| IED ID | IndEnz0002005737 |
| Enzyme Type ID | protease005737 |
| Protein Name |
Ras GTPase-activating protein-binding protein 1 G3BP-1 EC 3.6.4.12 EC 3.6.4.13 ATP-dependent DNA helicase VIII hDH VIII GAP SH3 domain-binding protein 1 |
| Gene Name | G3BP1 G3BP |
| 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 | MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ |
| Enzyme Length | 466 |
| Uniprot Accession Number | Q13283 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:9889278}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:9889278}; |
| DNA Binding | |
| EC Number | 3.6.4.12; 3.6.4.13 |
| Enzyme Function | FUNCTION: ATP- and magnesium-dependent helicase that plays an essential role in innate immunity (PubMed:30510222). 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 (PubMed:30804210). In addition, plays an essential role in stress granule formation (PubMed:12642610, PubMed:20180778, PubMed:23279204). 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 (PubMed:9889278). Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency (PubMed:9889278). Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA (PubMed:9889278). Phosphorylation-dependent sequence-specific endoribonuclease in vitro (PubMed:11604510). Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR (PubMed:11604510). {ECO:0000269|PubMed:11604510, ECO:0000269|PubMed:12642610, ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:23279204, ECO:0000269|PubMed:30510222, ECO:0000269|PubMed:30804210, ECO:0000269|PubMed:9889278}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (7); Chain (1); Compositional bias (4); Cross-link (1); Domain (2); Helix (5); Initiator methionine (1); Modified residue (16); Mutagenesis (5); Region (4); Site (1); Turn (1) |
| Keywords | 3D-structure;ATP-binding;Acetylation;Alternative splicing;Cytoplasm;DNA-binding;Direct protein sequencing;Endonuclease;Helicase;Host-virus interaction;Hydrolase;Immunity;Innate immunity;Isopeptide bond;Methylation;Nuclease;Nucleotide-binding;Nucleus;Phosphoprotein;RNA-binding;Reference proteome;Transport;Ubl conjugation |
| Interact With | Q99700; Q8WWM7; P42858; Q8N122; Q7KZF4; Q14694; P0DTC9; P59595 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:30510222}. Perikaryon {ECO:0000250|UniProtKB:P97855}. Cytoplasm, Stress granule {ECO:0000269|PubMed:12642610, ECO:0000269|PubMed:17210633, ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:23953116, ECO:0000269|PubMed:30404792}. Nucleus {ECO:0000269|PubMed:11604510}. 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). {ECO:0000269|PubMed:11604510, ECO:0000269|PubMed:12642610, ECO:0000269|PubMed:20180778}. |
| Modified Residue | MOD_RES 143; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648"; MOD_RES 149; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:11604510, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 231; /note="Phosphoserine"; /evidence="ECO:0000269|Ref.6"; MOD_RES 232; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:11604510, ECO:0000269|Ref.6, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"; MOD_RES 250; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 253; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 373; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"; MOD_RES 376; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 429; /note="Asymmetric dimethylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 435; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 435; /note="Dimethylated arginine; alternate"; /evidence="ECO:0000269|Ref.6"; MOD_RES 435; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315"; MOD_RES 447; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 460; /note="Dimethylated arginine; alternate"; /evidence="ECO:0000269|Ref.6"; MOD_RES 460; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315"; MOD_RES 465; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315" |
| Post Translational Modification | PTM: (Microbial infection) Cleaved by human enterovirus 71; this cleavage induces the disassembly of cytoplasmic stress granules (PubMed:30006004). Cleaved by Foot-and-mouth disease virus; this cleavage suppresses the formation of cytoplasmic stress granules (PubMed:30404792). {ECO:0000269|PubMed:30006004, ECO:0000269|PubMed:30404792}.; PTM: 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. {ECO:0000250, ECO:0000269|PubMed:11604510, ECO:0000269|PubMed:12642610, ECO:0000269|Ref.6}.; PTM: Arg-435 is dimethylated, probably to asymmetric dimethylarginine. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 3Q90; 4FCJ; 4FCM; 4IIA; 5FW5; 6TA7; |
| Mapped Pubmed ID | 15471883; 15602692; 15743820; 16996479; 17253181; 17297477; 17353931; 17620599; 17696235; 17721511; 18005740; 18698806; 19135240; 19367725; 19463016; 19615732; 20424128; 20562859; 20639877; 20643132; 20663914; 21182205; 21206022; 21257637; 21266361; 21304914; 21532619; 21665939; 21988832; 22190034; 22205990; 22414690; 22623428; 22703643; 22767504; 22833567; 22863774; 23163895; 23455922; 23902751; 23986595; 24321297; 24366813; 24992036; 24998844; 25229650; 25520508; 25578447; 25609649; 25653451; 25665578; 25784705; 25800057; 25809930; 25847539; 25962958; 26350772; 26432022; 26496610; 27022092; 27303792; 27601476; 27920254; 28011284; 28523344; 28972166; 29463567; 29588351; 29626090; 29717134; 30135423; 30989663; 31171631; 31171633; 31199850; 31481087; 31481451; 31501480; 31560169; 31827077; 31905230; 31941779; 31941782; 31956030; 32302571; 32302572; 32406909; 32663095; 32692974; 33000280; 33020468; 33065005; 33131924; 33199441; 33497611; 33547245; 33726799; 33941659; 33945510; 33987877; 34287041; 34517025; 34614161; 34739333; 34795264; |
| Motif | |
| Gene Encoded By | |
| Mass | 52,164 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:13065 |
| Cross Reference Brenda |