G3BP1

Protein-coding gene in the species Homo sapiens
G3BP1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3Q90, 4FCJ, 4FCM, 4IIA

Identifiers
AliasesG3BP1, G3BP, HDH-VIII, G3BP stress granule assembly factor 1
External IDsOMIM: 608431; MGI: 1351465; HomoloGene: 38096; GeneCards: G3BP1; OMA:G3BP1 - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for G3BP1
Genomic location for G3BP1
Band5q33.1Start151,771,045 bp[1]
End151,812,911 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for G3BP1
Genomic location for G3BP1
Band11|11 B1.3Start55,360,511 bp[2]
End55,395,664 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ventricular zone

  • epithelium of colon

  • ganglionic eminence

  • gonad

  • islet of Langerhans

  • stromal cell of endometrium

  • Achilles tendon

  • tonsil

  • muscle of thigh

  • gastrocnemius muscle
Top expressed in
  • Ileal epithelium

  • ventricular zone

  • corneal stroma

  • lactiferous gland

  • embryo

  • embryo

  • tail of embryo

  • plantaris muscle

  • epiblast

  • extensor digitorum longus muscle
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • DNA binding
  • nucleotide binding
  • helicase activity
  • DNA helicase activity
  • protein binding
  • nucleic acid binding
  • nuclease activity
  • endonuclease activity
  • ATP binding
  • hydrolase activity
  • mRNA binding
  • RNA binding
Cellular component
  • membrane
  • focal adhesion
  • plasma membrane
  • intracellular anatomical structure
  • cytoplasmic stress granule
  • nucleus
  • cytoplasm
  • cytosol
  • perikaryon
  • ribonucleoprotein complex
Biological process
  • nucleic acid phosphodiester bond hydrolysis
  • Ras protein signal transduction
  • negative regulation of canonical Wnt signaling pathway
  • DNA duplex unwinding
  • transport
  • stress granule assembly
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10146

27041

Ensembl

ENSG00000145907

ENSMUSG00000018583

UniProt

Q13283

P97855

RefSeq (mRNA)

NM_005754
NM_198395

NM_013716

RefSeq (protein)

NP_005745
NP_938405

NP_038744

Location (UCSC)Chr 5: 151.77 – 151.81 MbChr 11: 55.36 – 55.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ras GTPase-activating protein-binding protein 1 is an enzyme that in humans is encoded by the G3BP1 gene.[5][6][7]

This gene encodes one of the DNA-unwinding enzymes which prefers partially unwound 3'-tailed substrates and can also unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. This enzyme is a member of the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. It was originally reported to bind specifically to the Ras-GTPase-activating protein by associating with its SH3 domain, but this interaction has recently been challenged.[8] Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.[7]

G3BP1 can initiate stress granule formation and labeled G3BP1 is commonly used as a marker for stress granules.[9]

Interactions

G3BP1 has been shown to interact with USP10.[10] It also interacts with SND1[5].

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000145907 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018583 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Parker F, Maurier F, Delumeau I, Duchesne M, Faucher D, Debussche L, Dugue A, Schweighoffer F, Tocque B (Jul 1996). "A Ras-GTPase-activating protein SH3-domain-binding protein". Mol Cell Biol. 16 (6): 2561–9. doi:10.1128/MCB.16.6.2561. PMC 231246. PMID 8649363.
  6. ^ Costa M, Ochem A, Staub A, Falaschi A (Mar 1999). "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 (3): 817–21. doi:10.1093/nar/27.3.817. PMC 148252. PMID 9889278.
  7. ^ a b "Entrez Gene: G3BP1 GTPase activating protein (SH3 domain) binding protein 1".
  8. ^ Annibaldi, A; Dousse, A; Martin, S; Tazi, J; Widmann, C (2011). "Revisiting G3BP1 as a RasGAP binding protein: Sensitization of tumor cells to chemotherapy by the RasGAP 317-326 sequence does not involve G3BP1". PLOS ONE. 6 (12): e29024. Bibcode:2011PLoSO...629024A. doi:10.1371/journal.pone.0029024. PMC 3242762. PMID 22205990.
  9. ^ Mahboubi, Hicham; Stochaj, Ursula (2017-04-01). "Cytoplasmic stress granules: Dynamic modulators of cell signaling and disease". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1863 (4): 884–895. doi:10.1016/j.bbadis.2016.12.022. ISSN 0925-4439. PMID 28095315.
  10. ^ Soncini, C; Berdo I; Draetta G (Jun 2001). "Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease". Oncogene. 20 (29). England: 3869–79. doi:10.1038/sj.onc.1204553. ISSN 0950-9232. PMID 11439350.

[5]Gao X, Ge L, Shao J, Su C, Zhao H, Saarikettu J, Yao X, Yao Z, Silvennoinen O, Yang J., Tudor-SN interacts with and co-localizes with G3BP in stress granules under stress conditions.FEBS Letters, Volume 584, Issue 16, Pages 3525-3532.

Further reading

  • Irvine K, Stirling R, Hume D, Kennedy D (2005). "Rasputin, more promiscuous than ever: a review of G3BP". Int. J. Dev. Biol. 48 (10): 1065–77. doi:10.1387/ijdb.041893ki. PMID 15602692.
  • Onno M, Nakamura T, Hillova J, Hill M (1993). "Rearrangement of the human tre oncogene by homologous recombination between Alu repeats of nucleotide sequences from two different chromosomes". Oncogene. 7 (12): 2519–23. PMID 1461655.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Gallouzi IE, Parker F, Chebli K, et al. (1998). "A Novel Phosphorylation-Dependent RNase Activity of GAP-SH3 Binding Protein: a Potential Link between Signal Transduction and RNA Stability". Mol. Cell. Biol. 18 (7): 3956–65. doi:10.1128/MCB.18.7.3956. PMC 108980. PMID 9632780.
  • Kociok N, Esser P, Unfried K, et al. (1999). "Upregulation of the RAS-GTPase activating protein (GAP)-binding protein (G3BP) in proliferating RPE cells". J. Cell. Biochem. 74 (2): 194–201. doi:10.1002/(SICI)1097-4644(19990801)74:2<194::AID-JCB5>3.0.CO;2-M. PMID 10404389. S2CID 8259980.
  • Soncini C, Berdo I, Draetta G (2001). "Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease". Oncogene. 20 (29): 3869–79. doi:10.1038/sj.onc.1204553. PMID 11439350.
  • Tourrière H, Gallouzi IE, Chebli K, et al. (2001). "RasGAP-Associated Endoribonuclease G3BP: Selective RNA Degradation and Phosphorylation-Dependent Localization". Mol. Cell. Biol. 21 (22): 7747–60. doi:10.1128/MCB.21.22.7747-7760.2001. PMC 99945. PMID 11604510.
  • Barnes CJ, Li F, Mandal M, et al. (2002). "Heregulin induces expression, ATPase activity, and nuclear localization of G3BP, a Ras signaling component, in human breast tumors". Cancer Res. 62 (5): 1251–5. PMID 11888885.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
  • Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Katsafanas GC, Moss B (2005). "Vaccinia virus intermediate stage transcription is complemented by Ras-GTPase-activating protein SH3 domain-binding protein (G3BP) and cytoplasmic activation/proliferation-associated protein (p137) individually or as a heterodimer". J. Biol. Chem. 279 (50): 52210–7. doi:10.1074/jbc.M411033200. PMID 15471883.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Ong SE, Mittler G, Mann M (2005). "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nat. Methods. 1 (2): 119–26. doi:10.1038/nmeth715. PMID 15782174. S2CID 6654604.


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