dbPTM

PLDA1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLDA1_ARATH
UniProt AC	Q38882
Protein Name	Phospholipase D alpha 1 {ECO:0000303\|PubMed:11891260}
Gene Name	PLDALPHA1 {ECO:0000303\|PubMed:11891260}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	810
Subcellular Localization	Cytoplasm . Cell membrane Peripheral membrane protein . Mitochondrion membrane . Microsome membrane . Vacuole . Cytoplasmic vesicle, clathrin-coated vesicle . Not found in chloroplast or nuclei. The distribution of this conventional PLD between mem
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 and response to stress, characterized by acidification of the cell. [PubMed: 9437863 Involved in wound induction of jasmonic acid]
Protein Sequence	MAQHLLHGTLHATIYEVDALHGGGVRQGFLGKILANVEETIGVGKGETQLYATIDLQKARVGRTRKIKNEPKNPKWYESFHIYCAHLASDIIFTVKDDNPIGATLIGRAYIPVDQVINGEEVDQWVEILDNDRNPIQGGSKIHVKLQYFHVEEDRNWNMGIKSAKFPGVPYTFFSQRQGCKVSLYQDAHIPDNFVPRIPLAGGKNYEPQRCWEDIFDAISNAKHLIYITGWSVYAEIALVRDSRRPKPGGDVTIGELLKKKASEGVRVLLLVWDDRTSVDVLKKDGLMATHDEETENFFRGSDVHCILCPRNPDDGGSIVQSLQISTMFTHHQKIVVVDSEMPSRGGSEMRRIVSFVGGIDLCDGRYDTPFHSLFRTLDTVHHDDFHQPNFTGAAITKGGPREPWHDIHSRLEGPIAWDVMYNFEQRWSKQGGKDILVKLRDLSDIIITPSPVMFQEDHDVWNVQLFRSIDGGAAAGFPESPEAAAEAGLVSGKDNIIDRSIQDAYIHAIRRAKDFIYVENQYFLGSSFAWAADGITPEDINALHLIPKELSLKIVSKIEKGEKFRVYVVVPMWPEGLPESGSVQAILDWQRRTMEMMYKDVIQALRAQGLEEDPRNYLTFFCLGNREVKKDGEYEPAEKPDPDTDYMRAQEARRFMIYVHTKMMIVDDEYIIIGSANINQRSMDGARDSEIAMGGYQPHHLSHRQPARGQIHGFRMSLWYEHLGMLDETFLDPSSLECIEKVNRISDKYWDFYSSESLEHDLPGHLLRYPIGVASEGDITELPGFEFFPDTKARILGTKSDYLPPILTT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
48	Phosphorylation	IGVGKGETQLYATID CCCCCCCCEEEEEEE	32.32	19880383
51	Phosphorylation	GKGETQLYATIDLQK CCCCCEEEEEEECHH	7.59	19880383
290	Phosphorylation	KKDGLMATHDEETEN ECCCCCCCCCHHHCC	18.85	19880383
481	Phosphorylation	AAAGFPESPEAAAEA CCCCCCCCHHHHHHH	28.42	30291188
492	Phosphorylation	AAEAGLVSGKDNIID HHHHCCCCCCCCCCC	45.21	23776212
594	Phosphorylation	ILDWQRRTMEMMYKD HHHHHHHHHHHHHHH	21.48	19880383
770	Phosphorylation	LPGHLLRYPIGVASE CCCCCEEEEEEECCC	10.12	23776212
776	Phosphorylation	RYPIGVASEGDITEL EEEEEECCCCCCCCC	39.44	30291188
781	Phosphorylation	VASEGDITELPGFEF ECCCCCCCCCCCCEE	35.89	23776212
801	Phosphorylation	ARILGTKSDYLPPIL HHHCCCCCCCCCCCC	31.18	19880383

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 PLDA1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PLDA1_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 PLDA1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PLDA1_ARATH !!

Drug and Disease Associations

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

Regulatory Network of PLDA1_ARATH

Related Literatures of Post-Translational Modification