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. The protein encoded by this gene is phosphorylated and activated by ROCK, a downstream effector of Rho, and the encoded protein, in turn, phosphorylates cofilin, inhibiting its actin-depolymerizing activity. It is thought that this pathway contributes to Rho-induced reorganization of the actin cytoskeleton. At least three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
Overall distribution
Tissue specific distribution
Overall distribution
Tissue specific distribution
Gscore (Amp):
0.20
Gscore (Del):
0.00
Recurrently amplified in 1 cancer type(s)
Overall distribution
Tissue specific distribution
Mscore:
0.04
Recurrently mutated in 1 cancer type(s)
Overall
Tissue specific
Total fusion occurrence:
6
Fusions detected in 5 cancer type(s)
Overall
Tissue specific
Functional class:
Kinase (protein kinase)
JensenLab PubMed score:
41.32 (Percentile rank: 59.30%)
PubTator score:
40.05 (Percentile rank: 64.29%)
Target development/druggability level:
TchemThese targets have activities in ChEMBL or DrugCentral that satisfy the activity thresholds detailed below.
Tractability (small molecule):
Discovery PrecedenceTargets with ligands; Targets with crystal structures with ligands
