7uw7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 7uw7 is ON HOLD Authors: Kimani, S., Dong, A., Li, Y., Arrowsmith, C.H., Edwards, A.M., Halabelian, L., Structural Genomics Consortium (SGC) Descri...)
Current revision (17:21, 18 October 2023) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 7uw7 is ON HOLD
+
==Crystal structure of the Human TRIP12 WWE domain (isoform 2) in complex with ADP==
-
 
+
<StructureSection load='7uw7' size='340' side='right'caption='[[7uw7]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
-
Authors: Kimani, S., Dong, A., Li, Y., Arrowsmith, C.H., Edwards, A.M., Halabelian, L., Structural Genomics Consortium (SGC)
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[7uw7]] 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=7UW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UW7 FirstGlance]. <br>
-
Description: Crystal structure of the Human TRIP12 WWE domain (isoform 2) in complex with ADP
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.17&#8491;</td></tr>
-
[[Category: Unreleased Structures]]
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
-
[[Category: Edwards, A.M]]
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7uw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uw7 OCA], [https://pdbe.org/7uw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uw7 RCSB], [https://www.ebi.ac.uk/pdbsum/7uw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uw7 ProSAT]</span></td></tr>
-
[[Category: Arrowsmith, C.H]]
+
</table>
-
[[Category: Dong, A]]
+
== Disease ==
-
[[Category: Structural Genomics Consortium (Sgc)]]
+
[https://www.uniprot.org/uniprot/TRIPC_HUMAN TRIPC_HUMAN] Non-specific syndromic intellectual disability. The disease is caused by variants affecting the gene represented in this entry.
-
[[Category: Li, Y]]
+
== Function ==
-
[[Category: Halabelian, L]]
+
[https://www.uniprot.org/uniprot/TRIPC_HUMAN TRIPC_HUMAN] E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair (PubMed:19028681, PubMed:22884692). Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins (PubMed:19028681). Acts as a key regulator of DNA damage response by acting as a suppressor of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites, thereby acting as a guard against excessive spreading of ubiquitinated chromatin at damaged chromosomes (PubMed:22884692). In normal cells, mediates ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A, a lysine-less tumor suppressor required for p53/TP53 activation under oncogenic stress (PubMed:20208519). In cancer cells, however, isoform p19ARF/ARF and TRIP12 are located in different cell compartments, preventing isoform p19ARF/ARF ubiquitination and degradation (PubMed:20208519). Does not mediate ubiquitination of isoform p16-INK4a of CDKN2A (PubMed:20208519). Also catalyzes ubiquitination of NAE1 and SMARCE1, leading to their degradation (PubMed:18627766). Ubiquitination and degradation of target proteins is regulated by interaction with proteins such as MYC, TRADD or SMARCC1, which disrupt the interaction between TRIP12 and target proteins (PubMed:20829358). Mediates ubiquitination of ASXL1: following binding to N(6)-methyladenosine methylated DNA, ASXL1 is ubiquitinated by TRIP12, leading to its degradation and subsequent inactivation of the PR-DUB complex (PubMed:30982744).<ref>PMID:18627766</ref> <ref>PMID:19028681</ref> <ref>PMID:20208519</ref> <ref>PMID:20829358</ref> <ref>PMID:22884692</ref> <ref>PMID:30982744</ref>
-
[[Category: Kimani, S]]
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Arrowsmith CH]]
 +
[[Category: Dong A]]
 +
[[Category: Edwards AM]]
 +
[[Category: Halabelian L]]
 +
[[Category: Kimani S]]
 +
[[Category: Li Y]]

Current revision

Crystal structure of the Human TRIP12 WWE domain (isoform 2) in complex with ADP

PDB ID 7uw7

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7uw7"
Personal tools