Structural highlights
Function
[DJC24_MOUSE] The iron-bound form is redox-active and can function as electron carrier (By similarity). Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Kroczynska B, Blond SY. Cloning and characterization of a new soluble murine J-domain protein that stimulates BiP, Hsc70 and DnaK ATPase activity with different efficiencies. Gene. 2001 Aug 8;273(2):267-74. PMID:11595173
- ↑ Webb TR, Cross SH, McKie L, Edgar R, Vizor L, Harrison J, Peters J, Jackson IJ. Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development. J Cell Sci. 2008 Oct 1;121(Pt 19):3140-5. doi: 10.1242/jcs.035550. Epub 2008 Sep , 2. PMID:18765564 doi:http://dx.doi.org/10.1242/jcs.035550
