G3bp1
entrez
27041
canonical
uniprot
P97855
canonical
ensembl
ENSMUSG00000018583
resolver
ensp
ENSMUSP00000018727
resolver
ensp
ENSMUSP00000202055
resolver
ensp
ENSMUSP00000202088
resolver
enst
ENSMUST00000018727
resolver
genesymbol
G3bp1
resolver
genesymbol_syn
G3bp
resolver
uniprot
Q3UR88
resolver
uniprot_entry
G3BP1_MOUSE
resolver
uniprot_entry
Q3UR88_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Under physiological conditions, G3BP1 adopts a compact state that is stabilized by intramolecular interactions between the RG-rich and the acidic regions that inhibit phase separation. Upon stress, polysomes disassemble and mRNAs are released in an unfolded protein-free state. Binding of unfolded mRNA to G3BP1 outcompetes the intramolecular interactions and RNA-bound G3BP1 adopts an expanded conformation in which the RG-rich region becomes exposed to engage in protein-protein and protein-RNA interactions, allowing physical cross-linking of RNA molecules to form protein-RNA condensates, leading to liquid-liquid phase separation (LLPS). {ECO:0000250|UniProtKB:Q13283}.
uniprot
proteins
amino_acid_sequence
MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYAHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQTVSNDLEEHLEEPVVEPEPEPEPEPEPEPVSDIQEDKPEAALEEAAPDDVQKSTSPAPADVAPAQEDLRTFSWASVTSKNLPPSGAVPVTGTPPHVVKVPASQPRPESKPDSQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEPGDVEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQNFGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGAVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGPSGGMRGPPRGGMVQKPGFGVGRGITTPRQ
uniprot
proteins
ec_number
3.6.4.12
uniprot
proteins
ec_number
3.6.4.13
uniprot
proteins
function
FUNCTION: Protein involved in various processes, such as stress granule formation and innate immunity (By similarity). Plays an essential role in stress granule formation (By similarity). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (By similarity). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (By similarity). Also acts as an ATP- and magnesium-dependent helicase: unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency (By similarity). Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA (By similarity). 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 (By similarity). Plays an essential role in innate immunity by promoting CGAS and RIGI activity (By similarity). Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS (By similarity). Triggers the condensation of cGAS, a process probably linked to the formation of membrane-less organelles. Also enhances RIGI-induced type I interferon production probably by helping RIGI at sensing pathogenic RNA (By similarity). May also act as a phosphorylation-dependent sequence-specific endoribonuclease in vitro: Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR (PubMed:11604510). {ECO:0000250|UniProtKB:Q13283, ECO:0000269|PubMed:11604510}.
uniprot
proteins
mass_dalton
51829
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of the acidic disordered region regulates stress granule assembly. Dephosphorylation after HRAS activation is required for stress granule assembly. Ser-149 phosphorylation induces partial nuclear localization. {ECO:0000250|UniProtKB:Q13283}.; PTM: Arg-435 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250|UniProtKB:Q13283}.; PTM: Ubiquitinated by TRIM21 via 'Lys-63'-linked polyubiquitination in the NTF2 domain in response to heat shock, leading to stress granule disassembly: ubiquitination promotes interaction with the FAF2 adapter, followed by interaction with VCP, which extracts G3BP1 from stress granules, leading to stress granule disassembly. In case of prolonged stress, ubiquitination by TRIM21 leads to autophagy-dependent degradation of G3BP1 via recruitment of ubiquitinated G3BP1 by SQSTM1 and/or CALCOCO2 to autophagosomes. {ECO:0000250|UniProtKB:Q13283}.
uniprot
proteins
pubmed
11604510
uniprot
proteins
pubmed
15086518
uniprot
proteins
pubmed
15345747
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
30510222
uniprot
proteins
pubmed
8649363
uniprot
proteins
sequence_length
465
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15086518, ECO:0000269|PubMed:8649363}. Perikaryon {ECO:0000269|PubMed:15086518}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q13283}. Nucleus {ECO:0000250|UniProtKB:Q13283}. 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 in response to arsenite treatment. The unphosphorylated form is recruited to stress granules. HRAS signaling contributes to this process by regulating G3BP dephosphorylation. {ECO:0000250|UniProtKB:Q13283}.
uniprot
proteins