AFfirm™ G3BP-1 Mouse Monoclonal Antibody - #BF8863
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Fold/Unfold
ATP dependent DNA helicase VIII; ATP-dependent DNA helicase VIII; G3BP; G3BP stress granule assembly factor 1; G3BP-1; G3bp1; G3BP1_HUMAN; GAP binding protein; GAP SH3 domain binding protein 1; GAP SH3 domain-binding protein 1; GTPase activating protein (SH3 domain) binding protein 1; hDH VIII; Human DNA helicase VIII; MGC111040; Ras GTPase activating protein binding protein 1; Ras GTPase activating protein SH3 domain binding protein; Ras GTPase-activating protein-binding protein 1; RasGAP associated endoribonuclease G3BP;
Immunogens
- Q13283 G3BP1_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ
PTMs - Q13283 As Substrate
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| K5 | Methylation | Uniprot | |
| K5 | Ubiquitination | Uniprot | |
| S7 | Phosphorylation | Uniprot | |
| Y20 | Phosphorylation | Uniprot | |
| K36 | Ubiquitination | Uniprot | |
| S47 | Phosphorylation | Uniprot | |
| K50 | Ubiquitination | Uniprot | |
| Y56 | Phosphorylation | P06239 (LCK) | Uniprot |
| K59 | Ubiquitination | Uniprot | |
| K64 | Ubiquitination | Uniprot | |
| S67 | Phosphorylation | Uniprot | |
| T71 | Phosphorylation | Uniprot | |
| T75 | Phosphorylation | Uniprot | |
| K76 | Acetylation | Uniprot | |
| K76 | Ubiquitination | Uniprot | |
| S119 | Phosphorylation | Uniprot | |
| K123 | Ubiquitination | Uniprot | |
| Y125 | Phosphorylation | Uniprot | |
| Y133 | Phosphorylation | P12931 (SRC) | Uniprot |
| T143 | Phosphorylation | Uniprot | |
| S149 | Phosphorylation | Uniprot | |
| T162 | Phosphorylation | Uniprot | |
| T222 | Phosphorylation | Uniprot | |
| S230 | Phosphorylation | Uniprot | |
| S231 | Phosphorylation | Uniprot | |
| S232 | Phosphorylation | Uniprot | |
| T241 | Phosphorylation | Uniprot | |
| R247 | Methylation | Uniprot | |
| S250 | Phosphorylation | Uniprot | |
| S253 | Phosphorylation | Uniprot | |
| K287 | Ubiquitination | Uniprot | |
| S339 | Phosphorylation | Uniprot | |
| K353 | Ubiquitination | Uniprot | |
| K357 | Ubiquitination | Uniprot | |
| S362 | Phosphorylation | Uniprot | |
| Y363 | Phosphorylation | Uniprot | |
| S373 | Phosphorylation | Uniprot | |
| K376 | Acetylation | Uniprot | |
| K376 | Ubiquitination | Uniprot | |
| S388 | Phosphorylation | Uniprot | |
| K393 | Ubiquitination | Uniprot | |
| R403 | Methylation | Uniprot | |
| R427 | Methylation | Uniprot | |
| R429 | Methylation | Uniprot | |
| R435 | Methylation | Uniprot | |
| R443 | Methylation | Uniprot | |
| R447 | Methylation | Uniprot | |
| K453 | Methylation | Uniprot | |
| R460 | Methylation | Uniprot | |
| R465 | Methylation | Uniprot |
Research Backgrounds
ATP- and magnesium-dependent helicase that plays an essential role in innate immunity. Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS. Enhances also DDX58-induced type I interferon production probably by helping DDX58 at sensing pathogenic RNA. In addition, plays an essential role in stress granule formation. 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. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR.
(Microbial infection) Cleaved by human enterovirus 71; this cleavage induces the disassembly of cytoplasmic stress granules. Cleaved by Foot-and-mouth disease virus; this cleavage suppresses the formation of cytoplasmic stress granules.
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.
Cytoplasm>Cytosol. Perikaryon. Cytoplasm>Stress granule. Nucleus.
Note: Cytoplasmic in proliferating cells (PubMed:11604510). Cytosolic and partially nuclear in resting cells (PubMed:11604510). Recruited to stress granules in response to arsenite treatment (PubMed:12642610, PubMed:20180778). The unphosphorylated form is recruited to stress granules (PubMed:12642610). HRAS signaling contributes to this process by regulating G3BP dephosphorylation (PubMed:12642610).
Ubiquitous.
Homodimer and oligomer. 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. Interacts with RPTOR and SPAG5; this complex is increased by oxidative stress. Interacts with ATXN2L. Interacts with STYXL1. Interacts with CGAS (via N-terminus); this interaction promotes the DNA-binding and activation of CGAS. Interacts (via C-terminus) with DDX58. Interacts (via NTF2-like domain) with CAPRIN1. Interacts with PABPC1.
(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.
The NTF2 domain mediates multimerization.
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