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    EPRS1 glutamyl-prolyl-tRNA synthetase 1 [ Homo sapiens (human) ]

    Gene ID: 2058, updated on 3-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Homozygous EPRS1 missense variant causing hypomyelinating leukodystrophy-15 alters variant-distal mRNA m[6]A site accessibility.

    Homozygous EPRS1 missense variant causing hypomyelinating leukodystrophy-15 alters variant-distal mRNA m(6)A site accessibility.
    Khan D, Ramachandiran I, Vasu K, China A, Khan K, Cumbo F, Halawani D, Terenzi F, Zin I, Long B, Costain G, Blaser S, Carnevale A, Gogonea V, Dutta R, Blankenberg D, Yoon G, Fox PL., Free PMC Article

    05/28/2024
    Glutamyl-prolyl-tRNA synthetase (EPRS1) drives tubulointerstitial nephritis-induced fibrosis by enhancing T cell proliferation and activity.

    Glutamyl-prolyl-tRNA synthetase (EPRS1) drives tubulointerstitial nephritis-induced fibrosis by enhancing T cell proliferation and activity.
    Kang C, Yun D, Yoon H, Hong M, Hwang J, Shin HM, Park S, Cheon S, Han D, Moon KC, Kim HY, Choi EY, Lee EY, Kim MH, Jeong CW, Kwak C, Kim DK, Oh KH, Joo KW, Lee DS, Kim YS, Han SS.

    04/30/2024
    Prolyl-tRNA synthetase as a novel therapeutic target in multiple myeloma.

    Prolyl-tRNA synthetase as a novel therapeutic target in multiple myeloma.
    Kurata K, James-Bott A, Tye MA, Yamamoto L, Samur MK, Tai YT, Dunford J, Johansson C, Senbabaoglu F, Philpott M, Palmer C, Ramasamy K, Gooding S, Smilova M, Gaeta G, Guo M, Christianson JC, Payne NC, Singh K, Karagoz K, Stokes ME, Ortiz M, Hagner P, Thakurta A, Cribbs A, Mazitschek R, Hideshima T, Anderson KC, Oppermann U., Free PMC Article

    02/10/2023
    Disease-associated mutations in a bifunctional aminoacyl-tRNA synthetase gene elicit the integrated stress response.

    Disease-associated mutations in a bifunctional aminoacyl-tRNA synthetase gene elicit the integrated stress response.
    Jin D, Wek SA, Kudlapur NT, Cantara WA, Bakhtina M, Wek RC, Musier-Forsyth K., Free PMC Article

    11/27/2021
    Glutamyl-Prolyl-tRNA Synthetase Regulates Proline-Rich Pro-Fibrotic Protein Synthesis During Cardiac Fibrosis.

    Glutamyl-Prolyl-tRNA Synthetase Regulates Proline-Rich Pro-Fibrotic Protein Synthesis During Cardiac Fibrosis.
    Wu J, Subbaiah KCV, Xie LH, Jiang F, Khor ES, Mickelsen D, Myers JR, Tang WHW, Yao P., Free PMC Article

    05/29/2021
    The human glutamyl-prolyl-tRNA synthetase (EPRS) consisting of two fused synthetases .This study identified site-selective proteolysis as a mechanism that severs the linkage between the EPRS synthetases in vitro and in vivo Caspase action targeted Asp-929 in the third WHEP domain, thereby separating the two synthetases.

    Structural control of caspase-generated glutamyl-tRNA synthetase by appended noncatalytic WHEP domains.
    Halawani D, Gogonea V, DiDonato JA, Pipich V, Yao P, China A, Topbas C, Vasu K, Arif A, Hazen SL, Fox PL., Free PMC Article

    01/26/2019
    five different EPRS mutations were identified.

    Bi-allelic Mutations in EPRS, Encoding the Glutamyl-Prolyl-Aminoacyl-tRNA Synthetase, Cause a Hypomyelinating Leukodystrophy.
    Mendes MI, Gutierrez Salazar M, Guerrero K, Thiffault I, Salomons GS, Gauquelin L, Tran LT, Forget D, Gauthier MS, Waisfisz Q, Smith DEC, Simons C, van der Knaap MS, Marquardt I, Lemes A, Mierzewska H, Weschke B, Koehler W, Coulombe B, Wolf NI, Bernard G., Free PMC Article

    12/22/2018
    Data indicate the necessity of EPRS for proliferation of tamoxifen-resistant estrogen receptor (ER+) breast cancer, but not ER- breast cancer cells.

    EPRS is a critical regulator of cell proliferation and estrogen signaling in ER+ breast cancer.
    Katsyv I, Wang M, Song WM, Zhou X, Zhao Y, Park S, Zhu J, Zhang B, Irie HY., Free PMC Article

    02/17/2018
    analysis of the heterotetrameric complex structure of the glutathione transferase (GST) domains shared among the four MSC components, methionyl-tRNA synthetase (MRS), glutaminyl-prolyl-tRNA synthetase (EPRS), AIMP2 and AIMP3

    Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains.
    Cho HY, Maeng SJ, Cho HJ, Choi YS, Chung JM, Lee S, Kim HK, Kim JH, Eom CY, Kim YG, Guo M, Jung HS, Kang BS, Kim S., Free PMC Article

    04/23/2016
    Dynamic model simulations predicted an inhibitory GAIT-element-interacting factor to account for this relationship and led to the identification of a truncated form of EPRS, a GAIT constituent that mediates binding to target transcripts.

    Coding region polyadenylation generates a truncated tRNA synthetase that counters translation repression.
    Yao P, Potdar AA, Arif A, Ray PS, Mukhopadhyay R, Willard B, Xu Y, Yan J, Saidel GM, Fox PL., Free PMC Article

    06/9/2012
    Study reveals a unique role of Cdk5/p35 in activation of the major noncanonical function of EPRS, namely translational control of macrophage inflammatory gene expression.

    Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-dependent kinase 5 dictates transcript-selective translational control.
    Arif A, Jia J, Moodt RA, DiCorleto PE, Fox PL., Free PMC Article

    04/30/2011
    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    06/30/2010
    EPRS phosphorylation events regulate GAIT-mediated gene silencing.

    Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity.
    Arif A, Jia J, Mukhopadhyay R, Willard B, Kinter M, Fox PL., Free PMC Article

    01/21/2010
    Essentiality of this enzyme's domains in its noncanonical function of regulating inflammatory gene expression.

    WHEP domains direct noncanonical function of glutamyl-Prolyl tRNA synthetase in translational control of gene expression.
    Jia J, Arif A, Ray PS, Fox PL., Free PMC Article

    01/21/2010
    Results show that glutamyl-prolyl-tRNA synthetase has a regulated, noncanonical activity that blocks synthesis of a specific protein.

    Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation.
    Sampath P, Mazumder B, Seshadri V, Gerber CA, Chavatte L, Kinter M, Ting SM, Dignam JD, Kim S, Driscoll DM, Fox PL.

    01/21/2010
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