G3BP1_MOUSE
ID G3BP1_MOUSE Reviewed; 465 AA.
AC P97855;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ras GTPase-activating protein-binding protein 1;
DE Short=G3BP-1;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q13283};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q13283};
DE AltName: Full=ATP-dependent DNA helicase VIII;
DE AltName: Full=GAP SH3 domain-binding protein 1;
DE AltName: Full=HDH-VIII;
GN Name=G3bp1; Synonyms=G3bp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Saitoh H., Abe T.K., Masuko M., Tanaka H., Watanabe Y.G., Odani S.,
RA Kuwano R.;
RT "cDNA cloning of GAP SH3 binding protein from mouse brain.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 124-132; 334-351 AND 375-391, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP INTERACTION WITH RASA1, AND SUBCELLULAR LOCATION.
RX PubMed=8649363; DOI=10.1128/mcb.16.6.2561;
RA Parker F., Maurier F., Delumeau I., Duchesne M., Faucher D., Debussche L.,
RA Dugue A., Schweighoffer F., Tocque B.;
RT "A Ras-GTPase-activating protein SH3-domain-binding protein.";
RL Mol. Cell. Biol. 16:2561-2569(1996).
RN [5]
RP ENDORIBONUCLEASE ACTIVITY, AND PHOSPHORYLATION AT SER-149 AND SER-231.
RX PubMed=11604510; DOI=10.1128/mcb.21.22.7747-7760.2001;
RA Tourriere H., Gallouzi I.-E., Chebli K., Capony J.-P., Mouaikel J.,
RA van der Geer P., Tazi J.;
RT "RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and
RT phosphorylation-dependent localization.";
RL Mol. Cell. Biol. 21:7747-7760(2001).
RN [6]
RP IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND ELAVL4, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15086518; DOI=10.1111/j.1471-4159.2004.02371.x;
RA Atlas R., Behar L., Elliott E., Ginzburg I.;
RT "The insulin-like growth factor mRNA binding-protein IMP-1 and the Ras-
RT regulatory protein G3BP associate with tau mRNA and HuD protein in
RT differentiated P19 neuronal cells.";
RL J. Neurochem. 89:613-626(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-231, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-433; ARG-445 AND ARG-458, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=30510222; DOI=10.1038/s41590-018-0262-4;
RA Liu Z.S., Cai H., Xue W., Wang M., Xia T., Li W.J., Xing J.Q., Zhao M.,
RA Huang Y.J., Chen S., Wu S.M., Wang X., Liu X., Pang X., Zhang Z.Y., Li T.,
RA Dai J., Dong F., Xia Q., Li A.L., Zhou T., Liu Z.G., Zhang X.M., Li T.;
RT "G3BP1 promotes DNA binding and activation of cGAS.";
RL Nat. Immunol. 20:18-28(2019).
CC -!- FUNCTION: ATP- and magnesium-dependent helicase that plays an essential
CC role in innate immunity. Participates in the DNA-triggered cGAS/STING
CC pathway by promoting the DNA binding and activation of CGAS. Enhances
CC also DDX58-induced type I interferon production probably by helping
CC DDX58 at sensing pathogenic RNA. In addition, plays an essential role
CC in stress granule formation. Unwinds preferentially partial DNA and RNA
CC duplexes having a 17 bp annealed portion and either a hanging 3' tail
CC or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and
CC RNA/RNA substrates with comparable efficiency. Acts unidirectionally by
CC moving in the 5' to 3' direction along the bound single-stranded DNA.
CC Phosphorylation-dependent sequence-specific endoribonuclease in vitro
CC (PubMed:11604510). Cleaves exclusively between cytosine and adenine and
CC cleaves MYC mRNA preferentially at the 3'-UTR (PubMed:11604510).
CC {ECO:0000250|UniProtKB:Q13283, ECO:0000269|PubMed:11604510}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q13283};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q13283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q13283};
CC Note=Mg(2+) is required for helicase activity.
CC {ECO:0000250|UniProtKB:Q13283};
CC -!- SUBUNIT: Homodimer and oligomer (By similarity). Component of a TAU
CC mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP1
CC (PubMed:15086518). Binds to the SH3 domain of Ras GTPase-activating
CC protein (RASA1) in proliferating cells (PubMed:8649363). No interaction
CC in quiescent cells (By similarity). Interacts (via NTF2-like domain)
CC with USP10. Interacts with RPTOR and SPAG5; this complex is increased
CC by oxidative stress. Interacts with ATXN2L. Interacts with STYXL1.
CC Interacts with CGAS (via N-terminus); this interaction promotes the
CC DNA-binding and activation of CGAS. Interacts (via C-terminus) with
CC DDX58. Interacts (via NTF2-like domain) with CAPRIN1. Interacts with
CC PABPC1 (By similarity). {ECO:0000250|UniProtKB:Q13283,
CC ECO:0000269|PubMed:8649363}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15086518,
CC ECO:0000269|PubMed:8649363}. Perikaryon {ECO:0000269|PubMed:15086518}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q13283}. Nucleus
CC {ECO:0000250|UniProtKB:Q13283}. Note=Cytoplasmic in proliferating
CC cells, can be recruited to the plasma membrane in exponentially growing
CC cells. Cytosolic and partially nuclear in resting cells. Recruited to
CC stress granules in response to arsenite treatment. The unphosphorylated
CC form is recruited to stress granules. HRAS signaling contributes to
CC this process by regulating G3BP dephosphorylation.
CC {ECO:0000250|UniProtKB:Q13283}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:30510222}.
CC -!- DOMAIN: The NTF2 domain mediates multimerization. {ECO:0000250}.
CC -!- PTM: Phosphorylated exclusively on serine residues. Hyperphosphorylated
CC in quiescent fibroblasts. Hypophosphorylation leads to a decrease in
CC endoribonuclease activity. RASA1-dependent phosphorylation of Ser-149
CC induces a conformational change that prevents self-association.
CC Dephosphorylation after HRAS activation is required for stress granule
CC assembly. Ser-149 phosphorylation induces partial nuclear localization
CC (By similarity). {ECO:0000250}.
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DR EMBL; AB001927; BAA19469.1; -; mRNA.
DR EMBL; BC021156; AAH21156.1; -; mRNA.
DR CCDS; CCDS24714.1; -.
DR RefSeq; NP_038744.1; NM_013716.2.
DR AlphaFoldDB; P97855; -.
DR SMR; P97855; -.
DR BioGRID; 205102; 42.
DR IntAct; P97855; 7.
DR STRING; 10090.ENSMUSP00000018727; -.
DR iPTMnet; P97855; -.
DR PhosphoSitePlus; P97855; -.
DR SwissPalm; P97855; -.
DR EPD; P97855; -.
DR jPOST; P97855; -.
DR PaxDb; P97855; -.
DR PeptideAtlas; P97855; -.
DR PRIDE; P97855; -.
DR ProteomicsDB; 273017; -.
DR Antibodypedia; 1315; 555 antibodies from 37 providers.
DR DNASU; 27041; -.
DR Ensembl; ENSMUST00000018727; ENSMUSP00000018727; ENSMUSG00000018583.
DR GeneID; 27041; -.
DR KEGG; mmu:27041; -.
DR UCSC; uc007izl.1; mouse.
DR CTD; 10146; -.
DR MGI; MGI:1351465; G3bp1.
DR VEuPathDB; HostDB:ENSMUSG00000018583; -.
DR eggNOG; KOG0116; Eukaryota.
DR GeneTree; ENSGT00390000011365; -.
DR HOGENOM; CLU_022209_0_2_1; -.
DR InParanoid; P97855; -.
DR OMA; RCKGPQG; -.
DR OrthoDB; 1526879at2759; -.
DR PhylomeDB; P97855; -.
DR TreeFam; TF325464; -.
DR BioGRID-ORCS; 27041; 8 hits in 78 CRISPR screens.
DR ChiTaRS; G3bp1; mouse.
DR PRO; PR:P97855; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P97855; protein.
DR Bgee; ENSMUSG00000018583; Expressed in ileal epithelium and 279 other tissues.
DR Genevisible; P97855; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
DR GO; GO:0033677; F:DNA/RNA helicase activity; ISO:MGI.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0003724; F:RNA helicase activity; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0062029; P:positive regulation of stress granule assembly; ISO:MGI.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISO:MGI.
DR GO; GO:0034063; P:stress granule assembly; ISO:MGI.
DR CDD; cd00780; NTF2; 1.
DR CDD; cd12463; RRM_G3BP1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034375; G3BP1.
DR InterPro; IPR034374; G3BP1_RRM.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR039539; Ras_GTPase_bind_prot.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10693; PTHR10693; 1.
DR PANTHER; PTHR10693:SF21; PTHR10693:SF21; 1.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Endonuclease; Helicase; Hydrolase; Immunity; Innate immunity;
KW Isopeptide bond; Methylation; Nuclease; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transport;
KW Ubl conjugation.
FT CHAIN 1..465
FT /note="Ras GTPase-activating protein-binding protein 1"
FT /id="PRO_0000194799"
FT DOMAIN 11..133
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 338..413
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 144..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11604510,
FT ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11604510,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 374
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 427
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 433
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 433
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 445
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 458
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT MOD_RES 458
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 464
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13283"
SQ SEQUENCE 465 AA; 51829 MW; EB213303D21B1D57 CRC64;
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY AHGGLDSNGK PADAVYGQKE
IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV
ANKFYVHNDI FRYQDEVFGG FVTEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQTVSN
DLEEHLEEPV VEPEPEPEPE PEPEPVSDIQ EDKPEAALEE AAPDDVQKST SPAPADVAPA
QEDLRTFSWA SVTSKNLPPS GAVPVTGTPP HVVKVPASQP RPESKPDSQI PPQRPQRDQR
VREQRINIPP QRGPRPIREA GEPGDVEPRR MVRHPDSHQL FIGNLPHEVD KSELKDFFQN
FGNVVELRIN SGGKLPNFGF VVFDDSEPVQ KVLSNRPIMF RGAVRLNVEE KKTRAAREGD
RRDNRLRGPG GPRGGPSGGM RGPPRGGMVQ KPGFGVGRGI TTPRQ
