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| <StructureSection load='5ln1' size='340' side='right'caption='[[5ln1]], [[Resolution|resolution]] 3.14Å' scene=''> | | <StructureSection load='5ln1' size='340' side='right'caption='[[5ln1]], [[Resolution|resolution]] 3.14Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5ln1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LN1 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5ln1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LN1 FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPN10, MCB1, SUN1, YHR200W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), UBB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.14Å</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=5ln1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ln1 OCA], [http://pdbe.org/5ln1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ln1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ln1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ln1 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=5ln1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ln1 OCA], [https://pdbe.org/5ln1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ln1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ln1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ln1 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/RPN10_YEAST RPN10_YEAST]] Multiubiquitin binding protein. [[http://www.uniprot.org/uniprot/UBB_HUMAN UBB_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> | | [https://www.uniprot.org/uniprot/RPN10_YEAST RPN10_YEAST] Multiubiquitin binding protein. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| ==See Also== | | ==See Also== |
| *[[Proteasome|Proteasome]] | | *[[Proteasome 3D structures|Proteasome 3D structures]] |
| *[[Ubiquitin|Ubiquitin]]
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Baker's yeast]] | | [[Category: Homo sapiens]] |
| [[Category: Human]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Attali, I]] | | [[Category: Saccharomyces cerevisiae S288C]] |
| [[Category: Keren-Kaplan, T]] | | [[Category: Attali I]] |
| [[Category: Levin-Kravets, O]] | | [[Category: Keren-Kaplan T]] |
| [[Category: Prag, G]] | | [[Category: Levin-Kravets O]] |
| [[Category: Proteasome]]
| | [[Category: Prag G]] |
| [[Category: Ubiquitin]]
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| [[Category: Ubiquitin-binding protein]]
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| [[Category: Ubiquitylation]]
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| [[Category: Vwa]]
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