G3bp2
entrez
23881
canonical
uniprot
P97379
canonical
ensembl
ENSMUSG00000029405
resolver
ensp
ENSMUSP00000108752
resolver
ensp
ENSMUSP00000128244
resolver
ensp
ENSMUSP00000128353
resolver
ensp
ENSMUSP00000132469
resolver
ensp
ENSMUSP00000144456
resolver
ensp
ENSMUSP00000177071
resolver
ensp
ENSMUSP00000177074
resolver
genesymbol
G3bp2
resolver
uniprot
Q3TEL4
resolver
uniprot
Q3U541
resolver
uniprot
Q3U6B1
resolver
uniprot
Q3UL55
resolver
uniprot
Q542W3
resolver
uniprot
Q9R1B8
resolver
uniprot_entry
G3BP2_MOUSE
resolver
uniprot_entry
Q3TEL4_MOUSE
resolver
uniprot_entry
Q3U541_MOUSE
resolver
uniprot_entry
Q3U6B1_MOUSE
resolver
uniprot_entry
Q542W3_MOUSE
resolver
uniprot_sec
Q3UL55
resolver
uniprot_sec
Q9R1B8
resolver
activity_regulation
ACTIVITY REGULATION: Under physiological conditions, G3BP2 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 G3BP2 outcompetes the intramolecular interactions and RNA-bound G3BP2 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
MVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEDRQPSPEPVQENANSAYYDAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKHLEELEEKSATPPPAEPASLPQEPPKAFSWASVTSKNLPPSGTVSSSGIPPHVKAPVSQPRVDAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMTQKLGSGRGTGQMEGRFTGQRR
uniprot
proteins
function
FUNCTION: Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling. Plays an essential role in stress granule formation. 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). {ECO:0000250|UniProtKB:Q13283, ECO:0000250|UniProtKB:Q9UN86}.
uniprot
proteins
mass_dalton
54088
uniprot
proteins
pubmed
15345747
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
9575347
uniprot
proteins
sequence_length
482
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UN86}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9UN86}.
uniprot
proteins