Peptidyl-Prolyl Cis-Trans Isomerase FKBP7 (FKBP7) is a member of the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. FKBP7 contains two EF-hand domains and one PPIase FKBP-type domain. FKBP7 exhibits PPIase activity and function as molecular chaperones. In addition, FKBP7 accelerates the folding of proteins during protein synthesis. It has been shown that Hsp90 complex to the nucleus bind its PPIase domain to cytoplasmic dynein, the motor protein responsible for retrograde movement along microtubules.
PPIase is a member of the immunophilin protein family. It also belongs to the cyclophilin-type PPIase family, PPIL3 subfamily. PPIase contains 1 PPIase cyclophilin-type domain. Members of the immunophilin protein family play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. It has a very high substrate specificity for the four-residue peptide Ala-Ala-Pro-Phe only when the proline peptide bond is in the trans state. It interacts with several intracellular signal transduction proteins including type I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels, and coordinates multi-protein complex formation of the tetrameric skeletal muscle ryanodine receptor. In mouse, deletion of this homologous gene causes congenital heart disorder known as noncompaction of left ventricular myocardium.
Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 (PPIase) belongs to the cyclophilin-type PPIase family. PPIases can accelerate the folding of proteins and catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIase is a ubiquitous protein and has highly expression in heart ;skeletal and muscle. PPIase contains a PPIase cyclophilin-type domain and four Cyclosporin A binding regions. PPIase might play an important role in proliferation of cancer cells through modulation of phosphorylation of stathmin. It is suggested that PPIase can act as as a novel molecular target for colon-cancer therapy.
Peptidyl-Prolyl Cis-Trans Isomerase H (PPIH) belongs to the Cyclophilin-type PPIase family that accelerate the folding of proteins. PPIases can catalyze the cis-trans isomerization of Proline Imidic peptide bonds in oligopeptides. PPIH participates in pre-mRNA splicing. It is a specific component of the complex that includes pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. In addition, PPIH has PPIase activity and may play a role as a chaperone mediating the interactions between different proteins inside the spliceosome.
Protein Phosphatase 1A (PPM1A) is a member of the PP2C family of Ser/Thr protein phosphatases which are known to be negative regulators of cell stress response pathways. PPM1A has a broad specificity. PPM1A negatively regulates the activities of MAP kinases and MAP kinase kinases. Also, it negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. In addition, PPM1A can dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control.
Protein phosphatase 1G; also known as Protein phosphatase 1C; Protein phosphatase 2C isoform gamma; Protein phosphatase magnesium-dependent 1 gamma; PP2C-gamma; PPM1G and PPM1C; is a cytoplasm protein which belongs to thePP2C family. PPM1G / PP2C-gamma is widely expressed. It is most abundant in testis; skeletal muscle; and heart. Alternatively spliced transcript variants encoding the same protein have been described. PP2C family members are known to be negative regulators of cell stress response pathways. PPM1G / PP2C-gamma is found to be responsible for the dephosphorylation of Pre-mRNA splicing factors; which is important for the formation of functional spliceosome. PPM1G / PP2C-gamma also plays a role in regulating cell cycle progression.
Protein Phosphatase 1G (PP1MG) is a cytoplasmic protein that belongs to the PP2C family. PPM1G is widely expressed; it is abundant in testis; skeletal muscle; and heart. PPM1G is a negative regulator of cell stress response pathways. PPM1G is responsible for the dephosphorylation of Pre-mRNA splicing factors; an important factor for the formation of functional spliceosome. PPM1G also plays a role in regulating cell cycle progression.
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