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PNPLA8 PNPLA8 PLA2G12B PLA2G12B PLA2G2C PLA2G2C PLA2G1B PLA2G1B PLA2G2F PLA2G2F PNPLA7 PNPLA7 LPCAT1 LPCAT1 PTDSS1 PTDSS1 LPCAT4 LPCAT4 PLBD1 PLBD1 CHPT1 CHPT1 LPCAT2 LPCAT2 PLB1 PLB1 PNPLA6 PNPLA6 CEPT1 CEPT1 PAFAH1B3 PAFAH1B3 PEMT PEMT PLA2G16 PLA2G16 PLD4 PLD4 PAFAH1B1 PAFAH1B1 PLA2G12A PLA2G12A PLA2G4F PLA2G4F PLA2G4A PLA2G4A ENSG00000168970 ENSG00000168970 PLA2G4C PLA2G4C PLA2G4B PLA2G4B
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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small nodes:
protein of unknown 3D structure
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second shell of interactors
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CHPT1choline phosphotransferase 1 (406 aa)
PLBD1phospholipase B domain containing 1; Phospholipase acting on various phospholipids including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids. May have a role in the defense against invading microorganisms and in the generation of lipid mediators of inflammation (553 aa)
PLA2G12Aphospholipase A2, group XIIA; PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl- phosphatidylcholine or -phosphatidylethanolamine (189 aa)
PLA2G2Cphospholipase A2, group IIC; Inactive phospholipase (Probable) (150 aa)
PEMTphosphatidylethanolamine N-methyltransferase (236 aa)
PNPLA8patatin-like phospholipase domain containing 8 (782 aa)
LPCAT2lysophosphatidylcholine acyltransferase 2; Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Involved in platelet- activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso- PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-alkyl-phosphatidylcholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase [...] (544 aa)
PAFAH1B3platelet-activating factor acetylhydrolase 1b, catalytic subunit 3 (29kDa); Inactivates paf by removing the acetyl group at the sn-2 position. This is a catalytic subunit. Plays an important role during the development of brain (231 aa)
LPCAT1lysophosphatidylcholine acyltransferase 1; Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology (534 aa)
PLA2G1Bphospholipase A2, group IB (pancreas); PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides, this releases glycerophospholipids and arachidonic acid that serve as the precursors of signal molecules (148 aa)
LPCAT4lysophosphatidylcholine acyltransferase 4; Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1- alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl- phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acy [...] (524 aa)
PLA2G16phospholipase A2, group XVI; Exhibits PLA1/2 activity, catalyzing the calcium- independent hydrolysis of acyl groups in various phosphatidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. Specifically catalyzes the release of fatty acids from phospholipids in adipose tissue (By similarity). N- and O- acylation activity is hardly detectable. Might decrease protein phosphatase 2A (PP2A) activity (162 aa)
PLB1phospholipase B1; Membrane-associated phospholipase. Exhibits a calcium- independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids (By similarity) (1458 aa)
CEPT1choline/ethanolamine phosphotransferase 1; Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity (416 aa)
PLA2G4Aphospholipase A2, group IVA (cytosolic, calcium-dependent); Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response (749 aa)
PLA2G12Bphospholipase A2, group XIIB; Not known; does not seem to have catalytic activity (195 aa)
PLA2G2Fphospholipase A2, group IIF; PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference (211 aa)
PLA2G4Fphospholipase A2, group IVF; Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Has higher enzyme activity for phosphatidylethanolamine than phosphatidylcholine (By similarity) (849 aa)
ENSG00000168970JMJD7-PLA2G4B readthrough (1012 aa)
PLD4phospholipase D family, member 4 (506 aa)
PAFAH1B1platelet-activating factor acetylhydrolase 1b, regulatory subunit 1 (45kDa); Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet- activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated [...] (410 aa)
PNPLA7patatin-like phospholipase domain containing 7 (1342 aa)
PLA2G4Bphospholipase A2, group IVB (cytosolic); Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine. Isoform 5 does have activity against phosphatidylcholine (781 aa)
PLA2G4Cphospholipase A2, group IVC (cytosolic, calcium-independent); Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid (541 aa)
PNPLA6patatin-like phospholipase domain containing 6; Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy (1375 aa)
PTDSS1phosphatidylserine synthase 1; Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. In membranes, PTDSS1 catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine (473 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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