PLCD3_HUMAN - dbPTM
PLCD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLCD3_HUMAN
UniProt AC Q8N3E9
Protein Name 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3
Gene Name PLCD3
Organism Homo sapiens (Human).
Sequence Length 789
Subcellular Localization Membrane
Peripheral membrane protein. Cytoplasm. Cleavage furrow. Localizes at the cleavage furrow during cytokinesis.
Protein Description Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow..
Protein Sequence MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDEDVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREGHQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQRERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEGAEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYELNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQIGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFTLSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVKGKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRLRTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQEMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRTTLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTLQFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATLFIQIRIQRS
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
34PhosphorylationAAPVALPSPPTPSDG
HCCCCCCCCCCCCCC		44.3430266825
37PhosphorylationVALPSPPTPSDGGTK
CCCCCCCCCCCCCCC		38.5225849741
39PhosphorylationLPSPPTPSDGGTKRP
CCCCCCCCCCCCCCC		51.9030266825
43PhosphorylationPTPSDGGTKRPGLRA
CCCCCCCCCCCCHHH		29.4330266825
53UbiquitinationPGLRALKKMGLTEDE
CCHHHHHHCCCCCCH		38.7629967540
105PhosphorylationRRIPRAPSQHIFFVQ
CCCCCCCCCCEEEEE		33.1530266825
148UbiquitinationIAFKGRRKNLDLAAP
EEECCCCCCCCCCCC		61.5729967540
200PhosphorylationRADSNQDSKMSFKEI
HHCCCCCCCCCHHHH		22.0920166139
201UbiquitinationADSNQDSKMSFKEIK
HCCCCCCCCCHHHHH		47.0233845483
205UbiquitinationQDSKMSFKEIKSLLR
CCCCCCHHHHHHHHH		51.7433845483
209PhosphorylationMSFKEIKSLLRMVNV
CCHHHHHHHHHHHCC		37.9924719451
222PhosphorylationNVDMNDMYAYLLFKE
CCCHHHHHHHHHHHH		8.5829759185
224PhosphorylationDMNDMYAYLLFKECD
CHHHHHHHHHHHHCC		6.1029759185
252UbiquitinationEFLRRLLKRPELEEI
HHHHHHHCCHHHHHH		71.1929967540
396PhosphorylationPGGEPVIYHGHTLTS
CCCCCEEEECCCCHH		11.28-
489PhosphorylationKKLPAARSEDGRALS
CCCCCCCCCCCCCCC		35.0030576142
496PhosphorylationSEDGRALSDREEEEE
CCCCCCCCCCCHHCC		33.3722167270
534PhosphorylationELSALAVYCHATRLR
HHHHHHHHHHHHCCC		3.4927642862
542PhosphorylationCHATRLRTLHPAPNA
HHHHCCCCCCCCCCC		33.7323312004
556PhosphorylationAPQPCQVSSLSERKA
CCCCCCCCCCCHHHH		10.3223663014
557PhosphorylationPQPCQVSSLSERKAK
CCCCCCCCCCHHHHH		36.7422167270
559PhosphorylationPCQVSSLSERKAKKL
CCCCCCCCHHHHHHH		36.9823663014
573PhosphorylationLIREAGNSFVRHNAR
HHHHHHHHHHHCCHH		24.9730266825
583PhosphorylationRHNARQLTRVYPLGL
HCCHHHHCEEEECCC		15.11-
679UbiquitinationLPKLNAEKPHSIVDP
CCCCCCCCCCCCCCC		45.6933845483
704PhosphorylationADCARQETDYVLNNG
HHHHHHCCCEECCCC		25.0528102081
706PhosphorylationCARQETDYVLNNGFN
HHHHCCCEECCCCCC		17.7924927040
742PhosphorylationVVEDYDATSPNDFVG
EEECCCCCCCCCCCE		41.65-
756PhosphorylationGQFTLPLSSLKQGYR
EEEEEEHHHHCCCCC		31.5224719451
759UbiquitinationTLPLSSLKQGYRHIH
EEEHHHHCCCCCEEE		43.5621906983
779PhosphorylationGASLSPATLFIQIRI
CCCCCCEEEEEEEEE		26.1122210691
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 PLCD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLCD3_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 PLCD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PLCD3_HUMAN !!
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 PLCD3_HUMAN

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Related Literatures of Post-Translational Modification
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-105 AND SER-496, ANDMASS SPECTROMETRY.
"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-496, AND MASSSPECTROMETRY.

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