LOC102228835 protein (Xiphophorus maculatus)

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LOC102228835

Patatin-like phospholipase domain containing 2. (510 aa)

Predicted Functional Partners:

mgll

0.928

LOC102228168

0.914

mogat2

0.914

plpp4

0.911

plpp5

0.911

LOC102237891

0.907

LOC111611837

0.903

LOC102226589

0.903

LOC102226072

0.900

agk

0.900

Your Current Organism:

Xiphophorus maculatus

NCBI taxonomy Id: 8083
Other names: Platypoecilus maculatus, X. maculatus, southern platyfish

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
LOC102226072	LOC102226589	ENSXMAP00000003457	ENSXMAP00000029915	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	PNPLA domain-containing protein.	0.900
LOC102226072	LOC102228168	ENSXMAP00000003457	ENSXMAP00000008567	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	Monoacylglycerol O-acyltransferase 3a.	0.901
LOC102226072	LOC102228835	ENSXMAP00000003457	ENSXMAP00000003869	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	Patatin-like phospholipase domain containing 2.	0.900
LOC102226072	LOC102237891	ENSXMAP00000003457	ENSXMAP00000041400	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	PNPLA domain-containing protein.	0.900
LOC102226072	LOC111611837	ENSXMAP00000003457	ENSXMAP00000003140	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	Patatin-like phospholipase domain containing 3.	0.900
LOC102226072	mgll	ENSXMAP00000003457	ENSXMAP00000009080	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	Monoglyceride lipase.	0.900
LOC102226072	mogat2	ENSXMAP00000003457	ENSXMAP00000031888	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	Monoacylglycerol O-acyltransferase 2.	0.901
LOC102226072	plpp4	ENSXMAP00000003457	ENSXMAP00000004829	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	Phospholipid phosphatase 4.	0.903
LOC102226072	plpp5	ENSXMAP00000003457	ENSXMAP00000014812	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	Phospholipid phosphatase 5.	0.903
LOC102226589	LOC102226072	ENSXMAP00000029915	ENSXMAP00000003457	PNPLA domain-containing protein.	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	0.900
LOC102226589	LOC102228168	ENSXMAP00000029915	ENSXMAP00000008567	PNPLA domain-containing protein.	Monoacylglycerol O-acyltransferase 3a.	0.914
LOC102226589	LOC102228835	ENSXMAP00000029915	ENSXMAP00000003869	PNPLA domain-containing protein.	Patatin-like phospholipase domain containing 2.	0.903
LOC102226589	LOC102237891	ENSXMAP00000029915	ENSXMAP00000041400	PNPLA domain-containing protein.	PNPLA domain-containing protein.	0.909
LOC102226589	LOC111611837	ENSXMAP00000029915	ENSXMAP00000003140	PNPLA domain-containing protein.	Patatin-like phospholipase domain containing 3.	0.904
LOC102226589	agk	ENSXMAP00000029915	ENSXMAP00000005497	PNPLA domain-containing protein.	Acylglycerol kinase.	0.900
LOC102226589	mgll	ENSXMAP00000029915	ENSXMAP00000009080	PNPLA domain-containing protein.	Monoglyceride lipase.	0.926
LOC102226589	mogat2	ENSXMAP00000029915	ENSXMAP00000031888	PNPLA domain-containing protein.	Monoacylglycerol O-acyltransferase 2.	0.914
LOC102226589	plpp4	ENSXMAP00000029915	ENSXMAP00000004829	PNPLA domain-containing protein.	Phospholipid phosphatase 4.	0.908
LOC102226589	plpp5	ENSXMAP00000029915	ENSXMAP00000014812	PNPLA domain-containing protein.	Phospholipid phosphatase 5.	0.908
LOC102228168	LOC102226072	ENSXMAP00000008567	ENSXMAP00000003457	Monoacylglycerol O-acyltransferase 3a.	Lipoprotein lipase; Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.	0.901