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Your query returned 1 entry. Printable version
EC | 2.7.11.39 | ||||
Accepted name: | ROCK-subfamily protein kinase | ||||
Reaction: | (1) ATP + [protein]-L-serine = ADP + [protein]-O-phospho-L-serine (2) ATP + [protein]-L-threonine = ADP + [protein]-O-phospho-L-threonine The enzyme has wide range known substrates, mostly involved in cytoskeletal regulation, with a preference for positive charges at P1 to P5. |
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Other name(s): | ROCK; Rho Kinase; ROCK1; ROCK2; rok; let-402; ROCK-I (gene name); ROCK-II (gene name) | ||||
Systematic name: | ATP:cytoskeleton-protein phosphotransferase | ||||
Comments: | Requires Mg2+. An animal specific kinase that is duplicated in vertebrates (ROCK1, ROCK2), and with homologs in Drosophila (rok) and Caenorhabditis elegans (let-502). They are ~1300 amino-acid proteins, with an N-terminal kinase domain, with the AGC-specific kinase domain tail, followed by a central coiled-coil region, HR1 domain, Rho-binding domain (RBD), and PH domain. The PH domain is split by an inserted CRD (cysteine-rich Zn finger motif). ROCK is activated by the small GTPase Rho and modulates the cytoskeleton by phosphorylation of a wide array of other cytoskeletal proteins. Binding of Rho-GTP to the RBD relieves an intramolecular inhibition and activates the kinase activity. These kinases modulate the cytoskeleton in response to Rho GTPase signalling. Substrates include LIM-kinase (LIMK) which phosphorylates and inhibits cofilin, blocking its actin-depolymerizing function [1], and myosin regulatory light chain (MRLC2/MYL12B) that regulates Myosin II. In Drosophila it is involved in the planar cell polarity pathway, where it is genetically downstream of frizzled and dishevelled gene families, and phosphorylates the non-muscle myosin light chain, regulating Myosin II [2]. It is activated by Rho1, the single homolog of human RhoA/B/C, which also activate ROCK. | ||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||
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