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==SOLUTION STRUCTURE OF THE N-TERMINAL 37 AMINO ACIDS OF THE MOUSE ARF TUMOR SUPPRESSOR PROTEIN==
==SOLUTION STRUCTURE OF THE N-TERMINAL 37 AMINO ACIDS OF THE MOUSE ARF TUMOR SUPPRESSOR PROTEIN==
<StructureSection load='1hn3' size='340' side='right' caption='[[1hn3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1hn3' size='340' side='right'caption='[[1hn3]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1hn3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HN3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1hn3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HN3 FirstGlance]. <br>
</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=1hn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hn3 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn3 PDBsum]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1hn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn3 OCA], [https://pdbe.org/1hn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hn3 RCSB], [https://www.ebi.ac.uk/pdbsum/1hn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hn3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARF_MOUSE ARF_MOUSE] Capable of inducing cell cycle arrest in G1 and G2 phases (PubMed:8521522, PubMed:9393858). Acts as a tumor suppressor (PubMed:8521522, PubMed:9393858, PubMed:15601844, PubMed:17936562). Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus (PubMed:9529248, PubMed:10359817). This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis (PubMed:10359817). Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes (PubMed:15361884). Binds to BCL6 and down-regulates BCL6-induced transcriptional repression (PubMed:15567177). Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression (By similarity). Binds to TOP1/TOPOI and stimulates its activity (By similarity). This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation (By similarity). Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing (By similarity). Plays a role in inhibiting ribosome biogenesis, perhaps by binding to the nucleolar localization sequence of transcription termination factor TTF1, and thereby preventing nucleolar localization of TTF1 (PubMed:20513429). Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination (By similarity). Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1 (By similarity). Binds to HUWE1 and represses its ubiquitin ligase activity (By similarity). May play a role in controlling cell proliferation and apoptosis during mammary gland development (By similarity).[UniProtKB:Q8N726]<ref>PMID:10359817</ref> <ref>PMID:15361884</ref> <ref>PMID:15567177</ref> <ref>PMID:15601844</ref> <ref>PMID:17936562</ref> <ref>PMID:20513429</ref> <ref>PMID:8521522</ref> <ref>PMID:9393858</ref> <ref>PMID:9529248</ref>  May be involved in regulation of autophagy and caspase-independent cell death; the short-lived mitochondrial isoform is stabilized by C1QBP.<ref>PMID:16713577</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
<div class="pdbe-citations 1hn3" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Bothner, B]]
[[Category: Bothner B]]
[[Category: DiGiammarino, E L]]
[[Category: DiGiammarino EL]]
[[Category: Filippov, I]]
[[Category: Filippov I]]
[[Category: Kriwacki, R W]]
[[Category: Kriwacki RW]]
[[Category: Weber, J D]]
[[Category: Weber JD]]
[[Category: Antitumor protein]]
[[Category: Arf]]
[[Category: Mdm2]]
[[Category: P19arf]]
[[Category: P53]]
[[Category: Tumor suppressor]]

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