G3BP1_HUMAN
ID G3BP1_HUMAN Reviewed; 466 AA.
AC Q13283; Q5HYE9;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Ras GTPase-activating protein-binding protein 1;
DE Short=G3BP-1;
DE EC=3.6.4.12 {ECO:0000269|PubMed:9889278};
DE EC=3.6.4.13 {ECO:0000269|PubMed:9889278};
DE AltName: Full=ATP-dependent DNA helicase VIII;
DE Short=hDH VIII;
DE AltName: Full=GAP SH3 domain-binding protein 1;
GN Name=G3BP1; Synonyms=G3BP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pericardium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adipose tissue;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [6]
RP PROTEIN SEQUENCE OF 2-13; 18-32; 37-59; 65-76; 108-132; 230-276; 308-314;
RP 321-331; 336-370; 377-403; 430-443 AND 448-465, CLEAVAGE OF INITIATOR
RP METHIONINE, METHYLATION AT ARG-435 AND ARG-460, PHOSPHORYLATION AT SER-231
RP AND SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Calvo F.,
RA Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 248-257; 336-353; 394-403 AND 444-463, FUNCTION AS A
RP HELICASE, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=9889278; DOI=10.1093/nar/27.3.817;
RA Costa M., Ochem A., Staub A., Falaschi A.;
RT "Human DNA helicase VIII: a DNA and RNA helicase corresponding to the G3BP
RT protein, an element of the ras transduction pathway.";
RL Nucleic Acids Res. 27:817-821(1999).
RN [8]
RP FUNCTION AS AN ENDORIBONUCLEASE, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-149 AND SER-232, AND MUTAGENESIS OF SER-149 AND SER-232.
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 [9]
RP INTERACTION WITH USP10.
RX PubMed=11439350; DOI=10.1038/sj.onc.1204553;
RA Soncini C., Berdo I., Draetta G.;
RT "Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel
RT human ubiquitin specific protease.";
RL Oncogene 20:3869-3879(2001).
RN [10]
RP FUNCTION, RECRUITMENT TO STRESS GRANULES, DIMERIZATION, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-149.
RX PubMed=12642610; DOI=10.1083/jcb.200212128;
RA Tourriere H., Chebli K., Zekri L., Courselaud B., Blanchard J.-M.,
RA Bertrand E., Tazi J.;
RT "The RasGAP-associated endoribonuclease G3BP assembles stress granules.";
RL J. Cell Biol. 160:823-831(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [15]
RP INTERACTION WITH CAPRIN1, AND SUBCELLULAR LOCATION.
RX PubMed=17210633; DOI=10.1128/mcb.02300-06;
RA Solomon S., Xu Y., Wang B., David M.D., Schubert P., Kennedy D.,
RA Schrader J.W.;
RT "Distinct structural features of caprin-1 mediate its interaction with
RT G3BP-1 and its induction of phosphorylation of eukaryotic translation
RT initiation factor 2alpha, entry to cytoplasmic stress granules, and
RT selective interaction with a subset of mRNAs.";
RL Mol. Cell. Biol. 27:2324-2342(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-149; SER-232 AND
RP SER-373, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [22]
RP INTERACTION WITH SINBIS VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION).
RX PubMed=18684830; DOI=10.1128/jvi.01011-08;
RA Gorchakov R., Garmashova N., Frolova E., Frolov I.;
RT "Different types of nsP3-containing protein complexes in Sindbis virus-
RT infected cells.";
RL J. Virol. 82:10088-10101(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-376, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [27]
RP FUNCTION, INTERACTION WITH STYXL1, AND SUBCELLULAR LOCATION.
RX PubMed=20180778; DOI=10.1042/bj20091383;
RA Hinton S.D., Myers M.P., Roggero V.R., Allison L.A., Tonks N.K.;
RT "The pseudophosphatase MK-STYX interacts with G3BP and decreases stress
RT granule formation.";
RL Biochem. J. 427:349-357(2010).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-232 AND SER-373, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-232, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP INTERACTION WITH ATXN2L.
RX PubMed=23209657; DOI=10.1371/journal.pone.0050134;
RA Kaehler C., Isensee J., Nonhoff U., Terrey M., Hucho T., Lehrach H.,
RA Krobitsch S.;
RT "Ataxin-2-like is a regulator of stress granules and processing bodies.";
RL PLoS ONE 7:E50134-E50134(2012).
RN [32]
RP INTERACTION WITH SEMLIKI FOREST VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION).
RX PubMed=23087212; DOI=10.1091/mbc.e12-08-0619;
RA Panas M.D., Varjak M., Lulla A., Eng K.E., Merits A.,
RA Karlsson Hedestam G.B., McInerney G.M.;
RT "Sequestration of G3BP coupled with efficient translation inhibits stress
RT granules in Semliki Forest virus infection.";
RL Mol. Biol. Cell 23:4701-4712(2012).
RN [33]
RP INTERACTION WITH RPTOR AND SPAG5, AND SUBCELLULAR LOCATION.
RX PubMed=23953116; DOI=10.1016/j.cell.2013.07.031;
RA Thedieck K., Holzwarth B., Prentzell M.T., Boehlke C., Klasener K., Ruf S.,
RA Sonntag A.G., Maerz L., Grellscheid S.N., Kremmer E., Nitschke R.,
RA Kuehn E.W., Jonker J.W., Groen A.K., Reth M., Hall M.N., Baumeister R.;
RT "Inhibition of mTORC1 by astrin and stress granules prevents apoptosis in
RT cancer cells.";
RL Cell 154:859-874(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-250 AND SER-253, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [35]
RP FUNCTION, AND INTERACTION WITH G3BP2; USP10 AND PABPC1.
RX PubMed=23279204; DOI=10.1111/gtc.12023;
RA Matsuki H., Takahashi M., Higuchi M., Makokha G.N., Oie M., Fujii M.;
RT "Both G3BP1 and G3BP2 contribute to stress granule formation.";
RL Genes Cells 18:135-146(2013).
RN [36]
RP INTERACTION WITH SEMLIKI FOREST VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION), AND INTERACTION WITH CHIKUNGUNYA VIRUS NON-STRUCTURAL PROTEIN 3
RP (MICROBIAL INFECTION).
RX PubMed=24623412; DOI=10.1128/jvi.00439-14;
RA Panas M.D., Ahola T., McInerney G.M.;
RT "The C-terminal repeat domains of nsP3 from the Old World alphaviruses bind
RT directly to G3BP.";
RL J. Virol. 88:5888-5893(2014).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-232, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [38]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-429; ARG-435; ARG-447; ARG-460
RP AND ARG-465, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [39]
RP INTERACTION WITH SEMLIKI FOREST VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION).
RX PubMed=25658430; DOI=10.1371/journal.ppat.1004659;
RA Panas M.D., Schulte T., Thaa B., Sandalova T., Kedersha N., Achour A.,
RA McInerney G.M.;
RT "Viral and cellular proteins containing FGDF motifs bind G3BP to block
RT stress granule formation.";
RL PLoS Pathog. 11:E1004659-E1004659(2015).
RN [40]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [41]
RP INTERACTION WITH SEMLIKI FOREST VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION), AND INTERACTION WITH CHIKUNGUNYA VIRUS NON-STRUCTURAL PROTEIN 3
RP (MICROBIAL INFECTION).
RX PubMed=27383630; DOI=10.1098/rsob.160078;
RA Schulte T., Liu L., Panas M.D., Thaa B., Dickson N., Gotte B., Achour A.,
RA McInerney G.M.;
RT "Combined structural, biochemical and cellular evidence demonstrates that
RT both FGDF motifs in alphavirus nsP3 are required for efficient
RT replication.";
RL Open Biol. 6:0-0(2016).
RN [42]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-376, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [43]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLN-325, CLEAVAGE BY HUMAN ENTEROVIRUS
RP 71 PROTEASE 3C (MICROBIAL INFECTION), AND CLEAVAGE SITE.
RX PubMed=30006004; DOI=10.1016/j.virusres.2018.07.006;
RA Zhang Y., Yao L., Xu X., Han H., Li P., Zou D., Li X., Zheng L., Cheng L.,
RA Shen Y., Wang X., Wu X., Xu J., Song B., Xu S., Zhang H., Cao H.;
RT "Enterovirus 71 inhibits cytoplasmic stress granule formation during the
RT late stage of infection.";
RL Virus Res. 255:55-67(2018).
RN [44]
RP SUBCELLULAR LOCATION, AND CLEAVAGE BY FOOT-AND-MOUTH DISEASE VIRUS LEADER
RP PROTEASE (MICROBIAL INFECTION).
RX PubMed=30404792; DOI=10.1128/jvi.00922-18;
RA Visser L.J., Medina G.N., Rabouw H.H., de Groot R.J., Langereis M.A.,
RA de Los Santos T., van Kuppeveld F.J.M.;
RT "Foot-and-Mouth Disease Virus Leader Protease Cleaves G3BP1 and G3BP2 and
RT Inhibits Stress Granule Formation.";
RL J. Virol. 93:0-0(2019).
RN [45]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CGAS.
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).
RN [46]
RP FUNCTION, AND INTERACTION WITH DDX58.
RX PubMed=30804210; DOI=10.1074/jbc.ra118.005868;
RA Kim S.S., Sze L., Lam K.P.;
RT "The stress granule protein G3BP1 binds viral dsRNA and RIG-I to enhance
RT IFN-beta response.";
RL J. Biol. Chem. 294:6430-6438(2019).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-139.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the NTF2 domain of ras GTPase-activating protein-
RT binding protein 1.";
RL Submitted (FEB-2011) to the PDB data bank.
RN [48]
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 1-139, AND SUBUNIT.
RX PubMed=24324649; DOI=10.1371/journal.pone.0080947;
RA Vognsen T., Moeller I.R., Kristensen O.;
RT "Crystal structures of the human G3BP1 NTF2-like domain visualize FxFG Nup
RT repeat specificity.";
RL PLoS ONE 8:E80947-E80947(2013).
CC -!- FUNCTION: ATP- and magnesium-dependent helicase that plays an essential
CC role in innate immunity (PubMed:30510222). Participates in the DNA-
CC triggered cGAS/STING pathway by promoting the DNA binding and
CC activation of CGAS. Enhances also DDX58-induced type I interferon
CC production probably by helping DDX58 at sensing pathogenic RNA
CC (PubMed:30804210). In addition, plays an essential role in stress
CC granule formation (PubMed:12642610, PubMed:20180778, PubMed:23279204).
CC Unwinds preferentially partial DNA and RNA duplexes having a 17 bp
CC annealed portion and either a hanging 3' tail or hanging tails at both
CC 5'- and 3'-ends (PubMed:9889278). Unwinds DNA/DNA, RNA/DNA, and RNA/RNA
CC substrates with comparable efficiency (PubMed:9889278). Acts
CC unidirectionally by moving in the 5' to 3' direction along the bound
CC single-stranded DNA (PubMed:9889278). Phosphorylation-dependent
CC sequence-specific endoribonuclease in vitro (PubMed:11604510). Cleaves
CC exclusively between cytosine and adenine and cleaves MYC mRNA
CC preferentially at the 3'-UTR (PubMed:11604510).
CC {ECO:0000269|PubMed:11604510, ECO:0000269|PubMed:12642610,
CC ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:23279204,
CC ECO:0000269|PubMed:30510222, ECO:0000269|PubMed:30804210,
CC ECO:0000269|PubMed:9889278}.
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:0000269|PubMed:9889278};
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:0000269|PubMed:9889278};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9889278};
CC Note=Mg(2+) is required for helicase activity.
CC {ECO:0000269|PubMed:9889278};
CC -!- SUBUNIT: Homodimer and oligomer (PubMed:12642610, PubMed:24324649).
CC Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4
CC and G3BP1 (By similarity). Binds to the SH3 domain of Ras GTPase-
CC activating protein (RASA1) in proliferating cells (By similarity). No
CC interaction in quiescent cells (By similarity). Interacts (via NTF2-
CC like domain) with USP10 (PubMed:11439350, PubMed:23279204). Interacts
CC with RPTOR and SPAG5; this complex is increased by oxidative stress
CC (PubMed:23953116). Interacts with ATXN2L (PubMed:23209657). Interacts
CC with STYXL1 (PubMed:20180778). Interacts with CGAS (via N-terminus);
CC this interaction promotes the DNA-binding and activation of CGAS
CC (PubMed:30510222). Interacts (via C-terminus) with DDX58
CC (PubMed:30804210). Interacts (via NTF2-like domain) with CAPRIN1
CC (PubMed:17210633). Interacts with PABPC1 (PubMed:23279204).
CC {ECO:0000250|UniProtKB:P97855, ECO:0000269|PubMed:11439350,
CC ECO:0000269|PubMed:12642610, ECO:0000269|PubMed:17210633,
CC ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:23209657,
CC ECO:0000269|PubMed:23279204, ECO:0000269|PubMed:23953116,
CC ECO:0000269|PubMed:30510222, ECO:0000269|PubMed:30804210}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Semliki forest virus non-
CC structural protein 3 (via C-terminus); this interaction inhibits the
CC formation of host stress granules on viral mRNAs and the nsp3-G3BP1
CC complexes bind viral RNAs and probably orchestrate the assembly of
CC viral replication complexes. {ECO:0000269|PubMed:23087212,
CC ECO:0000269|PubMed:24623412, ECO:0000269|PubMed:25658430,
CC ECO:0000269|PubMed:27383630}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Chikungunya virus non-
CC structural protein 3 (via C-terminus); this interaction inhibits the
CC formation of host stress granules on viral mRNAs and the nsp3-G3BP1
CC complexes bind viral RNAs and probably orchestrate the assembly of
CC viral replication complexes. {ECO:0000269|PubMed:24623412,
CC ECO:0000269|PubMed:25658430}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Sindbis virus non-
CC structural protein 3 (via C-terminus); this interaction inhibits the
CC formation of host stress granules on viral mRNAs and the nsp3-G3BP1
CC complexes bind viral RNAs and probably orchestrate the assembly of
CC viral replication complexes. {ECO:0000269|PubMed:18684830}.
CC -!- INTERACTION:
CC Q13283; Q99700: ATXN2; NbExp=4; IntAct=EBI-1047359, EBI-697691;
CC Q13283; Q8WWM7: ATXN2L; NbExp=6; IntAct=EBI-1047359, EBI-948363;
CC Q13283; Q14444: CAPRIN1; NbExp=5; IntAct=EBI-1047359, EBI-1047080;
CC Q13283; P35638: DDIT3; NbExp=2; IntAct=EBI-1047359, EBI-742651;
CC Q13283; P42858: HTT; NbExp=16; IntAct=EBI-1047359, EBI-466029;
CC Q13283; Q8N122: RPTOR; NbExp=4; IntAct=EBI-1047359, EBI-1567928;
CC Q13283; Q7KZF4: SND1; NbExp=3; IntAct=EBI-1047359, EBI-1044112;
CC Q13283; Q14258: TRIM25; NbExp=2; IntAct=EBI-1047359, EBI-2341129;
CC Q13283; Q14157: UBAP2L; NbExp=3; IntAct=EBI-1047359, EBI-347762;
CC Q13283; Q14694: USP10; NbExp=11; IntAct=EBI-1047359, EBI-2510389;
CC Q13283; K9N4V7: N; Xeno; NbExp=5; IntAct=EBI-1047359, EBI-25592177;
CC Q13283; P0DTC9: N; Xeno; NbExp=54; IntAct=EBI-1047359, EBI-25475856;
CC Q13283; P59595: N; Xeno; NbExp=11; IntAct=EBI-1047359, EBI-7602718;
CC Q13283; Q809B7; Xeno; NbExp=2; IntAct=EBI-1047359, EBI-30810942;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20180778,
CC ECO:0000269|PubMed:30510222}. Perikaryon
CC {ECO:0000250|UniProtKB:P97855}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:12642610, ECO:0000269|PubMed:17210633,
CC ECO:0000269|PubMed:20180778, ECO:0000269|PubMed:23953116,
CC ECO:0000269|PubMed:30404792}. Nucleus {ECO:0000269|PubMed:11604510}.
CC Note=Cytoplasmic in proliferating cells (PubMed:11604510). Cytosolic
CC and partially nuclear in resting cells (PubMed:11604510). Recruited to
CC stress granules in response to arsenite treatment (PubMed:12642610,
CC PubMed:20180778). The unphosphorylated form is recruited to stress
CC granules (PubMed:12642610). HRAS signaling contributes to this process
CC by regulating G3BP dephosphorylation (PubMed:12642610).
CC {ECO:0000269|PubMed:11604510, ECO:0000269|PubMed:12642610,
CC ECO:0000269|PubMed:20180778}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13283-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13283-2; Sequence=VSP_056280, VSP_056281;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The NTF2 domain mediates multimerization.
CC -!- PTM: (Microbial infection) Cleaved by human enterovirus 71; this
CC cleavage induces the disassembly of cytoplasmic stress granules
CC (PubMed:30006004). Cleaved by Foot-and-mouth disease virus; this
CC cleavage suppresses the formation of cytoplasmic stress granules
CC (PubMed:30404792). {ECO:0000269|PubMed:30006004,
CC ECO:0000269|PubMed:30404792}.
CC -!- PTM: Phosphorylated exclusively on serine residues. Hyperphosphorylated
CC in quiescent fibroblasts. Hypophosphorylation leads to a decrease in
CC endoribonuclease activity (By similarity). RASA1-dependent
CC phosphorylation of Ser-149 induces a conformational change that
CC prevents self-association. Dephosphorylation after HRAS activation is
CC required for stress granule assembly. Ser-149 phosphorylation induces
CC partial nuclear localization. {ECO:0000250,
CC ECO:0000269|PubMed:11604510, ECO:0000269|PubMed:12642610,
CC ECO:0000269|Ref.6}.
CC -!- PTM: Arg-435 is dimethylated, probably to asymmetric dimethylarginine.
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DR EMBL; U32519; AAB07787.1; -; mRNA.
DR EMBL; AK300098; BAG61899.1; -; mRNA.
DR EMBL; BX647869; CAI46065.1; -; mRNA.
DR EMBL; AC091982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006997; AAH06997.1; -; mRNA.
DR CCDS; CCDS4319.1; -. [Q13283-1]
DR RefSeq; NP_005745.1; NM_005754.2. [Q13283-1]
DR RefSeq; NP_938405.1; NM_198395.1. [Q13283-1]
DR RefSeq; XP_006714812.1; XM_006714749.3.
DR RefSeq; XP_006714813.1; XM_006714750.3.
DR RefSeq; XP_016864411.1; XM_017008922.1.
DR RefSeq; XP_016864412.1; XM_017008923.1.
DR PDB; 3Q90; X-ray; 1.70 A; A/B=1-139.
DR PDB; 4FCJ; X-ray; 1.62 A; A/B=1-139.
DR PDB; 4FCM; X-ray; 2.69 A; A/B=1-139.
DR PDB; 4IIA; X-ray; 3.30 A; A=11-139.
DR PDB; 5FW5; X-ray; 1.92 A; A/B=1-139.
DR PDB; 6TA7; X-ray; 1.93 A; A/B/C/D/E/F=1-139.
DR PDB; 7SUO; X-ray; 2.35 A; A/B=2-139.
DR PDBsum; 3Q90; -.
DR PDBsum; 4FCJ; -.
DR PDBsum; 4FCM; -.
DR PDBsum; 4IIA; -.
DR PDBsum; 5FW5; -.
DR PDBsum; 6TA7; -.
DR PDBsum; 7SUO; -.
DR AlphaFoldDB; Q13283; -.
DR SMR; Q13283; -.
DR BioGRID; 115448; 577.
DR CORUM; Q13283; -.
DR ELM; Q13283; -.
DR IntAct; Q13283; 148.
DR MINT; Q13283; -.
DR STRING; 9606.ENSP00000377681; -.
DR GlyGen; Q13283; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q13283; -.
DR MetOSite; Q13283; -.
DR PhosphoSitePlus; Q13283; -.
DR SwissPalm; Q13283; -.
DR BioMuta; G3BP1; -.
DR DMDM; 14916572; -.
DR CPTAC; CPTAC-374; -.
DR EPD; Q13283; -.
DR jPOST; Q13283; -.
DR MassIVE; Q13283; -.
DR PaxDb; Q13283; -.
DR PeptideAtlas; Q13283; -.
DR PRIDE; Q13283; -.
DR ProteomicsDB; 59275; -. [Q13283-1]
DR ProteomicsDB; 62931; -.
DR Antibodypedia; 1315; 555 antibodies from 37 providers.
DR DNASU; 10146; -.
DR Ensembl; ENST00000356245.8; ENSP00000348578.3; ENSG00000145907.16. [Q13283-1]
DR Ensembl; ENST00000394123.7; ENSP00000377681.3; ENSG00000145907.16. [Q13283-1]
DR Ensembl; ENST00000522367.6; ENSP00000428926.1; ENSG00000145907.16. [Q13283-2]
DR Ensembl; ENST00000522761.6; ENSP00000430480.2; ENSG00000145907.16. [Q13283-1]
DR Ensembl; ENST00000676827.1; ENSP00000504627.1; ENSG00000145907.16. [Q13283-1]
DR Ensembl; ENST00000676978.1; ENSP00000503939.1; ENSG00000145907.16. [Q13283-1]
DR Ensembl; ENST00000677323.1; ENSP00000502880.1; ENSG00000145907.16. [Q13283-1]
DR Ensembl; ENST00000677381.1; ENSP00000504403.1; ENSG00000145907.16. [Q13283-2]
DR Ensembl; ENST00000678070.1; ENSP00000503039.1; ENSG00000145907.16. [Q13283-1]
DR Ensembl; ENST00000678101.1; ENSP00000504140.1; ENSG00000145907.16. [Q13283-1]
DR Ensembl; ENST00000678925.1; ENSP00000503699.1; ENSG00000145907.16. [Q13283-1]
DR GeneID; 10146; -.
DR KEGG; hsa:10146; -.
DR MANE-Select; ENST00000356245.8; ENSP00000348578.3; NM_005754.3; NP_005745.1.
DR UCSC; uc063iwq.1; human. [Q13283-1]
DR CTD; 10146; -.
DR DisGeNET; 10146; -.
DR GeneCards; G3BP1; -.
DR HGNC; HGNC:30292; G3BP1.
DR HPA; ENSG00000145907; Low tissue specificity.
DR MIM; 608431; gene.
DR neXtProt; NX_Q13283; -.
DR OpenTargets; ENSG00000145907; -.
DR PharmGKB; PA162389105; -.
DR VEuPathDB; HostDB:ENSG00000145907; -.
DR eggNOG; KOG0116; Eukaryota.
DR GeneTree; ENSGT00390000011365; -.
DR HOGENOM; CLU_022209_0_2_1; -.
DR InParanoid; Q13283; -.
DR OMA; RCKGPQG; -.
DR PhylomeDB; Q13283; -.
DR TreeFam; TF325464; -.
DR PathwayCommons; Q13283; -.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q13283; -.
DR SIGNOR; Q13283; -.
DR BioGRID-ORCS; 10146; 43 hits in 1080 CRISPR screens.
DR ChiTaRS; G3BP1; human.
DR GeneWiki; G3BP1; -.
DR GenomeRNAi; 10146; -.
DR Pharos; Q13283; Tbio.
DR PRO; PR:Q13283; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q13283; protein.
DR Bgee; ENSG00000145907; Expressed in ventricular zone and 207 other tissues.
DR ExpressionAtlas; Q13283; baseline and differential.
DR Genevisible; Q13283; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
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; IDA:FlyBase.
DR GO; GO:0033677; F:DNA/RNA helicase activity; IDA:FlyBase.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:FlyBase.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0062029; P:positive regulation of stress granule assembly; IMP:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0034063; P:stress granule assembly; IMP:UniProtKB.
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 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Endonuclease; Helicase;
KW Host-virus interaction; Hydrolase; Immunity; Innate immunity;
KW Isopeptide bond; Methylation; Nuclease; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..466
FT /note="Ras GTPase-activating protein-binding protein 1"
FT /id="PRO_0000194798"
FT DOMAIN 11..133
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 340..415
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 144..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 325..326
FT /note="Cleavage; by human enterovirus 71 protease 3C"
FT /evidence="ECO:0000269|PubMed:30006004"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11604510,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11604510, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 376
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 429
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 435
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 435
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 435
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315"
FT MOD_RES 447
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 460
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 460
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315"
FT MOD_RES 465
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 118..122
FT /note="GSVAN -> SLKKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_056280"
FT VAR_SEQ 123..466
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_056281"
FT MUTAGEN 149
FT /note="S->A: Cytoplasmic; no effect on stress granule
FT assembly."
FT /evidence="ECO:0000269|PubMed:11604510,
FT ECO:0000269|PubMed:12642610"
FT MUTAGEN 149
FT /note="S->E: Cytoplasmic and nuclear; no assembly of stress
FT granules; no homo-oligomerization."
FT /evidence="ECO:0000269|PubMed:11604510,
FT ECO:0000269|PubMed:12642610"
FT MUTAGEN 232
FT /note="S->A: Cytoplasmic. Partially nuclear; when
FT associated with E-149."
FT /evidence="ECO:0000269|PubMed:11604510"
FT MUTAGEN 232
FT /note="S->E: Cytoplasmic. Partially nuclear; when
FT associated with E-149."
FT /evidence="ECO:0000269|PubMed:11604510"
FT MUTAGEN 325
FT /note="Q->G: Loss of cleavage by human enterovirus 71
FT protease 3C."
FT /evidence="ECO:0000269|PubMed:30006004"
FT HELIX 8..25
FT /evidence="ECO:0007829|PDB:4FCJ"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:4FCJ"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4FCJ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:5FW5"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:4FCJ"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:4FCJ"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4FCJ"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:4FCJ"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4IIA"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:4FCJ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4FCJ"
FT STRAND 124..134
FT /evidence="ECO:0007829|PDB:4FCJ"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:6TA7"
SQ SEQUENCE 466 AA; 52164 MW; 0F9429D78E0C7F59 CRC64;
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK PADAVYGQKE
IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV
ANKFYVHNDI FRYQDEVFGG FVTEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQAVVS
NDMEEHLEEP VAEPEPDPEP EPEQEPVSEI QEEKPEPVLE ETAPEDAQKS SSPAPADIAQ
TVQEDLRTFS WASVTSKNLP PSGAVPVTGI PPHVVKVPAS QPRPESKPES QIPPQRPQRD
QRVREQRINI PPQRGPRPIR EAGEQGDIEP RRMVRHPDSH QLFIGNLPHE VDKSELKDFF
QSYGNVVELR INSGGKLPNF GFVVFDDSEP VQKVLSNRPI MFRGEVRLNV EEKKTRAARE
GDRRDNRLRG PGGPRGGLGG GMRGPPRGGM VQKPGFGVGR GLAPRQ
