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PROSITE documentation PDOC51284 [for PROSITE entry PS51284]

DOC domain profile





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

DOC, PS51284; DOC domain profile  (MATRIX)


References

1AuthorsGrossberger R. Gieffers C. Zachariae W. Podtelejnikov A.V. Schleiffer A. Nasmyth K. Mann M. Peters J.-M.
TitleCharacterization of the DOC1/APC10 subunit of the yeast and the human anaphase-promoting complex.
SourceJ. Biol. Chem. 274:14500-14507(1999).
PubMed ID10318877

2AuthorsWendt K.S. Vodermaier H.C. Jacob U. Gieffers C. Gmachl M. Peters J.-M. Huber R. Sondermann P.
TitleCrystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex.
SourceNat. Struct. Biol. 8:784-788(2001).
PubMed ID11524682
DOI10.1038/nsb0901-784

3AuthorsAu S.W.N. Leng X. Harper J.W. Barford D.
TitleImplications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit.
SourceJ. Mol. Biol. 316:955-968(2002).
PubMed ID11884135
DOI10.1006/jmbi.2002.5399



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