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Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. Additionally we are shipping Dullard Homolog (Xenopus Laevis) Antibodies (41) and many more products for this protein.
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CTDNEP1 is upregulated in non-alcoholic fatty liver disease. Up-regulation of miR (show MLXIP Proteins)-122 can trigger the compensatory response of LPIN1 (show LPIN1 Proteins) and CTDNEP1 in hepatosteatosis.
dullard shows specificity for the peptide corresponding to the insulin (show INS Proteins)-dependent phosphorylation site (Ser106) of lipin
Dullard participates in a unique phosphatase cascade regulating nuclear membrane biogenesis, a cascade that is conserved from yeast to mammals.
Dullard is involved in suppression of TGF-beta (show TGFB1 Proteins) signaling during endochondral ossification.
Dullard may play a role in the fine-tuning of WNT (show WNT2 Proteins) signalling activity by modulating the expression of ligands/antagonists and the availability of Dvl2 (show DVL2 Proteins) protein during specification of the germ cell lineage.
Dullard keeps BMP signalling at an appropriate level, which is required for nephron maintenance in the postnatal period.
Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at differents levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling.
, C-terminal domain nuclear envelope phosphatase 1
, dullard homolog
, serine/threonine-protein phosphatase dullard
, CTD nuclear envelope phosphatase 1A
, serine/threonine-protein phosphatase dullard-A