about
Lipase, hepaticAbhydrolase domain containing 3, phospholipasePhospholipase A and acyltransferase 3Phospholipase A and acyltransferase 1Phospholipase A and acyltransferase 5Phospholipase A and acyltransferase 4JMJD7-PLA2G4B readthroughPhospholipase A2 group IVEPhospholipase A2 group IVFPhospholipase A2 group IVDPhospholipase A2 group IVCPhospholipase A and acyltransferase 2Phospholipase A2 group IVAAbhydrolase domain containing 3Phospholipase A and acyltransferase 3Phospholipase A and acyltransferase 5Phospholipase A and acyltransferase 1Lipase, endothelialPhospholipase A1 member APhospholipase A ECIAI39_3188Membrane protein Rv3802cPhospholipase A Cj1351Lipase G, endothelial typeOuter membrane phospholipase A VF_1556Phospholipase A1 CBU_0489Phospholipase STM3957Phospholipase XCC1420Phospholipase A1 NMB0464Phospholipase A EAE_07930Outer membrane phospholipase A ECUMN_4347Phospholipase A O3K_24750Phospholipase A1-likePhospholipase A1-IIVespid venom allergen phospholipase A1Retinoic acid receptor responder protein 3Phospholipase A NRG857_18965Lipase G, endothelial typePhospholipase A1 member APhospholipase A and acyltransferase 3Phospholipase A and acyltransferase 5
P680
Cloning of a unique lipase from endothelial cells extends the lipase gene familyThe tumor suppressor gene H-Rev107 functions as a novel Ca2+-independent cytosolic phospholipase A1/2 of the thiol hydrolase typeRegulation of hepatic lipase activity by sphingomyelin in plasma lipoproteins.Characterization of the lipolytic activity of endothelial lipaseHuman hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity
P921
Q14914235-C55EC3CE-E333-4A53-A2BD-8078ACF0AF71Q21104853-03C2883D-D52A-4FC6-8EAA-9E0E09977B5BQ21104853-49B077DF-A2C2-4B97-A8E7-C0F7C3B30A93Q21114995-5820F7E4-0E7B-4D54-9125-269EECC7707EQ21119134-244329BE-63C9-4872-91E0-01B8A0B4061EQ21119134-F9A39023-B35E-4708-9E4E-0FFCDCC2CE84Q21119781-ECB2310D-D7D9-4FDE-A3AA-B7C0FA0E80CBQ21119781-F6FA2CF1-0826-4DF0-99B4-BF4FA0F905FFQ21119784-DEF62F5F-2E24-4864-9C60-C9A67F650F78Q21119784-E895B40E-D6BA-4A91-85CC-216F0E044F8FQ21123188-28C59FCA-5B6A-450B-A2AF-B72F2D819E0BQ21123193-CC0632BE-AAE7-42E7-A87D-125CF44EF953Q21123194-3498CA27-4A89-4BB5-8E0E-E9DCDEE7C8E3Q21123196-A4AAEAC7-94B8-4A1B-B82D-C950C5454512Q21123199-EA6B8D3F-AFE3-4896-A31C-4ECE5D3FF381Q21133353-207D646E-A6DB-4A12-951C-0F3BDA5F7814Q21133353-B0D5D8DB-D63B-4907-8CDF-718C2401F333Q21174697-CC927664-25D0-476E-986C-DA8872DADE9CQ21498778-CD01F636-4F86-44E7-8177-F75AB349BBA3Q21983340-1CF50C5A-9446-429A-AF97-7302192FAA95Q21983341-A85F5119-3FEC-4695-AC3C-104584B20DEEQ21983341-EF3AEEFF-52C1-4C00-A4C2-4D0093EEAA1FQ21983346-0B8FEBE0-7C5E-4CE9-A25A-8DEC96CD9F36Q21983346-688B775E-E8CB-4A99-87A4-DBED93652D33Q21983346-DC50ED10-E122-4512-AB12-2ED6E05BB879Q21987586-8F86A4D7-DACF-4CF2-8DC6-128E3E1556C7Q21990905-C0BA2BB9-FB80-4E65-B088-3E51A2F74B95Q21990905-C7AA1736-63D6-4E62-9071-6DD68BCAFD53Q22135713-4CFC2A62-8E52-44B8-A996-3C0C9E5520BFQ22234881-FB81FB57-9561-4CDB-A1CC-1CADDF9F0CD4Q22300661-CBDB536E-E4A3-40FE-909F-BE3AB8CB4E55Q22676900-7C95EBE8-A124-4B78-A9E4-7D6C32B8EFD6Q23437845-15579345-3C0D-4569-9F76-CB2E319FD04DQ23447167-39D1953E-40EB-4DCC-A302-F97D78D07AF8Q23447167-90AEAC50-C038-4120-8837-1C989ECAD664Q23562218-BE39BBF7-18E4-491A-88FD-7EC7548BE25AQ23562218-DEC69787-4976-4E63-AA0A-F1E653600AD5Q24099184-69F415CA-F767-489E-AFF0-25DBA79B3A4CQ24114191-340F8039-B425-4FA9-9C91-19A0CA0E5414Q24126943-DCAFE3E7-32ED-4817-8162-829C2C701826
P680
description
Catalysis of the reaction: pho ...... hosphocholine + a carboxylate.
@en
moleculaire functie
@nl
name
phospholipase A1 activity
@en
type
label
phospholipase A1 activity
@en
altLabel
GO:0008970
@en
phosphatidylcholine 1-acylhydrolase activity
@en
prefLabel
phospholipase A1 activity
@en
P2888
P591
P686
GO:0008970