EPRS1

Protein identityUniProt · HPA

UniProt accession

P07814

Gene

EPRS1

Ensembl

ENSG00000136628

Chromosome

1

Canonical length

1512 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Cytosol,Mid piece

Quaternary structure

Homodimer

OverviewNCBI Gene

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]

Canonical amino-acid sequenceUniProt

1512 residues, UniProt reviewed canonical sequence.

>P07814|EPRS1
     1  MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD VNSILRYLAR
    61  VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSTIN ELNHCLSLRT YLVGNSLSLA
   121  DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW FGFLEAQQAF QSVGTKWDVS TTKARVAPEK
   181  KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN
   241  PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
   301  AEREQRIDSK HRKNPIEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC MRDPTLYRCK
   361  IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI
   421  WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS
   481  SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG
   541  LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKLNLENKD
   601  YKKTTKVTWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK HEELMLGDPC
   661  LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCVLI YIPDGHTKEM PTSGSKEKTK
   721  VEATKNETSA PFKERPTPSL NNNCTTSEDS LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA
   781  VKQLLSLKAE YKEKTGQEYK PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL
   841  KAEKSPKAKI NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE
   901  AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY KPVSATGAED
   961  KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS GAGEGQGPKK QTRLGLEAKK
  1021  EENLADWYSQ VITKSEMIEY HDISGCYILR PWAYAIWEAI KDFFDAEIKK LGVENCYFPM
  1081  FVSQSALEKE KTHVADFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL
  1141  PIKLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL
  1201  LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK MFEIVFEDPK
  1261  IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA CVQVVIIPCG ITNALSEEDK
  1321  EALIAKCNDY RRRLLSVNIR VRADLRDNYS PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV
  1381  AVRRDTGEKL TVAENEAETK LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG
  1441  KIVQIPFCGE IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN
  1501  PAKYYTLFGR SY

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against EPRS1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.3

Highest tissue expression

79 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about EPRS1.

Disease | AllUniProt

Conditions EPRS1 is implicated in, by any mechanism.

• Leukodystrophy, hypomyelinating, 15 (HLD15) MIM:617951

Disease | GeneticClinVar

19 pathogenic / likely-pathogenic of 535 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Leukodystrophy, hypomyelinating, 15
• Global developmental delay
• Intellectual disability
• Inborn genetic diseases

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.51

gnomAD pLI

0

DepMap mean gene effect

-1.66

DepMap dependency class

pan

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 11% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cellular response to insulin stimulus
• cellular response to type II interferon
• glutamyl-tRNA aminoacylation
• negative regulation of translation
• prolyl-tRNA aminoacylation
• tRNA aminoacylation for protein translation
• regulation of long-chain fatty acid import into cell

Molecular functions

• ATP binding
• glutamate-tRNA ligase activity
• GTPase binding
• identical protein binding
• proline-tRNA ligase activity
• protein homodimerization activity
• RNA stem-loop binding
• zinc ion binding

Cellular components

• aminoacyl-tRNA synthetase multienzyme complex
• cytoplasm
• cytosol
• GAIT complex
• membrane
• plasma membrane
• ribonucleoprotein complex
• sperm midpiece

Protein domainsUniProt · Pfam · InterPro

• WHEP-TRS domain
• Glutamyl/glutaminyl-tRNA synthetase
• Aminoacyl-tRNA synthetase, class I, conserved site
• Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
• Anticodon-binding
• Aminoacyl-tRNA synthetase, class II
• uS15/NS1, RNA-binding domain superfamily
• Large ribosomal subunit protein bL25/Gln-tRNA synthetase, anti-codon-binding domain superfamily
• Rossmann-like alpha/beta/alpha sandwich fold
• Large ribosomal subunit protein bL25/Gln-tRNA synthetase, N-terminal
• Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain
• Glutamyl/glutaminyl-tRNA synthetase, class Ib, anti-codon binding domain
• Glutathione S-transferase, C-terminal domain superfamily
• Anticodon-binding domain superfamily
• Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
• tRNA synthetases class I (E and Q), anti-codon binding domain
• Nuclear-export cofactor Arc1-like, N-terminal domain
• WHEP-TRS domain
• tRNA synthetase class II core domain (G, H, P, S and T)
• tRNA synthetases class I (E and Q), catalytic domain
• Anticodon binding domain
• tRNA synthetases class I (E and Q), anti-codon binding domain
• tRNA synthetases class I (E and Q), anti-codon binding domain
• Nuclear-export cofactor Arc1p
• Proline-tRNA ligase, class IIa, archaeal-type
• Glutamyl-tRNA synthetase, archaeal/eukaryotic cytosolic
• Proline-tRNA ligase, class II, C-terminal
• Prolyl-tRNA synthetase, class II
• Prolyl-tRNA synthetase, catalytic domain
• Prolyl-tRNA synthetase, C-terminal

KeywordsUniProt

• Acetylation
• Aminoacyl-tRNA synthetase
• ATP-binding
• Cytoplasm
• Leukodystrophy
• Ligase
• Membrane
• Metal-binding
• Methylation
• Multifunctional enzyme
• Neurodegeneration
• Nucleotide-binding
• Phosphoprotein
• Protein biosynthesis
• Repeat
• RNA-binding
• Translation regulation
• Zinc

InteractionsUniProt · HPA

Protein binding partners of EPRS1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• DUS2L
• TARS3
• DUS2
• AIMP2
• SLC27A1
• HSP90AA1
• IARS1
• KARS1
• LARS1
• QARS1
• RARS1