about
Lecithin cholesterol acyltransferasePlatelet activating factor acetylhydrolase 1b regulatory subunit 1Abhydrolase domain containing 3, phospholipasePhospholipase A and acyltransferase 3Peroxiredoxin 6Phospholipase A and acyltransferase 1Platelet activating factor acetylhydrolase 1b catalytic subunit 3Phospholipase A and acyltransferase 5Phospholipase A and acyltransferase 4Otoconin 90Phospholipase A2 group IIAPutative inactive group IIC secretory phospholipase A2Phospholipase A2 group IIFPhospholipase A2 group IIIPhospholipase A2 group IIEPhospholipase A2 group IIDPhospholipase A2 group XIIBPhospholipase A2 group XIIAJMJD7-PLA2G4B readthroughPhospholipase A2 group IVEPhospholipase A2 group IVFPhospholipase A2 group IVDPhospholipase A2 group IVCProtein interacting with cyclin A1Phospholipase B domain containing 1Platelet activating factor acetylhydrolase 1b catalytic subunit 2Phospholipase A2 group VIPatatin like phospholipase domain containing 8Patatin like phospholipase domain containing 3Phospholipase A and acyltransferase 2Post-glycosylphosphatidylinositol attachment to proteins 6Phospholipase A2, group XIIA, isoform CRA_bPhospholipase A(2)Phospholipase A2 group XPhospholipase A2 group VPhospholipase A2 group IVAPhospholipase A2, group IICAbhydrolase domain containing 3Hypothetical protein PA1887Group XIIB secretory phospholipase A2-like protein
P680
Identification of essential residues for the catalytic function of 85-kDa cytosolic phospholipase A2. Probing the role of histidine, aspartic acid, cysteine, and arginineMultiple splice variants of the human calcium-independent phospholipase A2 and their effect on enzyme activityHyperoxidation of Peroxiredoxin 6 Induces Alteration from Dimeric to Oligomeric State
P921
Q14905448-725F7685-4BBA-4004-915B-4636B31426BDQ1982330-B28ADC4F-F39A-4746-8DCE-465DE7D36887Q21104853-24A4338F-9795-4049-8AE4-5C98CC437F03Q21104853-C70F9E1C-45C6-454C-86D6-44EAC9B3FE02Q21114995-6B4450C0-3105-46A6-8FF2-71B976EA4D06Q21114995-8A7BA124-86C1-4268-81D3-CB6CDDB74999Q21119022-06D4A3EB-CE03-4EB9-8390-EFE4B4FBE8A2Q21119134-78F13E28-569F-4148-870A-1373EA92366FQ21119134-8FB222AB-B290-4F07-9772-A583CCA10A7CQ21119303-A93A61E6-1CCA-40D9-952B-89EE3BF8EEC9Q21119781-DCB3DFBD-D3D5-43E8-8DCD-0BDB6256674BQ21119781-F7DC229C-9B7F-4650-B3AB-922937501E32Q21119784-397583C3-6ABD-44DE-84C5-C21B939E69B5Q21120308-5948EB99-C419-447F-B1D8-F9179333E887Q21121064-00DCDDE6-E4C7-45AA-A575-9C7DB72670CAQ21121064-01553F4F-898A-455A-BFA7-1879250410C8Q21121064-29DCF124-D79E-473C-9EF4-62A0849F5849Q21121065-A5F454D0-A891-4D33-AB58-F31C65DC6214Q21121066-85FAEB24-F97E-4651-A017-8074D4146E7BQ21121066-C8432312-3655-44DE-9F2E-1CBC5CCB5CFBQ21121066-E926B1FA-79E4-4840-8C85-9A8534FB68F9Q21121067-97D33D2A-D3FA-44BE-BB32-80937AA94676Q21121067-C49157BA-F395-4F97-8B8F-102711430AC9Q21121068-91F6B281-26BF-46A1-A659-A32A8899EE32Q21121068-EE45F7B4-F344-495F-8065-625466DA9AA8Q21121069-163ACD4A-4C5A-4206-BEEE-85804BFACC0FQ21121069-AA903580-8EBA-470A-A812-0FAC8446CF15Q21121885-04E57EC8-6C3B-405C-9DF9-891FA17E8C0EQ21121892-25A0524B-7BB8-4E89-B176-52A6A7F92E2DQ21121892-5FD15739-8817-428B-8B55-4CF2AB00A384Q21121892-7EF5A970-F4D3-4C9F-AEAF-B48B91DDEAE8Q21123188-7369A1A9-7038-49A0-94AF-374A012E2744Q21123188-7FF0CF30-5E5E-4864-930B-40A322B9B40AQ21123188-C70B3F96-37BA-494C-955C-61DAE36A4AE5Q21123193-3619C57A-F755-43CF-8B56-1355A223062FQ21123193-592CCE6D-9007-4E22-8DB4-8C3194641F5BQ21123193-E07D4BE2-48FC-4285-AD23-20C1350A6D9DQ21123194-5DB9F796-C651-481A-AEB6-1A2E62071161Q21123194-9A05EFA0-1C45-424E-84AB-984B97E8B4E3Q21123194-CA85734F-0F7C-4FBA-9FD4-C4CD4CA36F11
P680
description
Catalysis of the reaction: pho ...... hosphocholine + a carboxylate.
@en
biologisch proces
@nl
name
phospholipase A2 activity
@en
type
label
phospholipase A2 activity
@en
altLabel
GO:0004623
@en
lecithinase A activity
@en
phosphatidolipase activity
@en
phosphatidylcholine 2-acylhydrolase activity
@en
prefLabel
phospholipase A2 activity
@en
P2888
P591
P686
GO:0004623