4wij - Revision history

OCA at 00:53, 28 December 2023

OCA — Thu, 28 Dec 2023 00:53:32 GMT

←Older revision		Revision as of 00:53, 28 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4wij]] is a 2 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=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4wij]] is a 2 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=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>
-	</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=4wij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wij OCA], [https://pdbe.org/4wij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wij RCSB], [https://www.ebi.ac.uk/pdbsum/4wij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wij ProSAT]</span></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]] 3.49Å</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=4wij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wij OCA], [https://pdbe.org/4wij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wij RCSB], [https://www.ebi.ac.uk/pdbsum/4wij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wij ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 07:10, 7 April 2023

OCA — Fri, 07 Apr 2023 07:10:14 GMT

←Older revision		Revision as of 07:10, 7 April 2023
Line 3:		Line 3:
	<StructureSection load='4wij' size='340' side='right'caption='[[4wij]], [[Resolution\|resolution]] 3.49Å' scene=''>		<StructureSection load='4wij' size='340' side='right'caption='[[4wij]], [[Resolution\|resolution]] 3.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wij]] is a 2 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=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wij]] is a 2 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=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wii\|4wii]], [[4wik\|4wik]]</td></tr>~~	+	</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=4wij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wij OCA], [https://pdbe.org/4wij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wij RCSB], [https://www.ebi.ac.uk/pdbsum/4wij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wij ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SFPQ, PSF ([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=4wij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wij OCA], [~~http~~://pdbe.org/4wij PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4wij RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4wij PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4wij ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/SFPQ_HUMAN SFPQ_HUMAN]] Translocation renal cell carcinoma. A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.	+	[https://www.uniprot.org/uniprot/SFPQ_HUMAN SFPQ_HUMAN] Translocation renal cell carcinoma. A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SFPQ_HUMAN SFPQ_HUMAN]] DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation.<ref>PMID:10847580</ref> <ref>PMID:10858305</ref> <ref>PMID:10931916</ref> <ref>PMID:11259580</ref> <ref>PMID:11525732</ref> <ref>PMID:11897684</ref> <ref>PMID:15590677</ref> <ref>PMID:20932480</ref> <ref>PMID:8045264</ref> <ref>PMID:8449401</ref>	+	[https://www.uniprot.org/uniprot/SFPQ_HUMAN SFPQ_HUMAN] DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation.<ref>PMID:10847580</ref> <ref>PMID:10858305</ref> <ref>PMID:10931916</ref> <ref>PMID:11259580</ref> <ref>PMID:11525732</ref> <ref>PMID:11897684</ref> <ref>PMID:15590677</ref> <ref>PMID:20932480</ref> <ref>PMID:8045264</ref> <ref>PMID:8449401</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bond~~, c s~~]]	+	[[Category: Bond cs]]
-	[[Category: Lee, M]]	+	[[Category: Lee M]]
-	~~[[Category: Rrm]]~~	+
-	~~[[Category: Transcription~~]]	+

OCA at 07:49, 8 January 2020

OCA — Wed, 08 Jan 2020 07:49:50 GMT

←Older revision		Revision as of 07:49, 8 January 2020
Line 1:		Line 1:

	==HUMAN SPLICING FACTOR, CONSTRUCT 1==		==HUMAN SPLICING FACTOR, CONSTRUCT 1==
-	<StructureSection load='4wij' size='340' side='right' caption='[[4wij]], [[Resolution\|resolution]] 3.49Å' scene=''>	+	<StructureSection load='4wij' size='340' side='right'caption='[[4wij]], [[Resolution\|resolution]] 3.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4wij]] is a 2 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=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4wij]] is a 2 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=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bond, c s]]		[[Category: Bond, c s]]
	[[Category: Lee, M]]		[[Category: Lee, M]]
	[[Category: Rrm]]		[[Category: Rrm]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 15:10, 15 November 2017

OCA — Wed, 15 Nov 2017 15:10:51 GMT

←Older revision		Revision as of 15:10, 15 November 2017
Line 3:		Line 3:
	<StructureSection load='4wij' size='340' side='right' caption='[[4wij]], [[Resolution\|resolution]] 3.49Å' scene=''>		<StructureSection load='4wij' size='340' side='right' caption='[[4wij]], [[Resolution\|resolution]] 3.49Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wij]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wij]] is a 2 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=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wii\|4wii]], [[4wik\|4wik]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wii\|4wii]], [[4wik\|4wik]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SFPQ, PSF ([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=4wij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wij OCA], [http://pdbe.org/4wij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wij RCSB], [http://www.ebi.ac.uk/pdbsum/4wij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wij ProSAT]</span></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=4wij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wij OCA], [http://pdbe.org/4wij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wij RCSB], [http://www.ebi.ac.uk/pdbsum/4wij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wij ProSAT]</span></td></tr>
	</table>		</table>
Line 24:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Bond, c s]]		[[Category: Bond, c s]]
	[[Category: Lee, M]]		[[Category: Lee, M]]
	[[Category: Rrm]]		[[Category: Rrm]]
	[[Category: Transcription]]		[[Category: Transcription]]

OCA at 18:49, 1 February 2017

OCA — Wed, 01 Feb 2017 18:49:08 GMT

←Older revision		Revision as of 18:49, 1 February 2017
Line 1:		Line 1:
		+
	==HUMAN SPLICING FACTOR, CONSTRUCT 1==		==HUMAN SPLICING FACTOR, CONSTRUCT 1==
	<StructureSection load='4wij' size='340' side='right' caption='[[4wij]], [[Resolution\|resolution]] 3.49Å' scene=''>		<StructureSection load='4wij' size='340' side='right' caption='[[4wij]], [[Resolution\|resolution]] 3.49Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4wij]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[4wij]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wii\|4wii]], [[4wik\|4wik]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wii\|4wii]], [[4wik\|4wik]]</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=4wij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wij OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wij RCSB], [http://www.ebi.ac.uk/pdbsum/4wij PDBsum]</span></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=4wij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wij OCA], [http://pdbe.org/4wij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wij RCSB], [http://www.ebi.ac.uk/pdbsum/4wij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wij ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4wij" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:12, 1 April 2015

OCA — Wed, 01 Apr 2015 13:12:49 GMT

←Older revision		Revision as of 13:12, 1 April 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==HUMAN SPLICING FACTOR, CONSTRUCT 1==
		+	<StructureSection load='4wij' size='340' side='right' caption='[[4wij]], [[Resolution\|resolution]] 3.49Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4wij]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIJ FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wii\|4wii]], [[4wik\|4wik]]</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=4wij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wij OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wij RCSB], [http://www.ebi.ac.uk/pdbsum/4wij PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/SFPQ_HUMAN SFPQ_HUMAN]] Translocation renal cell carcinoma. A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SFPQ_HUMAN SFPQ_HUMAN]] DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as a heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the pre-mRNA in resting T-cells; T-cell activation and subsequent reduced phosphorylation is proposed to lead to release from THRAP3 allowing binding to pre-mRNA splicing regulatotry elements which represses exon inclusion. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex through histone deacetylation.<ref>PMID:10847580</ref> <ref>PMID:10858305</ref> <ref>PMID:10931916</ref> <ref>PMID:11259580</ref> <ref>PMID:11525732</ref> <ref>PMID:11897684</ref> <ref>PMID:15590677</ref> <ref>PMID:20932480</ref> <ref>PMID:8045264</ref> <ref>PMID:8449401</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	SFPQ, (a.k.a. PSF), is a human tumor suppressor protein that regulates many important functions in the cell nucleus including coordination of long non-coding RNA molecules into nuclear bodies. Here we describe the first crystal structures of Splicing Factor Proline and Glutamine Rich (SFPQ), revealing structural similarity to the related PSPC1/NONO heterodimer and a strikingly extended structure (over 265 A long) formed by an unusual anti-parallel coiled-coil that results in an infinite linear polymer of SFPQ dimers within the crystals. Small-angle X-ray scattering and transmission electron microscopy experiments show that polymerization is reversible in solution and can be templated by DNA. We demonstrate that the ability to polymerize is essential for the cellular functions of SFPQ: disruptive mutation of the coiled-coil interaction motif results in SFPQ mislocalization, reduced formation of nuclear bodies, abrogated molecular interactions and deficient transcriptional regulation. The coiled-coil interaction motif thus provides a molecular explanation for the functional aggregation of SFPQ that directs its role in regulating many aspects of cellular nucleic acid metabolism.

-	The ~~entry 4wij is ON HOLD until Paper Publication~~	+	The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulation.,Lee M, Sadowska A, Bekere I, Ho D, Gully BS, Lu Y, Iyer KS, Trewhella J, Fox AH, Bond CS Nucleic Acids Res. 2015 Mar 12. pii: gkv156. PMID:25765647<ref>PMID:25765647</ref>

-	~~Authors: lee~~, M.~~, bond, c~~.s.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: HUMAN SPLICING FACTOR, CONSTRUCT 1~~	+	== References ==
-	~~[[Category: Unreleased Structures]]~~	+	<references/>
-	[[Category: Bond, ~~C.S~~]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Bond, c s]]
	[[Category: Lee, M]]		[[Category: Lee, M]]
		+	[[Category: Rrm]]
		+	[[Category: Transcription]]

OCA at 19:32, 24 December 2014

OCA — Wed, 24 Dec 2014 19:32:51 GMT

←Older revision		Revision as of 19:32, 24 December 2014
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	Description: HUMAN SPLICING FACTOR, CONSTRUCT 1		Description: HUMAN SPLICING FACTOR, CONSTRUCT 1
		+	[[Category: Unreleased Structures]]
		+	[[Category: Bond, C.S]]
		+	[[Category: Lee, M]]

OCA at 10:15, 22 October 2014

OCA — Wed, 22 Oct 2014 10:15:36 GMT

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-	The entry 4wij is ON HOLD	+	The entry 4wij is ON HOLD until Paper Publication

	Authors: lee, M., bond, c.s.		Authors: lee, M., bond, c.s.

	Description: HUMAN SPLICING FACTOR, CONSTRUCT 1		Description: HUMAN SPLICING FACTOR, CONSTRUCT 1

OCA: Protected "4wij" [edit=sysop:move=sysop]

OCA — Wed, 01 Oct 2014 23:34:56 GMT

Protected "4wij" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:34, 1 October 2014

OCA: New page: '''Unreleased structure''' The entry 4wij is ON HOLD Authors: lee, M., bond, c.s. Description: HUMAN SPLICING FACTOR, CONSTRUCT 1

OCA — Wed, 01 Oct 2014 23:34:55 GMT

New page: '''Unreleased structure''' The entry 4wij is ON HOLD Authors: lee, M., bond, c.s. Description: HUMAN SPLICING FACTOR, CONSTRUCT 1

New page

'''Unreleased structure'''

The entry 4wij is ON HOLD

Authors: lee, M., bond, c.s.

Description: HUMAN SPLICING FACTOR, CONSTRUCT 1