PP6R3_HUMAN - dbPTM
PP6R3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP6R3_HUMAN
UniProt AC Q5H9R7
Protein Name Serine/threonine-protein phosphatase 6 regulatory subunit 3
Gene Name PPP6R3
Organism Homo sapiens (Human).
Sequence Length 873
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance..
Protein Sequence MFWKFDLHSSSHIDTLLEREDVTLKELMDEEDVLQECKAQNRKLIEFLLKAECLEDLVSFIIEEPPQDMDEKIRYKYPNISCELLTSDVSQMNDRLGEDESLLMKLYSFLLNDSPLNPLLASFFSKVLSILISRKPEQIVDFLKKKHDFVDLIIKHIGTSAIMDLLLRLLTCIEPPQPRQDVLNWLNEEKIIQRLVEIVHPSQEEDRHSNASQSLCEIVRLSRDQMLQIQNSTEPDPLLATLEKQEIIEQLLSNIFHKEKNESAIVSAIQILLTLLETRRPTFEGHIEICPPGMSHSACSVNKSVLEAIRGRLGSFHELLLEPPKKSVMKTTWGVLDPPVGNTRLNVIRLISSLLQTNTSSINGDLMELNSIGVILNMFFKYTWNNFLHTQVEICIALILASPFENTENATITDQDSTGDNLLLKHLFQKCQLIERILEAWEMNEKKQAEGGRRHGYMGHLTRIANCIVHSTDKGPNSALVQQLIKDLPDEVRERWETFCTSSLGETNKRNTVDLVTTCHIHSSSDDEIDFKETGFSQDSSLQQAFSDYQMQQMTSNFIDQFGFNDEKFADQDDIGNVSFDRVSDINFTLNTNESGNIALFEACCKERIQQFDDGGSDEEDIWEEKHIAFTPESQRRSSSGSTDSEESTDSEEEDGAKQDLFEPSSANTEDKMEVDLSEPPNWSANFDVPMETTHGAPLDSVGSDVWSTEEPMPTKETGWASFSEFTSSLSTKDSLRSNSPVEMETSTEPMDPLTPSAAALAVQPEAAGSVAMEASSDGEEDAESTDKVTETVMNGGMKETLSLTVDAKTETAVFKSEEGKLSTSQDAACKDAEECPETAEAKCAAPRPPSSSPEQRTGQPSAPGDTSVNGPV
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
9PhosphorylationFWKFDLHSSSHIDTL
CCEEECCCCHHHHHH		40.6123312004
10PhosphorylationWKFDLHSSSHIDTLL
CEEECCCCHHHHHHH		18.3923312004
11PhosphorylationKFDLHSSSHIDTLLE
EEECCCCHHHHHHHH		27.7223312004
25UbiquitinationEREDVTLKELMDEED
HHCCCCHHHHCCHHH		39.16-
28SulfoxidationDVTLKELMDEEDVLQ
CCCHHHHCCHHHHHH		6.8121406390
38UbiquitinationEDVLQECKAQNRKLI
HHHHHHHHHHCHHHH		52.86-
104SulfoxidationGEDESLLMKLYSFLL
CCCHHHHHHHHHHHH		3.2221406390
108PhosphorylationSLLMKLYSFLLNDSP
HHHHHHHHHHHCCCC		21.61-
125PhosphorylationPLLASFFSKVLSILI
HHHHHHHHHHHHHHH		21.6122210691
133PhosphorylationKVLSILISRKPEQIV
HHHHHHHHCCHHHHH		30.7022210691
1442-HydroxyisobutyrylationEQIVDFLKKKHDFVD
HHHHHHHHHCCCHHH		60.82-
190UbiquitinationLNWLNEEKIIQRLVE
HHHHCHHHHHHHHHH		38.6422053931
190 (in isoform 1)Ubiquitination-38.6421890473
190 (in isoform 2)Ubiquitination-38.6421890473
190 (in isoform 3)Ubiquitination-38.6421890473
190 (in isoform 4)Ubiquitination-38.6421890473
190 (in isoform 5)Ubiquitination-38.6421890473
190 (in isoform 6)Ubiquitination-38.6421890473
202PhosphorylationLVEIVHPSQEEDRHS
HHHHHCCCCHHHCCC		35.0320873877
207MethylationHPSQEEDRHSNASQS
CCCCHHHCCCCHHHH		38.11115493303
209PhosphorylationSQEEDRHSNASQSLC
CCHHHCCCCHHHHHH		34.6820873877
212PhosphorylationEDRHSNASQSLCEIV
HHCCCCHHHHHHHHH		25.2620873877
214PhosphorylationRHSNASQSLCEIVRL
CCCCHHHHHHHHHHH		32.2720873877
226SulfoxidationVRLSRDQMLQIQNST
HHHCHHHCHHCCCCC		3.3121406390
241PhosphorylationEPDPLLATLEKQEII
CCCCCHHHHCHHHHH		35.1024719451
274PhosphorylationSAIQILLTLLETRRP
HHHHHHHHHHHHCCC		26.3322210691
278PhosphorylationILLTLLETRRPTFEG
HHHHHHHHCCCCCCC		31.7622210691
295PhosphorylationEICPPGMSHSACSVN
EECCCCCCCCHHHCC		21.8728270605
297PhosphorylationCPPGMSHSACSVNKS
CCCCCCCCHHHCCHH		24.5428270605
300PhosphorylationGMSHSACSVNKSVLE
CCCCCHHHCCHHHHH		28.5728270605
315PhosphorylationAIRGRLGSFHELLLE
HHHHCCCCHHHHHCC		28.2029255136
315 (in isoform 5)Phosphorylation-28.2024719451
327PhosphorylationLLEPPKKSVMKTTWG
HCCCCCCCCCEEECC		33.3021060948
330UbiquitinationPPKKSVMKTTWGVLD
CCCCCCCEEECCCCC		40.4221906983
330 (in isoform 1)Ubiquitination-40.4221890473
330 (in isoform 2)Ubiquitination-40.4221890473
330 (in isoform 5)Ubiquitination-40.4221890473
330 (in isoform 6)Ubiquitination-40.4221890473
331PhosphorylationPKKSVMKTTWGVLDP
CCCCCCEEECCCCCC		15.0821060948
332PhosphorylationKKSVMKTTWGVLDPP
CCCCCEEECCCCCCC		18.0721060948
395 (in isoform 3)Ubiquitination-0.6621890473
395 (in isoform 4)Ubiquitination-0.6621890473
430UbiquitinationLLKHLFQKCQLIERI
HHHHHHHHHHHHHHH		19.33-
435 (in isoform 3)Ubiquitination-42.1121890473
435 (in isoform 4)Ubiquitination-42.1121890473
446UbiquitinationEAWEMNEKKQAEGGR
HHHHHCHHHHHCCCC		45.2221906983
446 (in isoform 1)Ubiquitination-45.2221890473
446 (in isoform 2)Ubiquitination-45.2221890473
446 (in isoform 5)Ubiquitination-45.2221890473
446 (in isoform 6)Ubiquitination-45.2221890473
474AcetylationCIVHSTDKGPNSALV
EEEECCCCCCCHHHH		76.1025953088
474UbiquitinationCIVHSTDKGPNSALV
EEEECCCCCCCHHHH		76.10-
486UbiquitinationALVQQLIKDLPDEVR
HHHHHHHHCCCHHHH		62.9021906983
486 (in isoform 1)Ubiquitination-62.9021890473
486 (in isoform 2)Ubiquitination-62.9021890473
486 (in isoform 5)Ubiquitination-62.9021890473
486 (in isoform 6)Ubiquitination-62.9021890473
499 (in isoform 4)Phosphorylation-2.65-
509UbiquitinationSSLGETNKRNTVDLV
HCCCCCCCCCCEEEE		55.21-
512PhosphorylationGETNKRNTVDLVTTC
CCCCCCCCEEEEEEE		21.3028450419
517PhosphorylationRNTVDLVTTCHIHSS
CCCEEEEEEEEECCC		30.8830278072
518PhosphorylationNTVDLVTTCHIHSSS
CCEEEEEEEEECCCC		8.4630278072
523PhosphorylationVTTCHIHSSSDDEID
EEEEEECCCCCCCCC		30.8230266825
523 (in isoform 5)Phosphorylation-30.8224719451
524PhosphorylationTTCHIHSSSDDEIDF
EEEEECCCCCCCCCC		24.5130266825
524 (in isoform 5)Phosphorylation-24.5124719451
525PhosphorylationTCHIHSSSDDEIDFK
EEEECCCCCCCCCCC		52.6930266825
525 (in isoform 5)Phosphorylation-52.6924719451
537PhosphorylationDFKETGFSQDSSLQQ
CCCHHCCCCCHHHHH		34.1319664994
537 (in isoform 4)Phosphorylation-34.13-
546 (in isoform 3)Ubiquitination-5.0521890473
546 (in isoform 4)Ubiquitination-5.0521890473
551 (in isoform 4)Phosphorylation-2.14-
554 (in isoform 4)Phosphorylation-2.20-
556PhosphorylationYQMQQMTSNFIDQFG
HHHHHHHHHHHHHHC		25.1330576142
568UbiquitinationQFGFNDEKFADQDDI
HHCCCCHHCCCCCCC		49.03-
579PhosphorylationQDDIGNVSFDRVSDI
CCCCCCEEEEEEEEE		25.9819664994
579 (in isoform 5)Phosphorylation-25.9821406692
597 (in isoform 6)Ubiquitination-26.1621890473
617PhosphorylationQQFDDGGSDEEDIWE
HCCCCCCCCHHHHHH		47.5919664994
617 (in isoform 5)Phosphorylation-47.5924719451
620 (in isoform 2)Ubiquitination-60.8421890473
626UbiquitinationEEDIWEEKHIAFTPE
HHHHHHHHEEEECHH		28.882190698
626 (in isoform 1)Ubiquitination-28.8821890473
626 (in isoform 5)Ubiquitination-28.8821890473
631PhosphorylationEEKHIAFTPESQRRS
HHHEEEECHHHHCCC		19.6817525332
631 (in isoform 5)Phosphorylation-19.6824719451
634PhosphorylationHIAFTPESQRRSSSG
EEEECHHHHCCCCCC		30.1417525332
634 (in isoform 5)Phosphorylation-30.1421406692
638PhosphorylationTPESQRRSSSGSTDS
CHHHHCCCCCCCCCC		30.9223401153
639PhosphorylationPESQRRSSSGSTDSE
HHHHCCCCCCCCCCC		36.5921406692
640PhosphorylationESQRRSSSGSTDSEE
HHHCCCCCCCCCCCC		37.7021406692
642PhosphorylationQRRSSSGSTDSEEST
HCCCCCCCCCCCCCC		30.8718669648
642 (in isoform 4)Phosphorylation-30.87-
643PhosphorylationRRSSSGSTDSEESTD
CCCCCCCCCCCCCCC		47.2530576142
645PhosphorylationSSSGSTDSEESTDSE
CCCCCCCCCCCCCCC		43.2721406692
648PhosphorylationGSTDSEESTDSEEED
CCCCCCCCCCCCCCC		33.2021406692
649PhosphorylationSTDSEESTDSEEEDG
CCCCCCCCCCCCCCC		46.9921406692
651PhosphorylationDSEESTDSEEEDGAK
CCCCCCCCCCCCCCC		47.1730576142
651 (in isoform 5)Phosphorylation-47.1721406692
660 (in isoform 4)Phosphorylation-53.25-
665PhosphorylationKQDLFEPSSANTEDK
CCCCCCCCCCCCCCC		34.5825850435
666PhosphorylationQDLFEPSSANTEDKM
CCCCCCCCCCCCCCE		35.9325850435
669PhosphorylationFEPSSANTEDKMEVD
CCCCCCCCCCCEECC		45.3225850435
718PhosphorylationEPMPTKETGWASFSE
CCCCCCCCCCCCHHH		39.3129978859
722PhosphorylationTKETGWASFSEFTSS
CCCCCCCCHHHHHHC		23.8521712546
722 (in isoform 5)Phosphorylation-23.8527251275
724PhosphorylationETGWASFSEFTSSLS
CCCCCCHHHHHHCCC		29.3429978859
727PhosphorylationWASFSEFTSSLSTKD
CCCHHHHHHCCCCHH		17.2227251275
728PhosphorylationASFSEFTSSLSTKDS
CCHHHHHHCCCCHHH		34.3027251275
729PhosphorylationSFSEFTSSLSTKDSL
CHHHHHHCCCCHHHH		24.2327251275
729 (in isoform 5)Phosphorylation-24.2327251275
731PhosphorylationSEFTSSLSTKDSLRS
HHHHHCCCCHHHHHC		35.0526074081
731 (in isoform 5)Phosphorylation-35.0527251275
732PhosphorylationEFTSSLSTKDSLRSN
HHHHCCCCHHHHHCC		44.1326074081
735PhosphorylationSSLSTKDSLRSNSPV
HCCCCHHHHHCCCCC		27.5126074081
738PhosphorylationSTKDSLRSNSPVEME
CCHHHHHCCCCCCCC		47.1326074081
738 (in isoform 5)Phosphorylation-47.1327251275
740PhosphorylationKDSLRSNSPVEMETS
HHHHHCCCCCCCCCC		31.4126074081
740 (in isoform 5)Phosphorylation-31.4127251275
745 (in isoform 4)Phosphorylation-26.54-
746PhosphorylationNSPVEMETSTEPMDP
CCCCCCCCCCCCCCC		39.3726074081
747PhosphorylationSPVEMETSTEPMDPL
CCCCCCCCCCCCCCC		19.9126074081
748PhosphorylationPVEMETSTEPMDPLT
CCCCCCCCCCCCCCC		52.0726074081
755PhosphorylationTEPMDPLTPSAAALA
CCCCCCCCCCHHHHH		22.1526074081
757PhosphorylationPMDPLTPSAAALAVQ
CCCCCCCCHHHHHCC		25.8826074081
770PhosphorylationVQPEAAGSVAMEASS
CCHHHHCCEEEECCC		11.2828348404
770 (in isoform 5)Phosphorylation-11.2827251275
771 (in isoform 4)Phosphorylation-6.02-
773 (in isoform 4)Phosphorylation-4.07-
776PhosphorylationGSVAMEASSDGEEDA
CCEEEECCCCCCCCH		18.6922468782
777PhosphorylationSVAMEASSDGEEDAE
CEEEECCCCCCCCHH		57.6027251275
777 (in isoform 5)Phosphorylation-57.6027251275
790PhosphorylationAESTDKVTETVMNGG
HHHCCHHHHHHHCCC		31.5126552605
792PhosphorylationSTDKVTETVMNGGMK
HCCHHHHHHHCCCCE		18.7126552605
803PhosphorylationGGMKETLSLTVDAKT
CCCEEEEEEEEECCC		29.4327251275
803 (in isoform 5)Phosphorylation-29.4327251275
816AcetylationKTETAVFKSEEGKLS
CCCEEEEECCCCCCC		50.8125953088
823PhosphorylationKSEEGKLSTSQDAAC
ECCCCCCCCCCCHHC		29.5122817901
824PhosphorylationSEEGKLSTSQDAACK
CCCCCCCCCCCHHCC		40.6225159151
825PhosphorylationEEGKLSTSQDAACKD
CCCCCCCCCCHHCCC		23.7625159151
831AcetylationTSQDAACKDAEECPE
CCCCHHCCCHHHCCH		56.0725953088
851PhosphorylationCAAPRPPSSSPEQRT
HCCCCCCCCCCCHHC		46.2423401153
852PhosphorylationAAPRPPSSSPEQRTG
CCCCCCCCCCCHHCC		56.5430266825
853PhosphorylationAPRPPSSSPEQRTGQ
CCCCCCCCCCHHCCC		36.4723927012
857 (in isoform 5)Phosphorylation-38.8827251275
858PhosphorylationSSSPEQRTGQPSAPG
CCCCCHHCCCCCCCC		39.6026074081
858 (in isoform 5)Phosphorylation-39.6024719451
862PhosphorylationEQRTGQPSAPGDTSV
CHHCCCCCCCCCCCC		38.9326074081
867PhosphorylationQPSAPGDTSVNGPV-
CCCCCCCCCCCCCC-		40.2525159151
868PhosphorylationPSAPGDTSVNGPV--
CCCCCCCCCCCCC--		20.5125159151
874 (in isoform 5)Phosphorylation-27251275
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 PP6R3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP6R3_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 PP6R3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRKDC_HUMANPRKDCphysical
20065038
GPSM1_HUMANGPSM1physical
23718855
UBP10_HUMANUSP10physical
24255178
ACD11_HUMANACAD11physical
24255178
ANR28_HUMANANKRD28physical
24255178
ANR44_HUMANANKRD44physical
24255178
ANR52_HUMANANKRD52physical
24255178
AP1B1_HUMANAP1B1physical
24255178
AP2A1_HUMANAP2A1physical
24255178
AP2A2_HUMANAP2A2physical
24255178
AURKA_HUMANAURKAphysical
24255178
DJC11_HUMANDNAJC11physical
24255178
ECH1_HUMANECH1physical
24255178
ERLN2_HUMANERLIN2physical
24255178
PPP6_HUMANPPP6Cphysical
24255178
PP6R1_HUMANPPP6R1physical
24255178
PP6R2_HUMANPPP6R2physical
24255178
CDC37_HUMANCDC37physical
22863883
ENAH_HUMANENAHphysical
22863883
ETFA_HUMANETFAphysical
22863883
HS90A_HUMANHSP90AA1physical
22863883
HS90B_HUMANHSP90AB1physical
22863883
DIEXF_HUMANDIEXFphysical
26344197
NSUN5_HUMANNSUN5physical
26344197
PPP6_HUMANPPP6Cphysical
26344197
TIPRL_HUMANTIPRLphysical
26344197
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 PP6R3_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 SER-579 AND SER-617, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASSSPECTROMETRY.
"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-617, 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-579; SER-617 ANDSER-722, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-631 AND SER-634, ANDMASS SPECTROMETRY.
"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-579, 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-617, 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 SER-579 AND SER-617, ANDMASS SPECTROMETRY.

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