PLPP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PLPP1_HUMAN
• UniProt AC: O14494
• Protein Name: Phospholipid phosphatase 1 {ECO:0000312|HGNC:HGNC:9228}
• Gene Name: PLPP1 {ECO:0000312|HGNC:HGNC:9228}
• Organism: Homo sapiens (Human).
• Sequence Length: 284
• Subcellular Localization: Cell membrane; Multi-pass membrane protein.
• Protein Description: Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma..
• Protein Sequence: MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLGGIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAKYSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAILVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP

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
28	Phosphorylation	GLPFAILTSRHTPFQ CCCHHHHCCCCCCCC		24719451
112	Phosphorylation	FLFGAAASQSLTDIA HHHHHHHCCCHHHHH		22210691
121	Phosphorylation	SLTDIAKYSIGRLRP CHHHHHHHHHHHCCC		22210691
142	N-linked_Glycosylation	DPDWSKINCSDGYIE CCCHHHCCCCCCEEE		UniProtKB CARBOHYD
185	Phosphorylation	CMLFVALYLQARMKG HHHHHHHHHHHHHCC		-
201	Phosphorylation	WARLLRPTLQFGLVA HHHHHHHHHHHCCEE		-
254	Phosphorylation	SDFFKERTSFKERKE HHHHHHCCCHHHHHH		-
255	Phosphorylation	DFFKERTSFKERKEE HHHHHCCCHHHHHHH		-
260	Ubiquitination	RTSFKERKEEDSHTT CCCHHHHHHHCCCCE		-
264	Phosphorylation	KERKEEDSHTTLHET HHHHHHCCCCEECCC		25159151
266	Phosphorylation	RKEEDSHTTLHETPT HHHHCCCCEECCCCC		25159151
267	Phosphorylation	KEEDSHTTLHETPTT HHHCCCCEECCCCCC		25159151
271	Phosphorylation	SHTTLHETPTTGNHY CCCEECCCCCCCCCC		25159151
273	Phosphorylation	TTLHETPTTGNHYPS CEECCCCCCCCCCCC		23312004
274	Phosphorylation	TLHETPTTGNHYPSN EECCCCCCCCCCCCC		29214152
278	Phosphorylation	TPTTGNHYPSNHQP- CCCCCCCCCCCCCC-		25159151
280	Phosphorylation	TTGNHYPSNHQP--- CCCCCCCCCCCC---		25002506

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PLPP1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PLPP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PLPP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLPP1_HUMAN	PPAP2A	physical	18215144
PLPP3_HUMAN	PPAP2B	physical	18215144
PLPP2_HUMAN	PPAP2C	physical	18215144
TRI68_HUMAN	TRIM68	physical	28514442

Drug and Disease Associations

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