Synthesized peptide derived from human LIMK1 (Phospho-Ser310)

This antibody detects endogenous levels of LIMK1 (Phospho-Ser310) at Human, Mouse,Rat.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):LGsPA

LIMK1 LIMK

LIMK1 (Phospho-Ser310)

LIM domain kinase 1 ;
LIMK-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 cog

Catalytic activity:ATP + a protein = ADP + a phosphoprotein.,Disease:Haploinsufficiency of LIMK1 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in Williams-Beuren syndrome (WBS), a rare developmental disorder. It is a contiguous gene deletion syndrome involving genes from chromosome band 7q11.23.,Function:Protein kinase which regulates actin filament dynamics. Phosphorylates and inactivates the actin binding/depolymerizing factor cofilin, thereby stabilizing the actin cytoskeleton. Isoform 3 has a dominant negative effect on actin cytoskeletal changes. May be involved in brain development.,PTM:Autophosphorylated.,PTM:Phosphorylated on serine and/or threonine residues by ROCK1. May be dephosphorylated and inactivated by SSH1.,similarity:Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.,similarity:Contains 1 PDZ (DHR) domain.,similarity:Contains 1 protein kinase domain.,similarity:Contains 2 LIM zinc-binding domains.,subunit:Self-associates. The LIM domain interacts with the cytoplasmic domain of NRG1. Binds ROCK1. Interacts with SSH1. Interacts with NISCH.,tissue specificity:Highest expression in both adult and fetal nervous system. Detected ubiquitously throughout the different regions of adult brain, with highest levels in the cerebral cortex. Expressed to a lesser extent in heart and skeletal muscle.,

Cytoplasm . Nucleus . Cytoplasm, cytoskeleton . Cell projection, lamellipodium . Predominantly found in the cytoplasm. Localizes in the lamellipodium in a CDC42BPA, CDC42BPB and FAM89B/LRAP25-dependent manner. .

>>Axon guidance ;
>>Fc gamma R-mediated phagocytosis ;
>>Regulation of actin cytoskeleton ;
>>Yersinia infection ;
>>Human immunodeficiency virus 1 infection