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The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. SPAK, also known as STK39 (serine threonine kinase 39), DCHT or PASK, is a 547 amino acid protein that localizes to both the cytoplasm and the nucleus ａ

The DOCK2 gene encodes dedicator of cytokinesis 2 (DOCK 2), a hematopoietic cell-specific CDM family protein that is indispensable for lymphocyte chemotaxis. DOCK 2 participates in the cytoskeletal rearrangements that are required for lymphocyte migration in response of chemokines. This peripheral membrane protein activates Rac 1 and Rac 2 small GTPases, while presumably acting as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. DOCK 2 may also participate in

Rho GTPase activating protein 5 negatively regulates RHO GTPases, a family which may mediate cytoskeleton changes by stimulating the hydrolysis of bound GTP. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Growth regulator. Inhibits the proliferation of a number of tumor cell lines. Stimulates proliferation of AIDS-KS cells. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. Uses both type I OSM receptor (heterodimers composed of LIPR and IL6ST) and type II OSM receptor.