4a3p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='4a3p' size='340' side='right'caption='[[4a3p]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='4a3p' size='340' side='right'caption='[[4a3p]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4a3p]] 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=4A3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A3P FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4a3p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A3P FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w6v|1w6v]], [[4a3o|4a3o]]</td></tr>
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w6v|1w6v]], [[4a3o|4a3o]]</div></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>
+
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></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=4a3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3p OCA], [http://pdbe.org/4a3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a3p RCSB], [http://www.ebi.ac.uk/pdbsum/4a3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3p 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=4a3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3p OCA], [https://pdbe.org/4a3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a3p RCSB], [https://www.ebi.ac.uk/pdbsum/4a3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3p ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN]] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>
+
[[https://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN]] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 22: Line 22:
==See Also==
==See Also==
-
*[[Thioesterase|Thioesterase]]
+
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 28: Line 28:
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
 +
[[Category: Large Structures]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Barsukov, I L]]
[[Category: Barsukov, I L]]

Revision as of 07:42, 18 August 2022

Structure of USP15 DUSP-UBL deletion mutant

PDB ID 4a3p

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/4a3p"
Personal tools