about
P361
Bromodomain containing 4Bromodomain containing 2Bromodomain containing 3Bromodomain testis associatedBromodomain containing 9Bromodomain containing 7SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4Lysine methyltransferase 2ABromodomain adjacent to zinc finger domain 2AProteasome activator subunit 4MLLT3 super elongation complex subunitATPase family AAA domain containing 2BDouble PHD fingers 2TATA-box binding protein associated factor 1 likeTripartite motif containing 24Zinc finger MYND-type containing 8TATA-box binding protein associated factor 1Bromodomain containing 2Bromodomain containing 3Bromodomain containing 7Bromodomain containing 9Bromodomain, testis-specificBromodomain containing 4Myeloid/lymphoid or mixed-lineage leukemia; translocated to, 3Coactivator-associated arginine methyltransferase 1Tripartite motif-containing 24Lysine (K)-specific methyltransferase 2ABromodomain adjacent to zinc finger domain protein 2ASWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4PH-interacting proteinProteasome (prosome, macropain) activator subunit 4D4, zinc and double PHD fingers family 2TATA-box binding protein associated factor 1Pleckstrin homology domain interacting proteinChromatin-binding protein BDF1 YLR399CRsc4p YKR008WBlm10p YFL007WSWI/SNF catalytic subunit SNF2 YOR290CRSC chromatin remodeling complex ATPase subunit STH1 YIL126WHistone acetyltransferase GCN5 YGR252W
P680
Selective inhibition of BET bromodomainsPhospho switch triggers Brd4 chromatin binding and activator recruitment for gene-specific targetingHistone recognition and large-scale structural analysis of the human bromodomain familyStructural ramification for acetyl-lysine recognition by the bromodomain of human BRG1 protein, a central ATPase of the SWI/SNF remodeling complexStructural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marksZMYND8 Reads the Dual Histone Mark H3K4me1-H3K14ac to Antagonize the Expression of Metastasis-Linked GenesAF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylationMolecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS DomainMutations in the BAF-Complex Subunit DPF2 Are Associated with Coffin-Siris Syndrome.
P921
Q21100441-B59D2594-C381-43AA-BC3F-11A0D6357016Q21100450-872466B5-2B38-4A8E-B509-1F4B08304312Q21100464-5B14CEBC-3BA6-4020-B50C-B637D22B972BQ21100472-61F3CA85-41DE-4541-908E-EBA2CFDACF1AQ21100491-A8592167-686B-440A-A8BF-E253E6B98E5DQ21100492-AF44912E-2A99-4BEC-8064-2D6F534D1AC9Q21101932-44D1FF16-5690-4AB9-BD1A-132F5BB93223Q21102206-B8AF1EE6-E8E4-46F6-A205-22B5A7248578Q21105459-0BF07FFD-26BE-4D84-B33D-AEED6DEF1B67Q21111805-1009A75F-065C-4D1F-9DB9-E638FBDA659DQ21116346-A7025A8E-4507-4C7E-BBB3-763D7AB21873Q21116749-186D0E63-CBEE-44EC-AB26-61F80DF350CCQ21119291-047828BB-5C3F-4C1F-8D6C-B378C6695D7FQ21125296-E38F0999-012A-4216-BA3F-DFBB1B83A420Q21126566-362BB38D-5F75-4E3C-92E3-5EF66E43A122Q21132422-18DEF850-3E67-427A-8DEA-99004771E490Q21170876-90167E2E-2AC3-433E-B9AE-EC59CAF89A70Q21494009-DA421C00-D9F6-4403-B74C-7E42F80A3B44Q21494024-F46D9A8D-308A-4D88-A1F9-B030F37B2E25Q21496148-F5B54FF6-DF8C-4472-B538-1F818462FA0DQ21496149-5B58B854-6A81-46AA-A79E-A5D75E7424FBQ21496155-FC98AC81-FD8C-4780-997F-B9FE4706B10AQ21496156-4C71CD62-AC20-498F-BA6E-5ECBD3626F20Q21496846-4BB6D5A7-007A-42B5-B174-80F186F01A23Q21497204-377DFB68-962E-4BB5-A7E6-F4F47519147CQ21498067-F6D62CAD-578F-4B71-84CD-7484F2468A4AQ21983442-D6F0DBE5-8B78-4E9C-927A-A287595EFBE6Q21983442-F7096B13-ABB7-4DC6-A386-5CA431F54352Q21984135-8AD6016C-D3C7-45A9-A91E-4CC69A09C970Q21984492-06A9E910-FFBD-47CE-B86B-8114E3C10968Q21986032-CADEAB64-BED1-419F-93BD-04B36832AAD5Q21988968-84970F03-75BB-455E-A5A6-D0167FA6FA7DQ21988968-8FF9F585-31A5-4DB4-A69D-03A5F6CC593CQ21989455-B69B6233-0EC4-40F9-A0CF-CBEE77419DECQ21992103-4BA31A1F-AB90-496B-806C-77A958A0154CQ22680260-E8844D55-0FBB-421C-98C5-1307D722EB0BQ27547392-3AE70937-89C1-41E1-B9E9-36FDDB99D271Q27549242-C0D96A05-B217-4D89-8DF0-5CB50167E9A2Q27551268-1138C7FA-D930-40A9-9F05-C71D2CF556EFQ27551696-6D883244-49FC-48B3-AC99-F95C6204AA31
P680
Q24301009-F101F057-A718-4D30-8FE3-C0E07C51A543Q24308867-6C3BA52F-71E3-4516-867E-4E05965B56E6Q24310431-D80AB61F-7340-4FB4-9A04-426ECCC6AF2FQ24312868-5F2F8934-0A1B-41FD-A4DB-776B257E9AEDQ24312868-93CB5D6D-C191-49D8-9EDA-8575CE2571CCQ24324784-0DBDFE8B-CC07-4815-A525-2921D93C5AE1Q28116530-DC4D777A-D85A-49E2-9E71-B9A7D0009FE7Q34449085-6863ECDF-D38F-4FFC-B8A7-E377F30830C4Q36827990-8BF8C6F4-02EA-49A9-A835-7212203F4D47Q48741684-E4890897-E82B-44D7-A1BD-644A35AB0EB2
P921
description
Interacting selectively and no ...... been modified by acetylation.
@en
moleculaire functie
@nl
name
lysine-acetylated histone binding
@en
type
label
lysine-acetylated histone binding
@en
altLabel
GO:0070577
@en
prefLabel
lysine-acetylated histone binding
@en
P2888
P527
P686
GO:0070577