PP1RA_MOUSE - dbPTM
PP1RA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP1RA_MOUSE
UniProt AC Q80W00
Protein Name Serine/threonine-protein phosphatase 1 regulatory subunit 10
Gene Name Ppp1r10
Organism Mus musculus (Mouse).
Sequence Length 888
Subcellular Localization Nucleus . Found in discrete nucleoplasmic bodies and within nucleoli (By similarity). Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase.
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..
Protein Sequence MGSGPIDPKELLKGLDSFLTRDGEVKSVDGISKIFSLMKEARKMVSRCTYLNIILQTRAPEVLVKFIDVGGYKLLNNWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKEEGKSRTTLPERPLTEVKAETRAEEAPEKKKEKPKSLRTTAPSHAKFRSTGLELDTPSLVPVKKNSSTVVVSDKYNLKPIPLKRQSATAAPGDAAPPAEKKYKPLNTAPNTTKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEQSTAKPSSPEPAPPAEPMDTDRPGTPVPPVEVPELMDAASSEPGALDAKPVDSPGDPNQLTRKGRKRKTVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVIPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECAMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKSPQGPGGGGINVQEILTSIMGSPNSHPSEELLKQPDYSDKLKQMLVPHGLLGPGPVANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPSRGGDPFWDGPGDPMRGGPMRGGPGPAPGPYHRGRGGRGGNEPPPPPPFRGARGGRSGGGPPNGRGGPGGGGMVGGGGHRPHEGPGGSMGSGHRSHDGPGGNMGSGHRSHDGPGGNMGGSGGHRSHEGPGHGGPHGHRPHDVPSHRGHDHRGPPPHEHRGHDGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP
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
227PhosphorylationLVPVKKNSSTVVVSD
CEECCCCCCEEEEEC		35.9427600695
228PhosphorylationVPVKKNSSTVVVSDK
EECCCCCCEEEEECC		34.3229109428
229PhosphorylationPVKKNSSTVVVSDKY
ECCCCCCEEEEECCC		19.6929109428
247PhosphorylationPIPLKRQSATAAPGD
ECCCCCCCCCCCCCC		31.4627149854
249PhosphorylationPLKRQSATAAPGDAA
CCCCCCCCCCCCCCC		28.7129899451
313PhosphorylationKKKKKVLSPTAAKPS
CCCCEECCCCCCCCC		24.1626824392
315PhosphorylationKKKVLSPTAAKPSPF
CCEECCCCCCCCCCC		35.5522942356
320PhosphorylationSPTAAKPSPFEGKTS
CCCCCCCCCCCCCCC		41.3326239621
382PhosphorylationLDAKPVDSPGDPNQL
CCCCCCCCCCCHHHC		30.8927818261
398PhosphorylationRKGRKRKTVTWPEEG
CCCCCCCCEECCCCC		27.48-
451PhosphorylationFETARRLSHDNMEEK
HHHHHHHCCCCHHHC		27.30-
471PhosphorylationPRPLVLPSPLVIPGS
CCCCCCCCCEEECCC		27.0628066266
491UbiquitinationYIQAEREKGILQELF
HHHHHHHHCHHHHHH		58.4322790023
503PhosphorylationELFLNKESPHEPDPE
HHHCCCCCCCCCCCC		32.92-
531PhosphorylationEECAMDETPYVETLE
CCCCCCCCCCEEECC		18.6925159016
533PhosphorylationCAMDETPYVETLEPG
CCCCCCCCEEECCCC		20.5225159016
536PhosphorylationDETPYVETLEPGGSG
CCCCCEEECCCCCCC		26.7825159016
542PhosphorylationETLEPGGSGGSPDGA
EECCCCCCCCCCCCC		45.9925159016
545PhosphorylationEPGGSGGSPDGAGGS
CCCCCCCCCCCCCCC		24.2825159016
552PhosphorylationSPDGAGGSKLPPVLA
CCCCCCCCCCCHHHH		30.0625159016
570PhosphorylationGSMGAGKSPQGPGGG
HHCCCCCCCCCCCCC		22.8725777480
586PhosphorylationINVQEILTSIMGSPN
CCHHHHHHHHHCCCC		23.1326745281
587PhosphorylationNVQEILTSIMGSPNS
CHHHHHHHHHCCCCC		13.7226745281
591PhosphorylationILTSIMGSPNSHPSE
HHHHHHCCCCCCCCH		11.9726239621
594PhosphorylationSIMGSPNSHPSEELL
HHHCCCCCCCCHHHH		39.9121149613
597PhosphorylationGSPNSHPSEELLKQP
CCCCCCCCHHHHHCC		37.9821149613
606PhosphorylationELLKQPDYSDKLKQM
HHHHCCCCHHHHHHH		26.0023984901
607PhosphorylationLLKQPDYSDKLKQML
HHHCCCCHHHHHHHH		35.3323984901
665MethylationPGGPVGPRLLGPPPP
CCCCCCHHHCCCCCC		36.29-
693MethylationPMRGGPMRGGPGPAP
CCCCCCCCCCCCCCC		50.4824129315
737MethylationGGGPPNGRGGPGGGG
CCCCCCCCCCCCCCC		54.2424129315
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
398TPhosphorylation

-
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP1A_HUMANPPP1CAphysical
20360068
WDR82_HUMANWDR82physical
20360068
PP1B_HUMANPPP1CBphysical
20360068
PP1RA_HUMANPPP1R10physical
20360068
ZC3H4_HUMANZC3H4physical
20360068
PP1G_HUMANPPP1CCphysical
20360068
TOX4_HUMANTOX4physical
20360068
TERF2_HUMANTERF2physical
20360068
IPP2_HUMANPPP1R2physical
20360068
PP1A_HUMANPPP1CAphysical
26496610
PP1B_HUMANPPP1CBphysical
26496610
PP1G_HUMANPPP1CCphysical
26496610
TOX4_HUMANTOX4physical
26496610
WDR82_HUMANWDR82physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PP1RA_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-313, AND MASSSPECTROMETRY.

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