2wx0
From Proteopedia
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<StructureSection load='2wx0' size='340' side='right'caption='[[2wx0]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2wx0' size='340' side='right'caption='[[2wx0]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2wx0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2wx0]] is a 6 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=2WX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WX0 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2wx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wx0 OCA], [https://pdbe.org/2wx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wx0 RCSB], [https://www.ebi.ac.uk/pdbsum/2wx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wx0 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=2wx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wx0 OCA], [https://pdbe.org/2wx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wx0 RCSB], [https://www.ebi.ac.uk/pdbsum/2wx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wx0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Disease == | ||
| - | [[https://www.uniprot.org/uniprot/TAB2_HUMAN TAB2_HUMAN]] Defects in TAB2 are the cause of congenital heart disease non-syndromic type 2 (CHTD2) [MIM:[https://omim.org/entry/612863 612863]]. It is a disease characterized by congenital developmental abnormalities involving structures of the heart. Clinical features include left ventricular outflow tract obstruction, subaortic stenosis, residual aortic regurgitation, atrial fibrillation, bicuspid aortic valve and aortic dilation. Note=A chromosomal aberration involving TAB2 has been found in a family with congenital heart disease. Translocation t(2;6)(q21;q25).<ref>PMID:20493459</ref> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/UBC_BOVIN UBC_BOVIN] 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 (By similarity). | |
== 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: | + | [[Category: Bos taurus]] |
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Akutsu | + | [[Category: Akutsu M]] |
| - | [[Category: Bremm | + | [[Category: Bremm A]] |
| - | [[Category: Hofmann | + | [[Category: Hofmann K]] |
| - | [[Category: Komander | + | [[Category: Komander D]] |
| - | [[Category: Kulathu | + | [[Category: Kulathu Y]] |
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Current revision
TAB2 NZF DOMAIN IN COMPLEX WITH Lys63-linked di-ubiquitin, P21
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Categories: Bos taurus | Homo sapiens | Large Structures | Akutsu M | Bremm A | Hofmann K | Komander D | Kulathu Y
