4oxa - Revision history

OCA: Replacing page with 'REMOVED: The PDB entry 4oxa was removed.'

OCA — Wed, 11 Mar 2015 11:41:36 GMT

Replacing page with 'REMOVED: The PDB entry 4oxa was removed.'

←Older revision		Revision as of 11:41, 11 March 2015
Line 1:		Line 1:
-	~~==S5A HOMOLOG==~~	+	REMOVED: The PDB entry 4oxa was removed.
-	~~<StructureSection load='4oxa' size='340' side='right' caption='[[4oxa]], [[Resolution\|resolution]] 3.14Å' scene=''>~~	+
-	~~== Structural highlights ==~~	+
-	~~<table><tr><td colspan='2'>[[4oxa]] is a 2 chain structure. Full crystallographic information is available from [http~~:~~//oca.weizmann.ac.il/oca-bin/ocashort?id=4OXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OXA FirstGlance]. <br>~~	+
-	~~</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5n\|2x5n]], [[1ubq\|1ubq]]</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=~~4oxa ~~FirstGlance], [http://oca~~.~~weizmann.ac.il/oca-bin/ocaids?id=4oxa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oxa RCSB], [http://www.ebi.ac.uk/pdbsum/4oxa PDBsum]</span></td></tr>~~	+
-	~~</table>~~	+
-	~~== Function ==~~	+
-	[[http://www.uniprot.org/uniprot/RPN10_YEAST RPN10_YEAST]] Multiubiquitin binding protein. [[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>	+
-	~~== References ==~~	+
-	~~<references/>~~	+
-	~~__TOC__~~	+
-	~~</StructureSection>~~	+
-	~~[[Category: Keren-Kaplan, T]]~~	+
-	~~[[Category: Prag, G]]~~	+
-	~~[[Category: Cytosol]]~~	+
-	~~[[Category: Proteasome]]~~	+
-	~~[[Category: Ubiquitin]]~~	+
-	~~[[Category: Ubiquitin-binding protein]]~~	+
-	~~[[Category: Ubiquitin-receptor]]~~	+
-	~~[[Category: Ubiquitylation]]~~	+
-	~~[[Category: Vwa]]~~	+

OCA at 11:33, 4 March 2015

OCA — Wed, 04 Mar 2015 11:33:11 GMT

←Older revision		Revision as of 11:33, 4 March 2015
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-	'''~~Unreleased structure~~'''	+	==S5A HOMOLOG==
-		+	<StructureSection load='4oxa' size='340' side='right' caption='[[4oxa]], [[Resolution\|resolution]] 3.14Å' scene=''>
-	~~The entry~~ 4oxa is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4oxa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OXA FirstGlance]. <br>
-	~~Authors~~: ~~Keren~~-~~Kaplan~~, T., ~~Prag~~, G.	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2x5n\|2x5n]], [[1ubq\|1ubq]]</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=4oxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oxa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oxa RCSB], [http://www.ebi.ac.uk/pdbsum/4oxa PDBsum]</span></td></tr>
-	~~Description: S5A HOMOLOG~~	+	</table>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	== Function ==
-	[[~~Category~~: ~~Prag, G~~]]	+	[[http://www.uniprot.org/uniprot/RPN10_YEAST RPN10_YEAST]] Multiubiquitin binding protein. [[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Keren-Kaplan, T]]		[[Category: Keren-Kaplan, T]]
		+	[[Category: Prag, G]]
		+	[[Category: Cytosol]]
		+	[[Category: Proteasome]]
		+	[[Category: Ubiquitin]]
		+	[[Category: Ubiquitin-binding protein]]
		+	[[Category: Ubiquitin-receptor]]
		+	[[Category: Ubiquitylation]]
		+	[[Category: Vwa]]

OCA at 14:37, 24 December 2014

OCA — Wed, 24 Dec 2014 14:37:51 GMT

←Older revision		Revision as of 14:37, 24 December 2014
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	Description: S5A HOMOLOG		Description: S5A HOMOLOG
		+	[[Category: Unreleased Structures]]
		+	[[Category: Prag, G]]
		+	[[Category: Keren-Kaplan, T]]

OCA at 08:27, 2 April 2014

OCA — Wed, 02 Apr 2014 08:27:25 GMT

←Older revision		Revision as of 08:27, 2 April 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Keren-Kaplan, T., Prag, G.		Authors: Keren-Kaplan, T., Prag, G.

	Description: S5A HOMOLOG		Description: S5A HOMOLOG

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

OCA — Thu, 13 Feb 2014 04:53:19 GMT

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

←Older revision

Revision as of 04:53, 13 February 2014

OCA: New page: '''Unreleased structure''' The entry 4oxa is ON HOLD Authors: Keren-Kaplan, T., Prag, G. Description: S5A HOMOLOG

OCA — Thu, 13 Feb 2014 04:53:18 GMT

New page: '''Unreleased structure''' The entry 4oxa is ON HOLD Authors: Keren-Kaplan, T., Prag, G. Description: S5A HOMOLOG

New page

'''Unreleased structure'''

The entry 4oxa is ON HOLD

Authors: Keren-Kaplan, T., Prag, G.

Description: S5A HOMOLOG