2m17: Difference between revisions

Latest revision as of 01:10, 21 November 2024

ubiquitin-like domain-containing C-terminal domain phosphatase (UBLCP1)

Structural highlights

2m17 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Ligands:	NH2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UBCP1_HUMAN Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.^[1] ^[2]

Publication Abstract from PubMed

The ubiquitin-like modifier (UBL) domain of ubiquitin-like domain proteins (UDPs) interacts specifically with subunits of the 26 S proteasome. A novel UDP, ubiquitin-like domain-containing C-terminal domain phosphatase (UBLCP1), has been identified as an interacting partner of the 26 S proteasome. We determined the high-resolution solution structure of the UBL domain of human UBLCP1 by nuclear magnetic resonance spectroscopy. The UBL domain of hUBLCP1 has a unique beta-strand (beta3) and beta3-alpha2 loop, instead of the canonical beta4 observed in other UBL domains. The molecular topology and secondary structures are different from those of known UBL domains including that of fly UBLCP1. Data from backbone dynamics shows that the beta3-alpha2 loop is relatively rigid although it might have intrinsic dynamic profile. The positively charged residues of the beta3-alpha2 loop are involved in interacting with the C-terminal leucine-rich repeat-like domain of Rpn1.

Solution Structure and Rpn1 Interaction of the UBL Domain of Human RNA Polymerase II C-Terminal Domain Phosphatase.,Yun JH, Ko S, Lee CK, Cheong HK, Cheong C, Yoon JB, Lee W PLoS One. 2013 May 7;8(5):e62981. doi: 10.1371/journal.pone.0062981. Print 2013. PMID:23667555^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zheng H, Ji C, Gu S, Shi B, Wang J, Xie Y, Mao Y. Cloning and characterization of a novel RNA polymerase II C-terminal domain phosphatase. Biochem Biophys Res Commun. 2005 Jun 17;331(4):1401-7. PMID:15883030 doi:S0006-291X(05)00831-4
↑ Guo X, Engel JL, Xiao J, Tagliabracci VS, Wang X, Huang L, Dixon JE. UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. Proc Natl Acad Sci U S A. 2011 Sep 26. PMID:21949367 doi:10.1073/pnas.1113170108
↑ Yun JH, Ko S, Lee CK, Cheong HK, Cheong C, Yoon JB, Lee W. Solution Structure and Rpn1 Interaction of the UBL Domain of Human RNA Polymerase II C-Terminal Domain Phosphatase. PLoS One. 2013 May 7;8(5):e62981. doi: 10.1371/journal.pone.0062981. Print 2013. PMID:23667555 doi:10.1371/journal.pone.0062981

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Zheng H, Ji C, Gu S, Shi B, Wang J, Xie Y, Mao Y. Cloning and characterization of a novel RNA polymerase II C-terminal domain phosphatase. Biochem Biophys Res Commun. 2005 Jun 17;331(4):1401-7. PMID:15883030 doi:S0006-291X(05)00831-4

[2] Guo X, Engel JL, Xiao J, Tagliabracci VS, Wang X, Huang L, Dixon JE. UBLCP1 is a 26S proteasome phosphatase that regulates nuclear proteasome activity. Proc Natl Acad Sci U S A. 2011 Sep 26. PMID:21949367 doi:10.1073/pnas.1113170108

[3] Yun JH, Ko S, Lee CK, Cheong HK, Cheong C, Yoon JB, Lee W. Solution Structure and Rpn1 Interaction of the UBL Domain of Human RNA Polymerase II C-Terminal Domain Phosphatase. PLoS One. 2013 May 7;8(5):e62981. doi: 10.1371/journal.pone.0062981. Print 2013. PMID:23667555 doi:10.1371/journal.pone.0062981

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
 ==ubiquitin-like domain-containing C-terminal domain phosphatase (UBLCP1)==
-<StructureSection load='2m17' size='340' side='right' caption='[[2m17]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2m17' size='340' side='right'caption='[[2m17]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2m17]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M17 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2m17]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M17 FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBLCP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=2m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m17 OCA], [https://pdbe.org/2m17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m17 RCSB], [https://www.ebi.ac.uk/pdbsum/2m17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m17 ProSAT]</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=2m17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m17 RCSB], [http://www.ebi.ac.uk/pdbsum/2m17 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/UBCP1_HUMAN UBCP1_HUMAN]] Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.<ref>PMID:15883030</ref> <ref>PMID:21949367</ref>
+[https://www.uniprot.org/uniprot/UBCP1_HUMAN UBCP1_HUMAN] Dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation may prevent assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.<ref>PMID:15883030</ref> <ref>PMID:21949367</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2m17" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 23: / Line 24: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Large Structures]]
-[[Category: Lee, W]]
+[[Category: Lee W]]
-[[Category: Yun, J]]
+[[Category: Yun J]]
-[[Category: Hydrolase]]

2m17: Difference between revisions

Latest revision as of 01:10, 21 November 2024

ubiquitin-like domain-containing C-terminal domain phosphatase (UBLCP1)

Structural highlights

Function

Publication Abstract from PubMed

References

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