MECP2_HUMAN - dbPTM
MECP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MECP2_HUMAN
UniProt AC P51608
Protein Name Methyl-CpG-binding protein 2
Gene Name MECP2
Organism Homo sapiens (Human).
Sequence Length 486
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 SIN3A. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC)..
Protein Sequence MVAGMLGLREEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSAEPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAGKYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGTGRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMVIKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIEVKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESPKAPVPLLPPLPPPPPEPESSEDPTSPPEPQDLSSSVCKEEKMPRGGSLESDGCPKEPAKTQPAVATAATAAEKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
10 (in isoform 2)Phosphorylation-74.8722673903
13PhosphorylationLGLREEKSEDQDLQG
CCCCCCCCCCCCCCC
50.0826657352
25 (in isoform 2)Phosphorylation-51.4125849741
49PhosphorylationKHEPVQPSAHHSAEP
CCCCCCCCCCCCCCH
24.1223927012
53PhosphorylationVQPSAHHSAEPAEAG
CCCCCCCCCCHHHCC
25.1825849741
64PhosphorylationAEAGKAETSEGSGSA
HHCCCCCCCCCCCCC
36.6222167270
65PhosphorylationEAGKAETSEGSGSAP
HCCCCCCCCCCCCCC
31.3122167270
68PhosphorylationKAETSEGSGSAPAVP
CCCCCCCCCCCCCCC
26.0622167270
70PhosphorylationETSEGSGSAPAVPEA
CCCCCCCCCCCCCCC
32.5422167270
78PhosphorylationAPAVPEASASPKQRR
CCCCCCCCCCHHHHH
27.8429255136
80PhosphorylationAVPEASASPKQRRSI
CCCCCCCCHHHHHHH
30.0929255136
80 (in isoform 2)Phosphorylation-30.0927251275
82 (in isoform 2)Phosphorylation-54.6727251275
86PhosphorylationASPKQRRSIIRDRGP
CCHHHHHHHHHCCCC
25.2622210691
90 (in isoform 2)Phosphorylation-49.8621406692
92 (in isoform 2)Phosphorylation-18.6724719451
95PhosphorylationIRDRGPMYDDPTLPE
HHCCCCCCCCCCCCC
21.9628509920
98 (in isoform 2)Phosphorylation-32.7024719451
115MethylationLKQRKSGRSAGKYDV
HHHHCCCCCCCCEEE
30.35115385825
116PhosphorylationKQRKSGRSAGKYDVY
HHHCCCCCCCCEEEE
44.9218669648
119"N6,N6-dimethyllysine"KSGRSAGKYDVYLIN
CCCCCCCCEEEEEEC
37.68-
119MethylationKSGRSAGKYDVYLIN
CCCCCCCCEEEEEEC
37.68-
120PhosphorylationSGRSAGKYDVYLINP
CCCCCCCEEEEEECC
15.1018669648
123PhosphorylationSAGKYDVYLINPQGK
CCCCEEEEEECCCCH
10.0429759185
130UbiquitinationYLINPQGKAFRSKVE
EEECCCCHHHHHHHH
38.822189047
130 (in isoform 1)Ubiquitination-38.8221890473
142 (in isoform 2)Ubiquitination-5.6021890473
148PhosphorylationYFEKVGDTSLDPNDF
EEEECCCCCCCCCCC
25.8430108239
149PhosphorylationFEKVGDTSLDPNDFD
EEECCCCCCCCCCCC
35.2025159151
158PhosphorylationDPNDFDFTVTGRGSP
CCCCCCCEECCCCCC
20.9923401153
160PhosphorylationNDFDFTVTGRGSPSR
CCCCCEECCCCCCCC
20.3623401153
161 (in isoform 2)Phosphorylation-27.8424719451
162MethylationFDFTVTGRGSPSRRE
CCCEECCCCCCCCCC
32.8130988067
164PhosphorylationFTVTGRGSPSRREQK
CEECCCCCCCCCCCC
20.5225159151
166PhosphorylationVTGRGSPSRREQKPP
ECCCCCCCCCCCCCC
45.7425159151
172 (in isoform 2)Phosphorylation-45.7127251275
176 (in isoform 2)Phosphorylation-48.7821406692
178PhosphorylationKPPKKPKSPKAPGTG
CCCCCCCCCCCCCCC
39.9130576142
178 (in isoform 2)Phosphorylation-39.9124719451
184PhosphorylationKSPKAPGTGRGRGRP
CCCCCCCCCCCCCCC
23.7324719451
196 (in isoform 2)Phosphorylation-22.7124719451
203PhosphorylationTTRPKAATSEGVQVK
CCCCCCCCCCCCEEE
31.9727362937
204PhosphorylationTRPKAATSEGVQVKR
CCCCCCCCCCCEEEE
27.8527362937
210"N6,N6-dimethyllysine"TSEGVQVKRVLEKSP
CCCCCEEEEHHHCCC
21.50-
2102-HydroxyisobutyrylationTSEGVQVKRVLEKSP
CCCCCEEEEHHHCCC
21.50-
210AcetylationTSEGVQVKRVLEKSP
CCCCCEEEEHHHCCC
21.5025953088
210MethylationTSEGVQVKRVLEKSP
CCCCCEEEEHHHCCC
21.50-
216PhosphorylationVKRVLEKSPGKLLVK
EEEHHHCCCCCEEEE
29.5223401153
219AcetylationVLEKSPGKLLVKMPF
HHHCCCCCEEEECCE
41.8725953088
223UbiquitinationSPGKLLVKMPFQTSP
CCCCEEEECCEECCC
40.60-
228PhosphorylationLVKMPFQTSPGGKAE
EEECCEECCCCCCCC
36.9530266825
228 (in isoform 2)Phosphorylation-36.9524719451
229PhosphorylationVKMPFQTSPGGKAEG
EECCEECCCCCCCCC
15.6829255136
240 (in isoform 2)Phosphorylation-25.2624719451
241 (in isoform 2)Phosphorylation-29.2821406692
246SulfoxidationATTSTQVMVIKRPGR
CCCCCEEEEECCCCC
1.5321406390
267MethylationDPQAIPKKRGRKPGS
CCCCCCCCCCCCCCH
55.52116252399
274PhosphorylationKRGRKPGSVVAAAAA
CCCCCCCHHHHHHHH
23.1924972180
285AcetylationAAAAEAKKKAVKESS
HHHHHHHHHHHHHHH
53.6830590361
286 (in isoform 2)Phosphorylation-58.6724719451
291PhosphorylationKKKAVKESSIRSVQE
HHHHHHHHHHCHHHH
25.9129970186
292PhosphorylationKKAVKESSIRSVQET
HHHHHHHHHCHHHHH
24.1029970186
295PhosphorylationVKESSIRSVQETVLP
HHHHHHCHHHHHEEC
26.8727499020
304AcetylationQETVLPIKKRKTRET
HHHEECCCCCCCCCE
44.5825953088
311PhosphorylationKKRKTRETVSIEVKE
CCCCCCCEEEEEHHH
19.0926657352
313PhosphorylationRKTRETVSIEVKEVV
CCCCCEEEEEHHHHH
22.0526657352
321AcetylationIEVKEVVKPLLVSTL
EEHHHHHHHHHHHCC
34.8123236377
323 (in isoform 2)Phosphorylation-6.4624719451
325 (in isoform 2)Phosphorylation-5.6027251275
326PhosphorylationVVKPLLVSTLGEKSG
HHHHHHHHCCCCCCC
20.2023312004
327PhosphorylationVKPLLVSTLGEKSGK
HHHHHHHCCCCCCCC
31.1623312004
331AcetylationLVSTLGEKSGKGLKT
HHHCCCCCCCCCCCC
63.8125953088
332PhosphorylationVSTLGEKSGKGLKTC
HHCCCCCCCCCCCCC
41.2421712546
347MethylationKSPGRKSKESSPKGR
CCCCCCCCCCCCCCC
65.73116054211
349PhosphorylationPGRKSKESSPKGRSS
CCCCCCCCCCCCCCC
56.5323312004
350PhosphorylationGRKSKESSPKGRSSS
CCCCCCCCCCCCCCC
31.5523312004
355PhosphorylationESSPKGRSSSASSPP
CCCCCCCCCCCCCCC
37.0023403867
356AcetylationSSPKGRSSSASSPPK
CCCCCCCCCCCCCCC
28.6719608861
356PhosphorylationSSPKGRSSSASSPPK
CCCCCCCCCCCCCCC
28.6728985074
357PhosphorylationSPKGRSSSASSPPKK
CCCCCCCCCCCCCCC
33.1625849741
359PhosphorylationKGRSSSASSPPKKEH
CCCCCCCCCCCCCCC
45.3824972180
360PhosphorylationGRSSSASSPPKKEHH
CCCCCCCCCCCCCCC
44.9624972180
371 (in isoform 2)Phosphorylation-23.0827251275
395PhosphorylationPPPPEPESSEDPTSP
CCCCCCCCCCCCCCC
50.1426657352
396PhosphorylationPPPEPESSEDPTSPP
CCCCCCCCCCCCCCC
44.3426657352
400PhosphorylationPESSEDPTSPPEPQD
CCCCCCCCCCCCCCC
67.2130278072
401PhosphorylationESSEDPTSPPEPQDL
CCCCCCCCCCCCCCC
43.7926657352
409PhosphorylationPPEPQDLSSSVCKEE
CCCCCCCCCHHCCCC
28.9330278072
410PhosphorylationPEPQDLSSSVCKEEK
CCCCCCCCHHCCCCC
33.8026657352
411PhosphorylationEPQDLSSSVCKEEKM
CCCCCCCHHCCCCCC
28.3230177828
413 (in isoform 2)Phosphorylation-5.0527251275
423PhosphorylationEKMPRGGSLESDGCP
CCCCCCCCCCCCCCC
31.6123401153
426O-linked_GlycosylationPRGGSLESDGCPKEP
CCCCCCCCCCCCCCC
44.5930379171
426PhosphorylationPRGGSLESDGCPKEP
CCCCCCCCCCCCCCC
44.5923401153
431AcetylationLESDGCPKEPAKTQP
CCCCCCCCCCCCCCC
79.1427452117
435 (in isoform 2)Phosphorylation-59.4124719451
436O-linked_GlycosylationCPKEPAKTQPAVATA
CCCCCCCCCCHHHHH
41.7230379171
436PhosphorylationCPKEPAKTQPAVATA
CCCCCCCCCCHHHHH
41.7223312004
442PhosphorylationKTQPAVATAATAAEK
CCCCHHHHHHHHHHH
15.3823312004
445PhosphorylationPAVATAATAAEKYKH
CHHHHHHHHHHHHCC
24.7623312004
449AcetylationTAATAAEKYKHRGEG
HHHHHHHHHCCCCCC
55.6719608861
449MalonylationTAATAAEKYKHRGEG
HHHHHHHHHCCCCCC
55.6726320211
450PhosphorylationAATAAEKYKHRGEGE
HHHHHHHHCCCCCCC
11.9723312004
463PhosphorylationGERKDIVSSSMPRPN
CCCCCCCCCCCCCCC
19.6128555341
465PhosphorylationRKDIVSSSMPRPNRE
CCCCCCCCCCCCCCC
25.8725159151
477PhosphorylationNREEPVDSRTPVTER
CCCCCCCCCCCCCCC
37.9829255136
479PhosphorylationEEPVDSRTPVTERVS
CCCCCCCCCCCCCCC
26.5129255136
482PhosphorylationVDSRTPVTERVS---
CCCCCCCCCCCC---
21.1928348404
486PhosphorylationTPVTERVS-------
CCCCCCCC-------
40.5028857561
491 (in isoform 2)Phosphorylation-24719451
498 (in isoform 2)Phosphorylation-24719451

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
80SPhosphorylationKinaseHIPK1Q86Z02
PSP
80SPhosphorylationKinaseHIPK2Q9H2X6
PSP
80SPhosphorylationKinaseHIPK2Q9QZR5
PSP
216SPhosphorylationKinaseHIPK1Q86Z02
PSP
216SPhosphorylationKinaseHIPK2Q9H2X6
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
423SPhosphorylation

-

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HMGB1_HUMANHMGB1physical
11748221
SKI_HUMANSKIphysical
11441023
NCOR1_HUMANNCOR1physical
11441023
SIN3A_HUMANSIN3Aphysical
9620779
SIN3A_HUMANSIN3Aphysical
9620804
TF2B_HUMANGTF2Bphysical
10756192
SIN3A_HUMANSIN3Aphysical
10773092
SUV91_HUMANSUV39H1physical
12399542
DNMT1_HUMANDNMT1physical
12473678
HDAC1_HUMANHDAC1physical
12473678
PR40A_HUMANPRPF40Aphysical
14618241
PR40B_HUMANPRPF40Bphysical
14618241
SPI1_HUMANSPI1physical
14647463
SIN3A_HUMANSIN3Aphysical
15322089
SMCA2_HUMANSMARCA2physical
15696166
SMCE1_HUMANSMARCE1physical
15696166
SNF5_HUMANSMARCB1physical
15696166
LBR_HUMANLBRphysical
19331822
YBOX1_HUMANYBX1physical
16251272
SP1_HUMANSP1physical
20385708
SP3_HUMANSP3physical
20385708
SOX2_HUMANSOX2physical
20368621
TYY1_HUMANYY1physical
20504995
PPARG_HUMANPPARGphysical
21151932
SIN3A_HUMANSIN3Aphysical
22615490
CBX5_HUMANCBX5physical
22615490
YBOX1_HUMANYBX1physical
22615490
SMC3_HUMANSMC3physical
22615490
CBX1_HUMANCBX1physical
22615490
CBX3_HUMANCBX3physical
22615490
H2A2C_HUMANHIST2H2ACphysical
21278419
H2B2E_HUMANHIST2H2BEphysical
21278419
H32_HUMANHIST2H3Cphysical
21278419
XPC_HUMANXPCphysical
22939629
HIPK2_MOUSEHipk2physical
19820693
HIPK2_HUMANHIPK2physical
19820693
SOX18_HUMANSOX18physical
21988832
H2B2F_HUMANHIST2H2BFphysical
28514442
NOL8_HUMANNOL8physical
28514442
E2AK2_HUMANEIF2AK2physical
28514442
NPA1P_HUMANURB1physical
28514442
CR021_HUMANC18orf21physical
28514442
TAF1D_HUMANTAF1Dphysical
28514442
RRP7A_HUMANRRP7Aphysical
28514442
NSD1_HUMANNSD1physical
28514442
IMA3_HUMANKPNA4physical
28514442
CENPV_HUMANCENPVphysical
28514442
URB2_HUMANURB2physical
28514442
H1T_HUMANHIST1H1Tphysical
28514442
PEO1_HUMANC10orf2physical
28514442
IMA4_HUMANKPNA3physical
28514442
RRP5_HUMANPDCD11physical
28514442
DDX51_HUMANDDX51physical
28514442
SRBD1_HUMANSRBD1physical
28514442
TFB1M_HUMANTFB1Mphysical
28514442
BAZ1A_HUMANBAZ1Aphysical
28514442
ZN800_HUMANZNF800physical
28514442
GTPBA_HUMANGTPBP10physical
28514442
BLM_HUMANBLMphysical
28514442
TRIPC_HUMANTRIP12physical
28514442
CHM1A_HUMANCHMP1Aphysical
28514442
RBAK_HUMANRBAKphysical
28514442
CENPR_HUMANITGB3BPphysical
28514442
NEPRO_HUMANC3orf17physical
28514442
TEX10_HUMANTEX10physical
28514442
TRM1L_HUMANTRMT1Lphysical
28514442
NOG1_HUMANGTPBP4physical
28514442
NO40_HUMANZCCHC17physical
28514442
TAF1B_HUMANTAF1Bphysical
28514442
RL13_HUMANRPL13physical
28514442
WDR36_HUMANWDR36physical
28514442
PWP2_HUMANPWP2physical
28514442
CEBPZ_HUMANCEBPZphysical
28514442
HIRA_HUMANHIRAphysical
28514442
NOP2_HUMANNOP2physical
28514442
DDX54_HUMANDDX54physical
28514442
NOG2_HUMANGNL2physical
28514442
KI67_HUMANMKI67physical
28514442
RIOX2_HUMANMINAphysical
28514442
DGCR8_HUMANDGCR8physical
28514442
RL18_HUMANRPL18physical
28514442
FCF1_HUMANFCF1physical
28514442
RS8_HUMANRPS8physical
28514442
MAP2_HUMANMETAP2physical
28514442
DDX31_HUMANDDX31physical
28514442
TAF1A_HUMANTAF1Aphysical
28514442
DDX24_HUMANDDX24physical
28514442
RL7A_HUMANRPL7Aphysical
28514442
NOL6_HUMANNOL6physical
28514442
RL8_HUMANRPL8physical
28514442
RPP40_HUMANRPP40physical
28514442
RL10A_HUMANRPL10Aphysical
28514442
NOC2L_HUMANNOC2Lphysical
28514442
MBB1A_HUMANMYBBP1Aphysical
28514442
RPF2_HUMANRPF2physical
28514442
ZN483_HUMANZNF483physical
28514442
NVL_HUMANNVLphysical
28514442
LENG8_HUMANLENG8physical
28514442
TAF1C_HUMANTAF1Cphysical
28514442
NAT10_HUMANNAT10physical
28514442
SRSF8_HUMANSRSF8physical
28514442
RL3_HUMANRPL3physical
28514442
RLA2_HUMANRPLP2physical
28514442
ESF1_HUMANESF1physical
28514442
RL36_HUMANRPL36physical
28514442
BBX_HUMANBBXphysical
28514442
CK057_HUMANC11orf57physical
28514442
BRX1_HUMANBRIX1physical
28514442
RL32_HUMANRPL32physical
28514442
RL29_HUMANRPL29physical
28514442
RL12_HUMANRPL12physical
28514442
RRP1B_HUMANRRP1Bphysical
28514442
ZN593_HUMANZNF593physical
28514442
DDX56_HUMANDDX56physical
28514442
Z354A_HUMANZNF354Aphysical
28514442
RBM28_HUMANRBM28physical
28514442
RL26L_HUMANRPL26L1physical
28514442
RL15_HUMANRPL15physical
28514442
RRP8_HUMANRRP8physical
28514442
NLE1_HUMANNLE1physical
28514442
RL27_HUMANRPL27physical
28514442
RL5_HUMANRPL5physical
28514442
TOP3A_HUMANTOP3Aphysical
28514442
FXR2_HUMANFXR2physical
28514442
CI114_HUMANC9orf114physical
28514442
NOP16_HUMANNOP16physical
28514442
SDA1_HUMANSDAD1physical
28514442
DDX21_HUMANDDX21physical
28514442
RL17_HUMANRPL17physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
105830Angelman syndrome (AS)
300055Mental retardation, X-linked, syndromic, 13 (MRXS13)
312750Rett syndrome (RTT)
300496Autism, X-linked 3 (AUTSX3)
300673Encephalopathy, neonatal severe, due to MECP2 mutations (ENS-MECP2)
300260Mental retardation, X-linked, syndromic, Lubs type (MRXSL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MECP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-116 AND SER-426,AND MASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.

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