MBD3_HUMAN - dbPTM
MBD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBD3_HUMAN
UniProt AC O95983
Protein Name Methyl-CpG-binding domain protein 3
Gene Name MBD3
Organism Homo sapiens (Human).
Sequence Length 291
Subcellular Localization Nucleus. Chromosome. Nuclear, in discrete foci. Detected on chromatin, at promoter regions of active genes.
Protein Description Acts as transcriptional repressor and plays a role in gene silencing. Does not bind to DNA by itself. [PubMed: 12124384 Binds to DNA with a preference for sites containing methylated CpG dinucleotides (in vitro Binds to a lesser degree DNA containing unmethylated CpG dinucleotides]
Protein Sequence MERKRWECPALPQGWEREEVPRRSGLSAGHRDVFYYSPSGKKFRSKPQLARYLGGSMDLSTFDFRTGKMLMSKMNKSRQRVRYDSSNQVKGKPDLNTALPVRQTASIFKQPVTKITNHPSNKVKSDPQKAVDQPRQLFWEKKLSGLNAFDIAEELVKTMDLPKGLQGVGPGCTDETLLSAIASALHTSTMPITGQLSAAVEKNPGVWLNTTQPLCKAFMVTDEDIRKQEELVQQVRKRLEEALMADMLAHVEELARDGEAPLDKACAEDDDEEDEEEEEEEPDPDPEMEHV
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
4Acetylation----MERKRWECPAL
----CCCCCCCCCCC		48.86-
4 (in isoform 2)Acetylation-48.86-
5 (in isoform 2)Phosphorylation-40.4229514088
7 (in isoform 2)Phosphorylation-34.3629514088
9 (in isoform 2)Acetylation-25.89-
20PhosphorylationQGWEREEVPRRSGLS
CCCCHHCCCCCCCCC		3.7132142685
24PhosphorylationREEVPRRSGLSAGHR
HHCCCCCCCCCCCCC		45.4212354758
35PhosphorylationAGHRDVFYYSPSGKK
CCCCCEEEECCCCCC		11.6829396449
36PhosphorylationGHRDVFYYSPSGKKF
CCCCEEEECCCCCCC		11.5721712546
36UbiquitinationGHRDVFYYSPSGKKF
CCCCEEEECCCCCCC		11.5724816145
37PhosphorylationHRDVFYYSPSGKKFR
CCCEEEECCCCCCCC		10.9523401153
39PhosphorylationDVFYYSPSGKKFRSK
CEEEECCCCCCCCCC		58.2521815630
41UbiquitinationFYYSPSGKKFRSKPQ
EEECCCCCCCCCCHH		53.7432142685
45PhosphorylationPSGKKFRSKPQLARY
CCCCCCCCCHHHHHH		52.39-
52PhosphorylationSKPQLARYLGGSMDL
CCHHHHHHHCCCCCC		12.2328464451
56PhosphorylationLARYLGGSMDLSTFD
HHHHHCCCCCCCCCC		13.8122617229
58UbiquitinationRYLGGSMDLSTFDFR
HHHCCCCCCCCCCHH		38.8829967540
60UbiquitinationLGGSMDLSTFDFRTG
HCCCCCCCCCCHHHH		23.8224816145
60PhosphorylationLGGSMDLSTFDFRTG
HCCCCCCCCCCHHHH		23.8230108239
61PhosphorylationGGSMDLSTFDFRTGK
CCCCCCCCCCHHHHH		34.2230108239
66PhosphorylationLSTFDFRTGKMLMSK
CCCCCHHHHHHHHHH		40.94-
68UbiquitinationTFDFRTGKMLMSKMN
CCCHHHHHHHHHHHH		28.4024816145
73SumoylationTGKMLMSKMNKSRQR
HHHHHHHHHHHHCCC		32.3128112733
73UbiquitinationTGKMLMSKMNKSRQR
HHHHHHHHHHHHCCC		32.31-
77PhosphorylationLMSKMNKSRQRVRYD
HHHHHHHHCCCEECC		28.7419664994
83PhosphorylationKSRQRVRYDSSNQVK
HHCCCEECCCCCCCC		19.8121955146
85PhosphorylationRQRVRYDSSNQVKGK
CCCEECCCCCCCCCC		23.4325159151
86PhosphorylationQRVRYDSSNQVKGKP
CCEECCCCCCCCCCC		28.5223401153
90SumoylationYDSSNQVKGKPDLNT
CCCCCCCCCCCCHHC		51.9928112733
90AcetylationYDSSNQVKGKPDLNT
CCCCCCCCCCCCHHC		51.9926051181
90UbiquitinationYDSSNQVKGKPDLNT
CCCCCCCCCCCCHHC		51.9929967540
92SumoylationSSNQVKGKPDLNTAL
CCCCCCCCCCHHCCC		29.6428112733
92UbiquitinationSSNQVKGKPDLNTAL
CCCCCCCCCCHHCCC		29.6424816145
97PhosphorylationKGKPDLNTALPVRQT
CCCCCHHCCCCHHHH		36.5521712546
106PhosphorylationLPVRQTASIFKQPVT
CCHHHHHHHHHCCCE		31.7624719451
109UbiquitinationRQTASIFKQPVTKIT
HHHHHHHHCCCEECC		52.6121890473
109AcetylationRQTASIFKQPVTKIT
HHHHHHHHCCCEECC		52.6119608861
109SumoylationRQTASIFKQPVTKIT
HHHHHHHHCCCEECC		52.61-
109SumoylationRQTASIFKQPVTKIT
HHHHHHHHCCCEECC		52.61-
109 (in isoform 2)Ubiquitination-52.6121890473
110UbiquitinationQTASIFKQPVTKITN
HHHHHHHCCCEECCC		27.2622817900
125UbiquitinationHPSNKVKSDPQKAVD
CCCCCCCCCHHHHCC		58.4732015554
129UbiquitinationKVKSDPQKAVDQPRQ
CCCCCHHHHCCCHHH		56.62-
141AcetylationPRQLFWEKKLSGLNA
HHHHHHHHHCCCCCH		50.0023749302
141UbiquitinationPRQLFWEKKLSGLNA
HHHHHHHHHCCCCCH		50.0022817900
141 (in isoform 1)Ubiquitination-50.0021890473
142UbiquitinationRQLFWEKKLSGLNAF
HHHHHHHHCCCCCHH		36.0522817900
144PhosphorylationLFWEKKLSGLNAFDI
HHHHHHCCCCCHHHH		50.5525159151
157UbiquitinationDIAEELVKTMDLPKG
HHHHHHHHHCCCCCC		51.2432015554
184UbiquitinationLLSAIASALHTSTMP
HHHHHHHHHHHCCCC		8.3732015554
195UbiquitinationSTMPITGQLSAAVEK
CCCCCCCCHHHHHHH		24.4833845483
216UbiquitinationNTTQPLCKAFMVTDE
ECCCHHHHHHCCCHH		52.9532015554
219SulfoxidationQPLCKAFMVTDEDIR
CHHHHHHCCCHHHHH		3.6621406390
221PhosphorylationLCKAFMVTDEDIRKQ
HHHHHCCCHHHHHHH		23.14-
227UbiquitinationVTDEDIRKQEELVQQ
CCHHHHHHHHHHHHH		63.5033845483
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
24SPhosphorylationKinaseAURKAO14965
PhosphoELM
85SPhosphorylationKinaseAURKAO14965
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBD3_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 MBD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MB3L1_HUMANMBD3L1physical
15456747
MBD3_HUMANMBD3physical
15456747
MBD2_HUMANMBD2physical
15456747
CHD4_HUMANCHD4physical
12354758
MTA2_HUMANMTA2physical
12354758
HDAC1_HUMANHDAC1physical
12354758
HDAC2_HUMANHDAC2physical
12354758
P66A_HUMANGATAD2Aphysical
12183469
P66B_HUMANGATAD2Bphysical
12183469
P66B_HUMANGATAD2Bphysical
11756549
MTA2_HUMANMTA2physical
10444591
HDAC1_HUMANHDAC1physical
10444591
RBBP7_HUMANRBBP7physical
10444591
RBBP4_HUMANRBBP4physical
10444591
MTA2_HUMANMTA2physical
12124384
HDAC1_HUMANHDAC1physical
12124384
MBD3_HUMANMBD3physical
10947852
MBD2_HUMANMBD2physical
10947852
EVI1_HUMANMECOMphysical
18500823
TRI27_HUMANTRIM27physical
17049487
HDAC1_HUMANHDAC1physical
19041848
HDAC2_HUMANHDAC2physical
19041848
P66A_HUMANGATAD2Aphysical
16738318
P66B_HUMANGATAD2Bphysical
16738318
HDAC1_HUMANHDAC1physical
16428440
BC11B_HUMANBCL11Bphysical
16091750
MB3L2_HUMANMBD3L2physical
15701600
MBD3_HUMANMBD3physical
15701600
MBD2_HUMANMBD2physical
15701600
BCL6_HUMANBCL6physical
15454082
HDAC1_HUMANHDAC1physical
17827154
HDAC2_HUMANHDAC2physical
17827154
DDX5_HUMANDDX5physical
20676135
JUN_HUMANJUNphysical
21196933
MTA1_HUMANMTA1physical
22196727
TET1_HUMANTET1physical
22196727
SMCA4_HUMANSMARCA4physical
22196727
TAB2_HUMANTAB2physical
16469706
MTA2_HUMANMTA2physical
22939629
RBBP7_HUMANRBBP7physical
22939629
RBBP4_HUMANRBBP4physical
22939629
P66A_HUMANGATAD2Aphysical
22939629
SMCA5_HUMANSMARCA5physical
22939629
KDM1A_HUMANKDM1Aphysical
23455924
TRI54_HUMANTRIM54physical
25416956
RCN3_HUMANRCN3physical
25416956
P66B_HUMANGATAD2Bphysical
25416956
CEP76_HUMANCEP76physical
25416956
HDAC1_HUMANHDAC1physical
26344197
HDAC2_HUMANHDAC2physical
26344197
MTA1_HUMANMTA1physical
26344197
MTA2_HUMANMTA2physical
26344197
P66B_HUMANGATAD2Bphysical
21516116
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 MBD3_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-4; LYS-109 AND LYS-141, ANDMASS 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-56 AND SER-144, 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-56, AND MASSSPECTROMETRY.

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