PP1RA_HUMAN - dbPTM
PP1RA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP1RA_HUMAN
UniProt AC Q96QC0
Protein Name Serine/threonine-protein phosphatase 1 regulatory subunit 10
Gene Name PPP1R10
Organism Homo sapiens (Human).
Sequence Length 940
Subcellular Localization Nucleus . Found in discrete nucleoplasmic bodies and within nucleoli. Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase (By similarity)..
Protein Description Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers (By similarity)..
Protein Sequence MGSGPIDPKELLKGLDSFLNRDGEVKSVDGISKIFSLMKEARKMVSRCTYLNILLQTRSPEILVKFIDVGGYKLLNNWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKDEGKSRTTLPERPLTEVKAETRAEEAPEKKREKPKSLRTTAPSHAKFRSTGLELETPSLVPVKKNASTVVVSDKYNLKPIPLKRQSNVAAPGDATPPAEKKYKPLNTTPNATKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAPPSEAMDADRPGTPVPPVEVPELMDTASLEPGALDAKPVESPGDPNQLTRKGRKRKSVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVTPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECSMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKGPQGPGGGGINVQEILTSIMGSPNSHPSEELLKQPDYSDKIKQMLVPHGLLGPGPIANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPPRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPPFRGARGGRSGGGPPNGRGGPGGGMVGGGGHRPHEGPGGGMGNSSGHRPHEGPGGGMGSGHRPHEGPGGSMGGGGGHRPHEGPGGGISGGSGHRPHEGPGGGMGAGGGHRPHEGPGGSMGGSGGHRPHEGPGHGGPHGHRPHDVPGHRGHDHRGPPPHEHRGHDGPGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP
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
3Phosphorylation-----MGSGPIDPKE
-----CCCCCCCHHH		39.8530631047
13UbiquitinationIDPKELLKGLDSFLN
CCHHHHHHHHHHHHC		70.7921890473
26AcetylationLNRDGEVKSVDGISK
HCCCCCCCCHHHHHH		40.2226051181
27PhosphorylationNRDGEVKSVDGISKI
CCCCCCCCHHHHHHH		30.5321406692
32PhosphorylationVKSVDGISKIFSLMK
CCCHHHHHHHHHHHH		25.8120068231
33AcetylationKSVDGISKIFSLMKE
CCHHHHHHHHHHHHH		45.9426051181
33UbiquitinationKSVDGISKIFSLMKE
CCHHHHHHHHHHHHH		45.9421890473
36PhosphorylationDGISKIFSLMKEARK
HHHHHHHHHHHHHHH		30.9020068231
39AcetylationSKIFSLMKEARKMVS
HHHHHHHHHHHHHHH		54.2225953088
49PhosphorylationRKMVSRCTYLNILLQ
HHHHHHHHHHHHHHH		29.9022210691
57PhosphorylationYLNILLQTRSPEILV
HHHHHHHCCCHHHEE		32.8422210691
115AcetylationLKQNNTAKLVKQLSK
HHHCCHHHHHHHHHC		52.3425953088
118AcetylationNNTAKLVKQLSKSSE
CCHHHHHHHHHCCCC		56.8327452117
118UbiquitinationNNTAKLVKQLSKSSE
CCHHHHHHHHHCCCC		56.83-
121PhosphorylationAKLVKQLSKSSEDEE
HHHHHHHHCCCCHHH		28.1830624053
134PhosphorylationEELRKLASVLVSDWM
HHHHHHHHHHHHHHH		26.81-
138PhosphorylationKLASVLVSDWMAVIR
HHHHHHHHHHHHHHH		22.76-
149PhosphorylationAVIRSQSSTQPAEKD
HHHHHCCCCCCCCHH		24.35-
150PhosphorylationVIRSQSSTQPAEKDK
HHHHCCCCCCCCHHH		43.76-
168PhosphorylationKDEGKSRTTLPERPL
HCCCCCCCCCCCCCC		39.5128555341
179SumoylationERPLTEVKAETRAEE
CCCCCHHHHHHHHHH		33.98-
179SumoylationERPLTEVKAETRAEE
CCCCCHHHHHHHHHH		33.9817000644
200PhosphorylationEKPKSLRTTAPSHAK
CCCCCCCCCCCCCHH		32.3830576142
207AcetylationTTAPSHAKFRSTGLE
CCCCCCHHHHCCCCE		35.5719608861
207UbiquitinationTTAPSHAKFRSTGLE
CCCCCCHHHHCCCCE		35.5719608861
211PhosphorylationSHAKFRSTGLELETP
CCHHHHCCCCEEECC		41.3428555341
217PhosphorylationSTGLELETPSLVPVK
CCCCEEECCCEEECC		30.7028555341
224AcetylationTPSLVPVKKNASTVV
CCCEEECCCCCCEEE		33.9525953088
236PhosphorylationTVVVSDKYNLKPIPL
EEEEECCCCCEECCC		30.62-
239AcetylationVSDKYNLKPIPLKRQ
EECCCCCEECCCCCC		36.9423236377
239UbiquitinationVSDKYNLKPIPLKRQ
EECCCCCEECCCCCC		36.9421890473
244AcetylationNLKPIPLKRQSNVAA
CCEECCCCCCCCCCC		42.9325953088
244MethylationNLKPIPLKRQSNVAA
CCEECCCCCCCCCCC		42.9369475
247PhosphorylationPIPLKRQSNVAAPGD
ECCCCCCCCCCCCCC		36.9930266825
256PhosphorylationVAAPGDATPPAEKKY
CCCCCCCCCCHHHCC		34.2530266825
261AcetylationDATPPAEKKYKPLNT
CCCCCHHHCCCCCCC		64.6123749302
262AcetylationATPPAEKKYKPLNTT
CCCCHHHCCCCCCCC		50.4330583163
262SumoylationATPPAEKKYKPLNTT
CCCCHHHCCCCCCCC		50.4328112733
263PhosphorylationTPPAEKKYKPLNTTP
CCCHHHCCCCCCCCC		28.9829396449
264AcetylationPPAEKKYKPLNTTPN
CCHHHCCCCCCCCCC		52.4926051181
268PhosphorylationKKYKPLNTTPNATKE
HCCCCCCCCCCCCCE		51.8421712546
269PhosphorylationKYKPLNTTPNATKEI
CCCCCCCCCCCCCEE		17.3025159151
273PhosphorylationLNTTPNATKEIKVKI
CCCCCCCCCEEEEEE		35.5322199227
274AcetylationNTTPNATKEIKVKII
CCCCCCCCEEEEEEC		55.8423749302
274UbiquitinationNTTPNATKEIKVKII
CCCCCCCCEEEEEEC		55.8419608861
297PhosphorylationGFLDALNSAPVPGIK
CHHHHHHCCCCCCCE		34.5020068231
313PhosphorylationKKKKKVLSPTAAKPS
CCCCEECCCCCCCCC		24.1629255136
315PhosphorylationKKKVLSPTAAKPSPF
CCEECCCCCCCCCCC		35.5522167270
318AcetylationVLSPTAAKPSPFEGK
ECCCCCCCCCCCCCC		43.4926051181
320PhosphorylationSPTAAKPSPFEGKTS
CCCCCCCCCCCCCCC		41.3323927012
326PhosphorylationPSPFEGKTSTEPSTA
CCCCCCCCCCCCCCC		52.3026074081
327PhosphorylationSPFEGKTSTEPSTAK
CCCCCCCCCCCCCCC		33.9726074081
328PhosphorylationPFEGKTSTEPSTAKP
CCCCCCCCCCCCCCC		58.0926074081
331PhosphorylationGKTSTEPSTAKPSSP
CCCCCCCCCCCCCCC		34.4626074081
332PhosphorylationKTSTEPSTAKPSSPE
CCCCCCCCCCCCCCC		49.7926074081
336PhosphorylationEPSTAKPSSPEPAPP
CCCCCCCCCCCCCCC		58.7928387310
337PhosphorylationPSTAKPSSPEPAPPS
CCCCCCCCCCCCCCH		41.6428387310
344PhosphorylationSPEPAPPSEAMDADR
CCCCCCCHHHCCCCC		36.6126074081
354PhosphorylationMDADRPGTPVPPVEV
CCCCCCCCCCCCCCC		24.6426074081
367PhosphorylationEVPELMDTASLEPGA
CCCCCCCCCCCCCCC		12.2726074081
369PhosphorylationPELMDTASLEPGALD
CCCCCCCCCCCCCCC		35.0426074081
382PhosphorylationLDAKPVESPGDPNQL
CCCCCCCCCCCHHHC		34.1219664994
390PhosphorylationPGDPNQLTRKGRKRK
CCCHHHCCCCCCCCC		22.1426552605
398PhosphorylationRKGRKRKSVTWPEEG
CCCCCCCCCCCCCCC		28.8925159151
400PhosphorylationGRKRKSVTWPEEGKL
CCCCCCCCCCCCCCE		42.2519691289
406AcetylationVTWPEEGKLREYFYF
CCCCCCCCEEEEEEE		47.8825953088
4252-HydroxyisobutyrylationTERVNVNKIKDFGEA
CCCCCHHHHHHHHHH		47.02-
441MethylationKREILSDRHAFETAR
HHHHHCCHHHHHHHH		21.47115488023
451PhosphorylationFETARRLSHDNMEEK
HHHHHHHCCCCHHHC		27.3024247654
471PhosphorylationPRPLVLPSPLVTPGS
CCCEECCCCCCCCCC		27.0629255136
475PhosphorylationVLPSPLVTPGSNSQE
ECCCCCCCCCCCHHH		29.6123312004
491UbiquitinationYIQAEREKGILQELF
HHHHHHHHCHHHHHH		58.43-
501UbiquitinationLQELFLNKESPHEPD
HHHHHCCCCCCCCCC		62.81-
503PhosphorylationELFLNKESPHEPDPE
HHHCCCCCCCCCCCC		32.9224719451
527PhosphorylationIPLDEECSMDETPYV
CCCCCCCCCCCCCCE		32.3320873877
531PhosphorylationEECSMDETPYVETLE
CCCCCCCCCCEEECC		18.6920873877
533PhosphorylationCSMDETPYVETLEPG
CCCCCCCCEEECCCC		20.5220873877
536PhosphorylationDETPYVETLEPGGSG
CCCCCEEECCCCCCC		26.7830576142
542PhosphorylationETLEPGGSGGSPDGA
EECCCCCCCCCCCCC		45.9930278072
545PhosphorylationEPGGSGGSPDGAGGS
CCCCCCCCCCCCCCC		24.2830278072
552PhosphorylationSPDGAGGSKLPPVLA
CCCCCCCCCCCHHHH		30.0630278072
586PhosphorylationINVQEILTSIMGSPN
CCHHHHHHHHHCCCC		23.1317081983
587PhosphorylationNVQEILTSIMGSPNS
CHHHHHHHHHCCCCC		13.7225159151
591PhosphorylationILTSIMGSPNSHPSE
HHHHHHCCCCCCCCH		11.9725159151
594PhosphorylationSIMGSPNSHPSEELL
HHHCCCCCCCCHHHH		39.9121712546
597PhosphorylationGSPNSHPSEELLKQP
CCCCCCCCHHHHHCC		37.9824300666
602UbiquitinationHPSEELLKQPDYSDK
CCCHHHHHCCCCHHH		72.85-
606PhosphorylationELLKQPDYSDKIKQM
HHHHCCCCHHHHHHH		26.0026074081
607PhosphorylationLLKQPDYSDKIKQML
HHHCCCCHHHHHHHH		39.5526074081
609UbiquitinationKQPDYSDKIKQMLVP
HCCCCHHHHHHHHCC		45.95-
665DimethylationPGGPVGPRLLGPPPP
CCCCCCHHHCCCCCC		36.29-
665MethylationPGGPVGPRLLGPPPP
CCCCCCHHHCCCCCC		36.2924129315
674DimethylationLGPPPPPRGGDPFWD
CCCCCCCCCCCCCCC		68.45-
674MethylationLGPPPPPRGGDPFWD
CCCCCCCCCCCCCCC		68.4530762913
688MethylationDGPGDPMRGGPMRGG
CCCCCCCCCCCCCCC		52.9154558187
693MethylationPMRGGPMRGGPGPGP
CCCCCCCCCCCCCCC		50.4824129315
705MethylationPGPGPYHRGRGGRGG
CCCCCCCCCCCCCCC		30.5724411411
707MethylationPGPYHRGRGGRGGNE
CCCCCCCCCCCCCCC		44.3354558195
710MethylationYHRGRGGRGGNEPPP
CCCCCCCCCCCCCCC		53.3154558211
723MethylationPPPPPPFRGARGGRS
CCCCCCCCCCCCCCC		43.5754558179
726MethylationPPPFRGARGGRSGGG
CCCCCCCCCCCCCCC		51.4254558203
729MethylationFRGARGGRSGGGPPN
CCCCCCCCCCCCCCC		34.6554558219
738MethylationGGGPPNGRGGPGGGM
CCCCCCCCCCCCCCC		54.24-
764PhosphorylationPGGGMGNSSGHRPHE
CCCCCCCCCCCCCCC		31.7822210691
765PhosphorylationGGGMGNSSGHRPHEG
CCCCCCCCCCCCCCC		42.4922210691
779PhosphorylationGPGGGMGSGHRPHEG
CCCCCCCCCCCCCCC		23.6426552605
790PhosphorylationPHEGPGGSMGGGGGH
CCCCCCCCCCCCCCC		21.8526552605
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 PP1RA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
398SPhosphorylation

23186163
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 PP1RA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR82_HUMANWDR82physical
20516061
PP1A_HUMANPPP1CAphysical
20516061
PP1B_HUMANPPP1CBphysical
20516061
PP1G_HUMANPPP1CCphysical
20516061
TOX4_HUMANTOX4physical
20516061
PP1RA_HUMANPPP1R10physical
20516061
HSP74_HUMANHSPA4physical
20516061
PP1A_HUMANPPP1CAphysical
12574161
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 PP1RA_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-207 AND LYS-239, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-545, 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-313 AND SER-591, ANDMASS SPECTROMETRY.
"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-313, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, 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 THR-256, AND MASSSPECTROMETRY.

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