3ixs
From Proteopedia
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{{STRUCTURE_3ixs| PDB=3ixs | SCENE= }} | {{STRUCTURE_3ixs| PDB=3ixs | SCENE= }} | ||
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===Ring1B C-terminal domain/RYBP C-terminal domain Complex=== | ===Ring1B C-terminal domain/RYBP C-terminal domain Complex=== | ||
| + | {{ABSTRACT_PUBMED_20696397}} | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/RING2_HUMAN RING2_HUMAN]] E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity.<ref>PMID:11513855</ref><ref>PMID:15386022</ref><ref>PMID:16359901</ref><ref>PMID:16714294</ref><ref>PMID:20696397</ref> | ||
| - | + | ==About this Structure== | |
| - | + | [[3ixs]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IXS OCA]. | |
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| - | == | + | ==See Also== |
| - | + | *[[Ubiquitin protein ligase|Ubiquitin protein ligase]] | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020696397</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Kim, C A.]] | [[Category: Kim, C A.]] | ||
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[[Category: Ubl conjugation pathway]] | [[Category: Ubl conjugation pathway]] | ||
[[Category: Zinc-finger]] | [[Category: Zinc-finger]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 25 08:55:06 2010'' | ||
Revision as of 09:34, 27 March 2013
Contents |
Ring1B C-terminal domain/RYBP C-terminal domain Complex
Template:ABSTRACT PUBMED 20696397
Function
[RING2_HUMAN] E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity.[1][2][3][4][5]
About this Structure
3ixs is a 12 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Wang R, Taylor AB, Leal BZ, Chadwell LV, Ilangovan U, Robinson AK, Schirf V, Hart PJ, Lafer EM, Demeler B, Hinck AP, McEwen DG, Kim CA. Polycomb group targeting through different binding partners of RING1B C-terminal domain. Structure. 2010 Aug 11;18(8):966-75. PMID:20696397 doi:10.1016/j.str.2010.04.013
- ↑ Lee SJ, Choi JY, Sung YM, Park H, Rhim H, Kang S. E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme. FEBS Lett. 2001 Aug 10;503(1):61-4. PMID:11513855
- ↑ Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS, Zhang Y. Role of histone H2A ubiquitination in Polycomb silencing. Nature. 2004 Oct 14;431(7010):873-8. Epub 2004 Sep 22. PMID:15386022 doi:10.1038/nature02985
- ↑ Cao R, Tsukada Y, Zhang Y. Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol Cell. 2005 Dec 22;20(6):845-54. PMID:16359901 doi:10.1016/j.molcel.2005.12.002
- ↑ Li Z, Cao R, Wang M, Myers MP, Zhang Y, Xu RM. Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex. J Biol Chem. 2006 Jul 21;281(29):20643-9. Epub 2006 May 18. PMID:16714294 doi:10.1074/jbc.M602461200
- ↑ Wang R, Taylor AB, Leal BZ, Chadwell LV, Ilangovan U, Robinson AK, Schirf V, Hart PJ, Lafer EM, Demeler B, Hinck AP, McEwen DG, Kim CA. Polycomb group targeting through different binding partners of RING1B C-terminal domain. Structure. 2010 Aug 11;18(8):966-75. PMID:20696397 doi:10.1016/j.str.2010.04.013
Categories: Homo sapiens | Kim, C A. | Taylor, A B. | Wang, R. | Apoptosis | Chromatin regulator | Chromosomal protein | Dna-binding | E3-ligase | Ligase | Metal-binding | Nucleus | Phosphoprotein | Polycomb | Protein binding | Repressor | Ring1b | Rybp | Transcription | Transcription regulation | Transcription repressor | Ubl conjugation pathway | Zinc-finger
