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Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

EPRS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA (PubMed:1756734, PubMed:24100331, PubMed:23263184). The phosphorylation of EPRS, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex and recruits it to the GAIT complex that binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin), suppressing their translation. Interferon-gamma can therefore redirect, in specific cells, the EPRS function from protein synthesis to translation inhibition (PubMed:15479637, PubMed:23071094). Also functions as an effector of the mTORC1 signaling pathway by promoting, through SLC27A1, the uptake of long-chain fatty acid by adipocytes. Thereby, it also plays a role in fat metabolism and more indirectly influences lifespan (PubMed:28178239).6 Publications

Caution

Was originally thought to be a glutaminyl-tRNA synthetase.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by halofuginone.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei211ATPBy similarity1
Binding sitei398ATPBy similarity1
Binding sitei1152L-prolineCombined sources1 Publication1
Binding sitei1242L-prolineCombined sources1 Publication1
Binding sitei1276ATPCombined sources2 Publications1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1448ZincCombined sources2 Publications1
Metal bindingi1453ZincCombined sources2 Publications1
Metal bindingi1495ZincCombined sources2 Publications1
Metal bindingi1497ZincCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi432 – 436ATPBy similarity5
Nucleotide bindingi1152 – 1154ATPCombined sources2 Publications3
Nucleotide bindingi1163 – 1164ATPCombined sources2 Publications2
Nucleotide bindingi1237 – 1240ATPCombined sources2 Publications4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminoacyl-tRNA synthetase, Ligase, Multifunctional enzyme, RNA-binding
Biological processProtein biosynthesis, Translation regulation
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.1.1.15 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2408517 SeMet incorporation into proteins
R-HSA-379716 Cytosolic tRNA aminoacylation
R-HSA-6782315 tRNA modification in the nucleus and cytosol

SIGNOR Signaling Network Open Resource

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SIGNORi
P07814

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
P07814

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bifunctional glutamate/proline--tRNA ligase
Alternative name(s):
Bifunctional aminoacyl-tRNA synthetase
Cell proliferation-inducing gene 32 protein
Glutamatyl-prolyl-tRNA synthetase
Including the following 2 domains:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Proline--tRNA ligase (EC:6.1.1.152 Publications)
Alternative name(s):
Prolyl-tRNA synthetase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EPRS
Synonyms:GLNS, PARS, QARS, QPRS
ORF Names:PIG32
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000136628.17

Human Gene Nomenclature Database

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HGNCi
HGNC:3418 EPRS

Online Mendelian Inheritance in Man (OMIM)

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MIMi
138295 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P07814

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Leukodystrophy, hypomyelinating, 15 (HLD15)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by hypomyelinating leukodystrophy with thinning of the corpus callosum. Clinical features include motor and cognitive impairment appearing in the first or second decade of life, dystonia, ataxia, spasticity, and dysphagia. Most patients develop severe optic atrophy, and some have hearing loss.
See also OMIM:617951
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080800339 – 1512Missing in HLD15. 1 PublicationAdd BLAST1174
Natural variantiVAR_0808011115P → R in HLD15; slightly decreased protein level; does not affect multisynthetase complex assembly. 1 PublicationCorresponds to variant dbSNP:rs1288116010Ensembl.1
Natural variantiVAR_0808021126M → T in HLD15; unknown pathological significance; small decrease in aminoacylation activity. 1 PublicationCorresponds to variant dbSNP:rs1474000585Ensembl.1
Natural variantiVAR_0808031160P → S in HLD15; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs898824971EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi886S → A: Abolishes release from the aminoacyl-tRNA synthetase multienzyme complex and association with the GAIT complex upon interferon-gamma treatment. Abolishes interaction with SYNCRIP. 1 Publication1
Mutagenesisi886S → D: Not active in translation inhibition (phosphomimetic) and abolishes GAIT complex association with eiF4G. No effect on interaction with SYNCRIP. 1 Publication1
Mutagenesisi999S → A: Not active in translation inhibition, abolishes release from the aminoacyl-tRNA synthetase multienzyme complex and association with the GAIT complex upon interferon-gamma treatment. 1 Publication1
Mutagenesisi999S → D: Active in translation inhibition (phosphomimetic). No effect on GAIT complex association with eiF4G. 1 Publication1
Mutagenesisi1097F → A: Almost complete loss of prolyl-tRNA ligase activity. 1 Publication1
Mutagenesisi1097F → W: No effect on prolyl-tRNA ligase activity. Decreases inhibition by halofuginone. 1 Publication1
Mutagenesisi1152R → K: No effect on prolyl-tRNA ligase activity. Decreases inhibition by halofuginone. 1 Publication1
Mutagenesisi1152R → L: Almost complete loss of prolyl-tRNA ligase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Leukodystrophy, Neurodegeneration

Organism-specific databases

DisGeNET

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DisGeNETi
2058

MalaCards human disease database

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MalaCardsi
EPRS
MIMi617951 phenotype

Open Targets

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OpenTargetsi
ENSG00000136628

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27837

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3873

Drug and drug target database

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DrugBanki
DB03376 '5'-O-(N-(L-Alanyl)-Sulfamoyl)Adenosine
DB02510 '5'-O-(N-(L-Prolyl)-Sulfamoyl)Adenosine
DB02684 5'-O-(N-(L-Cysteinyl)-Sulfamoyl)Adenosine
DB00142 L-Glutamic Acid
DB00172 L-Proline

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
EPRS

Domain mapping of disease mutations (DMDM)

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DMDMi
288558855

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001197431 – 1512Bifunctional glutamate/proline--tRNA ligaseAdd BLAST1512

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei300N6-acetyllysine; alternateCombined sources1
Modified residuei300N6-malonyllysine; alternate1 Publication1
Modified residuei355PhosphothreonineCombined sources1
Modified residuei417N6-acetyllysineCombined sources1
Modified residuei434PhosphoserineCombined sources1
Modified residuei498N6-acetyllysineCombined sources1
Modified residuei535N6-acetyllysineCombined sources1
Modified residuei542N6-acetyllysineCombined sources1
Modified residuei637N6-acetyllysineCombined sources1
Modified residuei747PhosphoserineCombined sources1
Modified residuei788N6-acetyllysineCombined sources1
Modified residuei861N6-acetyllysineBy similarity1
Modified residuei872PhosphotyrosineCombined sources1
Modified residuei882PhosphoserineCombined sources1
Modified residuei885PhosphoserineCombined sources1
Modified residuei886Phosphoserine; by CDK5Combined sources2 Publications1
Modified residuei891PhosphoserineCombined sources1
Modified residuei898PhosphothreonineCombined sources1
Modified residuei998PhosphoserineCombined sources1
Modified residuei999Phosphoserine; by RPS6KB12 Publications1
Modified residuei1000PhosphoserineCombined sources1
Modified residuei1152Omega-N-methylarginineCombined sources1
Modified residuei1350PhosphoserineCombined sources1
Modified residuei1503N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated at Ser-886 by CDK5 (PubMed:19647514, PubMed:21220307). Phosphorylated at Ser-999 by RPS6KB1; triggers EPRS release from the aminoacyl-tRNA synthetase multienzyme complex (PubMed:19647514, PubMed:21220307, PubMed:28178239). In monocytes, the IFN-gamma-induced sequential phosphorylation at Ser-886 and Ser-999 releases EPRS from the aminoacyl-tRNA synthetase multienzyme complex, allowing its association with the GAIT complex. Phosphorylation at Ser-999 is specifically required for the RPL13A-mediated interaction of the GAIT complex with eIF4G (PubMed:19647514, PubMed:21220307). Phosphorylation at Ser-999 by RPS6KB1, is also induced by insulin through activation of the mTORC1 signaling pathway and promotes the interaction of EPRS with SLC27A1 (PubMed:28178239).3 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P07814

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P07814

MaxQB - The MaxQuant DataBase

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MaxQBi
P07814

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P07814

PeptideAtlas

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PeptideAtlasi
P07814

PRoteomics IDEntifications database

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PRIDEi
P07814

ProteomicsDB human proteome resource

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ProteomicsDBi
52028

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P07814

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P07814

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P07814

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000136628 Expressed in 239 organ(s), highest expression level in parotid gland

CleanEx database of gene expression profiles

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CleanExi
HS_EPRS
HS_QARS

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P07814 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P07814 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA026490
HPA030052

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:24100331, PubMed:23263184). Part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex (MSC), that is composed of the tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:24312579, PubMed:19131329, PubMed:19289464). Forms a linear complex that contains MARS, EEF1E1, EPRS and AIMP2 that is at the core of the multisubunit complex (PubMed:26472928). Interacts with TARSL2 (PubMed:24312579). Interacts with DUS2L (PubMed:15994936). Component of the GAIT complex which is composed of EPRS, RPL13A and GAPDH. For human, the complex assembly seems to be a two-step process in which EPRS first associates with SYNCRIP to form a pre-GAIT complex which is deficient in GAIT element binding (PubMed:15479637). Interacts (phosphorylated at Ser-999) with SLC27A1; mediates the translocation of SLC27A1 from the cytoplasm to the plasma membrane thereby increasing the uptake of long-chain fatty acids (PubMed:28178239).10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108372, 207 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P07814

Database of interacting proteins

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DIPi
DIP-40825N

Protein interaction database and analysis system

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IntActi
P07814, 47 interactors

Molecular INTeraction database

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MINTi
P07814

STRING: functional protein association networks

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STRINGi
9606.ENSP00000355890

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P07814

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FYJNMR-A749-805[»]
4HVCX-ray2.00A/B1003-1512[»]
4K86X-ray2.40A1000-1512[»]
4K87X-ray2.30A1000-1512[»]
4K88X-ray2.62A1000-1512[»]
5A1NX-ray2.10A1-175[»]
5A34X-ray2.60A/C/E/G1-175[»]
5A5HX-ray2.32A/C/E/G1-175[»]
5BMUX-ray2.60B/D/F/H1-175[»]
5V58X-ray2.59A1003-1512[»]
5VADX-ray2.36A/B998-1512[»]
5Y6LX-ray2.90C1-175[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P07814

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P07814

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P07814

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini749 – 805WHEP-TRS 1Add BLAST57
Domaini822 – 878WHEP-TRS 2Add BLAST57
Domaini900 – 956WHEP-TRS 3Add BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni164 – 759Glutamate--tRNA ligaseAdd BLAST596
Regioni760 – 9563 X 57 AA approximate repeatsAdd BLAST197
Regioni959 – 991ChargedAdd BLAST33
Regioni1007 – 1512Proline--tRNA ligaseAdd BLAST506
Regioni1121 – 1123L-proline bindingCombined sources1 Publication3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi204 – 214"HIGH" regionAdd BLAST11
Motifi432 – 436"KMSKS" region5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi961 – 991Lys-richPROSITE-ProRule annotationAdd BLAST31

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The WHEP-TRS domains are involved in RNA binding.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1147 Eukaryota
KOG4163 Eukaryota
COG0008 LUCA
COG0442 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00550000074815

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG017875

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P07814

KEGG Orthology (KO)

More...
KOi
K14163

Identification of Orthologs from Complete Genome Data

More...
OMAi
KMFEIIF

Database of Orthologous Groups

More...
OrthoDBi
809861at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07814

TreeFam database of animal gene trees

More...
TreeFami
TF300380

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00778 ProRS_core_arch_euk, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.240.10, 2 hits
3.30.110.30, 1 hit
3.40.50.620, 1 hit
3.40.50.800, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_02076 Glu_tRNA_synth_type2, 1 hit
MF_01571 Pro_tRNA_synth_type3, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002314 aa-tRNA-synt_IIb
IPR001412 aa-tRNA-synth_I_CS
IPR006195 aa-tRNA-synth_II
IPR004154 Anticodon-bd
IPR036621 Anticodon-bd_dom_sf
IPR004526 Glu-tRNA-synth_arc/euk
IPR000924 Glu/Gln-tRNA-synth
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR020059 Glu/Gln-tRNA-synth_Ib_codon-bd
IPR036282 Glutathione-S-Trfase_C_sf
IPR004046 GST_C
IPR004499 Pro-tRNA-ligase_IIa_arc-type
IPR016061 Pro-tRNA_ligase_II_C
IPR017449 Pro-tRNA_synth_II
IPR033721 ProRS_core_arch_euk
IPR020056 Rbsml_L25/Gln-tRNA_synth_N
IPR011035 Ribosomal_L25/Gln-tRNA_synth
IPR014729 Rossmann-like_a/b/a_fold
IPR009068 S15_NS1_RNA-bd
IPR000738 WHEP-TRS_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00043 GST_C, 1 hit
PF03129 HGTP_anticodon, 1 hit
PF09180 ProRS-C_1, 1 hit
PF00749 tRNA-synt_1c, 1 hit
PF03950 tRNA-synt_1c_C, 1 hit
PF00587 tRNA-synt_2b, 1 hit
PF00458 WHEP-TRS, 3 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00987 TRNASYNTHGLU

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00946 ProRS-C_1, 1 hit
SM00991 WHEP-TRS, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47060 SSF47060, 3 hits
SSF47616 SSF47616, 1 hit
SSF50715 SSF50715, 1 hit
SSF64586 SSF64586, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00463 gltX_arch, 1 hit
TIGR00408 proS_fam_I, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 1 hit
PS50862 AA_TRNA_LIGASE_II, 1 hit
PS00762 WHEP_TRS_1, 3 hits
PS51185 WHEP_TRS_2, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P07814-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD
60 70 80 90 100
VNSILRYLAR VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSTIN
110 120 130 140 150
ELNHCLSLRT YLVGNSLSLA DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW
160 170 180 190 200
FGFLEAQQAF QSVGTKWDVS TTKARVAPEK KQDVGKFVEL PGAEMGKVTV
210 220 230 240 250
RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN PEKEKEDFEK
260 270 280 290 300
VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
310 320 330 340 350
AEREQRIDSK HRKNPIEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC
360 370 380 390 400
MRDPTLYRCK IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH
410 420 430 440 450
DRDEQFYWII EALGIRKPYI WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW
460 470 480 490 500
DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS SRSVVNMEWD KIWAFNKKVI
510 520 530 540 550
DPVAPRYVAL LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG LKPVWYSPKV
560 570 580 590 600
FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKLNLENKD
610 620 630 640 650
YKKTTKVTWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK
660 670 680 690 700
HEELMLGDPC LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCVLI
710 720 730 740 750
YIPDGHTKEM PTSGSKEKTK VEATKNETSA PFKERPTPSL NNNCTTSEDS
760 770 780 790 800
LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA VKQLLSLKAE YKEKTGQEYK
810 820 830 840 850
PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL KAEKSPKAKI
860 870 880 890 900
NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE
910 920 930 940 950
AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY
960 970 980 990 1000
KPVSATGAED KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS
1010 1020 1030 1040 1050
GAGEGQGPKK QTRLGLEAKK EENLADWYSQ VITKSEMIEY HDISGCYILR
1060 1070 1080 1090 1100
PWAYAIWEAI KDFFDAEIKK LGVENCYFPM FVSQSALEKE KTHVADFAPE
1110 1120 1130 1140 1150
VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL PIKLNQWCNV
1160 1170 1180 1190 1200
VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL
1210 1220 1230 1240 1250
LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK
1260 1270 1280 1290 1300
MFEIVFEDPK IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA
1310 1320 1330 1340 1350
CVQVVIIPCG ITNALSEEDK EALIAKCNDY RRRLLSVNIR VRADLRDNYS
1360 1370 1380 1390 1400
PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV AVRRDTGEKL TVAENEAETK
1410 1420 1430 1440 1450
LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG KIVQIPFCGE
1460 1470 1480 1490 1500
IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN
1510
PAKYYTLFGR SY
Length:1,512
Mass (Da):170,591
Last modified:February 9, 2010 - v5
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2CE4311076719403
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
V9GYZ6V9GYZ6_HUMAN
Bifunctional glutamate/proline--tRN...
EPRS
968Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9GZ76V9GZ76_HUMAN
Bifunctional glutamate/proline--tRN...
EPRS
194Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH15494 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH34797 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH46156 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH58921 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAS72877 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA30354 differs from that shown. Sequencing errors.Curated
The sequence CAA38224 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti532K → R in CAI45949 (PubMed:17974005).Curated1
Sequence conflicti594L → F in CAA38224 (PubMed:1988429).Curated1
Sequence conflicti594L → F in AAS72877 (Ref. 5) Curated1
Sequence conflicti943K → E in CAI45949 (PubMed:17974005).Curated1
Sequence conflicti1177 – 1179ATM → VTV in CAI45949 (PubMed:17974005).Curated3
Sequence conflicti1441K → R in CAI45949 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037288296A → P. Corresponds to variant dbSNP:rs35999099Ensembl.1
Natural variantiVAR_037289308D → E5 PublicationsCorresponds to variant dbSNP:rs2230301Ensembl.1
Natural variantiVAR_037290334Q → H3 PublicationsCorresponds to variant dbSNP:rs1063236Ensembl.1
Natural variantiVAR_080800339 – 1512Missing in HLD15. 1 PublicationAdd BLAST1174
Natural variantiVAR_037291893P → H. Corresponds to variant dbSNP:rs5030751Ensembl.1
Natural variantiVAR_057358913E → G. Corresponds to variant dbSNP:rs2230302Ensembl.1
Natural variantiVAR_0372921043I → V1 PublicationCorresponds to variant dbSNP:rs5030752Ensembl.1
Natural variantiVAR_0372931107S → F. Corresponds to variant dbSNP:rs12144752Ensembl.1
Natural variantiVAR_0808011115P → R in HLD15; slightly decreased protein level; does not affect multisynthetase complex assembly. 1 PublicationCorresponds to variant dbSNP:rs1288116010Ensembl.1
Natural variantiVAR_0808021126M → T in HLD15; unknown pathological significance; small decrease in aminoacylation activity. 1 PublicationCorresponds to variant dbSNP:rs1474000585Ensembl.1
Natural variantiVAR_0808031160P → S in HLD15; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs898824971EnsemblClinVar.1
Natural variantiVAR_0372941399T → N. Corresponds to variant dbSNP:rs34559775Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CR933648 mRNA Translation: CAI45949.1
AC103590 Genomic DNA No translation available.
BC015494 mRNA Translation: AAH15494.1 Sequence problems.
BC034797 mRNA Translation: AAH34797.1 Sequence problems.
BC046156 mRNA Translation: AAH46156.1 Sequence problems.
BC058921 mRNA Translation: AAH58921.1 Sequence problems.
BC126275 mRNA Translation: AAI26276.1
BC136465 mRNA Translation: AAI36466.1
X54326 mRNA Translation: CAA38224.1 Different initiation.
AY493416 mRNA Translation: AAS72877.1 Different initiation.
X07466 mRNA Translation: CAA30354.1 Sequence problems.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31027.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A38663 SYHUQT

NCBI Reference Sequences

More...
RefSeqi
NP_004437.2, NM_004446.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.497788

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000366923; ENSP00000355890; ENSG00000136628

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2058

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2058

UCSC genome browser

More...
UCSCi
uc001hly.2 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR933648 mRNA Translation: CAI45949.1
AC103590 Genomic DNA No translation available.
BC015494 mRNA Translation: AAH15494.1 Sequence problems.
BC034797 mRNA Translation: AAH34797.1 Sequence problems.
BC046156 mRNA Translation: AAH46156.1 Sequence problems.
BC058921 mRNA Translation: AAH58921.1 Sequence problems.
BC126275 mRNA Translation: AAI26276.1
BC136465 mRNA Translation: AAI36466.1
X54326 mRNA Translation: CAA38224.1 Different initiation.
AY493416 mRNA Translation: AAS72877.1 Different initiation.
X07466 mRNA Translation: CAA30354.1 Sequence problems.
CCDSiCCDS31027.1
PIRiA38663 SYHUQT
RefSeqiNP_004437.2, NM_004446.2
UniGeneiHs.497788

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FYJNMR-A749-805[»]
4HVCX-ray2.00A/B1003-1512[»]
4K86X-ray2.40A1000-1512[»]
4K87X-ray2.30A1000-1512[»]
4K88X-ray2.62A1000-1512[»]
5A1NX-ray2.10A1-175[»]
5A34X-ray2.60A/C/E/G1-175[»]
5A5HX-ray2.32A/C/E/G1-175[»]
5BMUX-ray2.60B/D/F/H1-175[»]
5V58X-ray2.59A1003-1512[»]
5VADX-ray2.36A/B998-1512[»]
5Y6LX-ray2.90C1-175[»]
ProteinModelPortaliP07814
SMRiP07814
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108372, 207 interactors
CORUMiP07814
DIPiDIP-40825N
IntActiP07814, 47 interactors
MINTiP07814
STRINGi9606.ENSP00000355890

Chemistry databases

BindingDBiP07814
ChEMBLiCHEMBL3873
DrugBankiDB03376 '5'-O-(N-(L-Alanyl)-Sulfamoyl)Adenosine
DB02510 '5'-O-(N-(L-Prolyl)-Sulfamoyl)Adenosine
DB02684 5'-O-(N-(L-Cysteinyl)-Sulfamoyl)Adenosine
DB00142 L-Glutamic Acid
DB00172 L-Proline

Protein family/group databases

MoonProtiP07814

PTM databases

iPTMnetiP07814
PhosphoSitePlusiP07814
SwissPalmiP07814

Polymorphism and mutation databases

BioMutaiEPRS
DMDMi288558855

Proteomic databases

EPDiP07814
jPOSTiP07814
MaxQBiP07814
PaxDbiP07814
PeptideAtlasiP07814
PRIDEiP07814
ProteomicsDBi52028

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366923; ENSP00000355890; ENSG00000136628
GeneIDi2058
KEGGihsa:2058
UCSCiuc001hly.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2058
DisGeNETi2058
EuPathDBiHostDB:ENSG00000136628.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EPRS
HGNCiHGNC:3418 EPRS
HPAiHPA026490
HPA030052
MalaCardsiEPRS
MIMi138295 gene
617951 phenotype
neXtProtiNX_P07814
OpenTargetsiENSG00000136628
PharmGKBiPA27837

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1147 Eukaryota
KOG4163 Eukaryota
COG0008 LUCA
COG0442 LUCA
GeneTreeiENSGT00550000074815
HOVERGENiHBG017875
InParanoidiP07814
KOiK14163
OMAiKMFEIIF
OrthoDBi809861at2759
PhylomeDBiP07814
TreeFamiTF300380

Enzyme and pathway databases

BRENDAi6.1.1.15 2681
ReactomeiR-HSA-2408517 SeMet incorporation into proteins
R-HSA-379716 Cytosolic tRNA aminoacylation
R-HSA-6782315 tRNA modification in the nucleus and cytosol
SIGNORiP07814

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
EPRS human
EvolutionaryTraceiP07814

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
EPRS

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
2058

Protein Ontology

More...
PROi
PR:P07814

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000136628 Expressed in 239 organ(s), highest expression level in parotid gland
CleanExiHS_EPRS
HS_QARS
ExpressionAtlasiP07814 baseline and differential
GenevisibleiP07814 HS

Family and domain databases

CDDicd00778 ProRS_core_arch_euk, 1 hit
Gene3Di2.40.240.10, 2 hits
3.30.110.30, 1 hit
3.40.50.620, 1 hit
3.40.50.800, 1 hit
HAMAPiMF_02076 Glu_tRNA_synth_type2, 1 hit
MF_01571 Pro_tRNA_synth_type3, 1 hit
InterProiView protein in InterPro
IPR002314 aa-tRNA-synt_IIb
IPR001412 aa-tRNA-synth_I_CS
IPR006195 aa-tRNA-synth_II
IPR004154 Anticodon-bd
IPR036621 Anticodon-bd_dom_sf
IPR004526 Glu-tRNA-synth_arc/euk
IPR000924 Glu/Gln-tRNA-synth
IPR020058 Glu/Gln-tRNA-synth_Ib_cat-dom
IPR020059 Glu/Gln-tRNA-synth_Ib_codon-bd
IPR036282 Glutathione-S-Trfase_C_sf
IPR004046 GST_C
IPR004499 Pro-tRNA-ligase_IIa_arc-type
IPR016061 Pro-tRNA_ligase_II_C
IPR017449 Pro-tRNA_synth_II
IPR033721 ProRS_core_arch_euk
IPR020056 Rbsml_L25/Gln-tRNA_synth_N
IPR011035 Ribosomal_L25/Gln-tRNA_synth
IPR014729 Rossmann-like_a/b/a_fold
IPR009068 S15_NS1_RNA-bd
IPR000738 WHEP-TRS_dom
PfamiView protein in Pfam
PF00043 GST_C, 1 hit
PF03129 HGTP_anticodon, 1 hit
PF09180 ProRS-C_1, 1 hit
PF00749 tRNA-synt_1c, 1 hit
PF03950 tRNA-synt_1c_C, 1 hit
PF00587 tRNA-synt_2b, 1 hit
PF00458 WHEP-TRS, 3 hits
PRINTSiPR00987 TRNASYNTHGLU
SMARTiView protein in SMART
SM00946 ProRS-C_1, 1 hit
SM00991 WHEP-TRS, 3 hits
SUPFAMiSSF47060 SSF47060, 3 hits
SSF47616 SSF47616, 1 hit
SSF50715 SSF50715, 1 hit
SSF64586 SSF64586, 1 hit
TIGRFAMsiTIGR00463 gltX_arch, 1 hit
TIGR00408 proS_fam_I, 1 hit
PROSITEiView protein in PROSITE
PS00178 AA_TRNA_LIGASE_I, 1 hit
PS50862 AA_TRNA_LIGASE_II, 1 hit
PS00762 WHEP_TRS_1, 3 hits
PS51185 WHEP_TRS_2, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSYEP_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07814
Secondary accession number(s): A0AVA9
, B9EGH3, Q05BP6, Q05DF8, Q5DSM1, Q5H9S5, Q6PD57, Q86X73
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 9, 2010
Last modified: January 16, 2019
This is version 222 of the entry and version 5 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  7. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
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