5zyq - Revision history

OCA at 10:29, 27 March 2024

OCA — Wed, 27 Mar 2024 10:29:56 GMT

←Older revision		Revision as of 10:29, 27 March 2024
Line 3:		Line 3:
	<StructureSection load='5zyq' size='340' side='right'caption='[[5zyq]], [[Resolution\|resolution]] 2.53Å' scene=''>		<StructureSection load='5zyq' size='340' side='right'caption='[[5zyq]], [[Resolution\|resolution]] 2.53Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zyq]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZYQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ZYQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zyq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZYQ FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~PAF1~~, ~~PD2 (~~[~~http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.531Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5zyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zyq OCA], [~~http~~://pdbe.org/5zyq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5zyq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5zyq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5zyq ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zyq OCA], [https://pdbe.org/5zyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zyq RCSB], [https://www.ebi.ac.uk/pdbsum/5zyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zyq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CTR9_HUMAN CTR9_HUMAN]] Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity).<ref>PMID:16024656</ref> <ref>PMID:16307923</ref> <ref>PMID:19345177</ref> <ref>PMID:19952111</ref> <ref>PMID:20178742</ref> <ref>PMID:20541477</ref> <ref>PMID:21329879</ref>	+	[https://www.uniprot.org/uniprot/CTR9_HUMAN CTR9_HUMAN] Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity).<ref>PMID:16024656</ref> <ref>PMID:16307923</ref> <ref>PMID:19345177</ref> <ref>PMID:19952111</ref> <ref>PMID:20178742</ref> <ref>PMID:20541477</ref> <ref>PMID:21329879</ref> [https://www.uniprot.org/uniprot/PAF1_HUMAN PAF1_HUMAN] Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors. Has oncogenic activity in vivo and in vitro.<ref>PMID:16491129</ref> <ref>PMID:19410543</ref> <ref>PMID:19952111</ref> <ref>PMID:20541477</ref> <ref>PMID:20178742</ref> <ref>PMID:21329879</ref> <ref>PMID:22419161</ref>
-	~~<div style="background-color~~:~~#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	~~The evolutionarily conserved multifunctional polymerase-associated factor 1 (Paf1)~~ complex (~~Paf1C~~), which ~~is composed of at least five subunits (Paf1, Leo1, Ctr9, Cdc73,~~ and ~~Rtf1), plays vital roles~~ in ~~gene~~ regulation ~~and has connections to~~ development and ~~human diseases. Here, we report two structures~~ of ~~each of the human~~ and ~~yeast Ctr9/Paf1 subcomplexes~~, ~~which assemble into heterodimers~~ with ~~very similar conformations, revealing an interface between the tetratricopeptide repeat module in Ctr9~~ and ~~Paf1. The structure of the Ctr9/Paf1 subcomplex may provide mechanistic explanations for disease-associated mutations~~ in ~~human PAF1~~ and ~~CTR9~~. ~~Our study reveals that the formation of the Ctr9/Paf1 heterodimer~~ is required for ~~the assembly~~ of ~~yeast Paf1C,~~ and ~~is essential for yeast viability~~. ~~In addition, disruption~~ of ~~the interaction between Paf1~~ and ~~Ctr9 greatly affects the level~~ of histone H3 methylation ~~in vivo. Collectively, our results shed light~~ on ~~Paf1C assembly and functional regulation~~.	+
-		+
-	~~Paf1~~ and ~~Ctr9 subcomplex formation~~ is ~~essential for Paf1 complex assembly~~ and ~~functional regulation~~.,~~Xie Y, Zheng M, Chu X, Chen Y, Xu H, Wang J, Zhou H~~, ~~Long J Nat Commun~~. ~~2018 Sep 18;9(1):3795. doi: 10.1038~~/~~s41467~~-~~018-06237-7~~. PMID:~~30228257~~<ref>PMID:~~30228257~~</ref>	+
-		+
-	~~From MEDLINE®~~/~~PubMed®, a database of the U.S. National Library of Medicine.~~<br>	+
-	</~~div~~>	+
-	<~~div class="pdbe-citations 5zyq" style="background-color~~:~~#fffaf0;"~~></~~div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Long, J]]	+	[[Category: Long J]]
-	[[Category: Xie, Y]]	+	[[Category: Xie Y]]
-	[[Category: Zheng, M]]	+	[[Category: Zheng M]]
-	[[Category: Zhou, H]]	+	[[Category: Zhou H]]
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Tpr]]~~	+
-	~~[[Category: Transcription~~]]	+

OCA at 07:25, 23 May 2019

OCA — Thu, 23 May 2019 07:25:12 GMT

←Older revision		Revision as of 07:25, 23 May 2019
Line 1:		Line 1:

	==The Structure of Human PAF1/CTR9 complex==		==The Structure of Human PAF1/CTR9 complex==
-	<StructureSection load='5zyq' size='340' side='right' caption='[[5zyq]], [[Resolution\|resolution]] 2.53Å' scene=''>	+	<StructureSection load='5zyq' size='340' side='right'caption='[[5zyq]], [[Resolution\|resolution]] 2.53Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zyq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZYQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zyq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZYQ FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zyq OCA], [http://pdbe.org/5zyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zyq RCSB], [http://www.ebi.ac.uk/pdbsum/5zyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zyq ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PAF1, PD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zyq OCA], [http://pdbe.org/5zyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zyq RCSB], [http://www.ebi.ac.uk/pdbsum/5zyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zyq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/CTR9_HUMAN CTR9_HUMAN]] Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity).<ref>PMID:16024656</ref> <ref>PMID:16307923</ref> <ref>PMID:19345177</ref> <ref>PMID:19952111</ref> <ref>PMID:20178742</ref> <ref>PMID:20541477</ref> <ref>PMID:21329879</ref>		[[http://www.uniprot.org/uniprot/CTR9_HUMAN CTR9_HUMAN]] Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity).<ref>PMID:16024656</ref> <ref>PMID:16307923</ref> <ref>PMID:19345177</ref> <ref>PMID:19952111</ref> <ref>PMID:20178742</ref> <ref>PMID:20541477</ref> <ref>PMID:21329879</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The evolutionarily conserved multifunctional polymerase-associated factor 1 (Paf1) complex (Paf1C), which is composed of at least five subunits (Paf1, Leo1, Ctr9, Cdc73, and Rtf1), plays vital roles in gene regulation and has connections to development and human diseases. Here, we report two structures of each of the human and yeast Ctr9/Paf1 subcomplexes, which assemble into heterodimers with very similar conformations, revealing an interface between the tetratricopeptide repeat module in Ctr9 and Paf1. The structure of the Ctr9/Paf1 subcomplex may provide mechanistic explanations for disease-associated mutations in human PAF1 and CTR9. Our study reveals that the formation of the Ctr9/Paf1 heterodimer is required for the assembly of yeast Paf1C, and is essential for yeast viability. In addition, disruption of the interaction between Paf1 and Ctr9 greatly affects the level of histone H3 methylation in vivo. Collectively, our results shed light on Paf1C assembly and functional regulation.
		+
		+	Paf1 and Ctr9 subcomplex formation is essential for Paf1 complex assembly and functional regulation.,Xie Y, Zheng M, Chu X, Chen Y, Xu H, Wang J, Zhou H, Long J Nat Commun. 2018 Sep 18;9(1):3795. doi: 10.1038/s41467-018-06237-7. PMID:30228257<ref>PMID:30228257</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5zyq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Long, J]]		[[Category: Long, J]]
	[[Category: Xie, Y]]		[[Category: Xie, Y]]

OCA at 07:58, 26 September 2018

OCA — Wed, 26 Sep 2018 07:58:48 GMT

←Older revision		Revision as of 07:58, 26 September 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 5zyq ~~is ON HOLD until Paper Publication~~	+	==The Structure of Human PAF1/CTR9 complex==
-		+	<StructureSection load='5zyq' size='340' side='right' caption='[[5zyq]], [[Resolution\|resolution]] 2.53Å' scene=''>
-	~~Authors~~: ~~Xie~~, Y., ~~Zheng, M~~., ~~Zhou~~, H., ~~Long, J~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5zyq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZYQ FirstGlance]. <br>
-	~~Description: The Structure of Human PAF1~~/~~CTR9 complex~~	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zyq OCA], [http://pdbe.org/5zyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zyq RCSB], [http://www.ebi.ac.uk/pdbsum/5zyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zyq ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CTR9_HUMAN CTR9_HUMAN]] Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 (By similarity).<ref>PMID:16024656</ref> <ref>PMID:16307923</ref> <ref>PMID:19345177</ref> <ref>PMID:19952111</ref> <ref>PMID:20178742</ref> <ref>PMID:20541477</ref> <ref>PMID:21329879</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Long, J]]		[[Category: Long, J]]
		+	[[Category: Xie, Y]]
		+	[[Category: Zheng, M]]
	[[Category: Zhou, H]]		[[Category: Zhou, H]]
-	[[Category: ~~Zheng, M~~]]	+	[[Category: Complex]]
-	[[Category: ~~Xie, Y~~]]	+	[[Category: Tpr]]
		+	[[Category: Transcription]]

OCA at 05:22, 14 June 2018

OCA — Thu, 14 Jun 2018 05:22:47 GMT

←Older revision		Revision as of 05:22, 14 June 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5zyq is ON HOLD	+	The entry 5zyq is ON HOLD until Paper Publication

-	Authors: ~~Ying~~, X., ~~Mingying~~, Z., ~~Hao~~, Z., ~~Jiafu~~, L.	+	Authors: Xie, Y., Zheng, M., Zhou, H., Long, J.

	Description: The Structure of Human PAF1/CTR9 complex		Description: The Structure of Human PAF1/CTR9 complex
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Hao~~, Z]]	+	[[Category: Long, J]]
-	[[Category: ~~Ying~~, X]]	+	[[Category: Zhou, H]]
-	[[Category: ~~Jiafu~~, L]]	+	[[Category: Zheng, M]]
-	[[Category: ~~Mingying~~, Z]]	+	[[Category: Xie, Y]]

OCA: Protected "5zyq" [edit=sysop:move=sysop]

OCA — Wed, 06 Jun 2018 04:11:11 GMT

Protected "5zyq" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:11, 6 June 2018

OCA: New page: '''Unreleased structure''' The entry 5zyq is ON HOLD Authors: Ying, X., Mingying, Z., Hao, Z., Jiafu, L. Description: The Structure of Human PAF1/CTR9 complex [[Category: Unreleased St...

OCA — Wed, 06 Jun 2018 04:11:10 GMT

New page: '''Unreleased structure''' The entry 5zyq is ON HOLD Authors: Ying, X., Mingying, Z., Hao, Z., Jiafu, L. Description: The Structure of Human PAF1/CTR9 complex [[Category: Unreleased St...

New page

'''Unreleased structure'''

The entry 5zyq is ON HOLD

Authors: Ying, X., Mingying, Z., Hao, Z., Jiafu, L.

Description: The Structure of Human PAF1/CTR9 complex
[[Category: Unreleased Structures]]
[[Category: Hao, Z]]
[[Category: Ying, X]]
[[Category: Jiafu, L]]
[[Category: Mingying, Z]]