an AGC kinase of the NDR family of kinases. Localized to the mitotic apparatus and specifically phosphorylated during mitosis. A likely tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint. Negatively regulates G2/M transition by down-regulating CDC2 kinase activity, causing G2 arrest. Involved in the control of p53 expression. Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1. Complexes with CDC2 in early mitosis. LATS1-associated CDC2 has no mitotic cyclin partner and no apparent kinase activity. Binds phosphorylated zyxin, locating this protein to the mitotic spindle and suggesting a role for actin regulatory proteins during mitosis. Binds to and colocalizes with LIMK1 at the actomyosin contractile ring during cytokinesis. Knockout mice are susceptible to soft-tissue sarcomas and sensitive to chemical carcinogenesis. Human soft tissue sarcomas have downregulated, mutated, and/or hypermethylated LATS1. Transgenic expression blocks anchorage independent growth in culture and tumor growth in xenografts. Two alternatively spliced isoforms of the human proteinhave been described. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, Ser/Thr (non-receptor); Kinase, protein; Tumor suppressor; Protein kinase, AGC; EC 184.108.40.206; AGC group; NDR family
Cellular Component: cytosol; microtubule organizing center; spindle pole
Molecular Function: ATP binding; magnesium ion binding; protein binding; protein kinase binding; protein serine/threonine kinase activity
Biological Process: cell division; cytoplasmic sequestering of protein; G1/S transition of mitotic cell cycle; G2/M transition of mitotic cell cycle; hormone-mediated signaling; inner cell mass cell fate commitment; inner cell mass cellular morphogenesis; keratinocyte differentiation; mitosis; negative regulation of cyclin-dependent protein kinase activity; peptidyl-serine phosphorylation; positive regulation of apoptosis; positive regulation of peptidyl-serine phosphorylation; protein amino acid phosphorylation; regulation of actin filament polymerization; regulation of organ growth; regulation of protein complex assembly; sister chromatid segregation
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.