAATSEGVQ VKRVLEKSPG KLLVKMPFQT 250 260 270 280 290 300 SPGGKAEGGG ATTSTQVMVI KRPGRKRKAE ADPQAIPKKR GRKPGSVVAA AAAEAKKKAV 310 320 330 340 350 360 KESSIRSVQE TVLPIKKRKT RETVSIEVKE VVKPLLVSTL GEKSGKGLKT CKSPGRKSKE 370 380 390 400 410 420 SSPKGRSSSA SSPPKKEHHH HHHHSESPKA PVPLLPPLPP PPPEPESSED PTSPPEPQDL 430 440 450 460 470 480 SSSVCKEEKM PRGGSLESDG CPKEPAKTQP AVATAATAAE KYKHRGEGER KDIVSSSMPR 490 PNREEPVDSR TPVTERVS

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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, MASS SPECTROMETRY.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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, MASS SPECTROMETRY.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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. , 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.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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.
[54]	"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.
[55]	"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.
[56]	"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.
[57]	"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.

IPI

IPI00418234.
IPI00645192.

RefSeq

NP_001104262.1. NM_001110792.1.
NP_004983.1. NM_004992.3.

UniGene

Hs.200716.
Hs.731393.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QK9	NMR	-	A	77-164	[»]
3C2I	X-ray	2.50	A	77-167	[»]

ProteinModelPortal

P51608.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51608. 2 interactions.

MINT

MINT-3019066.

STRING

9606.ENSP00000395535.

PTM databases

PhosphoSite

P51608.

Polymorphism databases

DMDM

1708973.

Proteomic databases

PaxDb

P51608.

PRIDE

P51608.

Protocols and materials databases

DNASU

4204.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000303391; ENSP00000301948; ENSG00000169057.
ENST00000453960; ENSP00000395535; ENSG00000169057.
ENST00000598049; ENSP00000472559; ENSG00000268563.
ENST00000601699; ENSP00000470011; ENSG00000268563.

GeneID

4204.

KEGG

hsa:4204.

UCSC

uc004fjv.2. human.
uc004fjw.2. human.

Organism-specific databases

CTD

4204.

GeneCards

GC0XM153287.

HGNC

HGNC:6990. MECP2.

HPA

HPA000593.
HPA001341.

MIM

105830. phenotype.
300005. gene.
300055. phenotype.
300260. phenotype.
300496. phenotype.
300673. phenotype.
312750. phenotype.

neXtProt

NX_P51608.

Orphanet

3095. Atypical Rett syndrome.
106. Autism.
3077. Intellectual deficit, X-linked - psychosis - macroorchidism.
778. Rett syndrome.
209370. Severe neonatal-onset encephalopathy with microcephaly.
1762. Trisomy Xq28.
777. X-linked nonsyndromic intellectual deficit.

PharmGKB

PA30729.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG237320.

HOGENOM

HOG000015809.

HOVERGEN

HBG052445.

KO

K11588.

OMA

HHSEPPK.

OrthoDB

EOG40VVQ3.

PhylomeDB

P51608.

Enzyme and pathway databases

SignaLink

P51608.

Gene expression databases

ArrayExpress

P51608.

Bgee

P51608.

CleanEx

HS_MECP2.

Genevestigator

P51608.

GermOnline

ENSG00000169057. Homo sapiens.

Family and domain databases

Gene3D

3.30.890.10. 1 hit.

InterPro

IPR017956. AT_hook_DNA-bd_motif.
IPR016177. DNA-bd_integrase-typ.
IPR017353. Me_CpG-bd_MeCP2.
IPR001739. Methyl_CpG_DNA-bd.
[Graphical view]

Pfam

PF01429. MBD. 1 hit.
[Graphical view]

PIRSF

PIRSF038006. Methyl_CpG_bd_MeCP2. 1 hit.

SMART

SM00384. AT_hook. 2 hits.
SM00391. MBD. 1 hit.
[Graphical view]

SUPFAM

SSF54171. DNA-binding_integrase-type. 1 hit.

PROSITE

PS50982. MBD. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MECP2. human.

EvolutionaryTrace

P51608.

GenomeRNAi

4204.

NextBio

16564.

SOURCE

Search...

Entry information

Entry name

MECP2_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 166 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.