4un2
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4un2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UN2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UN2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4un2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UN2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UN2 FirstGlance]. <br> | ||
| - | </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=4un2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4un2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4un2 RCSB], [http://www.ebi.ac.uk/pdbsum/4un2 PDBsum]</span></td></tr> | + | </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=4un2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4un2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4un2 RCSB], [http://www.ebi.ac.uk/pdbsum/4un2 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[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> [[http://www.uniprot.org/uniprot/DSK2_YEAST DSK2_YEAST]] Involved, with RAD23 in spindle pole body duplication. Involved in the ubiquitin-proteasome proteolytic pathway. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 19: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Ban, D | + | [[Category: Ban, D]] |
| - | [[Category: Becker, S | + | [[Category: Becker, S]] |
| - | [[Category: Giller, K | + | [[Category: Giller, K]] |
| - | [[Category: Griesinger, C | + | [[Category: Griesinger, C]] |
| - | [[Category: Groot, B L.de | + | [[Category: Groot, B L.de]] |
| - | [[Category: Lee, D | + | [[Category: Lee, D]] |
| - | [[Category: Michielssens, S | + | [[Category: Michielssens, S]] |
| - | [[Category: Peters, J H | + | [[Category: Peters, J H]] |
| - | [[Category: Pratihar, S | + | [[Category: Pratihar, S]] |
| - | [[Category: Sabo, T M | + | [[Category: Sabo, T M]] |
| - | [[Category: Seeliger, D | + | [[Category: Seeliger, D]] |
| - | [[Category: Sharma, M | + | [[Category: Sharma, M]] |
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Protein degradation]] | [[Category: Protein degradation]] | ||
[[Category: Ubiquitin-associated domain]] | [[Category: Ubiquitin-associated domain]] | ||
Revision as of 11:51, 25 December 2014
Crystal structure of the UBA domain of Dsk2 in complex with Ubiquitin
| |||||||||||
