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LIN9 (show LIN9 Proteins) is essential for proliferation and genome stability of ESCs (show NR2E3 Proteins) by activating genes with important functions in mitosis and cytokinesis
PIMT (show PCMT1 Proteins) is expressed in all cells of the E3.5day blastocyst in the mouse.
inactivation of LIN9 (show LIN9 Proteins), a subunit of DREAM, results in premature senescence, which can be overcome by the SV40 large T (LT) antigen
These experiments provide the first direct genetic evidence for the role of LIN9 (show LIN9 Proteins) in development and mitotic gene regulation and they suggest that it may function as a haploinsufficient tumor suppressor.
there is a feedback mechanism between ARF and Mip130/LIN-9 (show LIN9 Proteins) in which either the increase of ARF or the decrease in Mip130/LIN-9 (show LIN9 Proteins)
Mutation of BARA/LIN-9 (show LIN9 Proteins) restores the expression of E2F (show E2F1 Proteins) target genes in CDK4 (show CDK4 Proteins) null Mouse Embryo Fibroblasts, indicating that the wild-type protein plays a role in the expression of genes required for the G1/S transition.
Mip/LIN-9 (show LIN9 Proteins) is required for the expression of B-Myb (show MYBL2 Proteins), and both proteins collaborate in the control of the cell cycle progression via the regulation of S phase and cyclin A (show CCNA2 Proteins), cyclin B, and CDK1 (show CDK1 Proteins)
The repressor complex that Mip/LIN-9 (show LIN9 Proteins) forms with p107 (show RBL1 Proteins) takes functional precedence over the transcriptional activation linked to the Mip/LIN-9 (show LIN9 Proteins) and B-Myb (show MYBL2 Proteins) interaction.
Lin-9 (show LIN9 Proteins) and B-Myb (show MYBL2 Proteins) were both required for transcription of G(2)/M genes such as Cyclin B1 (show CCNB1 Proteins) and Survivin (show BIRC5 Proteins).
Mip130/LIN-9 (show LIN9 Proteins) contributes to the repression of these E2F (show E2F1 Proteins)-regulated genes in G0/G1 in mice.
Data highlight the importance of the catalytic activity of PIMT to mediate VEGF effects during endothelial cell migration and tube formation in angiogenesis.
PIMT (show PCMT1 Proteins) was identified as a key player responsible for glycated low density lipoproteins induced vascular endothelial cell apoptosis.
isoforms of the PIMT/Tgs1 protein with an RNA methyltransferase domain function both in the nucleus and in the cytoplasm
The protein L-isoaspartyl (D-aspartyl) methyltransferase (PIMT (show PCMT1 Proteins)) is an enzyme that recognizes and repairs the abnormal L-isoaspartyl residues in proteins.
Interaction of PIMT (show PCMT1 Proteins) with transcriptional coactivators CBP (show CREBBP Proteins), p300 (show EP300 Proteins), and PBP differential role in transcriptional regulation.
proteasome maturation constitutes a mechanism regulating Tgs1 (show LIN9 Proteins) function by generating Tgs1 (show LIN9 Proteins) species with different substrate specificities, subcellular localizations, and functions.
These results highlight that PIMT (show PCMT1 Proteins) expression is regulated by ROS (show ROS1 Proteins) and could primarily act as an antioxidant enzyme.
present a biochemical characterization of the human Tgs1 (show LIN9 Proteins) guanine-N2 methyltransferase reaction and identify individual amino acids required for methyltransferase activity in vitro and in vivo
m(7)GpppA binds via its adenosine moiety to the structurally conserved adenosylmethionine-binding pocket. The m(7) guanosine is unbound. The crystallized TGS1 (show LIN9 Proteins) fragment is catalytically inactive, but a fragment that is 17 AAs (show FGD1 Proteins) longer exhibits activity.
The crystal structure of the substrate bound methyltransferase domain as well as mutagenesis studies provide insight into the catalytic mechanism of TGS1 (show LIN9 Proteins).
Catalyzes the 2 serial methylation steps for the conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure. The enzyme is specific for guanine, and N7 methylation must precede N2 methylation. Hypermethylation of the m7G cap of U snRNAs leads to their concentration in nuclear foci, their colocalization with coilin and the formation of canonical Cajal bodies (CBs). Plays a role in transcriptional regulation (By similarity).
trimethylguanosine synthase homolog
, TUDOR gene similar 1 protein
, protein lin-9 homolog
, type I interferon receptor beta chain-associated protein
, CLL-associated antigen KW-2
, PRIP-interacting protein PIPMT
, PRIP-interacting protein with methyltransferase domain
, PRIP-interacting protein with methyltransferase motif
, cap-specific guanine-N2 methyltransferase
, hepatocellular carcinoma-associated antigen 137
, nuclear receptor coactivator 6 interacting protein
, nuclear receptor coactivator 6-interacting protein
, trimethylguanosine synthase