3.1.3.53	phosphoprotein	-	646357	
3.1.3.53	phosphoprotein	130/133 kDa myosin-binding subunits M130/M133 and 20 kDa regulatory subunit M20 are phosphorylated by protein kinase A to 3 and 1 mol phosphate/mol of subunit, phosphorylation of holoenzyme decreases phospholipid binding, M130/133: C-terminal phosphorylation site involved in regulation of phospholipid binding, no phosphorylation of the catalytic subunit PP-1cdelta, protein kinase C also phosphorylates M130/M133 and M20, but no effect on binding of phospholipids	646357	
3.1.3.53	phosphoprotein	Ca2+-desensitizing hypoxic relaxation requires dephosphorylation of myosin phosphatase regulatory subunit	666160	
3.1.3.53	phosphoprotein	inhibition of enzyme activity by phosphorylation of its myosin-targeting subunit, only in adult gizzard, not in adult aortic smooth muscle, phosphorylation is not required for Ca2+ sensitization of force	646360	
3.1.3.53	phosphoprotein	large subunit MYPT1: phosphorylation site Thr-695, potential site for phosphorylation by protein kinase A is Thr-853	646371	
3.1.3.53	phosphoprotein	myosin light chain phosphatase is regulated by phosphorylation of the catalytic subunit	715547	
3.1.3.53	phosphoprotein	myosin-binding subunit of MLCP is phosphorylated at Thr-641 and Thr-799 by Rho kinase to 2 mol phosphate/mol of MBS	646366	
3.1.3.53	phosphoprotein	MYPT1 is cleaved by caspase-3 at Asp-884 in apoptotic cells, and the cleaved MYPT1 is strongly phosphorylated at Thr-696 and Thr-853, phosphorylation of which is known to inhibit myosin II binding	732482	
3.1.3.53	phosphoprotein	Par-1 (cell polarity protein) activates Myo-II by phosphorylating and inhibiting the myosin phosphatase complex	731688	
3.1.3.53	phosphoprotein	phosphorylation at Thr-695 of the MLCP regulatory subunit MYPT1 inhibits MLCP activity, Thr-695 phosphorylation is independent of stimulation of G-proteins, Rho-kinase or protein kinase C, MYPT1 can also be phosphorylated at Thr-850, which is a non-inhibitory Rho-kinase site, Thr-850 phosphorylation is activated by G-proteins	646356	
3.1.3.53	phosphoprotein	phosphorylation of MYPT1 by Rho-associated coiled-coil kinase ROCK occurs at residues Thr697 and Thr855. cAMP-dependent protein kinase phosphorylates these two sites and the neighboring Ser696 and Ser854. Prior phosphorylation at Thr697 and Thr855 by ROCK precludes phosphorylation at Ser696 and Ser854 by cAMP-dependent protein kinase. Phosphorylation at Thr697 and Thr855 by ROCK exposes two other sites of phosphorylation by cAMP-dependent protein kinase	749533	
3.1.3.53	phosphoprotein	phosphorylation of MYPT1 is a major mechanism of MLCP regulation. Two major ROK phosphorylation sites, Thr697 and Thr855, on MYPT1 elicit MLCP inhibition. Phosphorylation of both sites inhibits MLCP activity. MYPT1-T855 phosphorylation may also interfere with the binding of MYPT1 to myosin	713963	
3.1.3.53	phosphoprotein	phosphorylation of MYPT1 residue T694 is a primary mechanism contributing to inhibition of myosin light chain phosphatase activity and enhancement of myosin regulatory light chain phosphorylation in vivo	751394	
3.1.3.53	phosphoprotein	phosphorylation of the myosin-binding subunit of MLCP at the inhibitory site Thr-641 inhibits MLCP activity, but may not play a significant role in a mechanism for MLCP regulation, Rho kinase phosphorylates Thr-799, but not Thr-641	646366	
3.1.3.53	phosphoprotein	regulatory subunit of enzmye is phopshorylated at T696, contraction of intact mouse arteries induced with noradrenaline is associated with a 2fold increase in phosphorylation, which is reversed in arteries relaxed with urocortin	664611	
3.1.3.53	phosphoprotein	selective thiophosphorylation of MYPT1 at Thr696 with ROCK inhibits the MLCP activity 30%, whereas the Thr853 thio-phosphorylation does not alter the phosphatase activity. Both Thr696 and Thr853 sites undergo autodephosphorylation	731315	
3.1.3.53	phosphoprotein	Thr-654 and Thr-695 are the major phosphorylation sites of the large subunit MYPT isoforms M130 and M133	646371	
3.1.3.53	phosphoprotein	treatment of Triton-skinned rat caudal arterial smooth muscle strips with the membrane-impermeant phosphatase inhibitor microcystin or treatment of intact tissue with the membrane-permeant phosphatase inhibitor calyculin A induces slow, sustained contractions that correlate with phosphorylation of MYPT1 at 7 to more than 10 sites	749533	
3.1.3.53	proteolytic modification	in apoptotic cells, the myosin-binding domain of myosin phosphatase targeting subunit 1 (MYPT1) is cleaved by caspase-3 at Asp-884	732482