3pow
From Proteopedia
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<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=3pow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pow OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pow RCSB], [http://www.ebi.ac.uk/pdbsum/3pow 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=3pow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pow OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pow RCSB], [http://www.ebi.ac.uk/pdbsum/3pow PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CALR_HUMAN CALR_HUMAN]] Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).<ref>PMID:7876246</ref> <ref>PMID:11149926</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 08:46, 24 December 2014
Crystal structure of the globular domain of human calreticulin
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