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MIF4GD encodes a protein which interacts with the N-terminus of the stem-loop binding protein (SLBP) and the 3' end of histone mRNA. Additionally we are shipping MIF4G Domain Containing Antibodies (19) and MIF4G Domain Containing Proteins (6) and many more products for this protein.
Results suggest that MIF4GD is a potential regulator of p27 (show PAK2 ELISA Kits)-dependent cell proliferation in HCC (show FAM126A ELISA Kits).
This paper describes the oligomeric state of SLIP1 and the SLIP1-SLBP (show SLBP ELISA Kits) complex and how it is regulated by SLBP (show SLBP ELISA Kits) phosphorylation. Using alanine scanning mutagenesis, the authors demonstrate that the binding site on SLIP1 for SLBP (show SLBP ELISA Kits) lies close to the dimer interface. A single-point mutant near the SLIP1 homodimer interface abolished interaction with SLBP (show SLBP ELISA Kits) in vitro and reduced the abundance of histone mRNA in vivo.
INT6 (show EIF3E ELISA Kits) and MIF4GD were observed to colocalize in cytoplasmic foci. It was concluded that INT6 (show EIF3E ELISA Kits), by establishing interactions with MIF4GD and SLBP (show SLBP ELISA Kits), plays an important role in translation of poly(A) minus histone mRNAs.
downregulation of endogenous SLIP1 reduces the rate of translation of endogenous histone mRNA and also reduces cell viability.
This gene encodes a protein which interacts with the N-terminus of the stem-loop binding protein (SLBP) and the 3' end of histone mRNA. This interaction facilitates the activation of histone mRNA translation. Alternative splicing results in multiple transcript variants encoding different isoforms.
MIF4G domain containing
, MIF4G domain-containing protein
, SLBP (stem loop binding protein)-interacting protein 1
, SLBP-interacting protein 1