MBD2_HUMAN - dbPTM
MBD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBD2_HUMAN
UniProt AC Q9UBB5
Protein Name Methyl-CpG-binding domain protein 2
Gene Name MBD2
Organism Homo sapiens (Human).
Sequence Length 411
Subcellular Localization Nucleus . Nuclear, in discrete foci. Detected at replication foci in late S phase.
Protein Description Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemimethylated DNA as well. Recruits histone deacetylases and DNA methyltransferases. Acts as transcriptional repressor and plays a role in gene silencing. Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression. May enhance the activation of some unmethylated cAMP-responsive promoters..
Protein Sequence MRAHPGGGRCCPEQEEGESAAGGSGAGGDSAIEQGGQGSALAPSPVSGVRREGARGGGRGRGRWKQAGRGGGVCGRGRGRGRGRGRGRGRGRGRGRPPSGGSGLGGDGGGCGGGGSGGGGAPRREPVPFPSGSAGPGPRGPRATESGKRMDCPALPPGWKKEEVIRKSGLSAGKSDVYYFSPSGKKFRSKPQLARYLGNTVDLSSFDFRTGKMMPSKLQKNKQRLRNDPLNQNKGKPDLNTTLPIRQTASIFKQPVTKVTNHPSNKVKSDPQRMNEQPRQLFWEKRLQGLSASDVTEQIIKTMELPKGLQGVGPGSNDETLLSAVASALHTSSAPITGQVSAAVEKNPAVWLNTSQPLCKAFIVTDEDIRKQEERVQQVRKKLEEALMADILSRAADTEEMDIEMDSGDEA
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
2Methylation------MRAHPGGGR
------CCCCCCCCC		41.4254557259
19PhosphorylationPEQEEGESAAGGSGA
CCCCCCCCCCCCCCC		33.9923927012
24PhosphorylationGESAAGGSGAGGDSA
CCCCCCCCCCCHHHH		25.2623927012
30PhosphorylationGSGAGGDSAIEQGGQ
CCCCCHHHHHHCCCC		34.1329978859
39PhosphorylationIEQGGQGSALAPSPV
HHCCCCCCCCCCCCC		16.5423927012
44PhosphorylationQGSALAPSPVSGVRR
CCCCCCCCCCCCCCC		32.1223927012
47PhosphorylationALAPSPVSGVRREGA
CCCCCCCCCCCCCCC		34.6529970186
61MethylationARGGGRGRGRWKQAG
CCCCCCCCCCCCCCC		30.0918966129
61DimethylationARGGGRGRGRWKQAG
CCCCCCCCCCCCCCC		30.09-
99PhosphorylationRGRGRPPSGGSGLGG
CCCCCCCCCCCCCCC		59.4723532336
116PhosphorylationGGCGGGGSGGGGAPR
CCCCCCCCCCCCCCC		37.2230257219
131PhosphorylationREPVPFPSGSAGPGP
CCCCCCCCCCCCCCC		45.8423312004
133PhosphorylationPVPFPSGSAGPGPRG
CCCCCCCCCCCCCCC		34.1021712546
168PhosphorylationKEEVIRKSGLSAGKS
HHHHHHHCCCCCCCC		34.8120068231
171PhosphorylationVIRKSGLSAGKSDVY
HHHHCCCCCCCCCEE		38.2020068231
175PhosphorylationSGLSAGKSDVYYFSP
CCCCCCCCCEEEECC		31.2420068231
178PhosphorylationSAGKSDVYYFSPSGK
CCCCCCEEEECCCCC		12.0924732914
179PhosphorylationAGKSDVYYFSPSGKK
CCCCCEEEECCCCCC		9.4624732914
181PhosphorylationKSDVYYFSPSGKKFR
CCCEEEECCCCCCCC		11.3123401153
183PhosphorylationDVYYFSPSGKKFRSK
CEEEECCCCCCCCCH		63.1425159151
186UbiquitinationYFSPSGKKFRSKPQL
EECCCCCCCCCHHHH		49.92-
189PhosphorylationPSGKKFRSKPQLARY
CCCCCCCCHHHHHHH		52.39-
196PhosphorylationSKPQLARYLGNTVDL
CHHHHHHHHCCCCCC		17.2228152594
217UbiquitinationTGKMMPSKLQKNKQR
CCCCCCHHHHHHHHH		49.41-
241PhosphorylationKGKPDLNTTLPIRQT
CCCCCCCCCCCHHHH		36.6928555341
242PhosphorylationGKPDLNTTLPIRQTA
CCCCCCCCCCHHHHH		29.4827251275
248PhosphorylationTTLPIRQTASIFKQP
CCCCHHHHHHHHCCC		16.7227251275
250PhosphorylationLPIRQTASIFKQPVT
CCHHHHHHHHCCCEE		31.7624719451
253SumoylationRQTASIFKQPVTKVT
HHHHHHHCCCEEEEC		52.61-
253AcetylationRQTASIFKQPVTKVT
HHHHHHHCCCEEEEC		52.6122639661
253SumoylationRQTASIFKQPVTKVT
HHHHHHHCCCEEEEC		52.61-
257PhosphorylationSIFKQPVTKVTNHPS
HHHCCCEEEECCCCC		26.8727251275
260PhosphorylationKQPVTKVTNHPSNKV
CCCEEEECCCCCCCC		29.3927251275
264PhosphorylationTKVTNHPSNKVKSDP
EEECCCCCCCCCCCH		41.5522210691
269PhosphorylationHPSNKVKSDPQRMNE
CCCCCCCCCHHHHCC		58.4720860994
2852-HydroxyisobutyrylationPRQLFWEKRLQGLSA
HHHHHHHHHHCCCCH		49.34-
293PhosphorylationRLQGLSASDVTEQII
HHCCCCHHHHHHHHH		29.27-
296PhosphorylationGLSASDVTEQIIKTM
CCCHHHHHHHHHHHC		27.45-
381UbiquitinationERVQQVRKKLEEALM
HHHHHHHHHHHHHHH		63.95-
382UbiquitinationRVQQVRKKLEEALMA
HHHHHHHHHHHHHHH		51.03-
398PhosphorylationILSRAADTEEMDIEM
HHHHHCCCCCCCCCC		29.1720873877
407PhosphorylationEMDIEMDSGDEA---
CCCCCCCCCCCC---		47.0025159151
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

Oops, there are no upstream regulatory protein records of MBD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBD2_HUMAN !!
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 MBD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GPN1_HUMANGPN1physical
12588985
MB3L1_HUMANMBD3L1physical
15456747
DHX9_HUMANDHX9physical
12665568
P66A_HUMANGATAD2Aphysical
12183469
HDAC1_HUMANHDAC1physical
12183469
HDAC2_HUMANHDAC2physical
12183469
P66B_HUMANGATAD2Bphysical
12183469
P66B_HUMANGATAD2Bphysical
11756549
HDAC1_HUMANHDAC1physical
10471499
HDAC2_HUMANHDAC2physical
10471499
RBBP4_HUMANRBBP4physical
10471499
CHD3_HUMANCHD3physical
10444591
MTA2_HUMANMTA2physical
10444591
HDAC1_HUMANHDAC1physical
10444591
HDAC2_HUMANHDAC2physical
10444591
MBD3_HUMANMBD3physical
10444591
SIN3A_HUMANSIN3Aphysical
10950960
HINFP_HUMANHINFPphysical
11553631
MBD2_HUMANMBD2physical
10947852
MBD3_HUMANMBD3physical
10947852
DNMT1_HUMANDNMT1physical
10947852
TRI27_HUMANTRIM27physical
17049487
FAK2_HUMANPTK2Bphysical
19661918
ANM1_HUMANPRMT1physical
16980624
ANM5_HUMANPRMT5physical
16980624
MEP50_HUMANWDR77physical
16980624
P66A_HUMANGATAD2Aphysical
16415179
TACC3_HUMANTACC3physical
16410616
HDAC2_HUMANHDAC2physical
16410616
MB3L2_HUMANMBD3L2physical
15701600
MBD3_HUMANMBD3physical
15701600
MBD2_HUMANMBD2physical
15701600
CHD3_HUMANCHD3physical
11297506
HDAC1_HUMANHDAC1physical
11297506
HDAC2_HUMANHDAC2physical
11297506
RBBP7_HUMANRBBP7physical
11297506
RBBP4_HUMANRBBP4physical
11297506
MTA2_HUMANMTA2physical
11297506
MBD3_HUMANMBD3physical
11297506
MTA2_HUMANMTA2physical
11102443
KDM1A_HUMANKDM1Aphysical
17634443
HDAC1_HUMANHDAC1physical
17634443
HDAC2_HUMANHDAC2physical
26344197
MTA1_HUMANMTA1physical
26344197
MTA2_HUMANMTA2physical
26344197
HDAC1_HUMANHDAC1physical
12665568
RPB1_HUMANPOLR2Aphysical
12665568
TBP_HUMANTBPphysical
25363021
HDAC1_HUMANHDAC1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MBD2_HUMAN

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Related Literatures of Post-Translational Modification
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-407, 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-407, 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-181 AND SER-407, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.

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