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  1. 1
    "The tyrosyl-tRNA synthetase from Escherichia coli. Complete nucleotide sequence of the structural gene."
    Barker D.G., Bruton C.J., Winter G.
    FEBS Lett. 150:419-423(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Category: Sequences.
    Strain: K12.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 412 other entries.

  3. 3
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4394 other entries.

  4. 4
    "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4273 other entries.

  5. 5
    "Characterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations."
    Lam H.-M., Winkler M.E.
    J. Bacteriol. 174:6033-6045(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
    Category: Sequences.
    Strain: K12.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  6. 6
    "D-tyrosyl RNA: formation, hydrolysis and utilization for protein synthesis."
    Calendar R., Berg P.
    J. Mol. Biol. 26:39-54(1967) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
    Category: Function.
    Strain: B.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  7. 7
    "Studies on the interaction of tyrosyl-tRNA synthetase from Escherichia coli K12 with tyrosine and with tyrosyl-AMP."
    Krajewska-Grynkiewicz K., Buonocore V., Schlesinger S.
    Biochim. Biophys. Acta 312:518-527(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT.
    Category: Function, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).
  8. 8
    "Neutron scattering studies of escherichia coli tyrosyl-trna synthetase and of its interaction with trna tyr."
    Dessen P., Zaccai G., Blanquet S.
    J. Mol. Biol. 159:651-664(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).
  9. 9
    "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 299 other entries.

  10. 10
    "Chloride affects the interaction between tyrosyl-tRNA synthetase and tRNA."
    Airas R.K.
    Biochim. Biophys. Acta 1472:51-61(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).
  11. 11
    "A mutant Escherichia coli tyrosyl-tRNA synthetase utilizes the unnatural amino acid azatyrosine more efficiently than tyrosine."
    Hamano-Takaku F., Iwama T., Saito-Yano S., Takaku K., Monden Y., Kitabatake M., Soll D., Nishimura S.
    J. Biol. Chem. 275:40324-40328(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, MUTAGENESIS OF PHE-130.
    Category: Function, Pathology & Biotech.
    Source: UniProtKB/Swiss-Prot (reviewed).
  12. 12
    "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144, IDENTIFICATION BY MASS SPECTROMETRY.
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 89 other entries.

  13. 13
    "Biochemical characterization of the lysine acetylation of tyrosyl-tRNA synthetase in Escherichia coli."
    Venkat S., Gregory C., Gan Q., Fan C.
    ChemBioChem 18:1928-1934(2017) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION, ACTIVITY REGULATION.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).
  14. 14
    "Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase."
    Kobayashi T., Takimura T., Sekine R., Vincent K., Kamata K., Sakamoto K., Nishimura S., Yokoyama S.
    J. Mol. Biol. 346:105-117(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-322 IN COMPLEX WITH TYROSINE AND TYR-AMP ANALOG, SUBUNIT.
    Category: Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  15. 15
    "Structural basis of nonnatural amino acid recognition by an engineered aminoacyl-tRNA synthetase for genetic code expansion."
    Kobayashi T., Sakamoto K., Takimura T., Sekine R., Kelly V.P., Kamata K., Nishimura S., Yokoyama S.
    Proc. Natl. Acad. Sci. U.S.A. 102:1366-1371(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-322 OF MUTANT VAL-37/CYS-195 IN COMPLEX WITH SUBSTRATE, SUBUNIT.
    Category: Pathology & Biotech, Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  16. 16
    "Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr pair by the archaeal tyrosine pair in Escherichia coli for genetic code expansion."
    Iraha F., Oki K., Kobayashi T., Ohno S., Yokogawa T., Nishikawa K., Yokoyama S., Sakamoto K.
    Nucleic Acids Res. 38:3682-3691(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-322 IN COMPLEX WITH 3-AZIDO-L-TYROSINE.
    Category: Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  17. 17
    "Interaction network containing conserved and essential protein complexes in Escherichia coli."
    Butland G., Peregrin-Alvarez J.M., Li J., Yang W., Yang X., Canadien V., Starostine A., Richards D., Beattie B., Krogan N., Davey M., Parkinson J., Greenblatt J., Emili A.
    Nature 433:531-537(2005) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P0AGJ9.

    This publication is mapped to 1271 other entries.

  18. 18
    Category: Interaction.
    Source: IntAct:P0AGJ9.

    This publication is mapped to 2443 other entries.

  19. 19
    "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis."
    Lasserre J.P., Beyne E., Pyndiah S., Lapaillerie D., Claverol S., Bonneu M.
    Electrophoresis 27:3306-3321(2006) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P0AGJ9.

    This publication is mapped to 225 other entries.

  20. 20
    "Comparative analysis of pyrimidine substituted aminoacyl-sulfamoyl nucleosides as potential inhibitors targeting class I aminoacyl-tRNA synthetases."
    Nautiyal M., De Graef S., Pang L., Gadakh B., Strelkov S.V., Weeks S.D., Van Aerschot A.
    Eur J Med Chem 173:154-166(2019) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:6HB5, PDB:6HB6, PDB:6I5Y, PDB:6HB7.

    This publication is mapped to 1 other entry.

1 to 20 of 20  Show
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