PROSITE documentation PDOC00835
CAP protein signatures


In budding and fission yeasts the CAP protein is a bifunctional protein whose N-terminal domain binds to adenylyl cyclase, thereby enabling that enzyme to be activated by upstream regulatory signals, such as Ras. The function of the C-terminal domain is less clear, but it is required for normal cellular morphology and growth control [1]. CAP is conserved in higher eukaryotic organisms where its function is not yet clear [2].

Structurally, CAP is a protein of 474 to 551 residues which consist of two domains separated by a proline-rich hinge. We have developed two signature patterns, one corresponds to a conserved region in the N-terminal extremity and the other to a C-terminal region.

Last update:

November 1997 / Pattern and text revised.


Technical section

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

CAP_1, PS01088; CAP protein signature 1  (PATTERN)

CAP_2, PS01089; CAP protein signature 2  (PATTERN)


1AuthorsKawamukai M. Gerst J. Field J. Riggs M. Rodgers L. Wigler M. Young D.
TitleGenetic and biochemical analysis of the adenylyl cyclase-associated protein, cap, in Schizosaccharomyces pombe.
SourceMol. Biol. Cell 3:167-180(1992).
PubMed ID1550959

2AuthorsYu G. Swiston J. Young D.
TitleComparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins.
SourceJ. Cell Sci. 107:1671-1678(1994).
PubMed ID7962207

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