Full text data of G3BP1
G3BP1
(G3BP)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ras GTPase-activating protein-binding protein 1; G3BP-1; 3.6.4.12; 3.6.4.13 (ATP-dependent DNA helicase VIII; hDH VIII; GAP SH3 domain-binding protein 1)
Ras GTPase-activating protein-binding protein 1; G3BP-1; 3.6.4.12; 3.6.4.13 (ATP-dependent DNA helicase VIII; hDH VIII; GAP SH3 domain-binding protein 1)
UniProt
Q13283
ID G3BP1_HUMAN Reviewed; 466 AA.
AC Q13283;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=Ras GTPase-activating protein-binding protein 1;
DE Short=G3BP-1;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8649363;
RA Parker F., Maurier F., Delumeau I., Duchesne M., Faucher D.,
RA Debussche L., 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].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-13; 18-32; 37-59; 65-76; 108-132; 230-276;
RP 308-314; 321-331; 336-370; 377-403; 430-443 AND 448-465, CLEAVAGE OF
RP INITIATOR METHIONINE, LACK OF N-TERMINAL ACETYLATION, METHYLATION AT
RP ARG-435 AND ARG-460, PHOSPHORYLATION AT SER-231 AND SER-232, AND MASS
RP 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 [4]
RP PROTEIN SEQUENCE OF 248-257; 336-353; 394-403 AND 444-463, AND
RP FUNCTION AS A HELICASE.
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
RT G3BP protein, an element of the ras transduction pathway.";
RL Nucleic Acids Res. 27:817-821(1999).
RN [5]
RP FUNCTION AS AN ENDORIBONUCLEASE, PHOSPHORYLATION AT SER-149 AND
RP 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
RT and phosphorylation-dependent localization.";
RL Mol. Cell. Biol. 21:7747-7760(2001).
RN [6]
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
RT novel human ubiquitin specific protease.";
RL Oncogene 20:3869-3879(2001).
RN [7]
RP RECRUITMENT TO STRESS GRANULES, DIMERIZATION, SUBCELLULAR LOCATION,
RP 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
RT granules.";
RL J. Cell Biol. 160:823-831(2003).
RN [8]
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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
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
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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.,
RA Li S.-J., 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
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-149; SER-232
RP AND SER-373, AND MASS SPECTROMETRY.
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-376, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-232 AND
RP SER-373, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
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.,
RA Buerckstuemmer T., 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-232, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
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
RT protein-binding protein 1.";
RL Submitted (FEB-2011) to the PDB data bank.
CC -!- FUNCTION: May be a regulated effector of stress granule assembly.
CC Phosphorylation-dependent sequence-specific endoribonuclease in
CC vitro. Cleaves exclusively between cytosine and adenine and
CC cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-
CC dependent helicase. Unwinds preferentially partial DNA and RNA
CC duplexes having a 17 bp annealed portion and either a hanging 3'
CC tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA,
CC RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts
CC unidirectionally by moving in the 5' to 3' direction along the
CC bound single-stranded DNA.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- COFACTOR: Magnesium. Required for helicase activity.
CC -!- SUBUNIT: Binds to the SH3 domain of Ras GTPase-activating protein
CC (RASA1) in proliferating cells. No interaction in quiescent cells
CC Component of a TAU mRNP complex, at least composed of IGF2BP1,
CC ELAVL4 and G3BP1 (By similarity). Interacts with USP10, and may
CC regulate it. Forms homodimers and oligomers.
CC -!- INTERACTION:
CC Q99700:ATXN2; NbExp=4; IntAct=EBI-1047359, EBI-697691;
CC Q8WWM7:ATXN2L; NbExp=5; IntAct=EBI-1047359, EBI-948363;
CC Q7KZF4:SND1; NbExp=3; IntAct=EBI-1047359, EBI-1044112;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytosol. Cell
CC membrane. Nucleus. Note=Cytoplasmic in proliferating cells, can be
CC recruited to the plasma membrane in exponentially growing cells
CC (By similarity). Cytosolic and partially nuclear in resting cells.
CC Recruited to stress granules (SGs) upon either arsenite or high
CC temperature treatment. Recruitment to SGs is influenced by HRAS.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The NTF2 domain mediates multimerization.
CC -!- PTM: Phosphorylated exclusively on serine residues.
CC Hyperphosphorylated in quiescent fibroblasts. Hypophosphorylation
CC leads to a decrease in endoribonuclease activity (By similarity).
CC RASA1-dependent phosphorylation of Ser-149 induces a
CC conformational change that prevents self-association.
CC Dephosphorylation after HRAS activation is required for stress
CC granule assembly. Ser-149 phosphorylation induces partial nuclear
CC localization.
CC -!- PTM: Arg-435 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- SIMILARITY: Contains 1 NTF2 domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; U32519; AAB07787.1; -; mRNA.
DR EMBL; BC006997; AAH06997.1; -; mRNA.
DR RefSeq; NP_005745.1; NM_005754.2.
DR RefSeq; NP_938405.1; NM_198395.1.
DR UniGene; Hs.587054; -.
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 PDBsum; 3Q90; -.
DR PDBsum; 4FCJ; -.
DR PDBsum; 4FCM; -.
DR ProteinModelPortal; Q13283; -.
DR SMR; Q13283; 7-138, 341-406.
DR IntAct; Q13283; 50.
DR MINT; MINT-5002789; -.
DR STRING; 9606.ENSP00000348578; -.
DR PhosphoSite; Q13283; -.
DR DMDM; 14916572; -.
DR PaxDb; Q13283; -.
DR PeptideAtlas; Q13283; -.
DR PRIDE; Q13283; -.
DR DNASU; 10146; -.
DR Ensembl; ENST00000356245; ENSP00000348578; ENSG00000145907.
DR Ensembl; ENST00000394123; ENSP00000377681; ENSG00000145907.
DR GeneID; 10146; -.
DR KEGG; hsa:10146; -.
DR UCSC; uc003lum.3; human.
DR CTD; 10146; -.
DR GeneCards; GC05P151151; -.
DR HGNC; HGNC:30292; G3BP1.
DR HPA; HPA004052; -.
DR MIM; 608431; gene.
DR neXtProt; NX_Q13283; -.
DR PharmGKB; PA162389105; -.
DR eggNOG; NOG324333; -.
DR HOGENOM; HOG000220838; -.
DR HOVERGEN; HBG007211; -.
DR InParanoid; Q13283; -.
DR KO; K17265; -.
DR OMA; YDQAVVS; -.
DR PhylomeDB; Q13283; -.
DR ChiTaRS; G3BP1; human.
DR GeneWiki; G3BP1; -.
DR GenomeRNAi; 10146; -.
DR NextBio; 38391; -.
DR PRO; PR:Q13283; -.
DR ArrayExpress; Q13283; -.
DR Bgee; Q13283; -.
DR CleanEx; HS_G3BP1; -.
DR Genevestigator; Q13283; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR002075; NTF2.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell membrane;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Endonuclease; Helicase; Hydrolase; Membrane; Methylation; Nuclease;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 466 Ras GTPase-activating protein-binding
FT protein 1.
FT /FTId=PRO_0000194798.
FT DOMAIN 11 133 NTF2.
FT DOMAIN 340 415 RRM.
FT COMPBIAS 144 225 Glu-rich.
FT COMPBIAS 430 461 Gly-rich.
FT SITE 2 2 Not acetylated.
FT MOD_RES 143 143 Phosphothreonine.
FT MOD_RES 149 149 Phosphoserine.
FT MOD_RES 231 231 Phosphoserine.
FT MOD_RES 232 232 Phosphoserine.
FT MOD_RES 373 373 Phosphoserine.
FT MOD_RES 376 376 N6-acetyllysine.
FT MOD_RES 435 435 Dimethylated arginine; alternate.
FT MOD_RES 435 435 Omega-N-methylarginine; alternate.
FT MOD_RES 460 460 Dimethylated arginine; alternate.
FT MOD_RES 460 460 Omega-N-methylated arginine; alternate.
FT MUTAGEN 149 149 S->A: Cytoplasmic; no effect on stress
FT granule assembly.
FT MUTAGEN 149 149 S->E: Cytoplasmic and nuclear; no
FT assembly of stress granules; no homo-
FT oligomerization.
FT MUTAGEN 232 232 S->A: Cytoplasmic. Partially nuclear;
FT when associated with E-149.
FT MUTAGEN 232 232 S->E: Cytoplasmic. Partially nuclear;
FT when associated with E-149.
FT HELIX 8 25
FT HELIX 27 33
FT STRAND 34 41
FT STRAND 47 51
FT HELIX 57 67
FT STRAND 74 84
FT HELIX 86 88
FT STRAND 90 99
FT STRAND 106 116
FT STRAND 118 120
FT STRAND 124 134
FT TURN 135 137
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
//
ID G3BP1_HUMAN Reviewed; 466 AA.
AC Q13283;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 147.
DE RecName: Full=Ras GTPase-activating protein-binding protein 1;
DE Short=G3BP-1;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8649363;
RA Parker F., Maurier F., Delumeau I., Duchesne M., Faucher D.,
RA Debussche L., 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].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-13; 18-32; 37-59; 65-76; 108-132; 230-276;
RP 308-314; 321-331; 336-370; 377-403; 430-443 AND 448-465, CLEAVAGE OF
RP INITIATOR METHIONINE, LACK OF N-TERMINAL ACETYLATION, METHYLATION AT
RP ARG-435 AND ARG-460, PHOSPHORYLATION AT SER-231 AND SER-232, AND MASS
RP 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 [4]
RP PROTEIN SEQUENCE OF 248-257; 336-353; 394-403 AND 444-463, AND
RP FUNCTION AS A HELICASE.
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
RT G3BP protein, an element of the ras transduction pathway.";
RL Nucleic Acids Res. 27:817-821(1999).
RN [5]
RP FUNCTION AS AN ENDORIBONUCLEASE, PHOSPHORYLATION AT SER-149 AND
RP 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
RT and phosphorylation-dependent localization.";
RL Mol. Cell. Biol. 21:7747-7760(2001).
RN [6]
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
RT novel human ubiquitin specific protease.";
RL Oncogene 20:3869-3879(2001).
RN [7]
RP RECRUITMENT TO STRESS GRANULES, DIMERIZATION, SUBCELLULAR LOCATION,
RP 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
RT granules.";
RL J. Cell Biol. 160:823-831(2003).
RN [8]
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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
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
RT cancer cells: identification of phosphoproteins in the LNCaP cell
RT line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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.,
RA Li S.-J., 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
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
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
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-149; SER-232
RP AND SER-373, AND MASS SPECTROMETRY.
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP SPECTROMETRY.
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
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP SPECTROMETRY.
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-376, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-232 AND
RP SER-373, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
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.,
RA Buerckstuemmer T., 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-232, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
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
RT protein-binding protein 1.";
RL Submitted (FEB-2011) to the PDB data bank.
CC -!- FUNCTION: May be a regulated effector of stress granule assembly.
CC Phosphorylation-dependent sequence-specific endoribonuclease in
CC vitro. Cleaves exclusively between cytosine and adenine and
CC cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-
CC dependent helicase. Unwinds preferentially partial DNA and RNA
CC duplexes having a 17 bp annealed portion and either a hanging 3'
CC tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA,
CC RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts
CC unidirectionally by moving in the 5' to 3' direction along the
CC bound single-stranded DNA.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- COFACTOR: Magnesium. Required for helicase activity.
CC -!- SUBUNIT: Binds to the SH3 domain of Ras GTPase-activating protein
CC (RASA1) in proliferating cells. No interaction in quiescent cells
CC Component of a TAU mRNP complex, at least composed of IGF2BP1,
CC ELAVL4 and G3BP1 (By similarity). Interacts with USP10, and may
CC regulate it. Forms homodimers and oligomers.
CC -!- INTERACTION:
CC Q99700:ATXN2; NbExp=4; IntAct=EBI-1047359, EBI-697691;
CC Q8WWM7:ATXN2L; NbExp=5; IntAct=EBI-1047359, EBI-948363;
CC Q7KZF4:SND1; NbExp=3; IntAct=EBI-1047359, EBI-1044112;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytosol. Cell
CC membrane. Nucleus. Note=Cytoplasmic in proliferating cells, can be
CC recruited to the plasma membrane in exponentially growing cells
CC (By similarity). Cytosolic and partially nuclear in resting cells.
CC Recruited to stress granules (SGs) upon either arsenite or high
CC temperature treatment. Recruitment to SGs is influenced by HRAS.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The NTF2 domain mediates multimerization.
CC -!- PTM: Phosphorylated exclusively on serine residues.
CC Hyperphosphorylated in quiescent fibroblasts. Hypophosphorylation
CC leads to a decrease in endoribonuclease activity (By similarity).
CC RASA1-dependent phosphorylation of Ser-149 induces a
CC conformational change that prevents self-association.
CC Dephosphorylation after HRAS activation is required for stress
CC granule assembly. Ser-149 phosphorylation induces partial nuclear
CC localization.
CC -!- PTM: Arg-435 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- SIMILARITY: Contains 1 NTF2 domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; U32519; AAB07787.1; -; mRNA.
DR EMBL; BC006997; AAH06997.1; -; mRNA.
DR RefSeq; NP_005745.1; NM_005754.2.
DR RefSeq; NP_938405.1; NM_198395.1.
DR UniGene; Hs.587054; -.
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 PDBsum; 3Q90; -.
DR PDBsum; 4FCJ; -.
DR PDBsum; 4FCM; -.
DR ProteinModelPortal; Q13283; -.
DR SMR; Q13283; 7-138, 341-406.
DR IntAct; Q13283; 50.
DR MINT; MINT-5002789; -.
DR STRING; 9606.ENSP00000348578; -.
DR PhosphoSite; Q13283; -.
DR DMDM; 14916572; -.
DR PaxDb; Q13283; -.
DR PeptideAtlas; Q13283; -.
DR PRIDE; Q13283; -.
DR DNASU; 10146; -.
DR Ensembl; ENST00000356245; ENSP00000348578; ENSG00000145907.
DR Ensembl; ENST00000394123; ENSP00000377681; ENSG00000145907.
DR GeneID; 10146; -.
DR KEGG; hsa:10146; -.
DR UCSC; uc003lum.3; human.
DR CTD; 10146; -.
DR GeneCards; GC05P151151; -.
DR HGNC; HGNC:30292; G3BP1.
DR HPA; HPA004052; -.
DR MIM; 608431; gene.
DR neXtProt; NX_Q13283; -.
DR PharmGKB; PA162389105; -.
DR eggNOG; NOG324333; -.
DR HOGENOM; HOG000220838; -.
DR HOVERGEN; HBG007211; -.
DR InParanoid; Q13283; -.
DR KO; K17265; -.
DR OMA; YDQAVVS; -.
DR PhylomeDB; Q13283; -.
DR ChiTaRS; G3BP1; human.
DR GeneWiki; G3BP1; -.
DR GenomeRNAi; 10146; -.
DR NextBio; 38391; -.
DR PRO; PR:Q13283; -.
DR ArrayExpress; Q13283; -.
DR Bgee; Q13283; -.
DR CleanEx; HS_G3BP1; -.
DR Genevestigator; Q13283; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR002075; NTF2.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell membrane;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Endonuclease; Helicase; Hydrolase; Membrane; Methylation; Nuclease;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 466 Ras GTPase-activating protein-binding
FT protein 1.
FT /FTId=PRO_0000194798.
FT DOMAIN 11 133 NTF2.
FT DOMAIN 340 415 RRM.
FT COMPBIAS 144 225 Glu-rich.
FT COMPBIAS 430 461 Gly-rich.
FT SITE 2 2 Not acetylated.
FT MOD_RES 143 143 Phosphothreonine.
FT MOD_RES 149 149 Phosphoserine.
FT MOD_RES 231 231 Phosphoserine.
FT MOD_RES 232 232 Phosphoserine.
FT MOD_RES 373 373 Phosphoserine.
FT MOD_RES 376 376 N6-acetyllysine.
FT MOD_RES 435 435 Dimethylated arginine; alternate.
FT MOD_RES 435 435 Omega-N-methylarginine; alternate.
FT MOD_RES 460 460 Dimethylated arginine; alternate.
FT MOD_RES 460 460 Omega-N-methylated arginine; alternate.
FT MUTAGEN 149 149 S->A: Cytoplasmic; no effect on stress
FT granule assembly.
FT MUTAGEN 149 149 S->E: Cytoplasmic and nuclear; no
FT assembly of stress granules; no homo-
FT oligomerization.
FT MUTAGEN 232 232 S->A: Cytoplasmic. Partially nuclear;
FT when associated with E-149.
FT MUTAGEN 232 232 S->E: Cytoplasmic. Partially nuclear;
FT when associated with E-149.
FT HELIX 8 25
FT HELIX 27 33
FT STRAND 34 41
FT STRAND 47 51
FT HELIX 57 67
FT STRAND 74 84
FT HELIX 86 88
FT STRAND 90 99
FT STRAND 106 116
FT STRAND 118 120
FT STRAND 124 134
FT TURN 135 137
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
//
MIM
608431
*RECORD*
*FIELD* NO
608431
*FIELD* TI
*608431 GTPase-ACTIVATING PROTEIN SH3 DOMAIN-BINDING PROTEIN 1; G3BP1
;;RAS-GTPase-ACTIVATING PROTEIN SH3 DOMAIN-BINDING PROTEIN;;
read moreGAP SH3 DOMAIN-BINDING PROTEIN; G3BP;;
HUMAN DNA HELICASE VIII;;
HDH-VIII
*FIELD* TX
CLONING
Parker et al. (1996) identified G3bp through its binding to the SH3
domain of GAP (RASA1; 139150) in lysates of exponentially growing
Chinese hamster lung fibroblasts engineered to overexpress human
epidermal growth factor receptor (131550). By PCR using primers designed
from the peptide sequence, followed by screening a placenta cDNA library
screening, they cloned human G3BP. The deduced 466-amino acid protein
has a calculated molecular mass of 52 kD. G3BP contains an acid-rich
amino acid domain between amino acids 144 and 221, followed by 2
consensus RNA-binding motifs and several C-terminal arg/gly-rich boxes,
which are also implicated in RNA binding. Northern blot analysis
detected a 3.3-kb G3BP transcript in all fetal and adult tissues
examined, with prominent expression in adult skeletal muscle.
Immunofluorescence analysis of several mammalian cell lines localized
G3BP within the cytoplasm. The staining intensity varied between cells,
but the intensity and localization were unaltered under various
experimental conditions. G3bp purified from Chinese hamster lung
fibroblasts and recombinant G3BP expressed in insect cells both showed
apparent molecular masses of 68 kD.
GENE FUNCTION
Parker et al. (1996) confirmed that recombinant G3BP expressed in insect
cells bound to the SH3 domain of GAP. G3BP coimmunoprecipitated with GAP
only when cells were proliferating. Parker et al. (1996) concluded that
recruitment of the GAP-G3BP complex occurs only when Ras (190020) is in
its activated conformation.
Costa et al. (1999) purified human G3BP, which they called HDH-VIII, in
a systematic study of DNA-unwinding enzymes present in HeLa cells. They
found that G3BP could unwind DNA and RNA partial duplexes in an ATP- and
Mg(2+)-dependent manner, even though it lacks the canonical helicase
domain. G3BP preferentially unwound partial duplex substrates having a
17-bp annealed portion and either a hanging 3-prime tail or hanging
tails at both the 3-prime and 5-prime ends. It unwound DNA/DNA, RNA/DNA,
and RNA/RNA substrates with comparable efficiency. G3BP failed to unwind
a substrate with a 40-bp annealed section. It appeared to unwind
unidirectionally by moving in the 5-prime-to-3-prime direction along the
bound single-stranded DNA.
Tourriere et al. (2003) found that endogenous G3bp localized in large
cytoplasmic structures resembling stress granules (SGs) in COS cells
following exposure to either arsenite or high temperature. They found
that the N-terminal NTF2 (605813)-like domain and the RNA-binding
domains of G3BP mediated its recruitment to SGs. Overexpression of G3BP
induced SG assembly, whereas overexpression of only the central
RasGAP-binding domain inhibited SG assembly. Within the RasGAP-binding
domain, dephosphorylation of a critical serine (ser149) was induced by
arsenite treatments. A phosphomimetic mutant at this position failed to
oligomerize and to assemble SGs, whereas a nonphosphorylatable G3BP
mutant did both. Tourriere et al. (2003) concluded that G3BP is an
effector of SG assembly and that Ras signaling contributes to this
process by regulating G3BP dephosphorylation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the G3BP
gene to chromosome 5 (TMAP SHGC-133085).
*FIELD* RF
1. 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.
2. 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. Molec. Cell. Biol. 16: 2561-2569,
1996.
3. 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.
*FIELD* CD
Patricia A. Hartz: 1/29/2004
*FIELD* ED
alopez: 08/26/2011
mgross: 1/29/2004
*RECORD*
*FIELD* NO
608431
*FIELD* TI
*608431 GTPase-ACTIVATING PROTEIN SH3 DOMAIN-BINDING PROTEIN 1; G3BP1
;;RAS-GTPase-ACTIVATING PROTEIN SH3 DOMAIN-BINDING PROTEIN;;
read moreGAP SH3 DOMAIN-BINDING PROTEIN; G3BP;;
HUMAN DNA HELICASE VIII;;
HDH-VIII
*FIELD* TX
CLONING
Parker et al. (1996) identified G3bp through its binding to the SH3
domain of GAP (RASA1; 139150) in lysates of exponentially growing
Chinese hamster lung fibroblasts engineered to overexpress human
epidermal growth factor receptor (131550). By PCR using primers designed
from the peptide sequence, followed by screening a placenta cDNA library
screening, they cloned human G3BP. The deduced 466-amino acid protein
has a calculated molecular mass of 52 kD. G3BP contains an acid-rich
amino acid domain between amino acids 144 and 221, followed by 2
consensus RNA-binding motifs and several C-terminal arg/gly-rich boxes,
which are also implicated in RNA binding. Northern blot analysis
detected a 3.3-kb G3BP transcript in all fetal and adult tissues
examined, with prominent expression in adult skeletal muscle.
Immunofluorescence analysis of several mammalian cell lines localized
G3BP within the cytoplasm. The staining intensity varied between cells,
but the intensity and localization were unaltered under various
experimental conditions. G3bp purified from Chinese hamster lung
fibroblasts and recombinant G3BP expressed in insect cells both showed
apparent molecular masses of 68 kD.
GENE FUNCTION
Parker et al. (1996) confirmed that recombinant G3BP expressed in insect
cells bound to the SH3 domain of GAP. G3BP coimmunoprecipitated with GAP
only when cells were proliferating. Parker et al. (1996) concluded that
recruitment of the GAP-G3BP complex occurs only when Ras (190020) is in
its activated conformation.
Costa et al. (1999) purified human G3BP, which they called HDH-VIII, in
a systematic study of DNA-unwinding enzymes present in HeLa cells. They
found that G3BP could unwind DNA and RNA partial duplexes in an ATP- and
Mg(2+)-dependent manner, even though it lacks the canonical helicase
domain. G3BP preferentially unwound partial duplex substrates having a
17-bp annealed portion and either a hanging 3-prime tail or hanging
tails at both the 3-prime and 5-prime ends. It unwound DNA/DNA, RNA/DNA,
and RNA/RNA substrates with comparable efficiency. G3BP failed to unwind
a substrate with a 40-bp annealed section. It appeared to unwind
unidirectionally by moving in the 5-prime-to-3-prime direction along the
bound single-stranded DNA.
Tourriere et al. (2003) found that endogenous G3bp localized in large
cytoplasmic structures resembling stress granules (SGs) in COS cells
following exposure to either arsenite or high temperature. They found
that the N-terminal NTF2 (605813)-like domain and the RNA-binding
domains of G3BP mediated its recruitment to SGs. Overexpression of G3BP
induced SG assembly, whereas overexpression of only the central
RasGAP-binding domain inhibited SG assembly. Within the RasGAP-binding
domain, dephosphorylation of a critical serine (ser149) was induced by
arsenite treatments. A phosphomimetic mutant at this position failed to
oligomerize and to assemble SGs, whereas a nonphosphorylatable G3BP
mutant did both. Tourriere et al. (2003) concluded that G3BP is an
effector of SG assembly and that Ras signaling contributes to this
process by regulating G3BP dephosphorylation.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the G3BP
gene to chromosome 5 (TMAP SHGC-133085).
*FIELD* RF
1. 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.
2. 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. Molec. Cell. Biol. 16: 2561-2569,
1996.
3. 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.
*FIELD* CD
Patricia A. Hartz: 1/29/2004
*FIELD* ED
alopez: 08/26/2011
mgross: 1/29/2004