| Dataset | PhosphoSitePlus Substrates of Kinases |
| Category | physical interactions |
| Type | kinase |
| Description | LIM domain kinase 1|There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. LIMK1 is a serine/threonine kinase that regulates actin polymerization via phosphorylation and inactivation of the actin binding factor cofilin. This protein is ubiquitously expressed during development and plays a role in many cellular processes associated with cytoskeletal structure. This protein also stimulates axon growth and may play a role in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome. Alternative splicing results in multiple transcript variants encoding distinct isoforms.[provided by RefSeq, Feb 2011] (NCBI Entrez Gene Database, 3984) |
| External Link | http://www.ncbi.nlm.nih.gov/gene/3984 |
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2 substrates of the kinase LIMK1 from the curated PhosphoSitePlus Substrates of Kinases dataset.
