about
Ubiquitin like with PHD and ring finger domains 1Bmi1 polycomb ring finger oncogeneChromobox 8HECT, UBA and WWE domain containing E3 ubiquitin protein ligase 1Ubiquitin specific peptidase 22Ring finger protein 20SUZ12 polycomb repressive complex 2 subunitUbiquitin conjugating enzyme E2 UPolyhomeotic homolog 1Ring finger protein 1Ring finger protein 2Ubiquitin conjugating enzyme E2 NSUZ12 polycomb repressive complex 2 subunitRing finger protein 20HECT, UBA and WWE domain containing 1Ring finger protein 1Ring finger protein 2Chromobox 8Polyhomeotic 1Ubiquitin-like, containing PHD and RING finger domains, 1Ubiquitin specific peptidase 22Ubiquitin-conjugating enzyme E2NUbiquitin-conjugating enzyme E2AE3 ubiquitin-protein ligase HEL1 YKR017CE3 ubiquitin-protein ligase HEL2 YDR266CE3 ubiquitin-protein ligase BRE1 YDL074CLge1p YPL055CDNA-binding E3 ubiquitin-protein ligase SNT2 YGL131CTethering complex subunit PEP5 YMR231WRing finger protein 1Ubiquitin-like with PHD and ring finger domains 1BMI1 proto-oncogene, polycomb ring fingerPolyhomeotic homolog 1Chromobox 8Ubiquitin conjugating enzyme E2 URing finger protein 20Ubiquitin specific peptidase 22Ubiquitin-conjugating enzyme E2 1 CELE_C35B1.1Bre1 Dmel_CG10542Uncharacterized protein Dmel_CG46338
P682
Characterization of E3Histone, a novel testis ubiquitin protein ligase which ubiquitinates histones.USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2AMutation in PHC1 implicates chromatin remodeling in primary microcephaly pathogenesisAbnormal level of CUL4B-mediated histone H2A ubiquitination causes disruptive HOX gene expressionOvercoming chromatin barriersHigh-resolution and high-accuracy topographic and transcriptional maps of the nucleosome barrier
P921
Q21101117-7F49DAF6-8419-4CDE-B150-E43A9460E376Q21109594-DF5A6216-F71A-46C4-A598-1F2558B92445Q21109622-FD23100A-11F5-42D9-BFB0-CDDFA5607363Q21110444-A8DBC93A-B3E5-403C-9C6F-4A08BA2963D0Q21112578-FA00CEA8-8538-4566-9039-D9F04847DE93Q21112634-A1CAE87A-9EEF-42DC-A4FD-E417327D2FD3Q21115982-14A875C7-CDFE-410E-9FB3-BD360EBA5761Q21118936-119D39A6-07FC-4253-8235-02C17C89778FQ21125850-6F970530-A723-4728-8DB5-84A372B4D9BDQ21131176-AD2D5EAF-318A-4B20-BD06-72D8FC395D69Q21131178-777A4B3F-46CA-4367-917D-92DAD11A7EC3Q21131847-FE40C841-2D1B-4116-997E-56152FE5AED3Q21431161-C4830B3B-9D6F-442A-A7D6-6DC2CFE742A7Q21496150-C8743946-4B49-44F1-80E8-3D73DA839E21Q21497840-7AE994F5-D257-4735-8DB7-0B2F0519B216Q21499175-DA22FEB3-7CBE-48CC-919F-F918C72BF070Q21499182-8864AF57-D5D8-4583-A3DF-45500320223BQ21499184-9460CCDA-AABB-409D-9004-BCCC4093F01EQ21986521-D4FF8ECE-D6F2-4FCE-9B87-F2601471F0C3Q21989280-B5E28FA0-E88E-469C-B277-CA81635E6F91Q21990290-3D91797E-D375-468F-8DBA-7DBD9C5B00B0Q21992536-68A48C63-3C25-40BF-BFAB-C76489EC9E08Q21992536-6AA307EA-D46C-4464-B4DB-17F4D070E68BQ21992554-14749CCA-0E32-4CEA-9A8D-B07877E15A56Q27547448-7F6C3389-15D2-4134-8C78-26BEA10425DEQ27547448-E5EDF262-FA81-44C1-AC3E-2AEE5DF27496Q27548028-E872B04C-2138-4144-AAA8-2DA35CB2FBBDQ27548506-B79B952F-B572-488F-BCED-55157178EE52Q27550455-A47380F3-6A77-43FC-B109-90E3D761868DQ27552808-B3B7A945-507E-4146-83CF-24CE167404EEQ27552808-BF8531FF-08F3-487F-90B3-B2BB6F875764Q27552965-C685B4A7-048B-4DB5-9FF1-C8453ECDE9B9Q28557701-B2F26FDE-7609-4346-BD59-596F868E141CQ28560365-8CF21C04-450F-4BFB-B564-BE75A8977C6CQ29516461-2ADFC95F-64A7-432E-9E66-1DE3AD7D05ADQ29517659-4B63DBA1-E395-42FF-ABFC-BD8BA9E47BDEQ29518565-DDB6CBAA-0569-41C1-93DF-99485688B65FQ29519063-C42C7655-9411-4F47-AA45-F36140A913C7Q29521658-A8C94045-0660-4630-A631-3F7A4BBE42D9Q29526905-6F2F9023-F8DA-4C09-9AC2-34F3B8D4C0E5
P682
description
The modification of histones by addition of ubiquitin groups.
@en
biologisch proces
@nl
name
histone ubiquitination
@en
type
label
histone ubiquitination
@en
altLabel
GO:0016574
@en
histone ubiquitinylation
@en
histone ubiquitylation
@en
prefLabel
histone ubiquitination
@en
P2888
P686
GO:0016574