dbPTM

PLDG1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLDG1_ARATH
UniProt AC	Q9T053
Protein Name	Phospholipase D gamma 1 {ECO:0000303\|PubMed:9353280}
Gene Name	PLDGAMMA1 {ECO:0000303\|PubMed:9353280}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	858
Subcellular Localization	Cytoplasm . Membrane Peripheral membrane protein . Found mainly associated with intracellular membranes but also with mitochondrial membranes, nuclei and clathrin-coated vesicles. Not found in chloroplast.
Protein Description	Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond to generate phosphatidic acids (PA). Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. [PubMed: 10441386 Can use phosphatidylserine (PS) and phosphatidylethanolamine (PE) as substrates only in the presence of PIP2. Can use phosphatidylcholine (PC), phosphatidylglycerol (PG) or N-acylphosphatidylethanolamine (NAPE) as substrates in the presence of PE and PIP2]
Protein Sequence	MAYHPAYTETMSMGGGSSHGGGQQYVPFATSSGSLRVELLHGNLDIWVKEAKHLPNMDGFHNRLGGMLSGLGRKKVEGEKSSKITSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDIIGSQIMGAVGIPTEQLCSGNRIEGLFPILNSSGKPCKQGAVLGLSIQYTPMERMRLYQMGVGSGNECVGVPGTYFPLRKGGRVTLYQDAHVDDGTLPSVHLDGGIQYRHGKCWEDMADAIRQARRLIYITGWSVFHPVRLVRRTNDPTEGTLGELLKVKSQEGVRVLVLVWDDPTSRSLLGFKTQGVMNTSDEETRRFFKHSSVQVLLCPRSGGKGHSFIKKSEVGTIYTHHQKTVIVDAEAAQNRRKIVAFVGGLDLCNGRFDTPKHPLFRTLKTLHKDDFHNPNFVTTADDGPREPWHDLHSKIDGPAAYDVLANFEERWMKASKPRGIGKLKSSSDDSLLRIDRIPDIVGLSEASSANDNDPESWHVQVFRSIDSSSVKGFPKDPKEATGRNLLCGKNILIDMSIHAAYVKAIRSAQHFIYIENQYFLGSSFNWDSNKDLGANNLIPMEIALKIANKIRAREKFAAYIVIPMWPEGAPTSNPIQRILYWQHKTMQMMYQTIYKALVEVGLDSQFEPQDFLNFFCLGTREVPVGTVSVYNSPRKPPQPNANANAAQVQALKSRRFMIYVHSKGMVVDDEFVLIGSANINQRSLEGTRDTEIAMGGYQPHYSWAMKGSRPHGQIFGYRMSLWAEHLGFLEQGFEEPENMECVRRVRQLSELNWRQYAAEEVTEMSGHLLKYPVQVDRTGKVSSLPGCETFPDLGGKIIGSFLALQENLTI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
69	Phosphorylation	NRLGGMLSGLGRKKV HHHHHHHHHCCCCCC	24.07	30407730
285	Phosphorylation	VRRTNDPTEGTLGEL EECCCCCCCCCHHHH	50.32	19880383
288	Phosphorylation	TNDPTEGTLGELLKV CCCCCCCCHHHHEEE	25.92	19880383
315	Phosphorylation	WDDPTSRSLLGFKTQ ECCCCCHHHCCCEEE	27.93	22074104
441	Phosphorylation	EPWHDLHSKIDGPAA CCHHHHHHCCCCHHH	38.31	24243849
674	Phosphorylation	TREVPVGTVSVYNSP CCEECCEEEEEECCC	15.16	29654922
676	Phosphorylation	EVPVGTVSVYNSPRK EECCEEEEEECCCCC	20.79	23776212
678	Phosphorylation	PVGTVSVYNSPRKPP CCEEEEEECCCCCCC	11.47	23776212
680	Phosphorylation	GTVSVYNSPRKPPQP EEEEEECCCCCCCCC	14.37	30291188

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 PLDG1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PLDG1_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 PLDG1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PLDG1_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND MASSSPECTROMETRY.	19376835 [Abstract]
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND MASSSPECTROMETRY.	19245862 [Abstract]