Ras GTP酶活化蛋白结合蛋白1重组兔单抗

G3BP1

Ras GTPase-activating protein-binding protein 1

Binds to the SH3 domain of Ras GTPase-activating protein (RASA1) in proliferating cells. No interaction in quiescent cells Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP (By similarity). Interacts with USP10, and may regulate it. Forms homodimers and oligomers.

Cytoplasm. Cytoplasm, cytosol. Cell membrane. Nucleus. Note=Cytoplasmic in proliferating cells, can be recruited to the plasma membrane in exponentially growing cells. Cytosolic and partially nuclear in resting cells. Recruited to stress granules (SGs) upon either arsenite or high temperature treatment. Recruitment to SGs is influenced by HRAS.

Ubiquitous.

Phosphorylated exclusively on serine residues. Hyperphosphorylated in quiescent fibroblasts. Hypophosphorylation leads to a decrease in endoribonuclease activity (By similarity). RASA1-dependent phosphorylation of Ser-149 induces a conformational change that prevents self-association. Dephosphorylation after HRAS activation is required for stress granule assembly. Ser-149 phosphorylation induces partial nuclear localization.
Arg-435 is dimethylated, probably to asymmetric dimethylarginine.

Contains 1 NTF2 domain.
Contains 1 RRM (RNA recognition motif) domain.

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.