MBD1_HUMAN - dbPTM
MBD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBD1_HUMAN
UniProt AC Q9UIS9
Protein Name Methyl-CpG-binding domain protein 1
Gene Name MBD1
Organism Homo sapiens (Human).
Sequence Length 605
Subcellular Localization Nucleus. Nucleus matrix. Nucleus speckle. Chromosome. Colocalizes with the Ten-1 ICD form of TENM1 in foci associated with the nuclear matrix (By similarity). Nuclear, in a punctate pattern. Associated with euchromatic regions of the chromosomes, wit
Protein Description Transcriptional repressor that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binding is abolished by the presence of 7-mG that is produced by DNA damage by methylmethanesulfonate (MMS). Acts as transcriptional repressor and plays a role in gene silencing by recruiting AFT7IP, which in turn recruits factors such as the histone methyltransferase SETDB1. Probably forms a complex with SETDB1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Isoform 1 and isoform 2 can also repress transcription from unmethylated promoters..
Protein Sequence MAEDWLDCPALGPGWKRREVFRKSGATCGRSDTYYQSPTGDRIRSKVELTRYLGPACDLTLFDFKQGILCYPAPKAHPVAVASKKRKKPSRPAKTRKRQVGPQSGEVRKEAPRDETKADTDTAPASFPAPGCCENCGISFSGDGTQRQRLKTLCKDCRAQRIAFNREQRMFKRVGCGECAACQVTEDCGACSTCLLQLPHDVASGLFCKCERRRCLRIVERSRGCGVCRGCQTQEDCGHCPICLRPPRPGLRRQWKCVQRRCLRGKHARRKGGCDSKMAARRRPGAQPLPPPPPSQSPEPTEPHPRALAPSPPAEFIYYCVDEDELQPYTNRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSNQKRQKCRWRQCLQFAMKRLLPSVWSESEDGAGSPPPYRRRKRPSSARRHHLGPTLKPTLATRTAQPDHTQAPTKQEAGGGFVLPPPGTDLVFLREGASSPVQVPGPVAASTEALLQEAQCSGLSWVVALPQVKQEKADTQDEWTPGTAVLTSPVLVPGCPSKAVDPGLPSVKQEPPDPEEDKEENKDDSASKLAPEEEAGGAGTPVITEIFSLGGTRFRDTAVWLPRSKDLKKPGARKQ
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
35PhosphorylationCGRSDTYYQSPTGDR
CCCCCCCCCCCCCCH		12.4728555341
37PhosphorylationRSDTYYQSPTGDRIR
CCCCCCCCCCCCHHH		14.3321815630
39PhosphorylationDTYYQSPTGDRIRSK
CCCCCCCCCCHHHHH		57.8928985074
46SumoylationTGDRIRSKVELTRYL
CCCHHHHHHHHHHHH		29.85-
46SumoylationTGDRIRSKVELTRYL
CCCHHHHHHHHHHHH		29.85-
46UbiquitinationTGDRIRSKVELTRYL
CCCHHHHHHHHHHHH		29.85-
52PhosphorylationSKVELTRYLGPACDL
HHHHHHHHHCCCCCE		15.6916094384
75UbiquitinationILCYPAPKAHPVAVA
EEEEECCCCCCCHHH		62.53-
84UbiquitinationHPVAVASKKRKKPSR
CCCHHHCCCCCCCCC		47.03-
84AcetylationHPVAVASKKRKKPSR
CCCHHHCCCCCCCCC		47.0325953088
104PhosphorylationKRQVGPQSGEVRKEA
CCCCCCCCCCCCCCC		39.8028555341
109UbiquitinationPQSGEVRKEAPRDET
CCCCCCCCCCCCCCC		64.50-
116PhosphorylationKEAPRDETKADTDTA
CCCCCCCCCCCCCCC		35.50-
117SumoylationEAPRDETKADTDTAP
CCCCCCCCCCCCCCC		42.0728112733
120PhosphorylationRDETKADTDTAPASF
CCCCCCCCCCCCCCC		39.86-
172MethylationNREQRMFKRVGCGEC
CHHHHHHHHCCCCCC		36.51-
172MethylationNREQRMFKRVGCGEC
CHHHHHHHHCCCCCC		36.51-
262 (in isoform 10)Phosphorylation-3.1124719451
277SumoylationRKGGCDSKMAARRRP
HHCCCCCHHHHHCCC		21.21-
277SumoylationRKGGCDSKMAARRRP
HHCCCCCHHHHHCCC		21.2128112733
277UbiquitinationRKGGCDSKMAARRRP
HHCCCCCHHHHHCCC		21.21-
295PhosphorylationPLPPPPPSQSPEPTE
CCCCCCCCCCCCCCC		49.4123401153
295 (in isoform 12)Phosphorylation-49.4127251275
297PhosphorylationPPPPPSQSPEPTEPH
CCCCCCCCCCCCCCC		35.2529255136
297 (in isoform 12)Phosphorylation-35.2524719451
301PhosphorylationPSQSPEPTEPHPRAL
CCCCCCCCCCCCCCC		61.5617525332
311PhosphorylationHPRALAPSPPAEFIY
CCCCCCCCCCCEEEE		37.6022617229
311 (in isoform 12)Phosphorylation-37.6024719451
311 (in isoform 11)Phosphorylation-37.6030266825
311 (in isoform 4)Phosphorylation-37.6030266825
311 (in isoform 7)Phosphorylation-37.6030266825
318PhosphorylationSPPAEFIYYCVDEDE
CCCCEEEEEECCHHH		8.9923663014
318 (in isoform 11)Phosphorylation-8.9926552605
318 (in isoform 4)Phosphorylation-8.9926552605
318 (in isoform 7)Phosphorylation-8.9926552605
319PhosphorylationPPAEFIYYCVDEDEL
CCCEEEEEECCHHHC		4.9123663014
319 (in isoform 11)Phosphorylation-4.9126552605
319 (in isoform 4)Phosphorylation-4.9126552605
319 (in isoform 7)Phosphorylation-4.9126552605
332 (in isoform 11)Phosphorylation-33.4929507054
332 (in isoform 4)Phosphorylation-33.4929507054
332 (in isoform 7)Phosphorylation-33.4929507054
335 (in isoform 11)Phosphorylation-43.5029116813
335 (in isoform 4)Phosphorylation-43.5029116813
335 (in isoform 7)Phosphorylation-43.5029116813
336PhosphorylationYTNRRQNRKCGACAA
CCCCCCCCCCCHHHH		27.5727251275
337UbiquitinationTNRRQNRKCGACAAC
CCCCCCCCCCHHHHH		44.57-
337 (in isoform 11)Phosphorylation-44.5729116813
337 (in isoform 4)Phosphorylation-44.5729116813
337 (in isoform 7)Phosphorylation-44.5729116813
365 (in isoform 12)Phosphorylation-36.1424719451
365PhosphorylationDKPKFGGSNQKRQKC
CCCCCCCCHHHHHHH		36.1424719451
366AcetylationKPKFGGSNQKRQKCR
CCCCCCCHHHHHHHH		55.4519608861
366UbiquitinationKPKFGGSNQKRQKCR
CCCCCCCHHHHHHHH		55.4519608861
366 (in isoform 4)Ubiquitination-55.4521890473
366 (in isoform 7)Ubiquitination-55.4521890473
373AcetylationNQKRQKCRWRQCLQF
HHHHHHHHHHHHHHH		38.3519608861
373UbiquitinationNQKRQKCRWRQCLQF
HHHHHHHHHHHHHHH		38.3519608861
373 (in isoform 5)Ubiquitination-38.3521890473
383UbiquitinationQCLQFAMKRLLPSVW
HHHHHHHHHHHHHHH		36.14-
388PhosphorylationAMKRLLPSVWSESED
HHHHHHHHHHCCCCC		35.8723927012
391PhosphorylationRLLPSVWSESEDGAG
HHHHHHHCCCCCCCC		29.1423927012
391 (in isoform 12)Phosphorylation-29.1424719451
393PhosphorylationLPSVWSESEDGAGSP
HHHHHCCCCCCCCCC		35.1623927012
393 (in isoform 12)Phosphorylation-35.1627251275
399PhosphorylationESEDGAGSPPPYRRR
CCCCCCCCCCCCCCC		33.4323927012
399 (in isoform 12)Phosphorylation-33.4324719451
399AcetylationESEDGAGSPPPYRRR
CCCCCCCCCCCCCCC		33.4319608861
399UbiquitinationESEDGAGSPPPYRRR
CCCCCCCCCCCCCCC		33.4319608861
399 (in isoform 2)Ubiquitination-33.4321890473
399 (in isoform 8)Ubiquitination-33.4321890473
403PhosphorylationGAGSPPPYRRRKRPS
CCCCCCCCCCCCCCC		23.6423927012
408 (in isoform 11)Phosphorylation-34.2223663014
408 (in isoform 4)Phosphorylation-34.2223663014
409 (in isoform 11)Phosphorylation-35.3523663014
409 (in isoform 4)Phosphorylation-35.3523663014
410PhosphorylationYRRRKRPSSARRHHL
CCCCCCCCHHHHCCC		40.4328509920
411PhosphorylationRRRKRPSSARRHHLG
CCCCCCCHHHHCCCC		28.6028509920
420 (in isoform 11)Phosphorylation-45.6923663014
420 (in isoform 4)Phosphorylation-45.6923663014
421 (in isoform 11)Phosphorylation-7.6223663014
421 (in isoform 4)Phosphorylation-7.6223663014
422AcetylationHHLGPTLKPTLATRT
CCCCCCCCCCCCCCC		38.1323749302
422SumoylationHHLGPTLKPTLATRT
CCCCCCCCCCCCCCC		38.13-
422UbiquitinationHHLGPTLKPTLATRT
CCCCCCCCCCCCCCC		38.132189047
422SumoylationHHLGPTLKPTLATRT
CCCCCCCCCCCCCCC		38.1328112733
422 (in isoform 1)Ubiquitination-38.1321890473
422 (in isoform 6)Ubiquitination-38.1321890473
440SumoylationDHTQAPTKQEAGGGF
CCCCCCCCCCCCCCC		45.1128112733
441 (in isoform 2)Phosphorylation-48.5323663014
441 (in isoform 8)Phosphorylation-48.5323663014
442 (in isoform 2)Phosphorylation-51.3323663014
442 (in isoform 8)Phosphorylation-51.3323663014
453 (in isoform 2)Phosphorylation-37.3223663014
453 (in isoform 8)Phosphorylation-37.3223663014
454 (in isoform 2)Phosphorylation-31.7523663014
454 (in isoform 8)Phosphorylation-31.7523663014
464PhosphorylationVFLREGASSPVQVPG
EEEECCCCCCCCCCC		46.1323663014
464 (in isoform 6)Phosphorylation-46.1323663014
465 (in isoform 12)Phosphorylation-28.6727251275
465PhosphorylationFLREGASSPVQVPGP
EEECCCCCCCCCCCC		28.6723663014
465 (in isoform 6)Phosphorylation-28.6723663014
473UbiquitinationPVQVPGPVAASTEAL
CCCCCCCHHCCHHHH		9.5921890473
476 (in isoform 6)Phosphorylation-19.6223663014
477 (in isoform 6)Phosphorylation-22.1323663014
499SumoylationVVALPQVKQEKADTQ
EEECHHHHHHHCCCC		47.71-
499SumoylationVVALPQVKQEKADTQ
EEECHHHHHHHCCCC		47.7117066076
502SumoylationLPQVKQEKADTQDEW
CHHHHHHHCCCCCCC		49.41-
502UbiquitinationLPQVKQEKADTQDEW
CHHHHHHHCCCCCCC		49.41-
505PhosphorylationVKQEKADTQDEWTPG
HHHHHCCCCCCCCCC		42.6628348404
505 (in isoform 12)Phosphorylation-42.6624719451
510 (in isoform 12)Phosphorylation-15.1427251275
510PhosphorylationADTQDEWTPGTAVLT
CCCCCCCCCCCEEEC		15.1423663014
511 (in isoform 11)Phosphorylation-38.9324719451
513PhosphorylationQDEWTPGTAVLTSPV
CCCCCCCCEEECCCE		18.1323663014
517 (in isoform 12)Phosphorylation-25.1227251275
517PhosphorylationTPGTAVLTSPVLVPG
CCCCEEECCCEECCC		25.1225850435
518 (in isoform 12)Phosphorylation-14.6224719451
518PhosphorylationPGTAVLTSPVLVPGC
CCCEEECCCEECCCC		14.6225850435
527PhosphorylationVLVPGCPSKAVDPGL
EECCCCCCCCCCCCC		37.0125850435
538SumoylationDPGLPSVKQEPPDPE
CCCCCCCCCCCCCHH		53.97-
538SumoylationDPGLPSVKQEPPDPE
CCCCCCCCCCCCCHH		53.9728112733
538AcetylationDPGLPSVKQEPPDPE
CCCCCCCCCCCCCHH		53.9726051181
555 (in isoform 12)Phosphorylation-44.5727251275
555PhosphorylationKEENKDDSASKLAPE
HHHCCCCHHHHHCCH		44.5730576142
557PhosphorylationENKDDSASKLAPEEE
HCCCCHHHHHCCHHH		31.9623401153
558UbiquitinationNKDDSASKLAPEEEA
CCCCHHHHHCCHHHH		48.67-
558SumoylationNKDDSASKLAPEEEA
CCCCHHHHHCCHHHH		48.6728112733
565 (in isoform 2)Phosphorylation-25.6228348404
570PhosphorylationEEAGGAGTPVITEIF
HHHCCCCCCEEEEEE		17.5325022875
570 (in isoform 12)Phosphorylation-17.5324719451
574PhosphorylationGAGTPVITEIFSLGG
CCCCCEEEEEEEECC		24.2220068231
578PhosphorylationPVITEIFSLGGTRFR
CEEEEEEEECCCCCC		31.5926074081
582PhosphorylationEIFSLGGTRFRDTAV
EEEEECCCCCCCEEE		25.4926074081
587PhosphorylationGGTRFRDTAVWLPRS
CCCCCCCEEEEEECC		20.8928634120
593MethylationDTAVWLPRSKDLKKP
CEEEEEECCCCCCCC		54.92115482735
595MethylationAVWLPRSKDLKKPGA
EEEEECCCCCCCCCC		69.25116253895
634 (in isoform 12)Phosphorylation-28348404
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
-KUbiquitinationE3 ubiquitin ligaseICP0P08393
PMID:32416261
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBD1_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 MBD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUV91_HUMANSUV39H1physical
12711603
CBX5_HUMANCBX5physical
12711603
CAF1A_HUMANCHAF1Aphysical
12697822
MCAF1_HUMANATF7IPphysical
12665582
RING2_HUMANRNF2physical
17428788
RING2_MOUSERnf2physical
17428788
CBX4_HUMANCBX4physical
17428788
STAT1_HUMANSTAT1physical
19074829
PIAS1_HUMANPIAS1physical
19074829
PIAS1_HUMANPIAS1physical
17066076
PIAS2_HUMANPIAS2physical
17066076
CAF1A_HUMANCHAF1Aphysical
17066076
SETB1_HUMANSETDB1physical
17066076
Z512B_HUMANZNF512Bphysical
20211142
MCAF1_HUMANATF7IPphysical
15691849
MCAF2_HUMANATF7IP2physical
15691849
SETB1_HUMANSETDB1physical
15327775
CAF1A_HUMANCHAF1Aphysical
15327775
H31_HUMANHIST1H3Aphysical
15327775
TEN1_HUMANTENM1physical
15777793
A4_HUMANAPPphysical
21832049
SP1_HUMANSP1physical
25363021
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 MBD1_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-422, 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-399, 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-391 AND SER-399, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND THR-301, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"Regulation of MBD1-mediated transcriptional repression by SUMO andPIAS proteins.";
Lyst M.J., Nan X., Stancheva I.;
EMBO J. 25:5317-5328(2006).
Cited for: INTERACTION WITH SETDB1, PHOSPHORYLATION, SUMOYLATION AT LYS-499 ANDLYS-538, AND MUTAGENESIS OF LYS-499; GLU-501; LYS-538 AND GLU-540.

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