glutamyl-prolyl-tRNA synthetase 1

mammalian protein found in Homo sapiens
Protein protein Q21122161
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Summary

glutamyl-prolyl-tRNA synthetase 1 is a protein[1]. It is known by 14 alternative names across languages and contexts.[2]

Key Facts

  • Part of: Proline-tRNA ligase, class IIa, archaeal-type[3], Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain superfamily[4], Rossmann fold[5], Anticodon-binding domain superfamily[6], glutamyl-tRNA synthetase, archaeal/eukaryotic cytosolic[7], Ribosomal protein L25/Gln-tRNA synthetase, N-terminal[8], Prolyl-tRNA synthetase, class II[9], S15/NS1, RNA-binding[10], Glutathione S-transferase, C-terminal domain superfamily[11], Glutamyl/glutaminyl-tRNA synthetase, class Ib, anti-codon binding domain, protein family[12], Glutathione S-transferase, C-terminal domain, protein family[13], Prolyl-tRNA synthetase, catalytic domain, protein family[14], Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain, protein family[15], Aminoacyl-tRNA synthetase, class II (G/ P/ S/T), protein family[16]
  • Has part(s): glutamyl/glutaminyl-tRNA synthetase, class Ib, anti-codon binding domain[17], aminoacyl-tRNA synthetase, class I, conserved site[18], glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain[19], Anticodon-binding[20], Prolyl-tRNA synthetase, catalytic domain[21], Glutathione S-transferase, C-terminal[22], WHEP-TRS domain[23], Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)[24], Aminoacyl-tRNA synthetase, class II domain[25], Proline-tRNA ligase, class II, C-terminal[26]
  • Molecular function: nucleotide binding[27], protein binding[28], RNA stem-loop binding[29], ATP binding[30], catalytic activity[31], ligase activity[32], aminoacyl-tRNA ligase activity[33], GTPase binding[34], RNA binding[35], glutamate-tRNA ligase activity[36], proline-tRNA ligase activity[37], zinc ion binding[38], protein homodimerization activity[39], metal ion binding[40]
  • Cell component: membrane[41], GAIT complex[42], cytoplasm[43], aminoacyl-tRNA synthetase multienzyme complex[44], cytosol[45], plasma membrane[46], ribonucleoprotein complex[47]
  • Biological process: regulation of translation[48], tRNA aminoacylation[49], metabolism[50], protein biosynthesis[51], tRNA aminoacylation for protein translation[52], negative regulation of translation[53], cellular response to interferon-gamma[54], glutamyl-tRNA aminoacylation[55], prolyl-tRNA aminoacylation[56], cellular response to insulin stimulus[57]

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [3] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  2. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [6] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [8] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [9] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [11] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [12] ↑ . wikidata.org.
  11. [13] ↑ . wikidata.org.
  12. [14] ↑ . wikidata.org.
  13. [15] ↑ . wikidata.org.
  14. [16] ↑ . wikidata.org.
  15. [17] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  26. [28] ↑ . Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  27. [29] ↑ . Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  28. [30] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  29. [31] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  30. [32] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  31. [33] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  32. [34] ↑ . Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  33. [35] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  34. [36] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  35. [37] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  36. [38] ↑ . Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  37. [39] ↑ . Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  38. [40] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  39. [41] ↑ . Defining the membrane proteome of NK cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  40. [42] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  41. [43] ↑ . The human EPRS locus (formerly the QARS locus): a gene encoding a class I and a class II aminoacyl-tRNA synthetase. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  42. [44] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  43. [45] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  44. [46] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  45. [47] ↑ . Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  46. [48] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  47. [49] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  48. [50] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  49. [51] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  50. [52] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  51. [53] ↑ . Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  52. [54] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  53. [55] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  54. [56] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  55. [57] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikidata aliases. wikidata.org.

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Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 13w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Found in taxon → Homo sapiens
    Mesh tree code → D08.811.464.263.200.250
    Wikidata description → mammalian protein found in Homo sapiens
    Pdb structure id → 1FYJ, 4HVC, 4K86 +6
    + 14 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 6.1.1.15, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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