peptidyl-lysine trimethylation - Wikidata - wikimedia - TriplyDB

peptidyl-lysine trimethylation

peptidyl-lysine trimethylation

http://www.wikidata.org/entity/Q21105872

about

histone H4-K20 trimethylation histone H3-K9 trimethylation histone H3-K4 trimethylation histone H3-K36 trimethylation

P279

Eukaryotic elongation factor 2 lysine methyltransferase Valosin containing protein lysine methyltransferase SET domain containing 2, histone lysine methyltransferase Electron transfer flavoprotein subunit beta lysine methyltransferase Citrate synthase lysine methyltransferase SET domain containing 3, actin histidine methyltransferase SET domain containing 4 Eukaryotic elongation factor 2 lysine methyltransferase SET domain containing 2 SET domain containing 4 Electron transfer flavoprotein beta subunit lysine methyltransferase SET domain containing 3 Valosin containing protein lysine (K) methyltransferase Protein-lysine N-methyltransferase YGR001C Protein-lysine N-methyltransferase YDR198C Protein-lysine N-methyltransferase YHL039W Protein-lysine N-methyltransferase YPL208W Protein-lysine N-methyltransferase YJR129C Cytochrome c lysine N-methyltransferase YHR109W Electron transfer flavoprotein subunit beta lysine methyltransferase ATP synthase c subunit lysine N-methyltransferase SET domain containing 4 SET domain containing 3, actin histidine methyltransferase SET (trithorax/polycomb) domain containing CELE_Y92H12BR.6 SET (trithorax/polycomb) domain containing CELE_Y71H2AM.8 Uncharacterized protein Dmel_CG5013 Uncharacterized protein Dmel_CG33230 Uncharacterized protein Dmel_CG7889 SET domain containing 3 Dmel_CG32732 SET domain containing 4 SET domain containing 3, actin histidine methyltransferase Citrate synthase lysine methyltransferase Electron transfer flavoprotein subunit beta lysine methyltransferase Citrate synthase lysine methyltransferase

P682

Lysine methylation of VCP by a member of a novel human protein methyltransferase family Human METTL20 methylates lysine residues adjacent to the recognition loop of the electron transfer flavoprotein in mitochondria Identification and characterization of a novel evolutionarily conserved lysine-specific methyltransferase targeting eukaryotic translation elongation factor 2 (eEF2)Structural insights into SETD3-mediated histidine methylation on β-actin Human FAM173A is a mitochondrial lysine-specific methyltransferase that targets adenine nucleotide translocase and affects mitochondrial respiration

P921

Q21101921-F21ED75C-4BAE-4309-BAF7-1A989F20D26B Q21101922-DBA509CA-E097-4902-8E59-A3ECBC51B4B3 Q21101923-1572571E-01E0-4F8E-9F9A-2596E853CC09 Q21118251-C11490F6-42D0-4E46-9183-CE90FAD4F46E

P279

Q21105873-1C7705A1-862A-43A2-AC26-57DF25E507A6 Q21105874-FE8B73BE-7DFF-4281-AC26-2437E744A5F3 Q21118252-CA08FF7A-2DDD-4D71-A1A6-383A54EE5622 Q21119434-409D4497-1927-4C58-AE09-58FBBE7CEAE9 Q21120825-100CDC7C-3924-4234-9FFE-145CD1BE89C0 Q21124480-BCBAF8F8-1BA8-44C2-A141-673C7AA26D51 Q21124486-969B40E1-CD9D-4AA6-A6E6-F711D150E3BF Q21498332-7A8B613D-117B-462C-A693-4082F8F78575 Q21988099-6E1F78A4-6390-4D32-9D2C-624D022EBDD4 Q21988100-03597C90-5EB6-49A4-902C-A3FE2A186DA3 Q21988294-038F0BF8-63E8-4A55-ABD3-CA4FFE56C0A6 Q21989804-5EE86A85-8139-428C-8B0F-DA3AA7468AF3 Q26250173-4E8EF58B-E6D2-4CF3-8531-5F7BE0C5058F Q27547234-F3BE348D-F9A7-469A-91A6-0713822E6C4D Q27550042-0D78B875-5688-411F-B35E-66991678E475 Q27550042-1354FB8D-5801-4652-B0D1-EB0B0C3A08D5 Q27551731-B969B206-F9DE-45DF-9F75-1289512A06C8 Q27551806-A51F23FA-6802-4526-9F19-EF69A71E6AC8 Q27552088-1034BC36-69C8-431B-9ABD-4BB577C63BF2 Q27552341-C812F1AE-1829-4AE1-AB3F-D7BAEB05EA50 Q28557498-BF99B7BE-33F9-41B0-8D6E-B0451DCE1CE6 Q29516959-5AD46DD1-C22E-44C9-86A6-446C24717656 Q29516959-5FF40E27-88D1-422D-9E0B-1E2D567E7117 Q29522875-B944A839-8FD9-4301-9A56-440474B1BD11 Q29526964-6794E14B-8E04-4FA4-81A8-CFFE728DF3BE Q29526964-A306FC05-3135-4936-AAE0-93C30AE09F77 Q29794006-DAE4DBBC-D3C2-4F75-B4B9-9C54D1D79541 Q29808639-8801E05F-0890-420B-A99B-6DF6786BBAA7 Q29810089-EE5601F7-D7CC-4F7A-9F5D-91D2B5AD0571 Q29817055-EA78870B-8087-4AE6-8322-677DDB2FD7B7 Q29818746-01B7F3F9-F606-4B60-9144-BF8919321EC0 Q29819567-4433639C-3971-4BE1-8AC4-4BEA1DF9B7A5 Q29822409-51539E40-951A-461E-AD43-E92B8BDA076D Q29823268-45ACBF0F-68EE-49F3-BBF4-86CFB860412B Q29823268-B0FADF6D-C537-498B-8B4E-FB2E9C8BC856 Q29824239-B14F513B-FF4F-46AA-A506-EEB4E01167CA Q29831088-97DBE080-5299-410F-B73F-C664A3BA0A6D Q55204643-C12E6AE4-7BF5-4D2A-853B-CB27AD354B77

P682

Q24298017-922C788B-A4AE-4B15-BA46-C8A12DBAA8E2 Q24300752-7178DC66-1D4E-4BBE-8A6A-8C94BD2F46EA Q24304158-F891D65B-516D-4568-8976-E5292F98D189 Q63379282-BB86E5ED-25FA-4B75-B261-D6344C6158D6 Q92859770-473B4A78-D804-4098-9B55-92880773E0F2

P921

peptidyl-lysine trimethylation

http://www.wikidata.org/entity/Q21105872

description

The methylation of peptidyl-lysine to form peptidyl-N6,N6,N6-trimethyl-L-lysine.

@en

biologisch proces

@nl

name

peptidyl-lysine trimethylation

@en

type

label

peptidyl-lysine trimethylation

@en

prefLabel

peptidyl-lysine trimethylation

@en

P279

Q21105872-CA3623FB-5041-4521-9DAB-6E7889337C67

P2888

Q21105872-ED69BDDF-505D-4A9D-AB03-F2F2F89DE693

P31

Q21105872-F2361E95-3CAB-446D-B6D6-BBBDCA8F6A72

P686

Q21105872-0A0E4161-4306-498F-813F-20D02D5E9DFF

P279

peptidyl-lysine methylation

P2888

P31

biological process

P686

GO:0018023

http://www.w3.org/2001/XMLSchema#string