The antiserum was produced against synthesized peptide derived from human PP1-alpha around the phosphorylation site of Thr320. AA range:281-330

Phospho-PP1α (T320) Polyclonal Antibody detects endogenous levels of PP1α protein only when phosphorylated at T320.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 When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports.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):PItPP

PPP1CA

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

PPP1CA ;
PPP1A ;
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit ;
PP-1A

The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1) . PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes , such as cell division , glycogen metabolism , muscle contractility , protein synthesis , and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Mouse studies also suggest that PP1 functions as a suppressor of learning and memory. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq , Jul 2008] ,

Catalytic activity:A phosphoprotein + H (2) O = a protein + phosphate. ,Caution:The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. ,cofactor:Binds 1 iron ion per subunit. ,cofactor:Binds 1 manganese ion per subunit. ,enzyme regulation:The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal , a drug that protects cells from endoplasmic reticulum stress. ,Function:Protein phosphatase 1 (PP1) is essential for cell division , and participates in the regulation of glycogen metabolism , muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca (2+) /calmodulin dependent protein kinase II. ,online information:The things we forget -Issue 32 of March 2003 ,similarity:Belongs to the PPP phosphatase family. ,similarity:Belongs to the PPP phosphatase family. PP-1 subfamily. ,subunit:PP1 comprises a catalytic subunit , PPP1CA , PPP1CB or PPP1CC , which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3 , and then complexed to one or several targeting or regulatory subunits. PPP1R12A , PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A , PPP1R3B , PPP1R3C and PPP1R3D mediate binding to glycogen. Interacts with PPP1R9A and PPP1R9B. Part of a complex containing PPP1R15B , PP1 and NCK1/2 (By similarity) . Interacts with PPP1R7. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Interacts with HHV-1 ICP34.5. ,

Cytoplasm . Nucleus . Nucleus , nucleoplasm . Nucleus , nucleolus . Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. Shuttles toward the cytosol during infection with VEEV (PubMed:29769351) . .

>>mRNA surveillance pathway ;
>>cGMP-PKG signaling pathway ;
>>cAMP signaling pathway ;
>>Oocyte meiosis ;
>>Cellular senescence ;
>>Adrenergic signaling in cardiomyocytes ;
>>Vascular smooth muscle contraction ;
>>Hippo signaling pathway ;
>>Focal adhesion ;
>>Platelet activation ;
>>Long-term potentiation ;
>>Dopaminergic synapse ;
>>Inflammatory mediator regulation of TRP channels ;
>>Regulation of actin cytoskeleton ;
>>Insulin signaling pathway ;
>>Oxytocin signaling pathway ;
>>Insulin resistance ;
>>Amphetamine addiction ;
>>Alcoholism ;
>>Herpes simplex virus 1 infection ;
>>Proteoglycans in cancer ;
>>Diabetic cardiomyopathy