Details for: G3BP1

Gene ID: 10146

Symbol: G3BP1

Ensembl ID: ENSG00000145907

Description: G3BP stress granule assembly factor 1

Associated with

Other Information

Genular Protein ID: 1151273719

Symbol: G3BP1_HUMAN

Name: Ras GTPase-activating protein-binding protein 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 8649363

Title: A Ras-GTPase-activating protein SH3-domain-binding protein.

PubMed ID: 8649363

DOI: 10.1128/mcb.16.6.2561

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 15372022

Title: The DNA sequence and comparative analysis of human chromosome 5.

PubMed ID: 15372022

DOI: 10.1038/nature02919

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9889278

Title: Human DNA helicase VIII: a DNA and RNA helicase corresponding to the G3BP protein, an element of the ras transduction pathway.

PubMed ID: 9889278

DOI: 10.1093/nar/27.3.817

PubMed ID: 11604510

Title: RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and phosphorylation-dependent localization.

PubMed ID: 11604510

DOI: 10.1128/mcb.21.22.7747-7760.2001

PubMed ID: 11439350

Title: Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease.

PubMed ID: 11439350

DOI: 10.1038/sj.onc.1204553

PubMed ID: 12642610

Title: The RasGAP-associated endoribonuclease G3BP assembles stress granules.

PubMed ID: 12642610

DOI: 10.1083/jcb.200212128

PubMed ID: 15144186

Title: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.

PubMed ID: 15144186

DOI: 10.1021/ac035352d

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17487921

Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.

PubMed ID: 17487921

DOI: 10.1002/elps.200600782

PubMed ID: 17210633

Title: Distinct structural features of caprin-1 mediate its interaction with G3BP-1 and its induction of phosphorylation of eukaryotic translation initiation factor 2alpha, entry to cytoplasmic stress granules, and selective interaction with a subset of mRNAs.

PubMed ID: 17210633

DOI: 10.1128/mcb.02300-06

PubMed ID: 17693683

Title: 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.

PubMed ID: 17693683

DOI: 10.1074/mcp.m700120-mcp200

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 18684830

Title: Different types of nsP3-containing protein complexes in Sindbis virus-infected cells.

PubMed ID: 18684830

DOI: 10.1128/jvi.01011-08

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20180778

Title: The pseudophosphatase MK-STYX interacts with G3BP and decreases stress granule formation.

PubMed ID: 20180778

DOI: 10.1042/bj20091383

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23209657

Title: Ataxin-2-like is a regulator of stress granules and processing bodies.

PubMed ID: 23209657

DOI: 10.1371/journal.pone.0050134

PubMed ID: 23087212

Title: Sequestration of G3BP coupled with efficient translation inhibits stress granules in Semliki Forest virus infection.

PubMed ID: 23087212

DOI: 10.1091/mbc.e12-08-0619

PubMed ID: 23953116

Title: Inhibition of mTORC1 by astrin and stress granules prevents apoptosis in cancer cells.

PubMed ID: 23953116

DOI: 10.1016/j.cell.2013.07.031

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23279204

Title: Both G3BP1 and G3BP2 contribute to stress granule formation.

PubMed ID: 23279204

DOI: 10.1111/gtc.12023

PubMed ID: 23785203

Title: Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses.

PubMed ID: 23785203

DOI: 10.1128/jvi.03248-12

PubMed ID: 24623412

Title: The C-terminal repeat domains of nsP3 from the Old World alphaviruses bind directly to G3BP.

PubMed ID: 24623412

DOI: 10.1128/jvi.00439-14

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25658430

Title: Viral and cellular proteins containing FGDF motifs bind G3BP to block stress granule formation.

PubMed ID: 25658430

DOI: 10.1371/journal.ppat.1004659

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27022092

Title: G3BP-Caprin1-USP10 complexes mediate stress granule condensation and associate with 40S subunits.

PubMed ID: 27022092

DOI: 10.1083/jcb.201508028

PubMed ID: 27383630

Title: Combined structural, biochemical and cellular evidence demonstrates that both FGDF motifs in alphavirus nsP3 are required for efficient replication.

PubMed ID: 27383630

DOI: 10.1098/rsob.160078

PubMed ID: 28794026

Title: Mammalian Orthoreovirus Factories Modulate Stress Granule Protein Localization by Interaction with G3BP1.

PubMed ID: 28794026

DOI: 10.1128/jvi.01298-17

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 28592527

Title: Zika virus hijacks stress granule proteins and modulates the host stress response.

PubMed ID: 28592527

DOI: 10.1128/jvi.00474-17

PubMed ID: 30006004

Title: Enterovirus 71 inhibits cytoplasmic stress granule formation during the late stage of infection.

PubMed ID: 30006004

DOI: 10.1016/j.virusres.2018.07.006

PubMed ID: 30404792

Title: Foot-and-Mouth Disease Virus Leader Protease Cleaves G3BP1 and G3BP2 and Inhibits Stress Granule Formation.

PubMed ID: 30404792

DOI: 10.1128/jvi.00922-18

PubMed ID: 30510222

Title: G3BP1 promotes DNA binding and activation of cGAS.

PubMed ID: 30510222

DOI: 10.1038/s41590-018-0262-4

PubMed ID: 30804210

Title: The stress granule protein G3BP1 binds viral dsRNA and RIG-I to enhance IFN-beta response.

PubMed ID: 30804210

DOI: 10.1074/jbc.ra118.005868

PubMed ID: 32302570

Title: Competing protein-RNA interaction networks control multiphase intracellular organization.

PubMed ID: 32302570

DOI: 10.1016/j.cell.2020.03.050

PubMed ID: 32302571

Title: G3BP1 is a tunable switch that triggers phase separation to assemble stress granules.

PubMed ID: 32302571

DOI: 10.1016/j.cell.2020.03.046

PubMed ID: 32302572

Title: RNA-Induced conformational switching and clustering of G3BP drive stress granule assembly by condensation.

PubMed ID: 32302572

DOI: 10.1016/j.cell.2020.03.049

PubMed ID: 31981475

Title: The G3BP1-family-USP10 deubiquitinase complex rescues ubiquitinated 40S subunits of ribosomes stalled in translation from lysosomal degradation.

PubMed ID: 31981475

DOI: 10.1016/j.molcel.2019.12.024

PubMed ID: 34739333

Title: Ubiquitination of G3BP1 mediates stress granule disassembly in a context-specific manner.

PubMed ID: 34739333

DOI: 10.1126/science.abf6548

PubMed ID: 34779554

Title: The stress granule protein G3BP1 promotes pre-condensation of cGAS to allow rapid responses to DNA.

PubMed ID: 34779554

DOI: 10.15252/embr.202153166

PubMed ID: 36692217

Title: Stress granule homeostasis is modulated by TRIM21-mediated ubiquitination of G3BP1 and autophagy-dependent elimination of stress granules.

PubMed ID: 36692217

DOI: 10.1080/15548627.2022.2164427

PubMed ID: 37379838

Title: QKI shuttles internal m7G-modified transcripts into stress granules and modulates mRNA metabolism.

PubMed ID: 37379838

DOI: 10.1016/j.cell.2023.05.047

PubMed ID: 24324649

Title: Crystal structures of the human G3BP1 NTF2-like domain visualize FxFG Nup repeat specificity.

PubMed ID: 24324649

DOI: 10.1371/journal.pone.0080947

PubMed ID: 36183834

Title: Tryptophan mutations in G3BP1 tune the stability of a cellular signaling hub by weakening transient interactions with Caprin1 and USP10.

PubMed ID: 36183834

DOI: 10.1016/j.jbc.2022.102552

PubMed ID: 36279435

Title: Yin and yang regulation of stress granules by Caprin-1.

PubMed ID: 36279435

DOI: 10.1073/pnas.2207975119

Sequence Information:

  • Length: 466
  • Mass: 52164
  • Checksum: 0F9429D78E0C7F59
  • Sequence:
  • 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

Genular Protein ID: 68659996

Symbol: Q6ZP53_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 307
  • Mass: 34576
  • Checksum: 02B7A3168AC798DE
  • Sequence:
  • MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK PADAVYGQKE 
    IQEEKPEPVL EETAPDDSGT FYDQAVVSND MEEHLEEPVA EPEPDPEPEP EQEPVSEIQE 
    EKPEPESKPE SQIPPQRPQR DQRVREQRIN IPPQRGPRPI REAGEQGDIE PRRMVRHPDS 
    HQLFIGNLPH EVDKSELKDF FQSYGNVVEL RINSGGKLPN FGFVVFDDSE PVQKVLSNRP 
    IMFRGEVRLN VEEKKTRAAR EGDRRDNRLR GPGGPRGGLG GGMRGPPRGG MVQKPGFGVG 
    RGLAPRQ

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.