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G3BP1

Engineered Antibody
This gene encodes one of the DNA-unwinding enzymes which prefers partially unwound 3'-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. This enzyme is a member of the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. It binds specifically to the Ras-GTPase-activating protein by associating with its SH3 domain. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined. [provided by RefSeq, Jul 2008]G3BP1 (G3BP Stress Granule Assembly Factor 1) is a Protein Coding gene. Gene Ontology (GO) annotations related to this gene include nucleic acid binding and mRNA binding. An important paralog of this gene is G3BP2.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.
Protein class

Enzymes, Plasma proteins

Predicted location

Intracellular, Membrane (different isoforms)

Single cell type specificity

Low cell type specificity

Immune cell specificity

Low immune cell specificity

Cell line specificity

Low cell line specificity

Interaction

Homodimer and oligomer (PubMed:12642610, 24324649). Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP1 (By similarity). Binds to the SH3 domain of Ras GTPase-activating protein (RASA1) in proliferating cells (By similarity). No interaction in quiescent cells (By similarity). Interacts (via NTF2-like domain) with USP10 (PubMed:11439350, 23279204). Interacts with RPTOR and SPAG5; this complex is increased by oxidative stress (PubMed:23953116). Interacts with ATXN2L (PubMed:23209657). Interacts with STYXL1 (PubMed:20180778). Interacts with CGAS (via N-terminus); this interaction promotes the DNA-binding and activation of CGAS (PubMed:30510222). Interacts (via C-terminus) with DDX58 (PubMed:30804210). Interacts (via NTF2-like domain) with CAPRIN1 (PubMed:17210633). Interacts with PABPC1 (PubMed:23279204). (Microbial infection) Interacts with Semliki forest virus non-structural protein 3 (via C-terminus); this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes. (Microbial infection) Interacts with Chikungunya virus non-structural protein 3 (via C-terminus); this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes. (Microbial infection) Interacts with Sindbis virus non-structural protein 3 (via C-terminus); this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes.

Molecular function

DNA-binding, Endonuclease, Helicase, Hydrolase, Nuclease, RNA-binding

More Types Infomation

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