2e2c
E2-C, AN UBIQUITIN CONJUGATING ENZYME REQUIRED FOR THE DESTRUCTION OF MITOTIC CYCLINSE2-C, AN UBIQUITIN CONJUGATING ENZYME REQUIRED FOR THE DESTRUCTION OF MITOTIC CYCLINS
Template:ABSTRACT PUBMED 10350465
FunctionFunction
[UBE2C_SPISO] Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that is essential for the transition from metaphase to anaphase in mitosis. Involved in both degradation of proteins responsible for maintaining sister chromatid cohesion at the onset of anaphase and of mitotic cyclins A and B at the exit of mitosis. Acts by initiating polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit (By similarity).
About this StructureAbout this Structure
2e2c is a 1 chain structure with sequence from Spisula solidissima. This structure supersedes the now removed PDB entries and 1e2c. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Jiang F, Basavappa R. Crystal structure of the cyclin-specific ubiquitin-conjugating enzyme from clam, E2-C, at 2.0 A resolution. Biochemistry. 1999 May 18;38(20):6471-8. PMID:10350465 doi:10.1021/bi9901329