2bf8 - Revision history

OCA at 13:32, 13 December 2023

2023-12-13T13:32:01Z

← Older revision		Revision as of 13:32, 13 December 2023
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	<StructureSection load='2bf8' size='340' side='right'caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2bf8' size='340' side='right'caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bovin Bovin~~] and [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>
	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[1a5r\|1a5r]], [[1tgz\|1tgz]]~~, [[~~2bep~~\|~~2bep~~]]~~</div></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]] 2.3Å</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2~~.19 6~~.3~~.2.19] </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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [https://pdbe.org/2bf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [https://www.ebi.ac.uk/pdbsum/2bf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bf8 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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [https://pdbe.org/2bf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [https://www.ebi.ac.uk/pdbsum/2bf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bf8 ProSAT]</span></td></tr>
	</table>		</table>
	~~== Disease ==~~
	[[https://www.uniprot.org/uniprot/SUMO1_HUMAN SUMO1_HUMAN]] Defects in SUMO1 are the cause of non-syndromic orofacial cleft type 10 (OFC10) [MIM:[https://omim.org/entry/613705 613705]]; also called non-syndromic cleft lip with or without cleft palate 10. OFC10 is a birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. Note=A chromosomal aberation involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.<ref>PMID:16990542</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/~~SUMO1_HUMAN SUMO1_HUMAN~~]~~] Ubiquitin-like protein that can be covalently attached~~ to proteins ~~as a monomer~~ or ~~a lysine~~-linked ~~polymer~~. ~~Covalent attachment via an isopeptide bond~~ to ~~its substrates requires prior activation by~~ the ~~E1 complex SAE1~~-~~SAE2~~ and ~~linkage to the E2 enzyme UBE2I~~, ~~and can be promoted by E3 ligases~~ such as ~~PIAS1~~-~~4, RANBP2 or CBX4~~. ~~This post-translational modification on lysine residues~~ of ~~proteins plays a crucial role in a number~~ of ~~cellular processes such as nuclear transport, DNA replication and repair, mitosis~~ and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of ~~modified proteins~~. ~~May also regulate a network~~ of ~~genes involved~~ in ~~palate development~~.~~<ref>PMID~~:~~9019411</ref> <ref>PMID:9162015</ref> <ref>PMID:18538659</ref>~~ <ref>PMID:~~18408734~~</ref>		[https://www.uniprot.org/uniprot/UBE2K_BOVIN UBE2K_BOVIN] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53 (By similarity). Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1.[UniProtKB:P61086]<ref>PMID:9535861</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bovin~~]]		[[Category: Bos taurus]]
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	~~[[Category: Ubiquitin--protein ligase]]~~		[[Category: Jentsch S]]
	~~[[Category: Dijk, W J.Van]]~~		[[Category: Knipscheer P]]
	[[Category: Jentsch, S]]		[[Category: Korner R]]
	[[Category: Knipscheer, P]]		[[Category: Melchior F]]
	[[Category: Korner, R]]		[[Category: Oberhofer E]]
	[[Category: Melchior, F]]		[[Category: Pichler A]]
	[[Category: Oberhofer, E]]		[[Category: Sixma TK]]
	~~[[Category: Olsen, J Velgaard~~]]		[[Category: Van Dijk WJ]]
	[[Category: Pichler, A]]		[[Category: Velgaard Olsen J]]
	[[Category: Sixma~~, T K~~]]
	[[Category: ~~E2 ubiquitin conjugating enzyme~~]]
	[[Category: ~~E2-25k]]~~
	~~[[Category: Ligase]]~~
	~~[[Category: Ligase-complex]]~~
	~~[[Category: Spine]]~~
	~~[[Category: Structural genomic]]~~
	~~[[Category: Structural proteomics in europe]]~~
	~~[[Category: Sumo]]~~
	~~[[Category: Sumo-target structure~~]]

OCA at 13:08, 24 November 2021

2021-11-24T13:08:54Z

← Older revision		Revision as of 13:08, 24 November 2021
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	<StructureSection load='2bf8' size='340' side='right'caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2bf8' size='340' side='right'caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bovin Bovin] and [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a5r\|1a5r]], [[1tgz\|1tgz]], [[2bep\|2bep]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a5r\|1a5r]], [[1tgz\|1tgz]], [[2bep\|2bep]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [~~http~~://pdbe.org/2bf8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2bf8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2bf8 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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [https://pdbe.org/2bf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [https://www.ebi.ac.uk/pdbsum/2bf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bf8 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/SUMO1_HUMAN SUMO1_HUMAN]] Defects in SUMO1 are the cause of non-syndromic orofacial cleft type 10 (OFC10) [MIM:[~~http~~://omim.org/entry/613705 613705]]; also called non-syndromic cleft lip with or without cleft palate 10. OFC10 is a birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. Note=A chromosomal aberation involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.<ref>PMID:16990542</ref>		[[https://www.uniprot.org/uniprot/SUMO1_HUMAN SUMO1_HUMAN]] Defects in SUMO1 are the cause of non-syndromic orofacial cleft type 10 (OFC10) [MIM:[https://omim.org/entry/613705 613705]]; also called non-syndromic cleft lip with or without cleft palate 10. OFC10 is a birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. Note=A chromosomal aberation involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.<ref>PMID:16990542</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/SUMO1_HUMAN SUMO1_HUMAN]] Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.<ref>PMID:9019411</ref> <ref>PMID:9162015</ref> <ref>PMID:18538659</ref> <ref>PMID:18408734</ref>		[[https://www.uniprot.org/uniprot/SUMO1_HUMAN SUMO1_HUMAN]] Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.<ref>PMID:9019411</ref> <ref>PMID:9162015</ref> <ref>PMID:18538659</ref> <ref>PMID:18408734</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[SUMO 3D Structures\|SUMO 3D Structures]]		*[[SUMO 3D Structures\|SUMO 3D Structures]]
	*[[~~Ubiquitin~~ conjugating enzyme\|~~Ubiquitin~~ conjugating enzyme]]		*[[3D structures of ubiquitin conjugating enzyme\|3D structures of ubiquitin conjugating enzyme]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:10, 19 February 2020

2020-02-19T08:10:38Z

← Older revision		Revision as of 08:10, 19 February 2020
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	==Crystal structure of SUMO modified ubiquitin conjugating enzyme E2- 25K==		==Crystal structure of SUMO modified ubiquitin conjugating enzyme E2- 25K==
	<StructureSection load='2bf8' size='340' side='right' caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2bf8' size='340' side='right'caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>
Line 33:		Line 33:

	==See Also==		==See Also==
	*[[SUMO\|SUMO]]		*[[SUMO 3D Structures\|SUMO 3D Structures]]
	*[[Ubiquitin conjugating enzyme\|Ubiquitin conjugating enzyme]]		*[[Ubiquitin conjugating enzyme\|Ubiquitin conjugating enzyme]]
	== References ==		== References ==
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	[[Category: Bovin]]		[[Category: Bovin]]
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Dijk, W J.Van]]		[[Category: Dijk, W J.Van]]

OCA at 06:37, 16 May 2018

2018-05-16T06:37:53Z

← Older revision		Revision as of 06:37, 16 May 2018
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	==~~CRYSTAL STRUCTURE OF~~ SUMO ~~MODIFIED UBIQUITIN CONJUGATING ENZYME~~ E2-25K==
			==Crystal structure of SUMO modified ubiquitin conjugating enzyme E2- 25K==
	<StructureSection load='2bf8' size='340' side='right' caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2bf8' size='340' side='right' caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a5r\|1a5r]], [[1tgz\|1tgz]], [[2bep\|2bep]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a5r\|1a5r]], [[1tgz\|1tgz]], [[2bep\|2bep]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [http://pdbe.org/2bf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bf8 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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [http://pdbe.org/2bf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bf8 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bf8_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bf8_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bf8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 09:21, 11 September 2015

2015-09-11T09:21:12Z

← Older revision		Revision as of 09:21, 11 September 2015
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	<StructureSection load='2bf8' size='340' side='right' caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='2bf8' size='340' side='right' caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bos_taurus Bos taurus~~] and [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a5r\|1a5r]], [[1tgz\|1tgz]], [[2bep\|2bep]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a5r\|1a5r]], [[1tgz\|1tgz]], [[2bep\|2bep]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bf8 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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [http://pdbe.org/2bf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bf8 PDBsum]</span></td></tr>
	</table>		</table>
			== Disease ==
			[[http://www.uniprot.org/uniprot/SUMO1_HUMAN SUMO1_HUMAN]] Defects in SUMO1 are the cause of non-syndromic orofacial cleft type 10 (OFC10) [MIM:[http://omim.org/entry/613705 613705]]; also called non-syndromic cleft lip with or without cleft palate 10. OFC10 is a birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum. Note=A chromosomal aberation involving SUMO1 is the cause of OFC10. Translocation t(2;8)(q33.1;q24.3). The breakpoint occurred in the SUMO1 gene and resulted in haploinsufficiency confirmed by protein assays.<ref>PMID:16990542</ref>
			== Function ==
			[[http://www.uniprot.org/uniprot/SUMO1_HUMAN SUMO1_HUMAN]] Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.<ref>PMID:9019411</ref> <ref>PMID:9162015</ref> <ref>PMID:18538659</ref> <ref>PMID:18408734</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 25:		Line 29:
	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 2bf8" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bos taurus~~]]		[[Category: Bovin]]
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Dijk, W J.Van]]		[[Category: Dijk, W J.Van]]

OCA at 09:30, 8 January 2015

2015-01-08T09:30:26Z

← Older revision		Revision as of 09:30, 8 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a5r\|1a5r]], [[1tgz\|1tgz]], [[2bep\|2bep]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a5r\|1a5r]], [[1tgz\|1tgz]], [[2bep\|2bep]]</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bf8 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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bf8 PDBsum]</span></td></tr>
	<table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 36:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Ubiquitin--protein ligase]]		[[Category: Ubiquitin--protein ligase]]
	[[Category: Dijk, W J.Van.]]		[[Category: Dijk, W J.Van]]
	[[Category: Jentsch, S.]]		[[Category: Jentsch, S]]
	[[Category: Knipscheer, P.]]		[[Category: Knipscheer, P]]
	[[Category: Korner, R.]]		[[Category: Korner, R]]
	[[Category: Melchior, F.]]		[[Category: Melchior, F]]
	[[Category: Oberhofer, E.]]		[[Category: Oberhofer, E]]
	[[Category: Olsen, J Velgaard.]]		[[Category: Olsen, J Velgaard]]
	[[Category: Pichler, A.]]		[[Category: Pichler, A]]
	[[Category: Sixma, T K.]]		[[Category: Sixma, T K]]
	[[Category: E2 ubiquitin conjugating enzyme]]		[[Category: E2 ubiquitin conjugating enzyme]]
	[[Category: E2-25k]]		[[Category: E2-25k]]

OCA at 01:58, 30 September 2014

2014-09-30T01:58:52Z

← Older revision		Revision as of 01:58, 30 September 2014
Line 1:		Line 1:
	~~{{STRUCTURE_2bf8\| PDB=2bf8 \| SCENE= }}~~		==CRYSTAL STRUCTURE OF SUMO MODIFIED UBIQUITIN CONJUGATING ENZYME E2-25K==
	===CRYSTAL STRUCTURE OF SUMO MODIFIED UBIQUITIN CONJUGATING ENZYME E2-25K===		<StructureSection load='2bf8' size='340' side='right' caption='[[2bf8]], [[Resolution\|resolution]] 2.30Å' scene=''>
	~~{{ABSTRACT_PUBMED_15723079}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[2bf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BF8 FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1a5r\|1a5r]], [[1tgz\|1tgz]], [[2bep\|2bep]]</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></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=2bf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bf8 RCSB], [http://www.ebi.ac.uk/pdbsum/2bf8 PDBsum]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bf8_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Post-translational modification with small ubiquitin-related modifier (SUMO) alters the function of many proteins, but the molecular mechanisms and consequences of this modification are still poorly defined. During a screen for novel SUMO1 targets, we identified the ubiquitin-conjugating enzyme E2-25K (Hip2). SUMO attachment severely impairs E2-25K ubiquitin thioester and unanchored ubiquitin chain formation in vitro. Crystal structures of E2-25K(1-155) and of the E2-25K(1-155)-SUMO conjugate (E2-25K(*)SUMO) indicate that SUMO attachment interferes with E1 interaction through its location on the N-terminal helix. The SUMO acceptor site in E2-25K, Lys14, does not conform to the consensus site found in most SUMO targets (PsiKXE), and functions only in the context of an alpha-helix. In contrast, adjacent SUMO consensus sites are modified only when in unstructured peptides. The demonstration that secondary structure elements are part of SUMO attachment signals could contribute to a better prediction of SUMO targets.

	~~==About this Structure==~~		SUMO modification of the ubiquitin-conjugating enzyme E2-25K.,Pichler A, Knipscheer P, Oberhofer E, van Dijk WJ, Korner R, Olsen JV, Jentsch S, Melchior F, Sixma TK Nat Struct Mol Biol. 2005 Mar;12(3):264-9. Epub 2005 Feb 20. PMID:15723079<ref>PMID:15723079</ref>
	~~[[2bf8]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bos_taurus Bos taurus] and [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=2BF8 OCA].~~
			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	==See Also==		==See Also==
	*[[SUMO\|SUMO]]		*[[SUMO\|SUMO]]
			*[[Ubiquitin conjugating enzyme\|Ubiquitin conjugating enzyme]]
	==~~Reference~~==		== References ==
	~~<ref group="xtra">PMID:015723079</ref>~~<references ~~group="xtra"~~/><~~references~~/>		<references/>
			__TOC__
			</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 05:57, 25 March 2013

2013-03-25T05:57:00Z

← Older revision		Revision as of 05:57, 25 March 2013
Line 1:		Line 1:
	~~[[Image:2bf8.png\|left\|200px]]~~

	{{STRUCTURE_2bf8\| PDB=2bf8 \| SCENE= }}		{{STRUCTURE_2bf8\| PDB=2bf8 \| SCENE= }}

	===CRYSTAL STRUCTURE OF SUMO MODIFIED UBIQUITIN CONJUGATING ENZYME E2-25K===		===CRYSTAL STRUCTURE OF SUMO MODIFIED UBIQUITIN CONJUGATING ENZYME E2-25K===

	{{ABSTRACT_PUBMED_15723079}}		{{ABSTRACT_PUBMED_15723079}}

Line 14:		Line 10:

	==Reference==		==Reference==
	<ref group="xtra">PMID:015723079</ref><references group="xtra"/>		<ref group="xtra">PMID:015723079</ref><references group="xtra"/><references/>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 17:48, 20 October 2012

2012-10-20T17:48:16Z

← Older revision		Revision as of 17:48, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[2bf8]] is a 2 chain structure ~~of [[SUMO]]~~ with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA].		[[2bf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF8 OCA].

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

OCA: Protected "2bf8" [edit=sysop:move=sysop]

2012-07-27T02:02:49Z

Protected "2bf8" [edit=sysop:move=sysop]

← Older revision	Revision as of 02:02, 27 July 2012
(No difference)