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Showing Protein Ras GTPase-activating protein-binding protein 1 (HMDBP08726)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 6 metabolites
Identification
HMDB Protein ID HMDBP08726
Secondary Accession Numbers
  • 14449
Name Ras GTPase-activating protein-binding protein 1
Synonyms
  1. ATP-dependent DNA helicase VIII
  2. G3BP-1
  3. GAP SH3 domain-binding protein 1
  4. hDH VIII
Gene Name G3BP1
Protein Type Unknown
Biological Properties
General Function Involved in nucleotide binding
Specific 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.
Pathways Not Available
Reactions
Adenosine triphosphate + Water → ADP + Phosphate details
GO Classification
Biological Process
transport
Ras protein signal transduction
nucleic acid phosphodiester bond hydrolysis
Cellular Component
cytosol
cytoplasm
plasma membrane
nucleus
Component
cell part
intracellular
Function
binding
nucleotide binding
nucleic acid binding
Molecular Function
endonuclease activity
ATP-dependent RNA helicase activity
ATP binding
ATP-dependent DNA helicase activity
RNA binding
DNA binding
Process
establishment of localization
transport
Cellular Location
  1. Cell membrane
  2. Nucleus
  3. Cytoplasm
  4. Cytoplasm
  5. cytosol
Gene Properties
Chromosome Location 5
Locus 5q33.1
SNPs G3BP1
Gene Sequence 
>1401 bp
ATGGTGATGGAGAAGCCTAGTCCCCTGCTGGTCGGGCGGGAATTTGTGAGACAGTATTAC
ACACTGCTGAACCAGGCCCCAGACATGCTGCATAGATTTTATGGAAAGAACTCTTCTTAT
GTCCATGGGGGATTGGATTCAAATGGAAAGCCAGCAGATGCAGTCTACGGACAGAAAGAA
ATCCACAGGAAAGTGATGTCACAAAACTTCACCAACTGCCACACCAAGATTCGCCATGTT
GATGCTCATGCCACGCTAAATGATGGTGTGGTAGTCCAGGTGATGGGGCTTCTCTCTAAC
AACAACCAGGCTTTGAGGAGATTCATGCAAACGTTTGTCCTTGCTCCTGAGGGGTCTGTT
GCAAATAAATTCTATGTTCACAATGATATCTTCAGATACCAAGATGAGGTCTTTGGTGGG
TTTGTCACTGAGCCTCAGGAGGAGTCTGAAGAAGAAGTAGAGGAACCTGAAGAAAGACAG
CAAACACCTGAGGTGGTACCTGATGATTCTGGAACTTTCTATGATCAGGCAGTTGTCAGT
AATGACATGGAAGAACATTTAGAGGAGCCTGTTGCTGAACCAGAGCCTGATCCTGAACCA
GAACCAGAACAAGAACCTGTATCTGAAATCCAAGAGGAAAAGCCTGAGCCAGTATTAGAA
GAAACTGCCCCTGAGGATGCTCAGAAGAGTTCTTCTCCAGCACCTGCAGACATAGCTCAG
ACAGTACAGGAAGACTTGAGGACATTTTCTTGGGCATCTGTGACCAGTAAGAATCTTCCA
CCCAGTGGAGCTGTTCCAGTTACTGGGATACCACCTCATGTTGTTAAAGTACCAGCTTCA
CAGCCCCGTCCAGAGTCTAAGCCTGAATCTCAGATTCCACCACAAAGACCTCAGCGGGAT
CAAAGAGTGCGAGAACAACGAATAAATATTCCTCCCCAAAGGGGACCCAGACCAATCCGT
GAGGCTGGTGAGCAAGGTGACATTGAACCCCGAAGAATGGTGAGACACCCTGACAGTCAC
CAACTCTTCATTGGCAACCTGCCTCATGAAGTGGACAAATCAGAGCTTAAAGATTTCTTT
CAAAGTTATGGAAACGTGGTGGAGTTGCGCATTAACAGTGGTGGGAAATTACCCAATTTT
GGTTTTGTTGTGTTTGATGATTCTGAGCCTGTTCAGAAAGTCCTTAGCAACAGGCCCATC
ATGTTCAGAGGTGAGGTCCGTCTGAATGTCGAAGAGAAGAAGACTCGAGCTGCCAGGGAA
GGCGACCGACGAGATAATCGCCTTCGGGGACCTGGAGGCCCTCGAGGTGGGCTGGGTGGT
GGAATGAGAGGCCCTCCCCGTGGAGGCATGGTGCAGAAACCAGGATTTGGAGTGGGAAGG
GGGCTTGCGCCACGGCAGTGA
Protein Properties
Number of Residues 466
Molecular Weight 52164.045
Theoretical pI 5.515
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Ras GTPase-activating protein-binding protein 1
MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKE
IHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSV
ANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVS
NDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQ
TVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRD
QRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFF
QSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAARE
GDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ
GenBank ID Protein 13937794
UniProtKB/Swiss-Prot ID Q13283
UniProtKB/Swiss-Prot Entry Name G3BP1_HUMAN
PDB IDs
GenBank Gene ID BC006997
GeneCard ID G3BP1
GenAtlas ID G3BP1
HGNC ID HGNC:30292
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, 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. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  6. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  9. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  10. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  12. Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [PubMed:17487921 ]
  13. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. doi: 10.1021/pr0705441. Epub 2008 Jan 26. [PubMed:18220336 ]
  14. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  15. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, 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. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed:17693683 ]
  16. Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R: Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Nat Methods. 2005 Aug;2(8):591-8. [PubMed:16094384 ]
  17. 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. 2008 Apr;8(7):1346-61. doi: 10.1002/pmic.200700884. [PubMed:18318008 ]
  18. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed:16565220 ]
  19. Ong SE, Mittler G, Mann M: Identifying and quantifying in vivo methylation sites by heavy methyl SILAC. Nat Methods. 2004 Nov;1(2):119-26. Epub 2004 Oct 21. [PubMed:15782174 ]
  20. 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. 1996 Jun;16(6):2561-9. [PubMed:8649363 ]
  21. 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. 1999 Feb 1;27(3):817-21. [PubMed:9889278 ]
  22. Tourriere H, Gallouzi IE, Chebli K, Capony JP, Mouaikel J, van der Geer P, Tazi J: RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and phosphorylation-dependent localization. Mol Cell Biol. 2001 Nov;21(22):7747-60. [PubMed:11604510 ]
  23. 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. 2001 Jun 28;20(29):3869-79. [PubMed:11439350 ]
  24. Tourriere H, Chebli K, Zekri L, Courselaud B, Blanchard JM, Bertrand E, Tazi J: The RasGAP-associated endoribonuclease G3BP assembles stress granules. J Cell Biol. 2003 Mar 17;160(6):823-31. [PubMed:12642610 ]