P66A_MOUSE - dbPTM
P66A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P66A_MOUSE
UniProt AC Q8CHY6
Protein Name Transcriptional repressor p66 alpha
Gene Name Gatad2a
Organism Mus musculus (Mouse).
Sequence Length 629
Subcellular Localization Nucleus speckle. Speckled nuclear localization requires both CR1 and CR2 regions..
Protein Description Transcriptional repressor (By similarity). Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B (By similarity)..
Protein Sequence MSEEACRTRSQKRTLEPDLTEDDVENKKMKMEKGSSELTVDGDSRVMPEPSAGSAQGLLRTTEAMGTGSGEGLLGDGPVDMRTSHSDMKSEKRPPSPDVIVLSDSEQPSSPRVNGLTTVALKDTSTEALLKSSPEERERMIKQLKEELRLEEAKLVLLKKLRQSQIQKEATAQKPTASSGSTVTTPPPLVRGTQNIPAGKTSLQTSSTRIPGSIIPPPLVRGGQQVSAKLGPQASSQVVMPPLVRGAQIHNIRQHSSTGPPPLLLAPRASVPSMQIQGQRIIQQGLIRVANVPNTSLLVNIPQPTAASMKGTAVASAQANSTPTSVASVVASAESPASRQAAAKLALRKQLEKTLLEIPPPKPPAPEMNFLPSAANNEFIYLVGLEEVVQNLLETQAGRISATAAAAVLSREPYMCVQCKTDFTCRWREKGGAVMCENCMTSNQKKALKVEHTSRLKAAFVKALQQEQEMEQRLLQQGVGTASIKAEPAAPHPTLKQVIKPRRKLAFRSGEARVWNNGSSLQASSQLSRGSATAPRGVLHTFSQSPKLQNAASATALVSRTGRHSERVVGTGKGTASNWKKTPLSTGGTLAFVSPSLAVHKTSSAVDRQREYLLDMIPPRSIPQSATWK
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
20PhosphorylationRTLEPDLTEDDVENK
CCCCCCCCHHHHHHC		44.7629550500
44PhosphorylationELTVDGDSRVMPEPS
EEEECCCCCCCCCCC		32.1027566939
90PhosphorylationTSHSDMKSEKRPPSP
CCHHHCCCCCCCCCC		41.5325367039
96PhosphorylationKSEKRPPSPDVIVLS
CCCCCCCCCCEEEEC		36.0927087446
103PhosphorylationSPDVIVLSDSEQPSS
CCCEEEECCCCCCCC		28.3527087446
105PhosphorylationDVIVLSDSEQPSSPR
CEEEECCCCCCCCCC		34.4527087446
109PhosphorylationLSDSEQPSSPRVNGL
ECCCCCCCCCCCCCE		53.3125521595
110PhosphorylationSDSEQPSSPRVNGLT
CCCCCCCCCCCCCEE		24.3327087446
117PhosphorylationSPRVNGLTTVALKDT
CCCCCCEEEEEEECC		22.1827600695
118PhosphorylationPRVNGLTTVALKDTS
CCCCCEEEEEEECCC		14.6127600695
122UbiquitinationGLTTVALKDTSTEAL
CEEEEEEECCCHHHH		49.58-
124PhosphorylationTTVALKDTSTEALLK
EEEEEECCCHHHHHH		35.6428066266
125PhosphorylationTVALKDTSTEALLKS
EEEEECCCHHHHHHC		34.0928066266
126PhosphorylationVALKDTSTEALLKSS
EEEECCCHHHHHHCC		27.6322817900
131UbiquitinationTSTEALLKSSPEERE
CCHHHHHHCCHHHHH		50.14-
132PhosphorylationSTEALLKSSPEERER
CHHHHHHCCHHHHHH		51.6126745281
133PhosphorylationTEALLKSSPEERERM
HHHHHHCCHHHHHHH		34.4425266776
168UbiquitinationLRQSQIQKEATAQKP
HHHHHHHHHHHCCCC		51.44-
171PhosphorylationSQIQKEATAQKPTAS
HHHHHHHHCCCCCCC		30.6125619855
174UbiquitinationQKEATAQKPTASSGS
HHHHHCCCCCCCCCC		41.70-
176PhosphorylationEATAQKPTASSGSTV
HHHCCCCCCCCCCCC		46.3225619855
178O-linked_GlycosylationTAQKPTASSGSTVTT
HCCCCCCCCCCCCCC		37.4062171419
178PhosphorylationTAQKPTASSGSTVTT
HCCCCCCCCCCCCCC		37.4025619855
179PhosphorylationAQKPTASSGSTVTTP
CCCCCCCCCCCCCCC		34.0125619855
181PhosphorylationKPTASSGSTVTTPPP
CCCCCCCCCCCCCCC		22.9625619855
182PhosphorylationPTASSGSTVTTPPPL
CCCCCCCCCCCCCCC		25.9525619855
184PhosphorylationASSGSTVTTPPPLVR
CCCCCCCCCCCCCCC		33.4025168779
185PhosphorylationSSGSTVTTPPPLVRG
CCCCCCCCCCCCCCC		29.4825521595
221MethylationIIPPPLVRGGQQVSA
CCCCCCEECCEEEEC		51.7324129315
245MethylationVVMPPLVRGAQIHNI
CCCCCCCCCCEEECH		42.2724129315
253MethylationGAQIHNIRQHSSTGP
CCEEECHHHCCCCCC		33.21-
268MethylationPPLLLAPRASVPSMQ
CCEEECCCCCCCCCE		33.61-
270PhosphorylationLLLAPRASVPSMQIQ
EEECCCCCCCCCEEC		35.52-
280MethylationSMQIQGQRIIQQGLI
CCEECCHHHHHCCCE		34.50-
288MethylationIIQQGLIRVANVPNT
HHHCCCEEEECCCCC		26.91-
321PhosphorylationVASAQANSTPTSVAS
EEECCCCCCCCCHHH		38.4925619855
322PhosphorylationASAQANSTPTSVASV
EECCCCCCCCCHHHH		30.3226643407
324PhosphorylationAQANSTPTSVASVVA
CCCCCCCCCHHHHHH		35.6026643407
325PhosphorylationQANSTPTSVASVVAS
CCCCCCCCHHHHHHC		19.5226643407
328PhosphorylationSTPTSVASVVASAES
CCCCCHHHHHHCCCC		18.2426643407
332PhosphorylationSVASVVASAESPASR
CHHHHHHCCCCHHHH		22.4325619855
335PhosphorylationSVVASAESPASRQAA
HHHHCCCCHHHHHHH		26.0322942356
338PhosphorylationASAESPASRQAAAKL
HCCCCHHHHHHHHHH		28.4525619855
403PhosphorylationQAGRISATAAAAVLS
CCHHHHHHHHHHHHC		15.2728059163
509PhosphorylationRRKLAFRSGEARVWN
CHHHHCCCCCEEEEC		34.2325338131
525PhosphorylationGSSLQASSQLSRGSA
CCCCCCCCCCCCCCC		37.8520531401
536MethylationRGSATAPRGVLHTFS
CCCCCCCCCCEECCC		45.4424129315
536Asymmetric dimethylarginineRGSATAPRGVLHTFS
CCCCCCCCCCEECCC		45.44-
541PhosphorylationAPRGVLHTFSQSPKL
CCCCCEECCCCCHHH		22.3325168779
543PhosphorylationRGVLHTFSQSPKLQN
CCCEECCCCCHHHCC		30.7925168779
545PhosphorylationVLHTFSQSPKLQNAA
CEECCCCCHHHCCHH		23.8626824392
553PhosphorylationPKLQNAASATALVSR
HHHCCHHHHHHHHHC		24.60-
559PhosphorylationASATALVSRTGRHSE
HHHHHHHHCCCCCCE		25.60-
585PhosphorylationNWKKTPLSTGGTLAF
CCEECCCCCCCEEEE		26.6423984901
586PhosphorylationWKKTPLSTGGTLAFV
CEECCCCCCCEEEEE		47.5223984901
589PhosphorylationTPLSTGGTLAFVSPS
CCCCCCCEEEEECHH		19.0923984901
594PhosphorylationGGTLAFVSPSLAVHK
CCEEEEECHHHHHHC		11.4325266776
596PhosphorylationTLAFVSPSLAVHKTS
EEEEECHHHHHHCCC		22.8126745281
625PhosphorylationPPRSIPQSATWK---
CCCCCCCCCCCC---		23.47-
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
96SPhosphorylationKinasePRKAA1Q13131
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P66A_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 P66A_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NANOG_MOUSENanogphysical
18454139
SIN3A_MOUSESin3aphysical
18454139
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P66A_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 SER-96, AND MASSSPECTROMETRY.
"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 SER-96, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-103 AND SER-105,AND MASS 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 SER-96; SER-103 AND SER-110,AND MASS SPECTROMETRY.

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