about
histone-arginine N-methyltransferase activityprotein-arginine omega-N asymmetric methyltransferase activityprotein-arginine omega-N symmetric methyltransferase activityprotein-arginine omega-N monomethyltransferase activity[myelin basic protein]-arginine N-methyltransferase activity[cytochrome c]-arginine N-methyltransferase activityprotein-arginine N5-methyltransferase activity
P279
F-box protein 11Protein arginine methyltransferase 9WD repeat domain 77Protein arginine methyltransferase 5Protein arginine methyltransferase 3Protein arginine methyltransferase 2Protein arginine methyltransferase 6Protein arginine methyltransferase 7Protein arginine methyltransferase 1F-box protein 11Coactivator-associated arginine methyltransferase 1Protein arginine methyltransferase 9Protein arginine N-methyltransferase 6Protein arginine N-methyltransferase 5Protein arginine N-methyltransferase 3Protein arginine N-methyltransferase 1Protein arginine N-methyltransferase 2Arginine N-methyltransferase 2Protein-arginine N5-methyltransferase YDR465CProtein arginine methyltransferase 3F-box protein 11Coactivator-associated arginine methyltransferase 1Protein arginine methyltransferase 1Protein arginine methyltransferase 5Protein arginine methyltransferase 9Protein arginine N-methyltransferase 5 CELE_C34E10.5Protein arginine N-methyltransferase 1 CELE_Y113G7B.17Capsuleen Dmel_CG3730Arginine methyltransferase 7 Dmel_CG9882Coactivator associated arginine methyltransferase 1Protein arginine methyltransferase 9protein arginine N-methyltransferase 5, putativeprotein arginine N-methyltransferase 1protein arginine N-methyltransferase 5, putativeprotein arginine N-methyltransferase 1, putativeprotein arginine N-methyltransferase 5, putativeprotein arginine N-methyltransferase 5, putativeprotein arginine N-methyltransferase 5, putativeprotein arginine N-methyltransferase 5, putativeprotein arginine N-methyltransferase 5, putative
P680
FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residuesPRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulationPromiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behaviorUnique Features of Human Protein Arginine Methyltransferase 9 (PRMT9) and Its Substrate RNA Splicing Factor SF3B2Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity.Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function.
P921
Q21112937-F49B67FF-657E-441E-AE09-DD775F8DD10BQ21112940-35BBB3A8-7C64-4055-A574-65DA77C49455Q21130992-D9083BAD-4644-4628-B37D-727528D53559Q21131672-5E569567-4881-4B9C-89FA-11F9AC43C621Q21131691-81F399FA-2360-4AED-83D5-44D12F7F19D5Q21426154-C51BEEA9-7E03-4C7D-A4AA-78DCE51AA4B1Q22323159-513155E7-8929-4C42-836A-CA989B0BBE9F
P279
Q21101352-3DEA7DB6-08AC-4885-BE90-02E4D3DBDD93Q21111394-7A9CB79E-BEAD-46EC-A053-72C9A583D2F9Q21111416-C18E6286-87C8-446B-B349-E9E83BBA268DQ21130994-56769A7C-ACD4-4BE0-810E-23D45A37689EQ21130994-A59F5788-2236-4069-AEE9-EFA382269842Q21131666-9ED6AB16-38A2-4B65-8402-76CE3BA3CE8CQ21131670-7CA8D3F8-44B1-4851-BB73-720A51D51FA4Q21131677-353C6127-9690-40A1-9461-4BAA31830D77Q21131695-8C2F4778-8819-4908-AEE3-EF72BCC85447Q21201642-6E418729-8549-464D-B9F4-B140BBB2BE51Q21201642-C69B1010-5460-4EC0-B4A2-AD5E8D77FFE2Q21495687-95D57182-0165-45D5-8886-1BD1966CEF92Q21497204-6EBBC9C3-73C9-42A3-8E08-25C0964FE871Q21981660-6951A00B-656E-4845-9F01-EF0CD8BBF5B2Q21981660-C1AAA37A-D0C0-4E9D-8E64-850A27A1EE70Q21981665-D07D9CA3-4988-4E3B-8085-0B7DAE2E650AQ21981670-F3BEED3A-A34C-4B2D-81BA-EC7D7D7FBB5BQ21981672-437BE4FF-7790-4BF5-972D-90247771CF3CQ21981677-0A8DF81D-6E5A-4083-BF32-19A3930FB0AEQ21981677-B4C10ACE-7FD7-4BF6-8F65-C7763344BCAEQ21981678-C237DE4D-B534-46AE-8BEA-EF9E1F7FE6F6Q24770307-A0628F1F-18BD-4993-8AB5-13B3D0D78FD1Q27549185-8C899E70-FF21-4326-90C1-AA30F562FC23Q28558503-B32283D3-F434-427F-AF3B-B8A894E270CDQ28560190-1DE6B4B5-1F64-4F30-8999-D5E003E28E47Q28561668-2C7DE177-7306-4BF7-8BBD-4F33ACC4D823Q28563206-1F7B3B0A-5E9E-4388-BAD1-D43312172A26Q28563206-D5E0F7FB-9E6A-43C0-B1FE-2B7F9E861963Q29520409-C9591014-7111-4C54-9C63-C48E221F5CF1Q29522669-975E04F9-B402-49C3-9146-D36D23CB6F38Q29802942-E997A103-9C3A-44F4-A9D8-DD90451B84BAQ29806899-A08B99C4-B167-4B55-B5AE-BFFA79470B0EQ29817928-75990370-F5FA-4434-A2F3-E23F44370923Q29819743-2E79F634-AE07-488A-B683-E139225F9A40Q5008826-0565EBEE-E7CA-425A-A7AD-67D1AC3A795BQ55200640-63FCFA77-D188-418C-B900-6B4EA099E567Q56590300-27B940E0-8268-476C-92E7-4BDD8151E677Q56593429-6034EFF2-6059-4C2B-BD46-0143CA490A5AQ56739827-C5123A81-2FA7-46C8-9E14-1DA28AEAF3C5Q56741553-27AC136F-2F1D-4C57-B90A-0411B208681A
P680
description
Catalysis of the reaction: S-a ...... + (protein)-N-methyl-arginine.
@en
biologisch proces
@nl
name
protein-arginine N-methyltransferase activity
@en
type
label
protein-arginine N-methyltransferase activity
@en
altLabel
GO:0016274
@en
PRMT activity
@en
prefLabel
protein-arginine N-methyltransferase activity
@en
P2888
P686
GO:0016274