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PROSITE documentation PDOC50085 [for PROSITE entry PS50085] |
Rap small G proteins have been implicated in various cellular processes such as exocytosis, cAMP signalling, cell adhesion and cell proliferation. Rap proteins acts as molecular switches, with an active GTP-bound form and an inactive GDP-bound form [1]. The inactive GDP bound form is promoted by GTPase-activating proteins (GAPs). GAP proteins specific for Rap contain a conserved region of around 200 amino-acid residues, the RapGAP domain. This domain can accelerate the GTP hydrolysis activity of Rap by five orders of magnitude [2].
Some proteins known to contain a Rap-GAP domain are listed below:
The profile we developed covers the entire RapGAP domain.
Last update:April 2003 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Bos J.L. de Rooij J. Reedquist K.A. |
Title | Rap1 signalling: adhering to new models. | |
Source | Nat. Rev. Mol. Cell Biol. 2:369-377(2001). | |
PubMed ID | 11331911 | |
DOI | 10.1038/35073073 |
2 | Authors | Kurachi H. Wada Y. Tsukamoto N. Maeda M. Kubota H. Hattori M. Iwai K. Minato N. |
Title | Human SPA-1 gene product selectively expressed in lymphoid tissues is a specific GTPase-activating protein for Rap1 and Rap2. Segregate expression profiles from a rap1GAP gene product. | |
Source | J. Biol. Chem. 272:28081-28088(1997). | |
PubMed ID | 9346962 |
3 | Authors | Xiao G.H. Shoarinejad F. Jin F. Golemis E.A. Yeung R.S. |
Title | The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis. | |
Source | J. Biol. Chem. 272:6097-6100(1997). | |
PubMed ID | 9045618 |
4 | Authors | Tsukamoto N. Hattori M. Yang H. Bos J.L. Minato N. |
Title | Rap1 GTPase-activating protein SPA-1 negatively regulates cell adhesion. | |
Source | J. Biol. Chem. 274:18463-18469(1999). | |
PubMed ID | 10373454 |