Database for Annotation, Visualization and Integrated Discovery 2.1
National Institute of Allergy and Infectious Disease
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protein phosphatase 1 catalytic subunit alpha(PPP1CA) protein phosphatase 1 catalytic subunit alpha(PPP1CA) Related Genes Homo sapiens
CHROMOSOME 11,
CYTOBAND 11q13,
ENSEMBL_GENE_ID ENSG00000172531,
GENERIF_SUMMARY PP1C has a role in binding to PKR protein kinase for its phosphorylation and disruption of dimerization, PP1C and Inh2 bind to KPI2 to form a regulatory complex that is localized to membranes, PPICalpha essential in proliferation in HeLa cells, PP1alpha expression interferes with oncogenic transformation., These findings provide a putative mechanism by which transcriptional activity of hnRNP K can be discretely controlled through the regulation of PP1 activity., These data suggest that amplification and overexpression of the PP1alpha gene, PPP1CA, may be involved in oral squamous cell carcinoma cell tumorigenesis and/or progression., Bcl-2 by competing with IP3R1 for the binding of PP1 can reduce the inositol trisphosphate-mediated calcium signal and protect cells from mitochondrial dysfunction and cell death., accumulation of C(16)-ceramide in mitochondria formed from the protein kinase C-dependent salvage pathway results at least in part from the action of longevity-assurance homologue 5, and the generated ceramide modulates the p38 cascade via PP1, data indicate that PP1alpha is a downstream target of the NGF/Egr-1/Cdk5 pathway during NGF-induced differentiation of PC12 cells and suggest that PP1 phosphorylation promotes neuronal differentiation, Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex., Results suggest that the protein-tyrosine phosphatase domain of tensin exhibits isoform-specific association with PP1alpha in a restricted spatial region of adhesions that are formed during cell migration., Sds22 and Inhibitor-3 form a heterotrimeric complex with PP1, both in cell lysates and after purification. A pool of PP1 is complexly controlled by both Sds22 and Inhibitor-3., PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling., Conserved together throughout eukaryotic evolution, I-2, PP1 and Aurora B function interdependently during mitosis., The PP1, Protein phosphatase 1 binding occurs through a conserved RVXF motif found in the KH domain of AKAP149., novel interaction between the catalytic subunit of protein phosphatase 1alpha and MEF2A. Interaction occurs within the nucleus, and binding of PP1alpha to MEF2 potently represses MEF2-dependent transcription, AR may function as a PP1 regulatory subunit and mediate PP1a recruitment to chromatin, where it can modulate transcription and splicing., Results suggest that PP1alpha bound to tensin1 has effects in reducing migration and invasion that are not mediated through DLC-1, and show the importance of PP1alpha binding to tensin1 for the regulation of cell polarization, migration, and invasion., conclusion, PP-1 ( PP-1alpha or PP-1beta ) acts as a major phosphatase to dephosphorylate AKT1 at Thr-450 and thus modulate its functions in regulating gene expression, cell survival and differentiation., mammalian Wdr82 functions in a variety of cellular processes; PTW/PP1 phosphatase complex (PNUTS, Tox4, Wdr82, PP1) has a role in the regulation of chromatin structure during the transition from mitosis into interphase, CSK21 and PP1A, whose functions are intimately associated with cell cycle regulation, might play key role in gliomagenesis., The deregulation of cellular NIPP1/PP1 holoenzyme affects RNAPII phosphorylation and pointing to NIPP1 as a potential regulatory factor in RNAPII-mediated transcription., Could use the urinary hTERT, SENP1, PPP1CA, and MCM5 mRNA to detect bladder cancer recurrence., PP1A and ASPP2 play a critical role in promoting TAZ function by antagonizing the LATS kinase through TAZ dephosphorylation., Results demonstrate that PP1-mediated inhibition of the key anti-apoptotic protein, Akt, plays an important role in SPH-mediated apoptosis in Jurkat cells., Results identify a molecular pathway by which leptin confers inhibitory action on insulin secretion, and impaired PP-1 inhibition by leptin may be involved in dysfunction of the adipoinsular axis during the development of hyperinsulinemia and NIDDM., Changes in cell polarity proteins Par-3 and PP-1 are associated with altered expression and assembly of tight junction proteins claudin-2, -3, -5 and -7 and ZO-1, causing paracellular leakage in active coeliac disease., These findings define a novel molecular mechanism that YAP2 is positively regulated by PP1-mediated dephosphorylation in the cell survival., We have identified a novel mechanism for direct activation of P-Rex1 through PP1alpha-dependent dephosphorylation., Studies suggest that any change in substrate specificity of the spinophilin , Studies indicate that the Ser/Thr phosphatases PP1 and PP2A are responsible for the dephosphorylation and activation of Rb proteins., a novel, acute mechanism of ERM regulation dependent on PP1alpha and plasma membrane ceramide., Results identify specific protein phosphatase 1alpha-interacting proteins in human brain., Studies indicate that the diversity of the PP1 interactome and the properties of the PP1 binding code account for the exquisite specificity of PP1 in vivo., Data show that knockdown of the catalytic subunit of PP1 (PP1Calpha), but not PP2A (PP2ACalpha), increased pS137-PFN1 levels., analysis of selective regulation of NR2B by protein phosphatase-1 for the control of the NMDA receptor in neuroprotection, Cell surface expression of the major amyloid-beta peptide (Abeta)-degrading enzyme, neprilysin, depends on phosphorylation by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK) and dephosphorylation by protein phosphatase 1a., PP1/NIPP1 is a novel molecular compass that controls directed cell migration., The molecular basis by which NIPP1 directs PP1 substrate specificity in the nucleus., PP-1alpha and PP-1gamma not only antagonize each other in lung cancer cells, but also display differential functions in tumorigenicity., PPP1C isoforms have distinct contribution to the outside-in alphaIIbbeta3 signalling-dependent functions in HEK293 alphaIIbbeta3 cells., The protein phosphatase 1 directly interacts with Mdmx and specifically dephosphorylates Mdmx at Ser367., Findings indicate that phosphatases PP1alpha and PP1gamma are key regulators of RIG-I and MDA5 antiviral signaling., Data indicate that the protein phosphatase 1 (PP1) binding domain in nuclear membrane protein lamina associated polypeptide 1B (LAP1B) was here identified as the REVRF motif at amino acids 55-59., Data show that tumor necrosis factor (TNF) tolerance in monocytic cells differentially inhibits NF-kappaB/transcription factor AP-1 and protein phosphatase 1 (PP1)-associated signaling., PP1alpha and class I histone deacetylase (HDAC1/2/3) signaling pathways are essential for the stress-induced BRD4 release from chromatin., 14-3-3zeta regulates nuclear trafficking of PP1alpha in mammalian cells, PP1alpha is an important proximal effector of Manumycin-A mediated lymphoma cell apoptosis., Data suggest that activation of TAZ (tafazzin) inhibits adipogenesis in mesenchymal stem cells; interaction of TAZ and protein phosphatases (PP1A, PP2A) up-regulates dephosphorylation and transport of TAZ to cell nucleus., Protein phosphatase 1 (PP1) activity is critical for radiosensitization in non-small cell lung cancer cells and PP1 activators can serve as promising radiosensitizers to improve therapeutic efficacy., ATG16L1 as a bona fide physiological CSNK2 and PPP1 substrate, which reveals a novel molecular link from CSNK2 to activation of the autophagy-specific ATG12-ATG5-ATG16L1 complex and autophagy induction, PARD3 promotes interaction between PP1A and LATS1 to induce LATS1 dephosphorylation and inactivation,leading to dephosphorylation and activation of TAZ, activation of the Nherf1-PP1alpha-TAZ pathway in osteoblasts is targeted by histone deacetylase inhibitors, Both PP-1 and PP-2A are directly involved in regulating eye development, and are aberrantly expressed in cataract and glaucoma patients. (Review),
SP_COMMENT 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.,
protein phosphatase 1 catalytic subunit beta(PPP1CB) protein phosphatase 1 catalytic subunit beta(PPP1CB) Related Genes Homo sapiens
CHROMOSOME 2,
CYTOBAND 2p23, 2p23.2,
ENSEMBL_GENE_ID ENSG00000213639,
GENERIF_SUMMARY In this study, we show that protein phosphatase-1 (PP1) inhibitor-3 (Inh3) is localized to the nucleoli and centrosomes in interphase HEK 293 cells., R16A at the membrane may mediate the PB signal to initiate CAR nuclear translocation, through a mechanism including its dimerization and inhibition of PP1beta activity., PP-1 ( PP-1alpha or PP-1beta ) acts as a major phosphatase to dephosphorylate AKT1 at Thr-450 and thus modulate its functions in regulating gene expression, cell survival and differentiation., mammalian Wdr82 functions in a variety of cellular processes; PTW/PP1 phosphatase complex (PNUTS, Tox4, Wdr82, PP1) has a role in the regulation of chromatin structure during the transition from mitosis into interphase, serine/threonine protein phosphatase PP1beta is a physiological Nucleophosmin (NPM) phosphatase under both the genotoxic stress and growth conditions., Data suggest that double-thiophosphorylation of TIMAP has minor effect on its binding ability to PP1c, but considerably attenuates its inhibitory effect on the activity of PP1c., PPP1CB is over expressed in malignant melanoma., Protein phosphatase 1beta (PP1beta) is identified as a phosphatase for the cluster of phosphorylated threonines ((353)TTETQRT(359)) within the sst(2A) somatostatin receptor carboxyl terminus that mediates beta-arrestin binding using siRNA knock-down screening., Studies suggest that any change in substrate specificity of the spinophilin , Studies indicate that the Ser/Thr phosphatases PP1 and PP2A are responsible for the dephosphorylation and activation of Rb proteins., Studies indicate that the diversity of the PP1 interactome and the properties of the PP1 binding code account for the exquisite specificity of PP1 in vivo., These findings provide evidence for the involvement of a particular PP1 complex, PPP1R12A/PP1cdelta, in insulin signaling., Interaction between protein phosphatase 1 beta and myosin phosphatase (MYPT)1 results in exclusion of Nkx2.5 from the cell nucleus., PPP1C isoforms have distinct contribution to the outside-in alphaIIbbeta3 signalling-dependent functions in HEK293 alphaIIbbeta3 cells., results indicate that SCN-iPS cells provide a useful disease model for SCN, and the activation of the Wnt3a/beta-catenin pathway may offer a novel therapy for SCN with ELANE mutation, In the title., Findings show that PP1cbeta plays a role in endothelial cell migration through a mechanism involving the interplay of actin cytoskeleton proteins and focal adhesion molecules signaling., These results suggest a unique functional role for the PP1beta isoform in affecting cardiac contractile function,
SP_COMMENT catalytic activity:A phosphoprotein + H(2)O = a protein + phosphate., cofactor:Binds 1 iron ion per subunit., cofactor:Binds 1 manganese ion per subunit., domain:The C-terminus is required for CDK2-activation, but not CDK2-binding., 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 (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity., function:Regulates the G1/S phase transition of the cell cycle by binding and activating CDC2, CDK2 and CDKN1B/KIP1. Can activate CDK2 without promoting CDK2 phosphorylation. Mediates cell survival during the DNA damage process through activation of CDK2., online information:The things we forget -Issue 32 of March 2003, similarity:Belongs to the PPP phosphatase family. PP-1 subfamily., similarity:Belongs to the Speedy/Ringo family., subunit:Interacts with CDC2, CDK2 and CDKN1B/KIP1. Found in a complex with both CDK2 and CDKN1B/KIP1., 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. Part of a complex containing PPP1R15B, PP1 and NCK1/2 (By similarity). Interacts with PPP1R7 and PPP1R12C. PPP1R15A and PPP1R15B mediate binding to EIF2S1., tissue specificity:Highly expressed in testis. Expressed at a low level in wide range of tissues including bone marrow, brain, heart, kidney, colon, liver, placenta, spleen, skeletal muscle, salivary gland, thyroid gland, thymus, trachea and uterus. Expressed at a slightly higher level in adrenal gland, cerebellum, small intestine, lung, prostate and trachea. Expression is cell cycle-dependent, being restricted to cells in G1/S phase.,
protein phosphatase 1 catalytic subunit gamma(PPP1CC) protein phosphatase 1 catalytic subunit gamma(PPP1CC) Related Genes Homo sapiens
CHROMOSOME 12,
CYTOBAND 12q24.1-q24.2,
ENSEMBL_GENE_ID ENSG00000186298,
GENERIF_SUMMARY gamma isoform of the human protein phosphatase-1 catalytic subunit (PP1c gamma) as a high affinity in vitro target of phosphatidic acid, Nek2.PP1C complex is regulated by Inh2 via inhibition of phosphatase activity to initiate centrosome separation, Tat might function as a nuclear regulator of PP1 and interaction of Tat with PP1 is critical for activation of HIV-1 transcription by Tat, analysis of novel phosphatidic acid (PA) binding region on PP1c gamma that contains a unique loop-strand structural fold responsible for the interaction with PA, crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c, We demonstrate that interaction with NIPP1 mediates decreased PP1gamma activity in hypoxia, an event which may constitute an inherent part of the cellular oxygen-sensing machinery and may play a role in physiologic adaptation to hypoxia., Data show that URI and PP1gamma are components of an S6K1-regulated mitochondrial pathway dedicated to oppose sustained S6K1 survival signaling and to ensure that the threshold for apoptosis is set based on nutrient and growth factor availability., Results describe a specific intracellular pathway involving the activation of PP1cgamma to mediate the effects of confluence-induced beta-catenin dephosphorylation., PP1cgamma1 overexpression promotes VSMC survival by interfering with JNK1 and p53 phosphorylation cascades involved in apoptosis, Protein phosphatase 1 binding occurs through a conserved RVXF motif found in the KH domain of AKAP149., mammalian Wdr82 functions in a variety of cellular processes; PTW/PP1 phosphatase complex (PNUTS, Tox4, Wdr82, PP1) has a role in the regulation of chromatin structure during the transition from mitosis into interphase, The ataxia telangiectasia, mutated and Rad3-related-Chk1 axis regulates H3-pThr 11 dephosphorylation on DNA damage, at least in part by the activation of PP1gamma through Chk1-dependent inhibition of cyclin dependent kinases., The counteracting Nek2A and PP1gamma activities on the centrosome linker are controlled by Plk1., NUAK1 and PPP1CC are identified as positional candidate loci for skeletal muscle strength phenotypes., Depletion of PP1gamma enhances the localization of the SMN complex and snRNPs to Cajal bodies., When the Px(T)PxR motif is deleted or mutated via insertion of a phosphorylation site mimic (T311D), PP-1c fails to bind to all three ASPP proteins, ASPP1, ASPP2 and iASPP., PP-1alpha and PP-1gamma not only antagonize each other in lung cancer cells, but also display differential functions in tumorigenicity., PPP1C isoforms have distinct contribution to the outside-in alphaIIbbeta3 signalling-dependent functions in HEK293 alphaIIbbeta3 cells., Findings indicate that phosphatases PP1alpha and PP1gamma are key regulators of RIG-I and MDA5 antiviral signaling., Protein phosphatase 1gamma promotes the alternative splicing of CaMKIIdelta through its interaction with alternative splice factor., the lipin-1 N-terminal domain is important for its catalytic activity, nuclear localization, and binding to PP-1cgamma, Although no obvious defects in the progression of mitosis were observed, the timing of dephosphorylation of the mutant Ki67 in anaphase was delayed, indicating that Ki67 itself is one of the substrates of PP1gamma-Ki67., PP1gamma may be a novel target of the HPV-16 oncoproteins and indicate that it might be a potential novel biomarker for HPV-16 induced malignancy.,
SP_COMMENT catalytic activity:A phosphoprotein + H(2)O = a protein + phosphate., 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., miscellaneous:Microcystin toxin is bound to Cys-273 through a thioether bond., 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., subcellular location:Colocalizes with SPZ1 in the nucleus., 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 cyanobacterial toxin microcystin; disulfide-linked. Interacts with PPP1R3B and PPP1R7. Isoform gamma-2 interacts with SPZ1 (By similarity). Interacts with CDCA2. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2.,
protein phosphatase 1 regulatory subunit 12A(PPP1R12A) protein phosphatase 1 regulatory subunit 12A(PPP1R12A) Related Genes Homo sapiens
CHROMOSOME 12,
CYTOBAND 12q15-q21,
ENSEMBL_GENE_ID ENSG00000058272,
GENERIF_SUMMARY Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton., Proper expression of MYPT1 or variant 2 is critical for RLC phosphorylation and actin assembly, thus maintaining normal cellular functions by simultaneously controlling cytoskeletal architecture and actomyosin activation., Stable transfection of HEK 293 cells with GFP-MYPT1 was obtained. MYPT1 and its N-terminal mutants bound to retinoblastoma protein (Rb), raising the possibility that Rb is implicated in the effects caused by overexpression of MYPT1., the leucine-zipper motif of PKG binds to that of MYPT1 to form a heterodimer; when the leucine-zipper motif of MYPT1 is absent, the PKG leucine-zipper motif binds to the coiled coil region and upstream segments of MYPT1 via formation of a heterotetramer, These data suggests different phosphorylation and regulation of MYPT1 activity by NUAK2., both eEF1A and MYPT1 have roles in EGCG signaling for cancer prevention through 67LR, These results identify a previously unrecognized role for MYPT1 in regulating mitosis by antagonizing PLK1., MYPT1 may regulate the phosphorylation level of pRb, thereby it may be involved in the control of cell cycle progression and in the mediation of chemoresistance of leukemic cells., Apolipoprotein(a), through its strong lysine-binding site in KIV(10'), mediates increased endothelial cell contraction and permeability via a Rho/Rho kinase/MYPT1-dependent pathway., Results show that expression of MYPT1 enhances HIF-CAD activity in a manner consistent with competition for FIH and that this property extends to other ARD proteins., MYPT1 phosphorylation at Thr-696 and Thr-853 causes an autoinhibition of MLCP that accounts for Ca(2+) sensitization of smooth muscle force, Solution structure of the inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1, The ability of myosin phosphatase to modulate myosin light chain might be regulated by the degradation of its targeting subunit MYPT1 through the SIAH2-ubiquitin-proteasomal pathway., cAMP/PKA regulates the endothelial barrier via inhibition of the contractile machinery, mainly by the activation of MLCP via inhibition of CPI-17 and RhoA/Rock., Findings define a new conserved pathway in which sexual development and pregnancy mediate smooth and striated muscle adaptations through SMTNL1 and MYPT1., hHS-M(21) is a heart-specific effector of ROCK and plays a regulatory role in the MYPT1 phosphorylation at Thr-696 by ROCK, Myosin phosphatase-targeting subunit 1 controls chromatid segregation., MYPT1 variant 2 shows decreased binding affinity compared to MYPT1 long for radixin (novel MLCP substrate and a member of ERM family proteins)., the defective protein level of MYPT1 in the diabetes mellitus (DM) group can partially explain the poor patency of saphenous vein graft harvested from patients with DM., Phosphorylation of MYPT1 (Thr853) changes dynamically with each contraction of the myometrium regulated by Rho-kinase., Site-specific phosphorylation of protein phosphatase 1 regulatory subunit 12A stimulated or suppressed by insulin., It found deoxyribonucleic acid (DNA) damage-induced LATS1 activation caused PLK1 suppression via the phosphorylation of MYPT1 S445., These findings provide evidence for the involvement of a particular PP1 complex, PPP1R12A/PP1cdelta, in insulin signaling., Calcineurin may modulate the phosphorylation level of MLC20 by influencing the phosphorylation state of MYPT1 to regulate endothelial barrier function., Mypt1 colocalizes outside the nucleus with Nkx2.5 in a manner dependent on Wnt signaling and Rho-associated protein kinase., in apoptotic cells, the myosin-binding domain of myosin phosphatase targeting subunit 1 is cleaved by caspase-3, and the cleaved MYPT1 is strongly phosphorylated at Thr-696 and Thr-853, phosphorylation of which is known to inhibit myosin II binding, results suggested that during atherosclerosis progression oxidative stress mediates the downregulation of MYPT1, which may inhibit smooth muscle cell migration and contribute to the aberrant contractility, distinct roles of two inhibitory phosphorylation sites of MYPT1, Expression of NUAK1 is controlled by cyclin-dependent kinase, PLK1, and the SCFbetaTrCP (Skp, Cullin and F-boxbetaTrCP) E3 ubiquitin ligase complex., These results indicate that PPP1R12A indeed plays a role in skeletal muscle insulin signaling, the relative expression of LZ+/LZ- MYPT1 isoforms, in part, defines the vascular response to NO and NO based vasodilators, and therefore, plays a role in the regulation of vascular tone in both health and disease,
SP_COMMENT function:Regulates myosin phosphatase activity., PTM:Phosphorylated by CIT (Rho-associated kinase) (By similarity). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-696. Phosphorylated on upon DNA damage, probably by ATM or ATR., sequence caution:Contaminating sequence. Potential poly-A sequence., similarity:Contains 6 ANK repeats., subcellular location:Along actomyosin filaments and stress fibers., subunit:PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12A mediates binding to myosin. Interacts with ARHA and CIT (By similarity). Binds PPP1R12B, ROCK1 and IL16.,
protein phosphatase 1 regulatory subunit 12B(PPP1R12B) protein phosphatase 1 regulatory subunit 12B(PPP1R12B) Related Genes Homo sapiens
CHROMOSOME 1,
CYTOBAND 1q32.1,
ENSEMBL_GENE_ID ENSG00000077157,
GENERIF_SUMMARY Results describe the characterization and function of MYPT2, a target subunit of myosin phosphatase in heart., analysis of the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase, PPP1R12B is associated with childhood asthma in a Russian population.,
SP_COMMENT caution:The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data., function:Regulates myosin phosphatase activity. Augments Ca(2+) sensitivity of the contractile apparatus., similarity:Contains 5 ANK repeats., subcellular location:Along actomyosin filaments and stress fibers., subunit:PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12B mediates binding to myosin. Isoform 3 and isoform 4 bind PPP1R12A, but not isoform 1 of PPP1R12B itself. Binds IL16., tissue specificity:Detected in skeletal muscle, fetal and adult heart, brain, placenta, kidney, spleen, thymus, pancreas and lung. Isoform 3 and isoform 4 are heart specific.,
protein phosphatase 1 regulatory subunit 12C(PPP1R12C) protein phosphatase 1 regulatory subunit 12C(PPP1R12C) Related Genes Homo sapiens
CHROMOSOME 19,
CYTOBAND 19q13.42,
ENSEMBL_GENE_ID ENSG00000125503,
GENERIF_SUMMARY M-RIP can assemble a complex containing both RhoA and Myosin phosphatase myosin binding subunit, suggesting that M-RIP may play a role in myosin phosphatase regulation by RhoA, Authors demonstrate that Rep proteins of adeno-associated virus serotype 2 efficiently repress expression from the target site PPP1R12C promoter.,
SP_COMMENT caution:Although assigned as two separate genes (PPP1R12C and LENG3), it is probable that LENG3 does not exist by itself and is a part of the PPP1R12C gene., function:Regulates myosin phosphatase activity., PTM:Phosphorylated upon DNA damage, probably by ATM or ATR., sequence caution:Unspliced mRNA., similarity:Contains 4 ANK repeats., subcellular location:Along actomyosin filaments and stress fibers., subunit:PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, and one or several targeting or regulatory subunits. PPP1R12C mediates binding to myosin. Interacts via its N-terminus with PPP1CB. Interacts with IL16. Interacts with the coiled-coil domain of MPRIP., tissue specificity:Ubiquitously expressed. Highly expressed in heart.,