EPRS: Difference between revisions

Jump to navigation Jump to search
Newer edit →
VisualWikitext
WikiBot (talk | contribs)
Bots, Bureaucrats, bureaucrats, interwiki, nocaptcha, Administrators
57,550 edits
m Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}})
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Bifunctional aminoacyl-tRNA synthetase''' is an [[enzyme]] that in humans is encoded by the ''EPRS'' [[gene]].<ref name="pmid1988429">{{cite journal | vauthors = Fett R, Knippers R | title = The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors | journal = J Biol Chem | volume = 266 | issue = 3 | pages = 1448–55 |date=February 1991 | pmid = 1988429 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2058| accessdate = }}</ref>
| update_page = yes
 
| require_manual_inspection = no
== Gene ==
| update_protein_box = yes
 
| update_summary = yes
Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.<ref name="entrez"/>
| update_citations = yes
 
}}
== Function ==
 
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species.<ref name="entrez"/>
 
Phosphorylation of EPRS is reported to be essential for the formation of GAIT (Gamma-interferon Activated Inhibitor of Translation) complex that regulates the translation of multiple genes in [[monocyte]]s and [[macrophage]]s.<ref name="pmid19647514">{{cite journal | vauthors = Arif A, Jia J, Mukhopadhyay R, Willard B, Kinter M, Fox PL | title = Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity | journal = Mol. Cell | volume = 35 | issue = 2 | pages = 164–80 |date=July 2009 | pmid = 19647514 | doi = 10.1016/j.molcel.2009.05.028 | url = | issn = | pmc = 2752289 }}</ref>


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image = PBB_Protein_EPRS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fyj.
| PDB = {{PDB2|1fyj}}
| Name = Glutamyl-prolyl-tRNA synthetase
| HGNCid = 3418
| Symbol = EPRS
| AltSymbols =; DKFZp313B047; EARS; PARS; PIG32; QARS; QPRS
| OMIM = 138295
| ECnumber = 
| Homologene = 5870
| MGIid = 97838
| GeneAtlas_image1 = PBB_GE_EPRS_200843_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004818 |text = glutamate-tRNA ligase activity}} {{GNF_GO|id=GO:0004827 |text = proline-tRNA ligase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006424 |text = glutamyl-tRNA aminoacylation}} {{GNF_GO|id=GO:0006433 |text = prolyl-tRNA aminoacylation}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2058
    | Hs_Ensembl = ENSG00000136628
    | Hs_RefseqProtein = NP_004437
    | Hs_RefseqmRNA = NM_004446
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 218208566
    | Hs_GenLoc_end = 218286623
    | Hs_Uniprot = P07814
    | Mm_EntrezGene = 107508
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = XM_001004369
    | Mm_RefseqProtein = XP_001004369
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Glutamyl-prolyl-tRNA synthetase''', also known as '''EPRS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2058| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
EPRS has been shown to [[Protein-protein interaction|interact]] with [[POU2F1]],<ref name=pmid9537509>{{cite journal |last=Nie |first=J |author2=Sakamoto S |author3=Song D |author4=Qu Z |author5=Ota K |author6=Taniguchi T  |date=March 1998  |title=Interaction of Oct–1 and automodification domain of poly(ADP-ribose) synthetase |journal=FEBS Lett. |volume=424 |issue=1–2 |pages=27–32 | pmid = 9537509 |doi=10.1016/S0014-5793(98)00131-8 }}</ref> [[Heat shock protein 90kDa alpha (cytosolic), member A1]]<ref name=pmid10913161>{{cite journal |last=Kang |first=J |author2=Kim T |author3=Ko Y G |author4=Rho S B |author5=Park S G |author6=Kim M J |author7=Kwon H J |author8=Kim S  |date=October 2000  |title=Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases |journal=J. Biol. Chem. |volume=275 |issue=41 |pages=31682–8 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10913161 |doi = 10.1074/jbc.M909965199 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[IARS]].<ref name=pmid9556618>{{cite journal |last=Rho |first=S B |author2=Lee J S |author3=Jeong E J |author4=Kim K S |author5=Kim Y G |author6=Kim S  |date=May 1998 |title=A multifunctional repeated motif is present in human bifunctional tRNA synthetase |journal=J. Biol. Chem. |volume=273 |issue=18 |pages=11267–73 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9556618 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.273.18.11267 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text = Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species. Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2058| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Kaiser E, Eberhard D, Knippers R |title=Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase. |journal=J. Mol. Evol. |volume=34 |issue= 1 |pages= 45-53 |year= 1992 |pmid= 1556743 |doi=  }}
*{{cite journal  | vauthors=Kaiser E, Eberhard D, Knippers R |title=Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase |journal=J. Mol. Evol. |volume=34 |issue= 1 |pages= 45–53 |year= 1992 |pmid= 1556743 |doi=10.1007/BF00163851 }}
*{{cite journal  | author=Norcum MT |title=Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15398-405 |year= 1991 |pmid= 1651330 |doi=  }}
*{{cite journal  | author=Norcum MT |title=Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15398–405 |year= 1991 |pmid= 1651330 |doi=  }}
*{{cite journal  | author=Cerini C, Kerjan P, Astier M, ''et al.'' |title=A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. |journal=EMBO J. |volume=10 |issue= 13 |pages= 4267-77 |year= 1992 |pmid= 1756734 |doi=  }}
*{{cite journal  | vauthors=Cerini C, Kerjan P, Astier M |title=A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase |journal=EMBO J. |volume=10 |issue= 13 |pages= 4267–77 |year= 1992 |pmid= 1756734 |doi=  | pmc=453179  |display-authors=etal}}
*{{cite journal  | author=Fett R, Knippers R |title=The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors. |journal=J. Biol. Chem. |volume=266 |issue= 3 |pages= 1448-55 |year= 1991 |pmid= 1988429 |doi=  }}
*{{cite journal  | vauthors=Kunze N, Bittler E, Fett R |title=The human QARS locus: assignment of the human gene for glutaminyl-tRNA synthetase to chromosome 1q32-42 |journal=Hum. Genet. |volume=85 |issue= 5 |pages= 527–30 |year= 1990 |pmid= 2227938 |doi=10.1007/BF00194231 |display-authors=etal}}
*{{cite journal  | author=Kunze N, Bittler E, Fett R, ''et al.'' |title=The human QARS locus: assignment of the human gene for glutaminyl-tRNA synthetase to chromosome 1q32-42. |journal=Hum. Genet. |volume=85 |issue= 5 |pages= 527-30 |year= 1990 |pmid= 2227938 |doi=  }}
*{{cite journal  | vauthors=Thömmes P, Fett R, Schray B |title=The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes |journal=Nucleic Acids Res. |volume=16 |issue= 12 |pages= 5391–406 |year= 1988 |pmid= 3290852 |doi=10.1093/nar/16.12.5391  | pmc=336774 |display-authors=etal}}
*{{cite journal  | author=Thömmes P, Fett R, Schray B, ''et al.'' |title=The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes. |journal=Nucleic Acids Res. |volume=16 |issue= 12 |pages= 5391-406 |year= 1988 |pmid= 3290852 |doi= }}
*{{cite journal  | vauthors=Kaiser E, Hu B, Becher S |title=The human EPRS locus (formerly the QARS locus): a gene encoding a class I and a class II aminoacyl-tRNA synthetase |journal=Genomics |volume=19 |issue= 2 |pages= 280–90 |year= 1994 |pmid= 8188258 |doi= 10.1006/geno.1994.1059 |display-authors=etal}}
*{{cite journal  | author=Kaiser E, Hu B, Becher S, ''et al.'' |title=The human EPRS locus (formerly the QARS locus): a gene encoding a class I and a class II aminoacyl-tRNA synthetase. |journal=Genomics |volume=19 |issue= 2 |pages= 280-90 |year= 1994 |pmid= 8188258 |doi= 10.1006/geno.1994.1059 }}
*{{cite journal  | vauthors=Hillier LD, Lennon G, Becker M |title=Generation and analysis of 280,000 human expressed sequence tags |journal=Genome Res. |volume=6 |issue= 9 |pages= 807–28 |year= 1997 |pmid= 8889549 |doi=10.1101/gr.6.9.807  |display-authors=etal}}
*{{cite journal  | author=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi=  }}
*{{cite journal  | vauthors=Rho SB, Lee JS, Jeong EJ |title=A multifunctional repeated motif is present in human bifunctional tRNA synthetase |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11267–73 |year= 1998 |pmid= 9556618 |doi=10.1074/jbc.273.18.11267 |display-authors=etal}}
*{{cite journal  | author=Rho SB, Lee JS, Jeong EJ, ''et al.'' |title=A multifunctional repeated motif is present in human bifunctional tRNA synthetase. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11267-73 |year= 1998 |pmid= 9556618 |doi= }}
*{{cite journal  | vauthors=Quevillon S, Robinson JC, Berthonneau E |title=Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein |journal=J. Mol. Biol. |volume=285 |issue= 1 |pages= 183–95 |year= 1999 |pmid= 9878398 |doi= 10.1006/jmbi.1998.2316 |display-authors=etal}}
*{{cite journal  | author=Quevillon S, Robinson JC, Berthonneau E, ''et al.'' |title=Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. |journal=J. Mol. Biol. |volume=285 |issue= 1 |pages= 183-95 |year= 1999 |pmid= 9878398 |doi= 10.1006/jmbi.1998.2316 }}
*{{cite journal  | vauthors=Kang J, Kim T, Ko YG |title=Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31682–8 |year= 2000 |pmid= 10913161 |doi= 10.1074/jbc.M909965199 |display-authors=etal}}
*{{cite journal  | author=Kang J, Kim T, Ko YG, ''et al.'' |title=Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31682-8 |year= 2000 |pmid= 10913161 |doi= 10.1074/jbc.M909965199 }}
*{{cite journal  | vauthors=Jeong EJ, Hwang GS, Kim KH |title=Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats |journal=Biochemistry |volume=39 |issue= 51 |pages= 15775–82 |year= 2001 |pmid= 11123902 |doi=10.1021/bi001393h  |display-authors=etal}}
*{{cite journal  | author=Jeong EJ, Hwang GS, Kim KH, ''et al.'' |title=Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. |journal=Biochemistry |volume=39 |issue= 51 |pages= 15775-82 |year= 2001 |pmid= 11123902 |doi= }}
*{{cite journal  | vauthors=Sang Lee J, Gyu Park S, Park H |title=Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 1 |pages= 158–64 |year= 2002 |pmid= 11829477 |doi= 10.1006/bbrc.2002.6398 |display-authors=etal}}
*{{cite journal  | author=Sang Lee J, Gyu Park S, Park H, ''et al.'' |title=Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 1 |pages= 158-64 |year= 2002 |pmid= 11829477 |doi= 10.1006/bbrc.2002.6398 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Bouwmeester T, Bauch A, Ruffner H |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 |display-authors=etal}}
*{{cite journal  | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal  | vauthors=Beausoleil SA, Jedrychowski M, Schwartz D |title=Large-scale characterization of HeLa cell nuclear phosphoproteins |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101  | pmc=514446 |display-authors=etal}}
*{{cite journal  | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{cite journal  | vauthors=Sampath P, Mazumder B, Seshadri V |title=Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation |journal=Cell |volume=119 |issue= 2 |pages= 195–208 |year= 2004 |pmid= 15479637 |doi= 10.1016/j.cell.2004.09.030 |display-authors=etal}}
*{{cite journal  | author=Sampath P, Mazumder B, Seshadri V, ''et al.'' |title=Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation. |journal=Cell |volume=119 |issue= 2 |pages= 195-208 |year= 2004 |pmid= 15479637 |doi= 10.1016/j.cell.2004.09.030 }}
*{{cite journal  | vauthors=Kato T, Daigo Y, Hayama S |title=A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis |journal=Cancer Res. |volume=65 |issue= 13 |pages= 5638–46 |year= 2005 |pmid= 15994936 |doi= 10.1158/0008-5472.CAN-05-0600 |display-authors=etal}}
*{{cite journal  | author=Kato T, Daigo Y, Hayama S, ''et al.'' |title=A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis. |journal=Cancer Res. |volume=65 |issue= 13 |pages= 5638-46 |year= 2005 |pmid= 15994936 |doi= 10.1158/0008-5472.CAN-05-0600 }}
*{{cite journal  | vauthors=Beausoleil SA, Villén J, Gerber SA |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285–92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 |display-authors=etal}}
*{{cite journal  | author=Beausoleil SA, Villén J, Gerber SA, ''et al.'' |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization. |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285-92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 }}
*{{cite journal  | vauthors=Ewing RM, Chu P, Elisma F |title=Large-scale mapping of human protein-protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue= 1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 |display-authors=etal}}
*{{cite journal | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=2058}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = no
| update_citations = yes
}}


{{protein-stub}}
{{gene-1-stub}}
{{WikiDoc Sources}}

Revision as of 00:33, 31 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.[1][2]

Gene

Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined.[2]

Function

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species.[2]

Phosphorylation of EPRS is reported to be essential for the formation of GAIT (Gamma-interferon Activated Inhibitor of Translation) complex that regulates the translation of multiple genes in monocytes and macrophages.[3]

Interactions

EPRS has been shown to interact with POU2F1,[4] Heat shock protein 90kDa alpha (cytosolic), member A1[5] and IARS.[6]

References

  1. ↑ Fett R, Knippers R (February 1991). "The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors". J Biol Chem. 266 (3): 1448–55. PMID 1988429.
  2. ↑ 2.0 2.1 2.2 "Entrez Gene: EPRS glutamyl-prolyl-tRNA synthetase".
  3. ↑ Arif A, Jia J, Mukhopadhyay R, Willard B, Kinter M, Fox PL (July 2009). "Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity". Mol. Cell. 35 (2): 164–80. doi:10.1016/j.molcel.2009.05.028. PMC 2752289. PMID 19647514.
  4. ↑ Nie, J; Sakamoto S; Song D; Qu Z; Ota K; Taniguchi T (March 1998). "Interaction of Oct–1 and automodification domain of poly(ADP-ribose) synthetase". FEBS Lett. 424 (1–2): 27–32. doi:10.1016/S0014-5793(98)00131-8. PMID 9537509.
  5. ↑ Kang, J; Kim T; Ko Y G; Rho S B; Park S G; Kim M J; Kwon H J; Kim S (October 2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". J. Biol. Chem. UNITED STATES. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. ISSN 0021-9258. PMID 10913161.
  6. ↑ Rho, S B; Lee J S; Jeong E J; Kim K S; Kim Y G; Kim S (May 1998). "A multifunctional repeated motif is present in human bifunctional tRNA synthetase". J. Biol. Chem. UNITED STATES. 273 (18): 11267–73. doi:10.1074/jbc.273.18.11267. ISSN 0021-9258. PMID 9556618.

Further reading



Retrieved from "https://www.wikidoc.org/index.php?title=EPRS&oldid=1411050"