PLCB3_HUMAN - dbPTM
PLCB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLCB3_HUMAN
UniProt AC Q01970
Protein Name 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
Gene Name PLCB3
Organism Homo sapiens (Human).
Sequence Length 1234
Subcellular Localization Membrane
Peripheral membrane protein.
Protein Description The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes..
Protein Sequence MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDSAGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGDEGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQLGSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVEDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLGDGPLVACASNGHAPGSSGHLSGADSESQEENTQL
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
2Acetylation------MAGAQPGVH
------CCCCCCCCE
33.0822223895
26PhosphorylationVETLRRGSKFIKWDE
HHHHHCCCCCEECCC
23.6811278298
30UbiquitinationRRGSKFIKWDEETSS
HCCCCCEECCCCCCC
52.29-
67PhosphorylationEVDTLDISSIRDTRT
EEEEEEHHHCCCCCC
21.2724719451
68PhosphorylationVDTLDISSIRDTRTG
EEEEEHHHCCCCCCC
23.2125954137
94UbiquitinationREVLGFGGPDARLEE
HHHHCCCCCCHHHHH
18.0429967540
106UbiquitinationLEEKLMTVVSGPDPV
HHHHHHHHHCCCCCC
1.6929967540
129UbiquitinationAVQDDTAKVWSEELF
EECCCHHHHHCHHHH
46.4521963094
148PhosphorylationNILAQNASRNTFLRK
HHHHHHCCCCHHHHH
33.3422210691
161MalonylationRKAYTKLKLQVNQDG
HHHHHHHCEEECCCC
38.1326320211
161UbiquitinationRKAYTKLKLQVNQDG
HHHHHHHCEEECCCC
38.1329967540
161AcetylationRKAYTKLKLQVNQDG
HHHHHHHCEEECCCC
38.1325953088
173UbiquitinationQDGRIPVKNILKMFS
CCCCCCHHHHHHHHC
32.6829967540
196UbiquitinationALESCGLKFNRSESI
HHHHCCCCCCCCCCC
26.3621963094
264PhosphorylationPRLNEVLYPPLRPSQ
CCHHHCCCCCCCHHH
14.1628060719
270PhosphorylationLYPPLRPSQARLLIE
CCCCCCHHHHHHHHH
30.0025159151
279PhosphorylationARLLIEKYEPNQQFL
HHHHHHHCCCCHHHH
24.67-
399PhosphorylationVLEAIAETAFKTSPY
HHHHHHHHHCCCCCC
28.5129514088
407PhosphorylationAFKTSPYPVILSFEN
HCCCCCCCEEEEEEC
15.2832645325
424UbiquitinationDSAKQQAKMAEYCRS
HHHHHHHHHHHHHHH
34.01-
428PhosphorylationQQAKMAEYCRSIFGD
HHHHHHHHHHHHHCC
5.4322817900
474PhosphorylationNKKRHRPSAGGPDSA
CCCCCCCCCCCCCCC
39.2325159151
480PhosphorylationPSAGGPDSAGRKRPL
CCCCCCCCCCCCCCH
35.4425159151
490PhosphorylationRKRPLEQSNSALSES
CCCCHHHHCCCCCCC
24.3121406692
492PhosphorylationRPLEQSNSALSESSA
CCHHHHCCCCCCCCC
35.5121406692
495PhosphorylationEQSNSALSESSAATE
HHHCCCCCCCCCCCC
34.8421406692
497PhosphorylationSNSALSESSAATEPS
HCCCCCCCCCCCCCC
23.1521406692
498PhosphorylationNSALSESSAATEPSS
CCCCCCCCCCCCCCC
20.1921406692
501PhosphorylationLSESSAATEPSSPQL
CCCCCCCCCCCCCCC
48.4121406692
504PhosphorylationSSAATEPSSPQLGSP
CCCCCCCCCCCCCCC
48.7130576142
505PhosphorylationSAATEPSSPQLGSPS
CCCCCCCCCCCCCCC
27.6421406692
510PhosphorylationPSSPQLGSPSSDSCP
CCCCCCCCCCCCCCC
30.1521406692
512PhosphorylationSPQLGSPSSDSCPGL
CCCCCCCCCCCCCCC
48.7721406692
513PhosphorylationPQLGSPSSDSCPGLS
CCCCCCCCCCCCCCC
36.6121406692
515PhosphorylationLGSPSSDSCPGLSNG
CCCCCCCCCCCCCCC
24.9421406692
520PhosphorylationSDSCPGLSNGEEVGL
CCCCCCCCCCCCCCC
49.0221406692
531PhosphorylationEVGLEKPSLEPQKSL
CCCCCCCCCCCCCCC
57.3321406692
537PhosphorylationPSLEPQKSLGDEGLN
CCCCCCCCCCCCCCC
32.1329255136
548PhosphorylationEGLNRGPYVLGPADR
CCCCCCCCCCCCCCC
15.9029978859
568PhosphorylationDEEEEEQTDPKKPTT
HHHHHHHCCCCCCCC
58.5130108239
572AcetylationEEQTDPKKPTTDEGT
HHHCCCCCCCCCCCC
53.6519822945
596PhosphorylationEMSTLVNYIEPVKFK
HHHHHHHHHHCCCCC
10.1327642862
603MalonylationYIEPVKFKSFEAARK
HHHCCCCCHHHHHHH
48.8232601280
619PhosphorylationNKCFEMSSFVETKAM
CCCCCHHHHHHHHHH
31.8127050516
632PhosphorylationAMEQLTKSPMEFVEY
HHHHHHCCCHHHHHH
25.0125159151
639PhosphorylationSPMEFVEYNKQQLSR
CCHHHHHHCHHHHHH
23.5126126808
737UbiquitinationVKVISGQFLSDRKVG
EEEEECCCCCCCEEE
8.8821890473
746PhosphorylationSDRKVGIYVEVDMFG
CCCEEEEEEEEECCC
5.66-
758PhosphorylationMFGLPVDTRRKYRTR
CCCCCCCCCHHHCCC
32.3830257219
761UbiquitinationLPVDTRRKYRTRTSQ
CCCCCCHHHCCCCCC
35.4721890473
793PhosphorylationVVLPTLASLRIAAFE
HHHHHHHHHHHEEEE
22.6924719451
804UbiquitinationAAFEEGGKFVGHRIL
EEEECCCEECCEEEE
47.9723000965
814PhosphorylationGHRILPVSAIRSGYH
CEEEEEHHHHHCCCE
18.9521406692
847PhosphorylationIYTEASDYIPDDHQD
HHHCHHHCCCCCCHH
16.3222817900
855PhosphorylationIPDDHQDYAEALINP
CCCCCHHHHHHHHCH
10.3625884760
859PhosphorylationHQDYAEALINPIKHV
CHHHHHHHHCHHHHH
2.6832142685
867PhosphorylationINPIKHVSLMDQRAR
HCHHHHHHHHHHHHH
20.0727251275
909PhosphorylationSQPSSNPTPSPLDAS
CCCCCCCCCCCCCCC
40.4224275569
911PhosphorylationPSSNPTPSPLDASPR
CCCCCCCCCCCCCCC
40.3424275569
916PhosphorylationTPSPLDASPRRPPGP
CCCCCCCCCCCCCCC
20.7128188228
924PhosphorylationPRRPPGPTTSPASTS
CCCCCCCCCCCCCCC
45.9122167270
925PhosphorylationRRPPGPTTSPASTSL
CCCCCCCCCCCCCCC
35.5322167270
926PhosphorylationRPPGPTTSPASTSLS
CCCCCCCCCCCCCCC
22.4322167270
929PhosphorylationGPTTSPASTSLSSPG
CCCCCCCCCCCCCCC
23.1630266825
930PhosphorylationPTTSPASTSLSSPGQ
CCCCCCCCCCCCCCC
35.4730266825
931PhosphorylationTTSPASTSLSSPGQR
CCCCCCCCCCCCCCH
24.6130266825
933PhosphorylationSPASTSLSSPGQRDD
CCCCCCCCCCCCHHH
33.9630266825
934PhosphorylationPASTSLSSPGQRDDL
CCCCCCCCCCCHHHH
38.0430266825
944PhosphorylationQRDDLIASILSEVAP
CHHHHHHHHHHHCCC
19.6429496963
947PhosphorylationDLIASILSEVAPTPL
HHHHHHHHHCCCCCH
28.4930177828
952PhosphorylationILSEVAPTPLDELRG
HHHHCCCCCHHHHCC
27.0920068231
962UbiquitinationDELRGHKALVKLRSR
HHHCCCHHHHHHHHH
16.3522817900
987PhosphorylationKHQRKAVTLTRRLLD
HHHHHHHHHHHHHHH
27.5424719451
1014UbiquitinationLRPGALGGAADVEDT
CCCCCCCCCCCCCCC
20.5933845483
1029UbiquitinationKEGEDEAKRYQEFQN
CCCHHHHHHHHHHHH
49.9822817900
1031PhosphorylationGEDEAKRYQEFQNRQ
CHHHHHHHHHHHHHH
16.2222817900
1038PhosphorylationYQEFQNRQVQSLLEL
HHHHHHHHHHHHHHH
45.1933259812
1081UbiquitinationDANTTQFKRLKEMNE
CCCCHHHHHHHHHHH
47.1833845483
1081AcetylationDANTTQFKRLKEMNE
CCCCHHHHHHHHHHH
47.1824179709
10812-HydroxyisobutyrylationDANTTQFKRLKEMNE
CCCCHHHHHHHHHHH
47.18-
1100UbiquitinationELQKILDRKRHNSIS
HHHHHHHHHHHCCHH
34.1729967540
1105PhosphorylationLDRKRHNSISEAKMR
HHHHHHCCHHHHHHH
22.7428176443
1107PhosphorylationRKRHNSISEAKMRDK
HHHHCCHHHHHHHHH
31.1828176443
1122PhosphorylationHKKEAELTEINRRHI
HHHHHHHHHHHHHHH
26.7322817900
1130PhosphorylationEINRRHITESVNSIR
HHHHHHHHHHHHHHH
18.97-
1167UbiquitinationQLAEEEPKLLAQLAQ
HHHHHCHHHHHHHHH
60.4529967540
1209PhosphorylationGPLVACASNGHAPGS
CCEEEECCCCCCCCC
43.1428348404
1216PhosphorylationSNGHAPGSSGHLSGA
CCCCCCCCCCCCCCC
31.8926074081
1217PhosphorylationNGHAPGSSGHLSGAD
CCCCCCCCCCCCCCC
35.8326074081
1221PhosphorylationPGSSGHLSGADSESQ
CCCCCCCCCCCCCCH
26.6826074081
1225PhosphorylationGHLSGADSESQEENT
CCCCCCCCCCHHHHC
38.3228348404
1227PhosphorylationLSGADSESQEENTQL
CCCCCCCCHHHHCCC
47.0128348404
1232PhosphorylationSESQEENTQL-----
CCCHHHHCCC-----
34.2328348404

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
26SPhosphorylationKinasePRKG2Q13237
GPS
26SPhosphorylationKinasePKG-FAMILY-GPS
537SPhosphorylationKinaseKCC2AQ9UQM7
PhosphoELM
537SPhosphorylationKinaseCAMK2-FAMILY-GPS
537SPhosphorylationKinaseCAM-KII_GROUP-PhosphoELM
1105SPhosphorylationKinasePRKACAP17612
GPS
1105SPhosphorylationKinasePRKG2Q13237
GPS
1105SPhosphorylationKinasePRKCAP17252
GPS
1105SPhosphorylationKinasePRKCBP05771
GPS
1105SPhosphorylationKinasePRKCGP05129
GPS
1105SPhosphorylationKinasePKA-FAMILY-GPS
1105SPhosphorylationKinasePKC-FAMILY-GPS
1105SPhosphorylationKinasePKG-FAMILY-GPS
1105SPhosphorylationKinasePKA_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLCB3_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 PLCB3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NHRF2_HUMANSLC9A3R2physical
10748023
ANXA6_MOUSEAnxa6physical
12821674
GNAQ_MOUSEGnaqphysical
20966218
GNAQ_MOUSEGnaqphysical
23377541
SMYD3_HUMANSMYD3physical
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 PLCB3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-537; SER-926; SER-931AND SER-934, AND MASS SPECTROMETRY.
"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-537, 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 THR-1122, AND MASSSPECTROMETRY.

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