PLCD2_ARATH - dbPTM
PLCD2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLCD2_ARATH
UniProt AC Q39033
Protein Name Phosphoinositide phospholipase C 2
Gene Name PLC2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 581
Subcellular Localization Cell 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. At physiological calcium concentration, the preferred substrate is phosphatidylinositol 4,5-bisphosphate versus phosphatidylinositol..
Protein Sequence MSKQTYKVCFCFRRRFRYTASEAPREIKTIFEKYSENGVMTVDHLHRFLIDVQKQDKATREDAQSIINSASSLLHRNGLHLDAFFKYLFGDNNPPLALHKVHHDMDAPISHYFIFTGHNSYLTGNQLSSDCSEVPIIDALKKGVRVIELDIWPNSNKDDIDVLHGMTLTTPVGLIKCLKAIRAHAFDVSDYPVVVTLEDHLTPDLQSKVAEMVTEIFGEILFTPPVGESLKEFPSPNSLKRRIIISTKPPKEYKEGKDVEVVQKGKDLGDEEVWGREVPSFIQRNKSEAKDDLDGNDDDDDDDDEDKSKINAPPQYKHLIAIHAGKPKGGITECLKVDPDKVRRLSLSEEQLEKAAEKYAKQIVRFTQHNLLRIYPKGTRVTSSNYNPLVGWSHGAQMVAFNMQGYGRSLWLMQGMFRANGGCGYIKKPDLLLKSGSDSDIFDPKATLPVKTTLRVTVYMGEGWYFDFRHTHFDQYSPPDFYTRVGIAGVPGDTVMKKTKTLEDNWIPAWDEVFEFPLTVPELALLRLEVHEYDMSEKDDFGGQTCLPVWELSEGIRAFPLHSRKGEKYKSVKLLVKVEFV
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
29PhosphorylationEAPREIKTIFEKYSE
CCCHHHHHHHHHHHH		36.2419880383
280PhosphorylationVWGREVPSFIQRNKS
HCCCCCHHHHHHCHH		39.9130291188
287PhosphorylationSFIQRNKSEAKDDLD
HHHHHCHHHCCCCCC		46.4620374526
332PhosphorylationGKPKGGITECLKVDP
CCCCCCCEECEECCH		24.7425561503
346PhosphorylationPDKVRRLSLSEEQLE
HHHHHHHCCCHHHHH		28.2130291188
348PhosphorylationKVRRLSLSEEQLEKA
HHHHHCCCHHHHHHH		35.3925561503
437PhosphorylationDLLLKSGSDSDIFDP
CEEEECCCCCCCCCC		40.8225561503
439PhosphorylationLLKSGSDSDIFDPKA
EEECCCCCCCCCCCC		34.0125561503
471PhosphorylationWYFDFRHTHFDQYSP
EEEEEECCCCCCCCC		21.7125368622
476PhosphorylationRHTHFDQYSPPDFYT
ECCCCCCCCCCCHHH		25.6225368622
477PhosphorylationHTHFDQYSPPDFYTR
CCCCCCCCCCCHHHH		25.0725368622
482PhosphorylationQYSPPDFYTRVGIAG
CCCCCCHHHHCEECC		10.8725368622
545PhosphorylationKDDFGGQTCLPVWEL
CCCCCCCCCEEHEEC		21.2023111157
553PhosphorylationCLPVWELSEGIRAFP
CEEHEECCCCEEEEE		23.4323111157
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 PLCD2_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLCD2_ARATH !!
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 PLCD2_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
Y1756_ARATHAT1G07560physical
21423366
ACA12_ARATHAT3G63380physical
21423366
MLO2_ARATHMLO2physical
21423366
WAXS6_ARATHAT5G55330physical
21423366
TET11_ARATHTET11physical
21423366
Y5838_ARATHBIR1physical
21423366
Y3804_ARATHAT3G28040physical
21423366
Y5639_ARATHAT5G63930physical
21423366
Y5129_ARATHAT5G10290physical
21423366
Y2289_ARATHAT2G28960physical
21423366
PXC3_ARATHAT2G41820physical
21423366
HA22J_ARATHHVA22Jphysical
21423366
Y2899_ARATHAT2G28990physical
21423366
C83A1_ARATHCYP83A1physical
21423366
Y4052_ARATHAT4G30520physical
21423366
AUX1_ARATHAUX1physical
21423366
RC21_ARATHAT1G57550physical
21423366
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLCD2_ARATH

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of plasma membrane proteinsreveals regulatory mechanisms of plant innate immune responses.";
Nuehse T.S., Bottrill A.R., Jones A.M.E., Peck S.C.;
Plant J. 51:931-940(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASSSPECTROMETRY.
"Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis.";
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.;
Mol. Cell. Proteomics 6:1711-1726(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASSSPECTROMETRY.
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Plant Cell 16:2394-2405(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory