1914
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=1914 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1914 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1914 RCSB], [http://www.ebi.ac.uk/pdbsum/1914 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=1914 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1914 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1914 RCSB], [http://www.ebi.ac.uk/pdbsum/1914 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SRP14_MOUSE SRP14_MOUSE]] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 23:46, 24 December 2014
SIGNAL RECOGNITION PARTICLE ALU RNA BINDING HETERODIMER, SRP9/14
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