Details for: G3BP2
Associated with
Other Information
Genular Protein ID: 2789392698
Symbol: G3BP2_HUMAN
Name: Ras GTPase-activating protein-binding protein 2
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 9734811
Title: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.
PubMed ID: 9734811
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
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: 10969074
Title: IkappaBalpha and IkappaBalpha /NF-kappa B complexes are retained in the cytoplasm through interaction with a novel partner, RasGAP SH3-binding protein 2.
PubMed ID: 10969074
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
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: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
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: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
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: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 24129315
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
PubMed ID: 24129315
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25944712
Title: N-terminome analysis of the human mitochondrial proteome.
PubMed ID: 25944712
PubMed ID: 27022092
Title: G3BP-Caprin1-USP10 complexes mediate stress granule condensation and associate with 40S subunits.
PubMed ID: 27022092
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: 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: 32302570
Title: Competing protein-RNA interaction networks control multiphase intracellular organization.
PubMed ID: 32302570
PubMed ID: 32302571
Title: G3BP1 is a tunable switch that triggers phase separation to assemble stress granules.
PubMed ID: 32302571
PubMed ID: 32302572
Title: RNA-Induced conformational switching and clustering of G3BP drive stress granule assembly by condensation.
PubMed ID: 32302572
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
PubMed ID: 26410532
Title: Crystal structure of the G3BP2 NTF2-like domain in complex with a canonical FGDF motif peptide.
PubMed ID: 26410532
PubMed ID: 16959974
Title: The consensus coding sequences of human breast and colorectal cancers.
PubMed ID: 16959974
Sequence Information:
- Length: 482
- Mass: 54121
- Checksum: 74B8EA43C0560229
- Sequence:
MVMEKPSPLL VGREFVRQYY TLLNKAPEYL HRFYGRNSSY VHGGVDASGK PQEAVYGQND IHHKVLSLNF SECHTKIRHV DAHATLSDGV VVQVMGLLSN SGQPERKFMQ TFVLAPEGSV PNKFYVHNDM FRYEDEVFGD SEPELDEESE DEVEEEQEER QPSPEPVQEN ANSGYYEAHP VTNGIEEPLE ESSHEPEPEP ESETKTEELK PQVEEKNLEE LEEKSTTPPP AEPVSLPQEP PKAFSWASVT SKNLPPSGTV SSSGIPPHVK APVSQPRVEA KPEVQSQPPR VREQRPRERP GFPPRGPRPG RGDMEQNDSD NRRIIRYPDS HQLFVGNLPH DIDENELKEF FMSFGNVVEL RINTKGVGGK LPNFGFVVFD DSEPVQRILI AKPIMFRGEV RLNVEEKKTR AARERETRGG GDDRRDIRRN DRGPGGPRGI VGGGMMRDRD GRGPPPRGGM AQKLGSGRGT GQMEGRFTGQ RR
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.