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

Gene ID: 2058, updated on 12-Jan-2019

Summary

Official Symbol
EPRSprovided by HGNC
Official Full Name
glutamyl-prolyl-tRNA synthetaseprovided by HGNC
Primary source
HGNC:HGNC:3418
See related
Ensembl:ENSG00000136628 MIM:138295
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
EARS; PARS; QARS; QPRS; HLD15; PIG32; GLUPRORS
Summary
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. [provided by RefSeq, Jul 2008]
Expression
Ubiquitous expression in thyroid (RPKM 31.6), appendix (RPKM 22.6) and 25 other tissues See more
Orthologs

Genomic context

See EPRS in Genome Data Viewer
Location:
1q41
Exon count:
33
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 1 NC_000001.11 (219968600..220046658, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 1 NC_000001.10 (220141940..220220000, complement)

Chromosome 1 - NC_000001.11Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC105372926 Neighboring gene RNA, 5S ribosomal pseudogene 76 Neighboring gene uncharacterized LOC107985281 Neighboring gene solute carrier family 30 member 10 Neighboring gene 3'(2'), 5'-bisphosphate nucleotidase 1 Neighboring gene uncharacterized LOC105373475 Neighboring gene isoleucyl-tRNA synthetase 2, mitochondrial

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

HIV-1 interactions

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env Tandem affinity purification and mass spectrometry analysis identify glutamyl-prolyl-tRNA synthetase (EPRS), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Gag-Pol gag-pol Tandem affinity purification and mass spectrometry analysis identify glutamyl-prolyl-tRNA synthetase (EPRS), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Nef nef Tandem affinity purification and mass spectrometry analysis identify glutamyl-prolyl-tRNA synthetase (EPRS), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Pr55(Gag) gag Cellular biotinylated glutamyl-prolyl-tRNA synthetase (EPRS, Bifunctional glutamate/proline tRNA ligase) protein is incorporated into HIV-1 Gag virus-like particles PubMed
gag Tandem affinity purification and mass spectrometry analysis identify glutamyl-prolyl-tRNA synthetase (EPRS), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
matrix gag HIV-1 MA is identified to have a physical interaction with glutamyl-prolyl-tRNA synthetase (EPRS) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses PubMed

Go to the HIV-1, Human Interaction Database

Pathways from BioSystems

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Clone Names

  • DKFZp313B047

Gene Ontology Provided by GOA

Function Evidence Code Pubs
ATP binding IEA
Inferred from Electronic Annotation
more info
 
GTPase binding IPI
Inferred from Physical Interaction
more info
PubMed 
RNA stem-loop binding IDA
Inferred from Direct Assay
more info
PubMed 
glutamate-tRNA ligase activity TAS
Traceable Author Statement
more info
 
identical protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
proline-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
proline-tRNA ligase activity IDA
Inferred from Direct Assay
more info
PubMed 
proline-tRNA ligase activity TAS
Traceable Author Statement
more info
 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein homodimerization activity IPI
Inferred from Physical Interaction
more info
PubMed 
zinc ion binding IDA
Inferred from Direct Assay
more info
PubMed 
Process Evidence Code Pubs
cellular response to insulin stimulus ISS
Inferred from Sequence or Structural Similarity
more info
 
cellular response to interferon-gamma IDA
Inferred from Direct Assay
more info
PubMed 
glutamyl-tRNA aminoacylation IEA
Inferred from Electronic Annotation
more info
 
long-chain fatty acid import IMP
Inferred from Mutant Phenotype
more info
PubMed 
negative regulation of translation IDA
Inferred from Direct Assay
more info
PubMed 
negative regulation of translation IMP
Inferred from Mutant Phenotype
more info
PubMed 
prolyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
prolyl-tRNA aminoacylation IDA
Inferred from Direct Assay
more info
PubMed 
protein-containing complex assembly TAS
Traceable Author Statement
more info
PubMed 
tRNA aminoacylation for protein translation TAS
Traceable Author Statement
more info
 
Component Evidence Code Pubs
GAIT complex IDA
Inferred from Direct Assay
more info
PubMed 
aminoacyl-tRNA synthetase multienzyme complex IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
aminoacyl-tRNA synthetase multienzyme complex IDA
Inferred from Direct Assay
more info
PubMed 
cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
cytosol IDA
Inferred from Direct Assay
more info
PubMed 
cytosol TAS
Traceable Author Statement
more info
 
membrane HDA PubMed 
plasma membrane ISS
Inferred from Sequence or Structural Similarity
more info
 
ribonucleoprotein complex IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

Preferred Names
bifunctional glutamate/proline--tRNA ligase
Names
bifunctional aminoacyl-tRNA synthetase
cell proliferation-inducing gene 32 protein
glutamate tRNA ligase
glutamatyl-prolyl-tRNA synthetase
glutaminyl-tRNA synthetase
proliferation-inducing gene 32 protein
proliferation-inducing protein 32
proline-tRNA ligase
prolyl-tRNA synthetase
NP_004437.2
XP_016856103.1

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_004446.3NP_004437.2  bifunctional glutamate/proline--tRNA ligase

    See identical proteins and their annotated locations for NP_004437.2

    Status: REVIEWED

    Source sequence(s)
    AA196283, AY493416, BC034797, BC046156, N85252
    Consensus CDS
    CCDS31027.1
    UniProtKB/Swiss-Prot
    P07814
    Related
    ENSP00000355890.3, ENST00000366923.7
    Conserved Domains (9) summary
    cd10309
    Location:74157
    GST_C_GluProRS_N; Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase
    PLN02907
    Location:13711
    PLN02907; glutamate-tRNA ligase
    PRK08661
    Location:10191512
    PRK08661; prolyl-tRNA synthetase; Provisional
    cd00778
    Location:10231286
    ProRS_core_arch_euk; Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
    cd00862
    Location:12921512
    ProRS_anticodon_zinc; ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in ...
    cd00936
    Location:904952
    WEPRS_RNA; WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates ...
    pfam00458
    Location:753805
    WHEP-TRS; WHEP-TRS domain
    pfam00749
    Location:197502
    tRNA-synt_1c; tRNA synthetases class I (E and Q), catalytic domain
    pfam03950
    Location:504681
    tRNA-synt_1c_C; tRNA synthetases class I (E and Q), anti-codon binding domain

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000001.11 Reference GRCh38.p12 Primary Assembly

    Range
    219968600..220046658 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_017000614.2XP_016856103.1  bifunctional glutamate/proline--tRNA ligase isoform X1

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