IED ID | IndEnz0002003800 |
Enzyme Type ID | protease003800 |
Protein Name |
Ras GTPase-activating protein-binding protein 2 G3BP-2 GAP SH3 domain-binding protein 2 |
Gene Name | G3BP2 KIAA0660 |
Organism | Homo sapiens (Human) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEERQPSPEPVQENANSGYYEAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKNLEELEEKSTTPPPAEPVSLPQEPPKAFSWASVTSKNLPPSGTVSSSGIPPHVKAPVSQPRVEAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMAQKLGSGRGTGQMEGRFTGQRR |
Enzyme Length | 482 |
Uniprot Accession Number | Q9UN86 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling. {ECO:0000269|PubMed:23279204}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (1); Beta strand (6); Chain (1); Compositional bias (5); Cross-link (1); Domain (2); Erroneous initiation (1); Helix (5); Initiator methionine (1); Modified residue (10); Natural variant (1); Region (3); Sequence conflict (3) |
Keywords | 3D-structure;Alternative splicing;Cytoplasm;Direct protein sequencing;Host-virus interaction;Immunity;Innate immunity;Isopeptide bond;Methylation;Phosphoprotein;RNA-binding;Reference proteome;Transport;Ubl conjugation;mRNA transport |
Interact With | Q15672; Q14694; P0DTC9; P26687; Q7Z417; Q14694; Q5T7W0 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23279204, ECO:0000269|PubMed:30404792}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23279204, ECO:0000269|PubMed:30404792}. |
Modified Residue | MOD_RES 141; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"; MOD_RES 149; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"; MOD_RES 225; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P97379"; MOD_RES 227; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"; MOD_RES 392; /note="N6-succinyllysine"; /evidence="ECO:0000250|UniProtKB:P97379"; MOD_RES 457; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 466; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 468; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES Q9UN86-2:227; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES Q9UN86-2:235; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648" |
Post Translational Modification | PTM: Arg-457 and Arg-468 are dimethylated, probably to asymmetric dimethylarginine.; 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}. |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 5DRV; |
Mapped Pubmed ID | 16973615; 17297477; 17353931; 17474147; 17620599; 19615732; 20467437; 20562859; 20711500; 21182205; 21985131; 22190034; 22536444; 23087212; 23902751; 23986595; 24992036; 25416956; 25609649; 25653451; 25893917; 26410532; 27022092; 28096337; 28692047; 29378906; 29379164; 30455363; 30804457; 31199850; 33476486; 33497611; 34517025; |
Motif | |
Gene Encoded By | |
Mass | 54,121 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |