dbPTM

MECP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MECP2_MOUSE
UniProt AC	Q9Z2D6
Protein Name	Methyl-CpG-binding protein 2
Gene Name	Mecp2
Organism	Mus musculus (Mouse).
Sequence Length	484
Subcellular Localization	Nucleus . Colocalized with methyl-CpG in the genome. Colocalized with TBL1X to the heterochromatin foci.
Protein Description	Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC)..
Protein Sequence	MVAGMLGLREEKSEDQDLQGLRDKPLKFKKAKKDKKEDKEGKHEPLQPSAHHSAEPAEAGKAETSESSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAGKYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGTGRGRGRPKGSGTGRPKAAASEGVQVKRVLEKSPGKLVVKMPFQASPGGKGEGGGATTSAQVMVIKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVHETVLPIKKRKTRETVSIEVKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESTKAPMPLLPSPPPPEPESSEDPISPPEPQDLSSSICKEEKMPRGGSLESDGCPKEPAKTQPMVATTTTVAEKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	LGLREEKSEDQDLQG CCCCCCCCCCCCCCC	50.08	27180971
15 (in isoform 2)	Phosphorylation	-	55.15	24068923
30 (in isoform 2)	Phosphorylation	-	69.44	24068923
49	Phosphorylation	KHEPLQPSAHHSAEP CCCCCCCCCCCCCCH	27.55	23984901
53	Phosphorylation	LQPSAHHSAEPAEAG CCCCCCCCCCHHHCC	25.18	23984901
64	Phosphorylation	AEAGKAETSESSGSA HHCCCCCCCCCCCCC	42.53	25619855
65	Phosphorylation	EAGKAETSESSGSAP HCCCCCCCCCCCCCC	27.30	25619855
67	Phosphorylation	GKAETSESSGSAPAV CCCCCCCCCCCCCCC	39.50	25619855
68	Phosphorylation	KAETSESSGSAPAVP CCCCCCCCCCCCCCC	32.49	24925903
70	Phosphorylation	ETSESSGSAPAVPEA CCCCCCCCCCCCCCC	32.78	24925903
78	Phosphorylation	APAVPEASASPKQRR CCCCCCCCCCHHHHH	27.84	25521595
80	Phosphorylation	AVPEASASPKQRRSI CCCCCCCCHHHHHHH	30.09	24925903
86	Phosphorylation	ASPKQRRSIIRDRGP CCHHHHHHHHHCCCC	25.26	-
95	Phosphorylation	IRDRGPMYDDPTLPE HHCCCCCCCCCCCCC	21.96	18266315
105	Phosphorylation	PTLPEGWTRKLKQRK CCCCCHHHHHHHHHC	28.87	18266315
116	Phosphorylation	KQRKSGRSAGKYDVY HHHCCCCCCCCEEEE	44.92	-
120	Phosphorylation	SGRSAGKYDVYLINP CCCCCCCEEEEEECC	15.10	-
148	Phosphorylation	YFEKVGDTSLDPNDF EEEECCCCCCCCCCC	25.84	29472430
149	Phosphorylation	FEKVGDTSLDPNDFD EEECCCCCCCCCCCC	35.20	29472430
158	Phosphorylation	DPNDFDFTVTGRGSP CCCCCCCEECCCCCC	20.99	24925903
160	Phosphorylation	NDFDFTVTGRGSPSR CCCCCEECCCCCCCC	20.36	25521595
162	Methylation	FDFTVTGRGSPSRRE CCCEECCCCCCCCCC	32.81	24129315
164	Phosphorylation	FTVTGRGSPSRREQK CEECCCCCCCCCCCC	20.52	24925903
166	Phosphorylation	VTGRGSPSRREQKPP ECCCCCCCCCCCCCC	45.74	25521595
167	Methylation	TGRGSPSRREQKPPK CCCCCCCCCCCCCCC	49.92	30988059
178	Phosphorylation	KPPKKPKSPKAPGTG CCCCCCCCCCCCCCC	39.91	29899451
184	Phosphorylation	KSPKAPGTGRGRGRP CCCCCCCCCCCCCCC	23.73	-
210	Malonylation	ASEGVQVKRVLEKSP HHCCCCEEEHHHCCC	21.50	26320211
216	Phosphorylation	VKRVLEKSPGKLVVK EEEHHHCCCCCEEEE	29.52	24068923
223	Sumoylation	SPGKLVVKMPFQASP CCCCEEEEECEECCC	33.12	-
227 (in isoform 2)	Malonylation	-	34.75	26320211
229	Phosphorylation	VKMPFQASPGGKGEG EEECEECCCCCCCCC	17.19	25521595
236 (in isoform 2)	Malonylation	-	48.80	32601280
240	Phosphorylation	KGEGGGATTSAQVMV CCCCCCCCCEEEEEE	25.26	29899451
242	Phosphorylation	EGGGATTSAQVMVIK CCCCCCCEEEEEEEC	16.61	27600695
274	Phosphorylation	KRGRKPGSVVAAAAA CCCCCCCHHHHHHHH	23.19	30352176
292	Phosphorylation	KKAVKESSIRSVHET HHHHHHHHHCHHHHC	24.10	-
295	Phosphorylation	VKESSIRSVHETVLP HHHHHHCHHHHCEEE	26.59	29472430
299	Phosphorylation	SIRSVHETVLPIKKR HHCHHHHCEEECCCC	16.68	29472430
308	Phosphorylation	LPIKKRKTRETVSIE EECCCCCCCCEEEEE	37.46	29899451
311	Phosphorylation	KKRKTRETVSIEVKE CCCCCCCEEEEEHHH	19.09	21183079
313	Phosphorylation	RKTRETVSIEVKEVV CCCCCEEEEEHHHHH	22.05	28833060
321	Acetylation	IEVKEVVKPLLVSTL EEHHHHHHHHHHHCC	34.81	23806337
341	Phosphorylation	KGLKTCKSPGRKSKE CCCCCCCCCCCCCCC	34.43	23684622
355	Phosphorylation	ESSPKGRSSSASSPP CCCCCCCCCCCCCCC	37.00	23375375
356	Phosphorylation	SSPKGRSSSASSPPK CCCCCCCCCCCCCCC	28.67	23375375
357	Phosphorylation	SPKGRSSSASSPPKK CCCCCCCCCCCCCCC	33.16	29472430
359	Phosphorylation	KGRSSSASSPPKKEH CCCCCCCCCCCCCCC	45.38	23684622
360	Phosphorylation	GRSSSASSPPKKEHH CCCCCCCCCCCCCCC	44.96	23684622
385	Phosphorylation	APMPLLPSPPPPEPE CCCCCCCCCCCCCCC	50.43	29899451
393	Phosphorylation	PPPPEPESSEDPISP CCCCCCCCCCCCCCC	50.14	29899451
394	Phosphorylation	PPPEPESSEDPISPP CCCCCCCCCCCCCCC	44.34	27717184
399	Phosphorylation	ESSEDPISPPEPQDL CCCCCCCCCCCCCCC	39.53	27717184
407	Phosphorylation	PPEPQDLSSSICKEE CCCCCCCCCHHCCCC	30.26	27717184
408	Phosphorylation	PEPQDLSSSICKEEK CCCCCCCCHHCCCCC	30.90	27717184
409	Phosphorylation	EPQDLSSSICKEEKM CCCCCCCHHCCCCCC	28.73	27717184
421	Phosphorylation	EKMPRGGSLESDGCP CCCCCCCCCCCCCCC	31.61	25521595
424	Phosphorylation	PRGGSLESDGCPKEP CCCCCCCCCCCCCCC	44.59	28833060
434	O-linked_Glycosylation	CPKEPAKTQPMVATT CCCCCCCCCCCEEEE	39.76	22517741
441	Phosphorylation	TQPMVATTTTVAEKY CCCCEEEEHHHHHHH	15.67	19854140
441	O-linked_Glycosylation	TQPMVATTTTVAEKY CCCCEEEEHHHHHHH	15.67	22517741
443	Phosphorylation	PMVATTTTVAEKYKH CCEEEEHHHHHHHCC	18.67	19854140
447	Acetylation	TTTTVAEKYKHRGEG EEHHHHHHHCCCCCC	50.27	23806337
464 (in isoform 2)	Acetylation	-	3.35	-
477	Phosphorylation	EEPVDSRTPVTERVS CCCCCCCCCCCCCCC	26.51	25521595
484	Phosphorylation	TPVTERVS------- CCCCCCCC-------	40.50	29514104

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
80	S	Phosphorylation	Kinase	HIPK2	Q9QZR5	PSP
421	S	Phosphorylation	Kinase	CAMK2B	P28652	GPS
421	S	Phosphorylation	Kinase	CAMK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
421	S	Phosphorylation	17046689
Does not seem to be phosphorylated on Ser-421 in other tissues.
421	S	Phosphorylation	17046689
Phosphorylated on Ser-421 by CaMK2 in brain upon synaptic activity, which attenuates its repressor activity and seems to regulate dendritic growth and spine maturation.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of MECP2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATRX_MOUSE	Atrx	physical	17296936
ATRX_MOUSE	Atrx	physical	20159591
ANM6_MOUSE	Prmt6	physical	21497756
SIR1_MOUSE	Sirt1	physical	22677942
SIN3A_MOUSE	Sin3a	physical	22119903
HDAC1_MOUSE	Hdac1	physical	22119903

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MECP2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.	17203969 [Abstract]
"Brain-specific phosphorylation of MeCP2 regulates activity-dependentBdnf transcription, dendritic growth, and spine maturation."; Zhou Z., Hong E.J., Cohen S., Zhao W.-N., Ho H.H., Schmidt L.,Chen W.G., Lin Y., Savner E., Griffith E.C., Hu L., Steen J.A.J.,Weitz C.J., Greenberg M.E.; Neuron 52:255-269(2006). Cited for: PHOSPHORYLATION AT SER-421.	17046689 [Abstract]

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