Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51377KIND domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC51377
The KIND (kinase non-catalytic C-lobe domain) is a putative protein interaction domain, which has been identified as being similar to the C-terminal protein kinase catalytic fold (C lobe) (see <PDOC00100>). Its presence at the N-terminus of signalling proteins and the absence of the active site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurence of the domain only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features [1,2].
Some proteins known to contain a KIND domain are listed below:
- Animal Spir proteins. In the central region they contain a WH2 domain (see <PDOC51082>) cluster, which is known to bind actin. The C-terminal region encodes a modified FYVE zinc-finger domain, which directs the subcellular localization of the proteins.
- Animal non-receptor phosphatase type 13 (PTP type 13), which also contains a FERM domain (see <PDOC00566>), PDZ domains (see <PDOC50106>) and a tyrosine specific protein phosphatase (see <PDOC00323>).
- Vertebrate very KIND (VKIND or KIAA1768), a signalling protein specifically expressed in the nervous system of vertebrates. It has two KIND domains in the N-terminal half, and a guanine nucleotide exchange factor domain for Ras-like GTPases (RasGEF) at the C-terminal end with a structural domain attached at its N-terminal (RasGEFN) (see <PDOC00594>).
The profile we developed covers the entire KIND domain.
Last update:April 2008 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Ciccarelli F.D. Bork P. Kerkhoff E. |
| Title | The KIND module: a putative signalling domain evolved from the C lobe of the protein kinase fold. | |
| Source | Trends Biochem. Sci. 28:349-352(2003). | |
| PubMed ID | 12877999 |
| 2 | Authors | Mees A. Rock R. Ciccarelli F.D. Leberfinger C.B. Borawski J.M. Bork P. Wiese S. Gessler M. Kerkhoff E. |
| Title | Very-KIND is a novel nervous system specific guanine nucleotide exchange factor for Ras GTPases. | |
| Source | Gene Expr. Patterns 6:79-85(2005). | |
| PubMed ID | 16099729 | |
| DOI | 10.1016/j.modgep.2005.04.015 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.