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PROSITE documentation PDOC51284DOC domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51284
The anaphase-promoting complex (APC) is a multi-subunit E3 protein ubiquitin ligase that is reponsible for the metaphase to anaphase transition and the exit from mitosis. The subunit APC10 is a one-domain protein homologous to a sequence element, termed the DOC domain, found in several hypothetical proteins that may also mediate ubiquitination reactions, because they contain combinations of either RING finger (see <PDOC00449>), cullin (see <PDOC00967>) or HECT (see <PDOC50237>) domains [1,2,3].
The DOC domain consists of a β-sandwich, in which a five-stranded antiparallel β-sheet is packed on top of a three stranded antiparallel β-sheet, exhibiting a 'jellyroll' fold (see <PDB:1JHJ; A>) [2,3].
Some proteins known to contain a DOC domain are listed below:
- Eucaryotic Doc1/Apc10.
- Mammalian protein associated with the transcription factor Myc (PAM).
- Mouse runty-jerky-sterile (RJS) protein.
- Human HERC2, the ortholog of RJS.
The profile we developed covers the entire DOC domain.
Last update:January 2007 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Grossberger R. Gieffers C. Zachariae W. Podtelejnikov A.V. Schleiffer A. Nasmyth K. Mann M. Peters J.-M. |
| Title | Characterization of the DOC1/APC10 subunit of the yeast and the human anaphase-promoting complex. | |
| Source | J. Biol. Chem. 274:14500-14507(1999). | |
| PubMed ID | 10318877 |
| 2 | Authors | Wendt K.S. Vodermaier H.C. Jacob U. Gieffers C. Gmachl M. Peters J.-M. Huber R. Sondermann P. |
| Title | Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex. | |
| Source | Nat. Struct. Biol. 8:784-788(2001). | |
| PubMed ID | 11524682 | |
| DOI | 10.1038/nsb0901-784 |
| 3 | Authors | Au S.W.N. Leng X. Harper J.W. Barford D. |
| Title | Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit. | |
| Source | J. Mol. Biol. 316:955-968(2002). | |
| PubMed ID | 11884135 | |
| DOI | 10.1006/jmbi.2002.5399 |
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