G3BP2
entrez
9908
canonical
uniprot
Q9UN86
canonical
ensembl
ENSG00000138757
resolver
ensp
ENSP00000350518
resolver
ensp
ENSP00000352738
resolver
ensp
ENSP00000379069
resolver
ensp
ENSP00000503209
resolver
ensp
ENSP00000503228
resolver
ensp
ENSP00000503239
resolver
ensp
ENSP00000503496
resolver
ensp
ENSP00000503504
resolver
ensp
ENSP00000503586
resolver
ensp
ENSP00000503669
resolver
ensp
ENSP00000503688
resolver
ensp
ENSP00000503911
resolver
ensp
ENSP00000504101
resolver
ensp
ENSP00000504206
resolver
ensp
ENSP00000504316
resolver
ensp
ENSP00000504363
resolver
ensp
ENSP00000504371
resolver
ensp
ENSP00000504564
resolver
ensp
ENSP00000504588
resolver
ensp
ENSP00000504591
resolver
ensp
ENSP00000504599
resolver
ensp
ENSP00000504698
resolver
ensp
ENSP00000504764
resolver
ensp
ENSP00000578136
resolver
enst
ENST00000677889
resolver
enst
ENST00000677970
resolver
enst
ENST00000678244
resolver
genesymbol
G3BP2
resolver
genesymbol_syn
KIAA0660
resolver
hgnc
HGNC:30291
resolver
uniprot
A0A7I2V3P9
resolver
uniprot
A0A7I2V647
resolver
uniprot
A8K6X1
resolver
uniprot
O60606
resolver
uniprot
O75149
resolver
uniprot
Q9UPA1
resolver
uniprot_entry
A0A7I2V3P9_HUMAN
resolver
uniprot_entry
A0A7I2V647_HUMAN
resolver
uniprot_entry
G3BP2_HUMAN
resolver
uniprot_sec
A8K6X1
resolver
uniprot_sec
O60606
resolver
uniprot_sec
O75149
resolver
uniprot_sec
Q9UPA1
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
MVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEERQPSPEPVQENANSGYYEAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKNLEELEEKSTTPPPAEPVSLPQEPPKAFSWASVTSKNLPPSGTVSSSGIPPHVKAPVSQPRVEAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMAQKLGSGRGTGQMEGRFTGQRR
uniprot
proteins
function
FUNCTION: Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling (PubMed:23279204, PubMed:32302570, PubMed:32302571, PubMed:32302572). Plays an essential role in stress granule formation (PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:35977029). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed:32302570, PubMed:32302571, PubMed:32302572). 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:0000269|PubMed:23279204, ECO:0000269|PubMed:27022092, ECO:0000269|PubMed:32302570, ECO:0000269|PubMed:32302571, ECO:0000269|PubMed:32302572, ECO:0000269|PubMed:35977029}.
uniprot
proteins
mass_dalton
54121
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Cleaved by foot-and-mouth disease virus leader protease; this cleavage suppresses the formation of cytoplasmic stress granules. {ECO:0000269|PubMed:30404792}.
uniprot
proteins
pubmed
10969074
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18684830
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23279204
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26410532
uniprot
proteins
pubmed
27022092
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30404792
uniprot
proteins
pubmed
31981475
uniprot
proteins
pubmed
32302570
uniprot
proteins
pubmed
32302571
uniprot
proteins
pubmed
32302572
uniprot
proteins
pubmed
35977029
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
482
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23279204, ECO:0000269|PubMed:30404792}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23279204, ECO:0000269|PubMed:27022092, ECO:0000269|PubMed:30404792}.
uniprot
proteins