2yle
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yle]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YLE FirstGlance]. <br> | <table><tr><td colspan='2'>[[2yle]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YLE FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ylf|2ylf]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ylf|2ylf]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yle OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yle RCSB], [http://www.ebi.ac.uk/pdbsum/2yle PDBsum]</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=2yle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yle OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yle RCSB], [http://www.ebi.ac.uk/pdbsum/2yle PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FMN2_HUMAN FMN2_HUMAN]] Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation.<ref>PMID:22330775</ref> <ref>PMID:23375502</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Kerkhoff, E | + | [[Category: Kerkhoff, E]] |
| - | [[Category: Pechlivanis, M | + | [[Category: Pechlivanis, M]] |
| - | [[Category: Vonrhein, C | + | [[Category: Vonrhein, C]] |
| - | [[Category: Zeth, K | + | [[Category: Zeth, K]] |
[[Category: Actin polymerization]] | [[Category: Actin polymerization]] | ||
[[Category: Actin-binding protein]] | [[Category: Actin-binding protein]] | ||
Revision as of 08:06, 25 December 2014
Crystal structure of the human Spir-1 KIND FSI domain in complex with the FSI peptide
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