P66B_MOUSE - dbPTM
P66B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P66B_MOUSE
UniProt AC Q8VHR5
Protein Name Transcriptional repressor p66-beta
Gene Name Gatad2b
Organism Mus musculus (Mouse).
Sequence Length 594
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 (By similarity). Targets MBD3 to discrete loci in the nucleus (By similarity). Plays a role in synapse development (By similarity)..
Protein Sequence MDRMTEDALRLNLLKRSLDPADERDDVLAKRLKMEGHEAMERLKMLALLKRKDLANLEVPHELPTKQDGSGVKGYEEKLNGNLRPHGDNNRTAGRPGKENINDEPVDMSARRSEPDRGRLTPSPDIIVLSDNEASSPRSSSRMEERLKAANLEMFKGKGMEERQQLIKQLRDELRLEEARLVLLKKLRQSQLQKENVVQKTPVVQNAASIVQPSPAHVGQQGLSKLPSRPGAQGIEPQNMRTLQGHSVIRSATNTTLPHMLMSQRVIAPNPAQLQGQRGPPKPGIVRTTTPNMNPAISYQPQSSSSVPCQRTTSSAIYMNLASHIQPGTVNRVSSPLPSPSAMSDAANSQAAAKLALRKQLEKTLLEIPPPKPPAPLLHFLPSAANSEFIYMVGLEEVVQSVIDSQGKNCASLLRVEPFVCAQCRTDFTPHWKQEKNGKILCEQCMTSNQKKALKAEHTNRLKNAFVKALQQEQEIEQRLQQQAALSPTTAPAVSSVSKQETIMRHHTLRQAPQPQSSLQRGIPTSARSMLSNFAQAPQLSVPGGLLGMPGVNIAYLNTGIGGHKAPSLADRQREYLLDMIPPRSISQSISGQK
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
17PhosphorylationRLNLLKRSLDPADER
HHHHHHHCCCCCHHH
35.2222817900
52AcetylationMLALLKRKDLANLEV
HHHHHHCHHHCCCCC
56.356569251
73AcetylationKQDGSGVKGYEEKLN
CCCCCCCCCCHHHHC
60.346569083
113PhosphorylationVDMSARRSEPDRGRL
CCCCCCCCCCCCCCC
48.1827087446
121PhosphorylationEPDRGRLTPSPDIIV
CCCCCCCCCCCCEEE
21.9918388127
123PhosphorylationDRGRLTPSPDIIVLS
CCCCCCCCCCEEEEC
29.9324925903
130PhosphorylationSPDIIVLSDNEASSP
CCCEEEECCCCCCCC
27.7424925903
135PhosphorylationVLSDNEASSPRSSSR
EECCCCCCCCCCCHH
34.4024925903
136PhosphorylationLSDNEASSPRSSSRM
ECCCCCCCCCCCHHH
31.2327087446
139PhosphorylationNEASSPRSSSRMEER
CCCCCCCCCHHHHHH
35.7326745281
140PhosphorylationEASSPRSSSRMEERL
CCCCCCCCHHHHHHH
24.2026745281
141PhosphorylationASSPRSSSRMEERLK
CCCCCCCHHHHHHHH
36.5726745281
190PhosphorylationLLKKLRQSQLQKENV
HHHHHHHHHHHHCCC
26.8227841257
194UbiquitinationLRQSQLQKENVVQKT
HHHHHHHHCCCCCCC
60.9027667366
200UbiquitinationQKENVVQKTPVVQNA
HHCCCCCCCHHHCCH
43.09-
209PhosphorylationPVVQNAASIVQPSPA
HHHCCHHHHHCCCCC
22.38-
214PhosphorylationAASIVQPSPAHVGQQ
HHHHHCCCCCCCCCC
20.0226745281
224PhosphorylationHVGQQGLSKLPSRPG
CCCCCCCCCCCCCCC
38.6826643407
228PhosphorylationQGLSKLPSRPGAQGI
CCCCCCCCCCCCCCC
62.6425338131
247PhosphorylationMRTLQGHSVIRSATN
CCEECCCCHHHCCCC
26.5129176673
288PhosphorylationPKPGIVRTTTPNMNP
CCCCCCEECCCCCCC
24.9126643407
289PhosphorylationKPGIVRTTTPNMNPA
CCCCCEECCCCCCCC
29.6826643407
290PhosphorylationPGIVRTTTPNMNPAI
CCCCEECCCCCCCCC
16.4427600695
318PhosphorylationRTTSSAIYMNLASHI
CCCCCCHHHHHHHHC
4.62-
334PhosphorylationPGTVNRVSSPLPSPS
CCCCCCCCCCCCCHH
24.0125521595
335PhosphorylationGTVNRVSSPLPSPSA
CCCCCCCCCCCCHHH
27.8327087446
339PhosphorylationRVSSPLPSPSAMSDA
CCCCCCCCHHHCCHH
38.8925521595
341PhosphorylationSSPLPSPSAMSDAAN
CCCCCCHHHCCHHHH
40.7225521595
344PhosphorylationLPSPSAMSDAANSQA
CCCHHHCCHHHHHHH
24.6627087446
349PhosphorylationAMSDAANSQAAAKLA
HCCHHHHHHHHHHHH
19.2325619855
463AcetylationAEHTNRLKNAFVKAL
HHHHHHHHHHHHHHH
42.8923806337
468UbiquitinationRLKNAFVKALQQEQE
HHHHHHHHHHHHHHH
36.6022790023
487PhosphorylationLQQQAALSPTTAPAV
HHHHHCCCCCCHHHH
18.5725521595
489PhosphorylationQQAALSPTTAPAVSS
HHHCCCCCCHHHHHC
32.0125521595
490PhosphorylationQAALSPTTAPAVSSV
HHCCCCCCHHHHHCC
33.7524925903
495PhosphorylationPTTAPAVSSVSKQET
CCCHHHHHCCCHHHH
27.4225619855
496PhosphorylationTTAPAVSSVSKQETI
CCHHHHHCCCHHHHH
24.6625619855
498PhosphorylationAPAVSSVSKQETIMR
HHHHHCCCHHHHHHH
30.4825619855
518PhosphorylationQAPQPQSSLQRGIPT
CCCCCCCHHHCCCCH
24.2329899451
585O-linked_GlycosylationLDMIPPRSISQSISG
HHHCCCCHHHHHCCC
32.1630059200
587PhosphorylationMIPPRSISQSISGQK
HCCCCHHHHHCCCCC
21.0827600695
589PhosphorylationPPRSISQSISGQK--
CCCHHHHHCCCCC--
16.3629514104

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P66B_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NANOG_MOUSENanogphysical
18454139

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P66B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121 AND SER-123, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121 AND SER-123, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121; SER-123; SER-130AND SER-136, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND MASSSPECTROMETRY.

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