P66B_HUMAN - dbPTM
P66B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P66B_HUMAN
UniProt AC Q8WXI9
Protein Name Transcriptional repressor p66-beta
Gene Name GATAD2B
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Nucleus speckle . Speckled nuclear localization requires both CR1 and CR2 regions.
Protein Description Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2A. Targets MBD3 to discrete loci in the nucleus. May play a role in synapse development..
Protein Sequence MDRMTEDALRLNLLKRSLDPADERDDVLAKRLKMEGHEAMERLKMLALLKRKDLANLEVPHELPTKQDGSGVKGYEEKLNGNLRPHGDNRTAGRPGKENINDEPVDMSARRSEPERGRLTPSPDIIVLSDNEASSPRSSSRMEERLKAANLEMFKGKGIEERQQLIKQLRDELRLEEARLVLLKKLRQSQLQKENVVQKTPVVQNAASIVQPSPAHVGQQGLSKLPSRPGAQGVEPQNLRTLQGHSVIRSATNTTLPHMLMSQRVIAPNPAQLQGQRGPPKPGLVRTTTPNMNPAINYQPQSSSSVPCQRTTSSAIYMNLASHIQPGTVNRVSSPLPSPSAMTDAANSQAAAKLALRKQLEKTLLEIPPPKPPAPLLHFLPSAANSEFIYMVGLEEVVQSVIDSQGKSCASLLRVEPFVCAQCRTDFTPHWKQEKNGKILCEQCMTSNQKKALKAEHTNRLKNAFVKALQQEQEIEQRLQQQAALSPTTAPAVSSVSKQETIMRHHTLRQAPQPQSSLQRGIPTSARSMLSNFAQAPQLSVPGGLLGMPGVNIAYLNTGIGGHKGPSLADRQREYLLDMIPPRSISQSISGQK
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
5O-linked_Glycosylation---MDRMTEDALRLN
---CCCCHHHHHHHH		31.4430059200
5Phosphorylation---MDRMTEDALRLN
---CCCCHHHHHHHH		31.4420363803
10MethylationRMTEDALRLNLLKRS
CCHHHHHHHHHHHHC		24.21-
17PhosphorylationRLNLLKRSLDPADER
HHHHHHHCCCCCHHH		35.2223663014
30UbiquitinationERDDVLAKRLKMEGH
HHHHHHHHHHHHCHH		54.8524816145
33SumoylationDVLAKRLKMEGHEAM
HHHHHHHHHCHHHHH		38.65-
33SumoylationDVLAKRLKMEGHEAM
HHHHHHHHHCHHHHH		38.6528112733
44UbiquitinationHEAMERLKMLALLKR
HHHHHHHHHHHHHHC		37.7822817900
502-HydroxyisobutyrylationLKMLALLKRKDLANL
HHHHHHHHCHHHCCC		59.25-
52UbiquitinationMLALLKRKDLANLEV
HHHHHHCHHHCCCCC		56.3529967540
66SumoylationVPHELPTKQDGSGVK
CCCCCCCCCCCCCCC		44.4428112733
66UbiquitinationVPHELPTKQDGSGVK
CCCCCCCCCCCCCCC		44.4432015554
78AcetylationGVKGYEEKLNGNLRP
CCCCCHHHHCCCCCC		35.0023236377
97AcetylationRTAGRPGKENINDEP
CCCCCCCCCCCCCCC		50.7126051181
97SumoylationRTAGRPGKENINDEP
CCCCCCCCCCCCCCC		50.7128112733
97UbiquitinationRTAGRPGKENINDEP
CCCCCCCCCCCCCCC		50.7124816145
107SulfoxidationINDEPVDMSARRSEP
CCCCCCCCHHCCCCC		3.2521406390
112PhosphorylationVDMSARRSEPERGRL
CCCHHCCCCCCCCCC		52.5330576142
120PhosphorylationEPERGRLTPSPDIIV
CCCCCCCCCCCCEEE		21.9929255136
122PhosphorylationERGRLTPSPDIIVLS
CCCCCCCCCCEEEEC		29.9329255136
129PhosphorylationSPDIIVLSDNEASSP
CCCEEEECCCCCCCC		27.7429255136
134PhosphorylationVLSDNEASSPRSSSR
EECCCCCCCCCCCHH		34.4029255136
135PhosphorylationLSDNEASSPRSSSRM
ECCCCCCCCCCCHHH		31.2329255136
138PhosphorylationNEASSPRSSSRMEER
CCCCCCCCCHHHHHH		35.7327174698
139PhosphorylationEASSPRSSSRMEERL
CCCCCCCCHHHHHHH		24.2027174698
140PhosphorylationASSPRSSSRMEERLK
CCCCCCCHHHHHHHH		36.5725159151
147AcetylationSRMEERLKAANLEMF
HHHHHHHHHHCHHHH		52.237674241
147SumoylationSRMEERLKAANLEMF
HHHHHHHHHHCHHHH		52.2328112733
147UbiquitinationSRMEERLKAANLEMF
HHHHHHHHHHCHHHH		52.2329967540
153SulfoxidationLKAANLEMFKGKGIE
HHHHCHHHHCCCCHH		4.7921406390
155AcetylationAANLEMFKGKGIEER
HHCHHHHCCCCHHHH		59.4026051181
155UbiquitinationAANLEMFKGKGIEER
HHCHHHHCCCCHHHH		59.4024816145
167UbiquitinationEERQQLIKQLRDELR
HHHHHHHHHHHHHHH		52.4524816145
193UbiquitinationLRQSQLQKENVVQKT
HHHHHHHHCCCCCCC		60.9029967540
199AcetylationQKENVVQKTPVVQNA
HHCCCCCCCHHHCCH		43.0926051181
199SumoylationQKENVVQKTPVVQNA
HHCCCCCCCHHHCCH		43.0928112733
200PhosphorylationKENVVQKTPVVQNAA
HCCCCCCCHHHCCHH		12.2930108239
208PhosphorylationPVVQNAASIVQPSPA
HHHCCHHHHHCCCCC		22.3824732914
213PhosphorylationAASIVQPSPAHVGQQ
HHHHHCCCCCCCCCC		20.0225159151
223PhosphorylationHVGQQGLSKLPSRPG
CCCCCCCCCCCCCCC		38.6824732914
224AcetylationVGQQGLSKLPSRPGA
CCCCCCCCCCCCCCC		70.2526051181
227PhosphorylationQGLSKLPSRPGAQGV
CCCCCCCCCCCCCCC		62.6423312004
240MethylationGVEPQNLRTLQGHSV
CCCCCCCCCCCCCCH		40.72-
246PhosphorylationLRTLQGHSVIRSATN
CCCCCCCCHHHCCCC		26.5127080861
249MethylationLQGHSVIRSATNTTL
CCCCCHHHCCCCCCH		20.34-
250PhosphorylationQGHSVIRSATNTTLP
CCCCHHHCCCCCCHH		28.4627080861
252PhosphorylationHSVIRSATNTTLPHM
CCHHHCCCCCCHHHH		34.0527080861
262PhosphorylationTLPHMLMSQRVIAPN
CHHHHHHHCCEECCC		15.7527080861
264MethylationPHMLMSQRVIAPNPA
HHHHHHCCEECCCHH		17.95-
277MethylationPAQLQGQRGPPKPGL
HHHHCCCCCCCCCCC		67.42-
281MethylationQGQRGPPKPGLVRTT
CCCCCCCCCCCCEEC		55.65-
281SumoylationQGQRGPPKPGLVRTT
CCCCCCCCCCCCEEC		55.6528112733
286DimethylationPPKPGLVRTTTPNMN
CCCCCCCEECCCCCC		31.25-
286MethylationPPKPGLVRTTTPNMN
CCCCCCCEECCCCCC		31.25-
287O-linked_GlycosylationPKPGLVRTTTPNMNP
CCCCCCEECCCCCCC		27.7830059200
287PhosphorylationPKPGLVRTTTPNMNP
CCCCCCEECCCCCCC		27.7827732954
288O-linked_GlycosylationKPGLVRTTTPNMNPA
CCCCCEECCCCCCCC		29.6830059200
288PhosphorylationKPGLVRTTTPNMNPA
CCCCCEECCCCCCCC		29.6827732954
289PhosphorylationPGLVRTTTPNMNPAI
CCCCEECCCCCCCCC		16.4428985074
298PhosphorylationNMNPAINYQPQSSSS
CCCCCCCCCCCCCCC		18.5627080861
311O-linked_GlycosylationSSVPCQRTTSSAIYM
CCCCCCCCCCCHHHH		12.7330059200
311PhosphorylationSSVPCQRTTSSAIYM
CCCCCCCCCCCHHHH		12.7321945579
312PhosphorylationSVPCQRTTSSAIYMN
CCCCCCCCCCHHHHH		23.9121945579
313O-linked_GlycosylationVPCQRTTSSAIYMNL
CCCCCCCCCHHHHHH		19.7030059200
313PhosphorylationVPCQRTTSSAIYMNL
CCCCCCCCCHHHHHH		19.7021945579
314PhosphorylationPCQRTTSSAIYMNLA
CCCCCCCCHHHHHHH		19.3221945579
317PhosphorylationRTTSSAIYMNLASHI
CCCCCHHHHHHHHHC		4.6221945579
322O-linked_GlycosylationAIYMNLASHIQPGTV
HHHHHHHHHCCCCCC		25.0430059200
322PhosphorylationAIYMNLASHIQPGTV
HHHHHHHHHCCCCCC		25.0421945579
328O-linked_GlycosylationASHIQPGTVNRVSSP
HHHCCCCCCCCCCCC		22.6930059200
328PhosphorylationASHIQPGTVNRVSSP
HHHCCCCCCCCCCCC		22.6921945579
331MethylationIQPGTVNRVSSPLPS
CCCCCCCCCCCCCCC		25.92-
333PhosphorylationPGTVNRVSSPLPSPS
CCCCCCCCCCCCCHH		24.0129255136
334PhosphorylationGTVNRVSSPLPSPSA
CCCCCCCCCCCCHHH		27.8329255136
338PhosphorylationRVSSPLPSPSAMTDA
CCCCCCCCHHHHCHH		38.8929255136
340PhosphorylationSSPLPSPSAMTDAAN
CCCCCCHHHHCHHHH		34.7029255136
343PhosphorylationLPSPSAMTDAANSQA
CCCHHHHCHHHHHHH		23.3929255136
348PhosphorylationAMTDAANSQAAAKLA
HHCHHHHHHHHHHHH		19.2323927012
353SumoylationANSQAAAKLALRKQL
HHHHHHHHHHHHHHH		29.5728112733
353UbiquitinationANSQAAAKLALRKQL
HHHHHHHHHHHHHHH		29.57-
411PhosphorylationSQGKSCASLLRVEPF
CCCCCHHHHHCCCCE		32.0628555341
432SumoylationTDFTPHWKQEKNGKI
CCCCCCCCCCCCCEE		45.61-
432AcetylationTDFTPHWKQEKNGKI
CCCCCCCCCCCCCEE		45.6126051181
432SumoylationTDFTPHWKQEKNGKI
CCCCCCCCCCCCCEE		45.61-
445SulfoxidationKILCEQCMTSNQKKA
EEEEHHHCCCCHHHH		4.6221406390
451UbiquitinationCMTSNQKKALKAEHT
HCCCCHHHHHHHHHH		49.54-
454SumoylationSNQKKALKAEHTNRL
CCHHHHHHHHHHHHH		57.5028112733
454UbiquitinationSNQKKALKAEHTNRL
CCHHHHHHHHHHHHH		57.5029967540
462UbiquitinationAEHTNRLKNAFVKAL
HHHHHHHHHHHHHHH		42.8923000965
467SumoylationRLKNAFVKALQQEQE
HHHHHHHHHHHHHHH		36.6028112733
467UbiquitinationRLKNAFVKALQQEQE
HHHHHHHHHHHHHHH		36.6023000965
486PhosphorylationLQQQAALSPTTAPAV
HHHHHCCCCCCHHHH		18.5729255136
488PhosphorylationQQAALSPTTAPAVSS
HHHCCCCCCHHHHHC		32.0130266825
489O-linked_GlycosylationQAALSPTTAPAVSSV
HHCCCCCCHHHHHCC		33.7530059200
489PhosphorylationQAALSPTTAPAVSSV
HHCCCCCCHHHHHCC		33.7530266825
494O-linked_GlycosylationPTTAPAVSSVSKQET
CCCHHHHHCCCHHHH		27.4230059200
494PhosphorylationPTTAPAVSSVSKQET
CCCHHHHHCCCHHHH		27.4230266825
495PhosphorylationTTAPAVSSVSKQETI
CCHHHHHCCCHHHHH		24.6630266825
497O-linked_GlycosylationAPAVSSVSKQETIMR
HHHHHCCCHHHHHHH		30.4830059200
497PhosphorylationAPAVSSVSKQETIMR
HHHHHCCCHHHHHHH		30.4825159151
498SumoylationPAVSSVSKQETIMRH
HHHHCCCHHHHHHHH		50.42-
498AcetylationPAVSSVSKQETIMRH
HHHHCCCHHHHHHHH		50.4226051181
498SumoylationPAVSSVSKQETIMRH
HHHHCCCHHHHHHHH		50.4228112733
498UbiquitinationPAVSSVSKQETIMRH
HHHHCCCHHHHHHHH		50.4224816145
501PhosphorylationSSVSKQETIMRHHTL
HCCCHHHHHHHHHCH		19.9922210691
509MethylationIMRHHTLRQAPQPQS
HHHHHCHHCCCCCCC		31.60-
516PhosphorylationRQAPQPQSSLQRGIP
HCCCCCCCHHHCCCC		39.4324173317
517PhosphorylationQAPQPQSSLQRGIPT
CCCCCCCHHHCCCCH		24.2328674419
520MethylationQPQSSLQRGIPTSAR
CCCCHHHCCCCHHHH		50.75-
525O-linked_GlycosylationLQRGIPTSARSMLSN
HHCCCCHHHHHHHHH		19.1430059200
527MethylationRGIPTSARSMLSNFA
CCCCHHHHHHHHHHH		23.51-
540PhosphorylationFAQAPQLSVPGGLLG
HHCCCCCCCCCCCCC		22.48-
558PhosphorylationVNIAYLNTGIGGHKG
CEEEEECCCCCCCCC		27.81-
571MethylationKGPSLADRQREYLLD
CCCCHHHHHHHHHHH		31.67-
584O-linked_GlycosylationLDMIPPRSISQSISG
HHHCCCCHHHHHCCC		32.1631373491
584O-linked_GlycosylationLDMIPPRSISQSISG
HHHCCCCHHHHHCCC		32.1620068230
586O-linked_GlycosylationMIPPRSISQSISGQK
HCCCCHHHHHCCCCC		21.0831373491
586PhosphorylationMIPPRSISQSISGQK
HCCCCHHHHHCCCCC		21.0826714015
588O-linked_GlycosylationPPRSISQSISGQK--
CCCHHHHHCCCCC--		16.3630059200
588PhosphorylationPPRSISQSISGQK--
CCCHHHHHCCCCC--		16.3627251275
590O-linked_GlycosylationRSISQSISGQK----
CHHHHHCCCCC----		40.1830059200
590PhosphorylationRSISQSISGQK----
CHHHHHCCCCC----		40.1827251275
593AcetylationSQSISGQK-------
HHHCCCCC-------		66.8730591111
593UbiquitinationSQSISGQK-------
HHHCCCCC-------		66.8724816145
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 P66B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P66B_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 P66B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTA2_HUMANMTA2physical
11756549
HDAC1_HUMANHDAC1physical
11756549
HDAC2_HUMANHDAC2physical
11756549
RBBP4_HUMANRBBP4physical
11756549
RBBP7_HUMANRBBP7physical
11756549
MBD2_HUMANMBD2physical
11756549
MBD3_HUMANMBD3physical
11756549
CEP70_HUMANCEP70physical
25416956
USBP1_HUMANUSHBP1physical
25416956
CHD3_HUMANCHD3physical
26186194
CHD4_HUMANCHD4physical
26186194
CHD5_HUMANCHD5physical
26186194
MBD2_HUMANMBD2physical
26186194
MBD3_HUMANMBD3physical
26186194
MTA2_HUMANMTA2physical
26186194
MTA3_HUMANMTA3physical
26186194
MTA1_HUMANMTA1physical
26186194
RBBP7_HUMANRBBP7physical
26186194
IMA6_HUMANKPNA5physical
26186194
HDAC2_HUMANHDAC2physical
26186194
HDAC1_HUMANHDAC1physical
26186194
CDKA1_HUMANCDK2AP1physical
26186194
KAISO_HUMANZBTB33physical
26186194
CHD3_HUMANCHD3physical
26344197
P66A_HUMANGATAD2Aphysical
26344197
MBD2_HUMANMBD2physical
26344197
MBD3_HUMANMBD3physical
26344197
MTA1_HUMANMTA1physical
26344197
MTA2_HUMANMTA2physical
26344197
HDAC1_HUMANHDAC1physical
28514442
CHD5_HUMANCHD5physical
28514442
RBBP7_HUMANRBBP7physical
28514442
MBD2_HUMANMBD2physical
28514442
MBD3_HUMANMBD3physical
28514442
MTA3_HUMANMTA3physical
28514442
CHD3_HUMANCHD3physical
28514442
CHD4_HUMANCHD4physical
28514442
MTA1_HUMANMTA1physical
28514442
CDKA1_HUMANCDK2AP1physical
28514442
MTA2_HUMANMTA2physical
28514442
HDAC2_HUMANHDAC2physical
28514442
RBBP4_HUMANRBBP4physical
28514442
ZN827_HUMANZNF827physical
25150861
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615074Mental retardation, autosomal dominant 18 (MRD18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P66B_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 THR-120; SER-122; SER-129;SER-134 AND SER-135, AND MASS SPECTROMETRY.
"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 THR-120; SER-122; SER-129;SER-135; SER-333; SER-334; SER-338 AND SER-486, AND MASS SPECTROMETRY.
"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 THR-120; SER-122; SER-129;SER-134; SER-135; SER-333; SER-338 AND SER-486, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334 AND SER-338, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, 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 THR-120; SER-122; SER-129AND SER-135, AND MASS SPECTROMETRY.

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