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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)

 G3BP1_HUMAN             Reviewed;         466 AA.
Q13283; Q5HYE9;
11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 186.
RecName: Full=Ras GTPase-activating protein-binding protein 1;
Short=G3BP-1;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=ATP-dependent DNA helicase VIII;
Short=hDH VIII;
AltName: Full=GAP SH3 domain-binding protein 1;
Name=G3BP1; Synonyms=G3BP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8649363; DOI=10.1128/MCB.16.6.2561;
Parker F., Maurier F., Delumeau I., Duchesne M., Faucher D.,
Debussche L., Dugue A., Schweighoffer F., Tocque B.;
"A Ras-GTPase-activating protein SH3-domain-binding protein.";
Mol. Cell. Biol. 16:2561-2569(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pericardium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Adipose tissue;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-13; 18-32; 37-59; 65-76; 108-132; 230-276;
308-314; 321-331; 336-370; 377-403; 430-443 AND 448-465, CLEAVAGE OF
INITIATOR METHIONINE, METHYLATION AT ARG-435 AND ARG-460,
PHOSPHORYLATION AT SER-231 AND SER-232, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Cervix carcinoma, Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Calvo F.,
Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 248-257; 336-353; 394-403 AND 444-463, AND
FUNCTION AS A HELICASE.
PubMed=9889278; DOI=10.1093/nar/27.3.817;
Costa M., Ochem A., Staub A., Falaschi A.;
"Human DNA helicase VIII: a DNA and RNA helicase corresponding to the
G3BP protein, an element of the ras transduction pathway.";
Nucleic Acids Res. 27:817-821(1999).
[8]
FUNCTION AS AN ENDORIBONUCLEASE, PHOSPHORYLATION AT SER-149 AND
SER-232, AND MUTAGENESIS OF SER-149 AND SER-232.
PubMed=11604510; DOI=10.1128/MCB.21.22.7747-7760.2001;
Tourriere H., Gallouzi I.-E., Chebli K., Capony J.-P., Mouaikel J.,
van der Geer P., Tazi J.;
"RasGAP-associated endoribonuclease G3Bp: selective RNA degradation
and phosphorylation-dependent localization.";
Mol. Cell. Biol. 21:7747-7760(2001).
[9]
INTERACTION WITH USP10.
PubMed=11439350; DOI=10.1038/sj.onc.1204553;
Soncini C., Berdo I., Draetta G.;
"Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a
novel human ubiquitin specific protease.";
Oncogene 20:3869-3879(2001).
[10]
RECRUITMENT TO STRESS GRANULES, DIMERIZATION, SUBCELLULAR LOCATION,
PHOSPHORYLATION, AND MUTAGENESIS OF SER-149.
PubMed=12642610; DOI=10.1083/jcb.200212128;
Tourriere H., Chebli K., Zekri L., Courselaud B., Blanchard J.-M.,
Bertrand E., Tazi J.;
"The RasGAP-associated endoribonuclease G3BP assembles stress
granules.";
J. Cell Biol. 160:823-831(2003).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-149; SER-232
AND SER-373, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-376, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-232 AND
SER-373, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-232, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
INTERACTION WITH ATXN2L.
PubMed=23209657; DOI=10.1371/journal.pone.0050134;
Kaehler C., Isensee J., Nonhoff U., Terrey M., Hucho T., Lehrach H.,
Krobitsch S.;
"Ataxin-2-like is a regulator of stress granules and processing
bodies.";
PLoS ONE 7:E50134-E50134(2012).
[29]
INTERACTION WITH RPTOR AND SPAG5, AND SUBCELLULAR LOCATION.
PubMed=23953116; DOI=10.1016/j.cell.2013.07.031;
Thedieck K., Holzwarth B., Prentzell M.T., Boehlke C., Klasener K.,
Ruf S., Sonntag A.G., Maerz L., Grellscheid S.N., Kremmer E.,
Nitschke R., Kuehn E.W., Jonker J.W., Groen A.K., Reth M., Hall M.N.,
Baumeister R.;
"Inhibition of mTORC1 by astrin and stress granules prevents apoptosis
in cancer cells.";
Cell 154:859-874(2013).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-250 AND
SER-253, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-232, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-429; ARG-435; ARG-447;
ARG-460 AND ARG-465, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-376, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[35]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-139.
Structural genomics consortium (SGC);
"Crystal structure of the NTF2 domain of ras GTPase-activating
protein-binding protein 1.";
Submitted (FEB-2011) to the PDB data bank.
-!- FUNCTION: May be a regulated effector of stress granule assembly.
Phosphorylation-dependent sequence-specific endoribonuclease in
vitro. Cleaves exclusively between cytosine and adenine and
cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-
dependent helicase. 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. Unwinds DNA/DNA,
RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts
unidirectionally by moving in the 5' to 3' direction along the
bound single-stranded DNA. {ECO:0000269|PubMed:11604510,
ECO:0000269|PubMed:9889278}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Mg(2+) is required for helicase activity.;
-!- SUBUNIT: Binds to the SH3 domain of Ras GTPase-activating protein
(RASA1) in proliferating cells. No interaction in quiescent cells
Component of a TAU mRNP complex, at least composed of IGF2BP1,
ELAVL4 and G3BP1 (By similarity). Interacts with USP10, and may
regulate it. Forms homodimers and oligomers. Interacts with RPTOR
and SPAG5; this complex is increased by oxidative stress.
Interacts with ATXN2L (PubMed:23209657). {ECO:0000250,
ECO:0000250|UniProtKB:P97855, ECO:0000269|PubMed:11439350,
ECO:0000269|PubMed:23209657, ECO:0000269|PubMed:23953116}.
-!- INTERACTION:
Q99700:ATXN2; NbExp=4; IntAct=EBI-1047359, EBI-697691;
Q8WWM7:ATXN2L; NbExp=5; IntAct=EBI-1047359, EBI-948363;
Q8N122:RPTOR; NbExp=4; IntAct=EBI-1047359, EBI-1567928;
Q7KZF4:SND1; NbExp=3; IntAct=EBI-1047359, EBI-1044112;
Q14694:USP10; NbExp=4; IntAct=EBI-1047359, EBI-2510389;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytosol. Cytoplasmic
granule. Cell membrane. Nucleus. Note=Cytoplasmic in proliferating
cells, can be recruited to the plasma membrane in exponentially
growing cells (By similarity). Cytosolic and partially nuclear in
resting cells. Recruited to stress granules (SGs) upon either
arsenite or high temperature treatment. Recruitment to SGs is
influenced by HRAS. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13283-1; Sequence=Displayed;
Name=2;
IsoId=Q13283-2; Sequence=VSP_056280, VSP_056281;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The NTF2 domain mediates multimerization.
-!- 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.
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EMBL; U32519; AAB07787.1; -; mRNA.
EMBL; AK300098; BAG61899.1; -; mRNA.
EMBL; BX647869; CAI46065.1; -; mRNA.
EMBL; AC091982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006997; AAH06997.1; -; mRNA.
CCDS; CCDS4319.1; -. [Q13283-1]
RefSeq; NP_005745.1; NM_005754.2. [Q13283-1]
RefSeq; NP_938405.1; NM_198395.1. [Q13283-1]
RefSeq; XP_006714812.1; XM_006714749.3. [Q13283-1]
RefSeq; XP_006714813.1; XM_006714750.3. [Q13283-1]
RefSeq; XP_016864411.1; XM_017008922.1. [Q13283-1]
RefSeq; XP_016864412.1; XM_017008923.1. [Q13283-1]
UniGene; Hs.3353; -.
UniGene; Hs.587054; -.
PDB; 3Q90; X-ray; 1.70 A; A/B=1-139.
PDB; 4FCJ; X-ray; 1.62 A; A/B=1-139.
PDB; 4FCM; X-ray; 2.69 A; A/B=1-139.
PDB; 4IIA; X-ray; 3.30 A; A=11-139.
PDB; 5FW5; X-ray; 1.92 A; A/B=1-139.
PDBsum; 3Q90; -.
PDBsum; 4FCJ; -.
PDBsum; 4FCM; -.
PDBsum; 4IIA; -.
PDBsum; 5FW5; -.
ProteinModelPortal; Q13283; -.
SMR; Q13283; -.
BioGrid; 115448; 126.
CORUM; Q13283; -.
ELM; Q13283; -.
IntAct; Q13283; 79.
MINT; MINT-5002789; -.
STRING; 9606.ENSP00000348578; -.
iPTMnet; Q13283; -.
PhosphoSitePlus; Q13283; -.
SwissPalm; Q13283; -.
BioMuta; G3BP1; -.
DMDM; 14916572; -.
EPD; Q13283; -.
PaxDb; Q13283; -.
PeptideAtlas; Q13283; -.
PRIDE; Q13283; -.
DNASU; 10146; -.
Ensembl; ENST00000356245; ENSP00000348578; ENSG00000145907. [Q13283-1]
Ensembl; ENST00000394123; ENSP00000377681; ENSG00000145907. [Q13283-1]
Ensembl; ENST00000520177; ENSP00000427810; ENSG00000145907. [Q13283-2]
Ensembl; ENST00000522367; ENSP00000428926; ENSG00000145907. [Q13283-2]
GeneID; 10146; -.
KEGG; hsa:10146; -.
UCSC; uc063iwq.1; human. [Q13283-1]
CTD; 10146; -.
DisGeNET; 10146; -.
EuPathDB; HostDB:ENSG00000145907.14; -.
GeneCards; G3BP1; -.
HGNC; HGNC:30292; G3BP1.
HPA; CAB037068; -.
HPA; HPA004052; -.
MIM; 608431; gene.
neXtProt; NX_Q13283; -.
OpenTargets; ENSG00000145907; -.
PharmGKB; PA162389105; -.
eggNOG; KOG0116; Eukaryota.
eggNOG; ENOG410YV57; LUCA.
GeneTree; ENSGT00390000011365; -.
HOGENOM; HOG000220838; -.
HOVERGEN; HBG007211; -.
InParanoid; Q13283; -.
KO; K17265; -.
OMA; PKDEVGW; -.
OrthoDB; EOG091G0GAN; -.
PhylomeDB; Q13283; -.
TreeFam; TF325464; -.
ChiTaRS; G3BP1; human.
GeneWiki; G3BP1; -.
GenomeRNAi; 10146; -.
PRO; PR:Q13283; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000145907; -.
CleanEx; HS_G3BP1; -.
ExpressionAtlas; Q13283; baseline and differential.
Genevisible; Q13283; HS.
GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
CDD; cd00780; NTF2; 1.
CDD; cd12463; RRM_G3BP1; 1.
InterPro; IPR034375; G3BP1.
InterPro; IPR034374; G3BP1_RRM.
InterPro; IPR002075; NTF2.
InterPro; IPR032710; NTF2-like_dom_sf.
InterPro; IPR018222; Nuclear_transport_factor_2_euk.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR10693:SF21; PTHR10693:SF21; 1.
Pfam; PF02136; NTF2; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54427; SSF54427; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50177; NTF2_DOMAIN; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA-binding; Endonuclease; Helicase;
Hydrolase; Isopeptide bond; Membrane; Methylation; Nuclease;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
RNA-binding; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}.
CHAIN 2 466 Ras GTPase-activating protein-binding
protein 1.
/FTId=PRO_0000194798.
DOMAIN 11 133 NTF2. {ECO:0000255|PROSITE-
ProRule:PRU00137}.
DOMAIN 340 415 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 144 225 Glu-rich.
COMPBIAS 430 461 Gly-rich.
MOD_RES 143 143 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:11604510}.
MOD_RES 231 231 Phosphoserine. {ECO:0000269|Ref.6}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:11604510,
ECO:0000269|Ref.6}.
MOD_RES 250 250 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 376 376 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 429 429 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 435 435 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 435 435 Dimethylated arginine; alternate.
{ECO:0000269|Ref.6}.
MOD_RES 435 435 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315,
ECO:0000269|Ref.6}.
MOD_RES 447 447 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 460 460 Dimethylated arginine; alternate.
{ECO:0000269|Ref.6}.
MOD_RES 460 460 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 460 460 Omega-N-methylated arginine; alternate.
{ECO:0000269|Ref.6}.
MOD_RES 465 465 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 376 376 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 118 122 GSVAN -> SLKKK (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_056280.
VAR_SEQ 123 466 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_056281.
MUTAGEN 149 149 S->A: Cytoplasmic; no effect on stress
granule assembly.
{ECO:0000269|PubMed:11604510,
ECO:0000269|PubMed:12642610}.
MUTAGEN 149 149 S->E: Cytoplasmic and nuclear; no
assembly of stress granules; no homo-
oligomerization.
{ECO:0000269|PubMed:11604510,
ECO:0000269|PubMed:12642610}.
MUTAGEN 232 232 S->A: Cytoplasmic. Partially nuclear;
when associated with E-149.
{ECO:0000269|PubMed:11604510}.
MUTAGEN 232 232 S->E: Cytoplasmic. Partially nuclear;
when associated with E-149.
{ECO:0000269|PubMed:11604510}.
HELIX 8 25 {ECO:0000244|PDB:4FCJ}.
HELIX 27 33 {ECO:0000244|PDB:4FCJ}.
STRAND 34 41 {ECO:0000244|PDB:4FCJ}.
STRAND 49 51 {ECO:0000244|PDB:5FW5}.
HELIX 57 67 {ECO:0000244|PDB:4FCJ}.
STRAND 74 84 {ECO:0000244|PDB:4FCJ}.
HELIX 86 88 {ECO:0000244|PDB:4FCJ}.
STRAND 90 99 {ECO:0000244|PDB:4FCJ}.
HELIX 100 102 {ECO:0000244|PDB:4IIA}.
STRAND 106 116 {ECO:0000244|PDB:4FCJ}.
STRAND 118 120 {ECO:0000244|PDB:4FCJ}.
STRAND 124 134 {ECO:0000244|PDB:4FCJ}.
TURN 135 137 {ECO:0000244|PDB:4FCM}.
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


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