5af5: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Structure of Lys33-linked triUb S.G. P 212121==
-<StructureSection load='5af5' size='340' side='right' caption='[[5af5]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
+<StructureSection load='5af5' size='340' side='right'caption='[[5af5]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5af5]] is a 1 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=5AF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AF5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5af5]] is a 1 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=5AF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AF5 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5af4|5af4]], [[5af6|5af6]]</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]] 1.68&#8491;</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=5af5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af5 OCA], [http://pdbe.org/5af5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5af5 RCSB], [http://www.ebi.ac.uk/pdbsum/5af5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5af5 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=5af5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5af5 OCA], [https://pdbe.org/5af5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5af5 RCSB], [https://www.ebi.ac.uk/pdbsum/5af5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5af5 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 </div>
 <div class="pdbe-citations 5af5" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[3D structures of ubiquitin|3D structures of ubiquitin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Elliott, P R]]
+[[Category: Large Structures]]
-[[Category: Freund, S M.V]]
+[[Category: Elliott PR]]
-[[Category: Komander, D]]
+[[Category: Freund SMV]]
-[[Category: Michel, M A]]
+[[Category: Komander D]]
-[[Category: Pruneda, J N]]
+[[Category: Michel MA]]
-[[Category: Simicek, M]]
+[[Category: Pruneda JN]]
-[[Category: Swatek, K N]]
+[[Category: Simicek M]]
-[[Category: Wagstaff, J L]]
+[[Category: Swatek KN]]
-[[Category: Signaling protein]]
+[[Category: Wagstaff JL]]
-[[Category: Signalling protein]]
-[[Category: Ubiquitin]]