4eew - Revision history

OCA at 14:59, 14 March 2024

2024-03-14T14:59:43Z

← Older revision		Revision as of 14:59, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eew]] 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=4EEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EEW FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eew]] 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=4EEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EEW 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=4eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eew OCA], [https://pdbe.org/4eew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eew RCSB], [https://www.ebi.ac.uk/pdbsum/4eew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eew 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]] 1.3Å</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=4eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eew OCA], [https://pdbe.org/4eew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eew RCSB], [https://www.ebi.ac.uk/pdbsum/4eew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eew ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/BAG6_HUMAN BAG6_HUMAN]] Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Acts in part by regulating stability of proteins and their degradation by the proteasome. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2. Required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cell (NK) activation and cytotoxicity.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref>		[https://www.uniprot.org/uniprot/BAG6_HUMAN BAG6_HUMAN] Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Acts in part by regulating stability of proteins and their degradation by the proteasome. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2. Required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cell (NK) activation and cytotoxicity.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref>

	==See Also==		==See Also==

OCA at 07:08, 28 September 2022

2022-09-28T07:08:09Z

← Older revision		Revision as of 07:08, 28 September 2022
Line 1:		Line 1:

	==Crystal structure of the Ubl domain of BAG6==		==Crystal structure of the Ubl domain of BAG6==
	<StructureSection load='4eew' size='340' side='right' caption='[[4eew]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='4eew' size='340' side='right'caption='[[4eew]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eew]] 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=4EEW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EEW FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eew]] 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=4EEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EEW FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BAG6, BAT3, G3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eew OCA], [https://pdbe.org/4eew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eew RCSB], [https://www.ebi.ac.uk/pdbsum/4eew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eew 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=4eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eew OCA], [~~http~~://pdbe.org/4eew PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4eew RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4eew PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4eew ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/BAG6_HUMAN BAG6_HUMAN]] Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Acts in part by regulating stability of proteins and their degradation by the proteasome. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2. Required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cell (NK) activation and cytotoxicity.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref>		[[https://www.uniprot.org/uniprot/BAG6_HUMAN BAG6_HUMAN]] Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Acts in part by regulating stability of proteins and their degradation by the proteasome. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2. Required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cell (NK) activation and cytotoxicity.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref>

	==See Also==		==See Also==
	*[[BAG ~~protein~~\|BAG ~~protein~~]]		*[[BAG family proteins 3D structures\|BAG family proteins 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Gehring, K]]		[[Category: Large Structures]]
	[[Category: Kozlov, G]]		[[Category: Gehring K]]
	[[Category: LePage, K]]		[[Category: Kozlov G]]
	[[Category: Vinaik, R]]		[[Category: LePage K]]
	~~[[Category: Chaperone]]~~		[[Category: Vinaik R]]
	~~[[Category: Gp78-binding]]~~
	~~[[Category: Ubiquitin-like fold~~]]

OCA at 18:57, 5 August 2016

2016-08-05T18:57:14Z

← Older revision		Revision as of 18:57, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of the Ubl domain of BAG6==		==Crystal structure of the Ubl domain of BAG6==
	<StructureSection load='4eew' size='340' side='right' caption='[[4eew]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='4eew' size='340' side='right' caption='[[4eew]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eew]] is a 2 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=4EEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EEW FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eew]] 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=4EEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EEW FirstGlance]. <br>
	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BAG6, BAT3, G3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BAG6, BAT3, G3 ([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=4eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eew OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eew RCSB], [http://www.ebi.ac.uk/pdbsum/4eew 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=4eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eew OCA], [http://pdbe.org/4eew PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eew RCSB], [http://www.ebi.ac.uk/pdbsum/4eew PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eew ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 16:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Gehring, K]]		[[Category: Gehring, K]]
	[[Category: Kozlov, G]]		[[Category: Kozlov, G]]

OCA at 05:01, 25 December 2014

2014-12-25T05:01:03Z

← Older revision		Revision as of 05:01, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eew]] is a 2 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=4EEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EEW FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eew]] is a 2 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=4EEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EEW FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BAG6, BAT3, G3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>		</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BAG6, BAT3, G3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eew OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eew RCSB], [http://www.ebi.ac.uk/pdbsum/4eew 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=4eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eew OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eew RCSB], [http://www.ebi.ac.uk/pdbsum/4eew PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/BAG6_HUMAN BAG6_HUMAN]] Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Acts in part by regulating stability of proteins and their degradation by the proteasome. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2. Required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref> Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cell (NK) activation and cytotoxicity.<ref>PMID:14960581</ref> <ref>PMID:17403783</ref> <ref>PMID:18055229</ref> <ref>PMID:18765639</ref> <ref>PMID:18852879</ref> <ref>PMID:20516149</ref> <ref>PMID:20676083</ref>

	==See Also==		==See Also==
	*[[BAG protein\|BAG protein]]		*[[BAG protein\|BAG protein]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Gehring, K.]]		[[Category: Gehring, K]]
	[[Category: Kozlov, G.]]		[[Category: Kozlov, G]]
	[[Category: LePage, K.]]		[[Category: LePage, K]]
	[[Category: Vinaik, R.]]		[[Category: Vinaik, R]]
	[[Category: Chaperone]]		[[Category: Chaperone]]
	[[Category: Gp78-binding]]		[[Category: Gp78-binding]]
	[[Category: Ubiquitin-like fold]]		[[Category: Ubiquitin-like fold]]

OCA at 08:00, 5 June 2014

2014-06-05T08:00:20Z

← Older revision		Revision as of 08:00, 5 June 2014
Line 1:		Line 1:
	[[~~Image~~:4eew.~~jpg\|left\|200px~~]]		==Crystal structure of the Ubl domain of BAG6==
			<StructureSection load='4eew' size='340' side='right' caption='[[4eew]], [[Resolution\|resolution]] 1.30Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4eew]] is a 2 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=4EEW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EEW FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BAG6, BAT3, G3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4eew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eew OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eew RCSB], [http://www.ebi.ac.uk/pdbsum/4eew PDBsum]</span></td></tr>
			<table>

	~~<!--~~		==See Also==
	~~The line below this paragraph, containing "STRUCTURE_4eew", creates the "Structure Box" on the page.~~		*[[BAG protein\|BAG protein]]
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~		__TOC__
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~		</StructureSection>
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	~~{{STRUCTURE_4eew\| PDB=4eew \| SCENE= }}~~

	~~===Crystal structure of the Ubl domain of BAG6===~~


	==~~About this Structure~~==
	[[~~4eew~~]] ~~is a 2 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=4EEW OCA].~~
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Gehring, K.]]		[[Category: Gehring, K.]]

OCA at 07:14, 11 April 2012

2012-04-11T07:14:08Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+[[Image:4eew.jpg|left|200px]]
-The entry 4eew is ON HOLD
+<!--
-Authors: Kozlov, G., LePage, K., Vinaik, R., Gehring, K.
+===Crystal structure of the Ubl domain of BAG6===
-Description: Crystal structure of the Ubl domain of BAG6

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

2012-04-04T05:50:58Z

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

← Older revision	Revision as of 05:50, 4 April 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4eew is ON HOLD Authors: Kozlov, G., LePage, K., Vinaik, R., Gehring, K. Description: Crystal structure of the Ubl domain of BAG6

2012-04-04T05:50:56Z

New page: '''Unreleased structure''' The entry 4eew is ON HOLD Authors: Kozlov, G., LePage, K., Vinaik, R., Gehring, K. Description: Crystal structure of the Ubl domain of BAG6

New page

'''Unreleased structure'''

The entry 4eew is ON HOLD

Authors: Kozlov, G., LePage, K., Vinaik, R., Gehring, K.

Description: Crystal structure of the Ubl domain of BAG6