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P07814

- SYEP_HUMAN

UniProt

P07814 - SYEP_HUMAN

Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

EPRS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 5 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    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. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.3 Publications

    Catalytic activityi

    ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
    ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei211 – 2111ATPBy similarity
    Binding sitei398 – 3981ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi432 – 4365ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate-tRNA ligase activity Source: Reactome
    3. proline-tRNA ligase activity Source: Reactome
    4. protein binding Source: IntAct
    5. RNA stem-loop binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to interferon-gamma Source: UniProtKB
    2. gene expression Source: Reactome
    3. glutamyl-tRNA aminoacylation Source: InterPro
    4. negative regulation of translation Source: UniProtKB
    5. prolyl-tRNA aminoacylation Source: InterPro
    6. protein complex assembly Source: ProtInc
    7. tRNA aminoacylation for protein translation Source: Reactome

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis, Translation regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    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:6.1.1.15)
    Alternative name(s):
    Prolyl-tRNA synthetase
    Gene namesi
    Name:EPRS
    Synonyms:GLNS, PARS, QARS, QPRS
    ORF Names:PIG32
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3418. EPRS.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. GAIT complex Source: UniProtKB
    4. membrane Source: UniProtKB
    5. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi886 – 8861S → A: Abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. Abolishes interaction with SYNCRIP. 1 Publication
    Mutagenesisi886 – 8861S → D: Not active in translation inhibition (phosphomimetic) and abolishes GAIT complex association with eiF4G. No effect on interaction with SYNCRIP. 1 Publication
    Mutagenesisi999 – 9991S → A: Not active in translation inhibition, and abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. 1 Publication
    Mutagenesisi999 – 9991S → D: Active in translation inhibition (phosphomimetic). No effect on GAIT complex association with eiF4G. 1 Publication

    Organism-specific databases

    PharmGKBiPA27837.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15121512Bifunctional glutamate/proline--tRNA ligasePRO_0000119743Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei300 – 3001N6-acetyllysine; alternate1 Publication
    Modified residuei300 – 3001N6-malonyllysine; alternate1 Publication
    Modified residuei417 – 4171N6-acetyllysine1 Publication
    Modified residuei498 – 4981N6-acetyllysine1 Publication
    Modified residuei535 – 5351N6-acetyllysine1 Publication
    Modified residuei542 – 5421N6-acetyllysine1 Publication
    Modified residuei637 – 6371N6-acetyllysine1 Publication
    Modified residuei788 – 7881N6-acetyllysine1 Publication
    Modified residuei861 – 8611N6-acetyllysineBy similarity
    Modified residuei872 – 8721Phosphotyrosine1 Publication
    Modified residuei882 – 8821Phosphoserine2 Publications
    Modified residuei885 – 8851Phosphoserine1 Publication
    Modified residuei886 – 8861Phosphoserine; by CDK55 Publications
    Modified residuei891 – 8911Phosphoserine1 Publication
    Modified residuei898 – 8981Phosphothreonine2 Publications
    Modified residuei999 – 9991Phosphoserine1 Publication
    Modified residuei1000 – 10001Phosphoserine1 Publication
    Modified residuei1503 – 15031N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated at Ser-886 by CDK5 and at Ser-999 by an unknown kinase in a IFN-gamma-dependent manner in monocytes; these sequential phosphorylations are causing release from the multisynthetase complex, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition. Phosphorylation at Ser-999 is specifically required for the interaction of GAIT complex-associated RPL13A with eIF4G.7 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP07814.
    PaxDbiP07814.
    PRIDEiP07814.

    PTM databases

    PhosphoSiteiP07814.

    Expressioni

    Gene expression databases

    BgeeiP07814.
    CleanExiHS_EPRS.
    HS_QARS.
    GenevestigatoriP07814.

    Organism-specific databases

    HPAiHPA026490.
    HPA030052.

    Interactioni

    Subunit structurei

    Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43. Interacts with DUS2L. Component of the GAIT complex; in humans 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.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IARSP412525EBI-355315,EBI-355303

    Protein-protein interaction databases

    BioGridi108372. 73 interactions.
    DIPiDIP-40825N.
    IntActiP07814. 21 interactions.
    MINTiMINT-141120.

    Structurei

    Secondary structure

    1
    1512
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi750 – 76920
    Helixi774 – 79522
    Turni1020 – 10223
    Helixi1024 – 103411
    Beta strandi1038 – 10403
    Beta strandi1042 – 10454
    Beta strandi1047 – 10493
    Helixi1051 – 107020
    Beta strandi1080 – 10834
    Helixi1084 – 10874
    Turni1088 – 10903
    Helixi1095 – 11006
    Beta strandi1102 – 11076
    Beta strandi1110 – 11189
    Beta strandi1120 – 11223
    Helixi1123 – 113311
    Helixi1137 – 11393
    Beta strandi1142 – 115110
    Turni1160 – 11623
    Beta strandi1165 – 117814
    Helixi1179 – 119820
    Beta strandi1206 – 12094
    Turni1212 – 12143
    Beta strandi1219 – 122911
    Turni1230 – 12334
    Beta strandi1234 – 124512
    Helixi1247 – 12526
    Beta strandi1255 – 12573
    Beta strandi1261 – 12644
    Beta strandi1265 – 12673
    Beta strandi1269 – 12768
    Helixi1278 – 128710
    Turni1297 – 12993
    Beta strandi1303 – 13086
    Beta strandi1313 – 13153
    Helixi1317 – 133620
    Beta strandi1341 – 13433
    Beta strandi1347 – 13493
    Helixi1351 – 136010
    Beta strandi1364 – 13696
    Helixi1371 – 13766
    Beta strandi1378 – 13836
    Turni1384 – 13863
    Beta strandi1389 – 13935
    Helixi1394 – 13963
    Helixi1397 – 142327
    Beta strandi1424 – 14263
    Helixi1430 – 14389
    Beta strandi1442 – 14476
    Helixi1451 – 146212
    Beta strandi1477 – 14848
    Beta strandi1498 – 15014
    Beta strandi1504 – 15096

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FYJNMR-A749-805[»]
    4HVCX-ray2.00A/B1003-1512[»]
    4K86X-ray2.40A1000-1512[»]
    4K87X-ray2.30A1000-1512[»]
    4K88X-ray2.62A1000-1512[»]
    ProteinModelPortaliP07814.
    SMRiP07814. Positions 189-696, 749-805, 826-875, 903-952, 1016-1512.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07814.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini749 – 80557WHEP-TRS 1Add
    BLAST
    Domaini822 – 87857WHEP-TRS 2Add
    BLAST
    Domaini900 – 95657WHEP-TRS 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni164 – 759596Glutamate--tRNA ligaseAdd
    BLAST
    Regioni760 – 9561973 X 57 AA approximate repeatsAdd
    BLAST
    Regioni959 – 99133ChargedAdd
    BLAST
    Regioni1007 – 1512506Proline--tRNA ligaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi204 – 21411"HIGH" regionAdd
    BLAST
    Motifi432 – 4365"KMSKS" region

    Domaini

    The WHEP-TRS domain is involved in RNA binding.

    Sequence similaritiesi

    In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family.Curated
    In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family.Curated
    Contains 3 WHEP-TRS domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0442.
    HOVERGENiHBG017875.
    InParanoidiP07814.
    KOiK14163.
    OMAiVAMLHIK.
    OrthoDBiEOG754HNH.
    PhylomeDBiP07814.
    TreeFamiTF300380.

    Family and domain databases

    Gene3Di1.10.1160.10. 1 hit.
    1.10.287.10. 3 hits.
    1.20.1050.10. 1 hit.
    2.40.240.10. 2 hits.
    3.30.110.30. 1 hit.
    3.40.50.620. 2 hits.
    3.40.50.800. 1 hit.
    HAMAPiMF_01571. Pro_tRNA_synth_type3.
    InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR004526. Glu-tRNA-synth_arc/euk.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR004046. GST_C.
    IPR004499. Pro-tRNA-ligase_IIa_arc-type.
    IPR016061. Pro-tRNA_ligase_II_C.
    IPR017449. Pro-tRNA_synth_II.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009068. S15_NS1_RNA-bd.
    IPR000738. WHEP-TRS.
    [Graphical view]
    PANTHERiPTHR10119. PTHR10119. 1 hit.
    PfamiPF14497. GST_C_3. 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.
    [Graphical view]
    PRINTSiPR00987. TRNASYNTHGLU.
    SMARTiSM00946. ProRS-C_1. 1 hit.
    SM00991. WHEP-TRS. 3 hits.
    [Graphical view]
    SUPFAMiSSF47060. SSF47060. 3 hits.
    SSF47616. SSF47616. 1 hit.
    SSF50715. SSF50715. 1 hit.
    SSF52954. SSF52954. 1 hit.
    SSF64586. SSF64586. 1 hit.
    TIGRFAMsiTIGR00463. gltX_arch. 1 hit.
    TIGR00408. proS_fam_I. 1 hit.
    PROSITEiPS00178. 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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07814-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD     50
    VNSILRYLAR VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSTIN 100
    ELNHCLSLRT YLVGNSLSLA DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW 150
    FGFLEAQQAF QSVGTKWDVS TTKARVAPEK KQDVGKFVEL PGAEMGKVTV 200
    RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN PEKEKEDFEK 250
    VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK 300
    AEREQRIDSK HRKNPIEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC 350
    MRDPTLYRCK IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH 400
    DRDEQFYWII EALGIRKPYI WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW 450
    DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS SRSVVNMEWD KIWAFNKKVI 500
    DPVAPRYVAL LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG LKPVWYSPKV 550
    FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKLNLENKD 600
    YKKTTKVTWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK 650
    HEELMLGDPC LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCVLI 700
    YIPDGHTKEM PTSGSKEKTK VEATKNETSA PFKERPTPSL NNNCTTSEDS 750
    LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA VKQLLSLKAE YKEKTGQEYK 800
    PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL KAEKSPKAKI 850
    NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE 900
    AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY 950
    KPVSATGAED KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS 1000
    GAGEGQGPKK QTRLGLEAKK EENLADWYSQ VITKSEMIEY HDISGCYILR 1050
    PWAYAIWEAI KDFFDAEIKK LGVENCYFPM FVSQSALEKE KTHVADFAPE 1100
    VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL PIKLNQWCNV 1150
    VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL 1200
    LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK 1250
    MFEIVFEDPK IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA 1300
    CVQVVIIPCG ITNALSEEDK EALIAKCNDY RRRLLSVNIR VRADLRDNYS 1350
    PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV AVRRDTGEKL TVAENEAETK 1400
    LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG KIVQIPFCGE 1450
    IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN 1500
    PAKYYTLFGR SY 1512
    Length:1,512
    Mass (Da):170,591
    Last modified:February 9, 2010 - v5
    Checksum:i2CE4311076719403
    GO

    Sequence cautioni

    The sequence AAH15494.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH34797.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH46156.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH58921.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence CAA30354.1 differs from that shown. Reason: Sequencing errors.
    The sequence AAS72877.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA38224.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti532 – 5321K → R in CAI45949. (PubMed:17974005)Curated
    Sequence conflicti594 – 5941L → F in CAA38224. (PubMed:1988429)Curated
    Sequence conflicti594 – 5941L → F in AAS72877. 1 PublicationCurated
    Sequence conflicti943 – 9431K → E in CAI45949. (PubMed:17974005)Curated
    Sequence conflicti1177 – 11793ATM → VTV in CAI45949. (PubMed:17974005)Curated
    Sequence conflicti1441 – 14411K → R in CAI45949. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti296 – 2961A → P.
    Corresponds to variant rs35999099 [ dbSNP | Ensembl ].
    VAR_037288
    Natural varianti308 – 3081D → E.5 Publications
    Corresponds to variant rs2230301 [ dbSNP | Ensembl ].
    VAR_037289
    Natural varianti334 – 3341Q → H.3 Publications
    Corresponds to variant rs1063236 [ dbSNP | Ensembl ].
    VAR_037290
    Natural varianti893 – 8931P → H.
    Corresponds to variant rs5030751 [ dbSNP | Ensembl ].
    VAR_037291
    Natural varianti913 – 9131E → G.
    Corresponds to variant rs2230302 [ dbSNP | Ensembl ].
    VAR_057358
    Natural varianti1043 – 10431I → V.1 Publication
    Corresponds to variant rs5030752 [ dbSNP | Ensembl ].
    VAR_037292
    Natural varianti1107 – 11071S → F.
    Corresponds to variant rs12144752 [ dbSNP | Ensembl ].
    VAR_037293
    Natural varianti1399 – 13991T → N.
    Corresponds to variant rs34559775 [ dbSNP | Ensembl ].
    VAR_037294

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

    EnsembliENST00000366923; ENSP00000355890; ENSG00000136628.
    GeneIDi2058.
    KEGGihsa:2058.
    UCSCiuc001hly.1. human.

    Polymorphism databases

    DMDMi288558855.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS31027.1.
    PIRi A38663. SYHUQT.
    RefSeqi NP_004437.2. NM_004446.2.
    UniGenei Hs.497788.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FYJ NMR - A 749-805 [» ]
    4HVC X-ray 2.00 A/B 1003-1512 [» ]
    4K86 X-ray 2.40 A 1000-1512 [» ]
    4K87 X-ray 2.30 A 1000-1512 [» ]
    4K88 X-ray 2.62 A 1000-1512 [» ]
    ProteinModelPortali P07814.
    SMRi P07814. Positions 189-696, 749-805, 826-875, 903-952, 1016-1512.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108372. 73 interactions.
    DIPi DIP-40825N.
    IntActi P07814. 21 interactions.
    MINTi MINT-141120.

    Chemistry

    ChEMBLi CHEMBL3873.
    DrugBanki DB00142. L-Glutamic Acid.
    DB00172. L-Proline.

    PTM databases

    PhosphoSitei P07814.

    Polymorphism databases

    DMDMi 288558855.

    Proteomic databases

    MaxQBi P07814.
    PaxDbi P07814.
    PRIDEi P07814.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366923 ; ENSP00000355890 ; ENSG00000136628 .
    GeneIDi 2058.
    KEGGi hsa:2058.
    UCSCi uc001hly.1. human.

    Organism-specific databases

    CTDi 2058.
    GeneCardsi GC01M220141.
    HGNCi HGNC:3418. EPRS.
    HPAi HPA026490.
    HPA030052.
    MIMi 138295. gene.
    neXtProti NX_P07814.
    PharmGKBi PA27837.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0442.
    HOVERGENi HBG017875.
    InParanoidi P07814.
    KOi K14163.
    OMAi VAMLHIK.
    OrthoDBi EOG754HNH.
    PhylomeDBi P07814.
    TreeFami TF300380.

    Enzyme and pathway databases

    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    EvolutionaryTracei P07814.
    GeneWikii EPRS.
    GenomeRNAii 2058.
    NextBioi 8369.
    PROi P07814.
    SOURCEi Search...

    Gene expression databases

    Bgeei P07814.
    CleanExi HS_EPRS.
    HS_QARS.
    Genevestigatori P07814.

    Family and domain databases

    Gene3Di 1.10.1160.10. 1 hit.
    1.10.287.10. 3 hits.
    1.20.1050.10. 1 hit.
    2.40.240.10. 2 hits.
    3.30.110.30. 1 hit.
    3.40.50.620. 2 hits.
    3.40.50.800. 1 hit.
    HAMAPi MF_01571. Pro_tRNA_synth_type3.
    InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR001412. aa-tRNA-synth_I_CS.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR004526. Glu-tRNA-synth_arc/euk.
    IPR000924. Glu/Gln-tRNA-synth.
    IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
    IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
    IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR004046. GST_C.
    IPR004499. Pro-tRNA-ligase_IIa_arc-type.
    IPR016061. Pro-tRNA_ligase_II_C.
    IPR017449. Pro-tRNA_synth_II.
    IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
    IPR011035. Ribosomal_L25/Gln-tRNA_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009068. S15_NS1_RNA-bd.
    IPR000738. WHEP-TRS.
    [Graphical view ]
    PANTHERi PTHR10119. PTHR10119. 1 hit.
    Pfami PF14497. GST_C_3. 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.
    [Graphical view ]
    PRINTSi PR00987. TRNASYNTHGLU.
    SMARTi SM00946. ProRS-C_1. 1 hit.
    SM00991. WHEP-TRS. 3 hits.
    [Graphical view ]
    SUPFAMi SSF47060. SSF47060. 3 hits.
    SSF47616. SSF47616. 1 hit.
    SSF50715. SSF50715. 1 hit.
    SSF52954. SSF52954. 1 hit.
    SSF64586. SSF64586. 1 hit.
    TIGRFAMsi TIGR00463. gltX_arch. 1 hit.
    TIGR00408. proS_fam_I. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-308 AND VAL-1043.
      Tissue: Bone marrow.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-308.
      Tissue: Brain, Duodenum, Eye, Lung, Placenta and Testis.
    4. "The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors."
      Fett R., Knippers R.
      J. Biol. Chem. 266:1448-1455(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-1512, VARIANTS GLU-308 AND HIS-334.
    5. "Identification of a proliferation inducing gene."
      Kim J.W.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-1512, VARIANTS GLU-308 AND HIS-334.
    6. "The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes."
      Thoemmes P., Fett R., Schray B., Kunze N., Knippers R.
      Nucleic Acids Res. 16:5391-5406(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 168-959, VARIANTS GLU-308 AND HIS-334.
      Tissue: Cervix carcinoma.
    7. "A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase."
      Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M.
      EMBO J. 10:4267-4277(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase."
      Kaiser E., Eberhard D., Knippers R.
      J. Mol. Evol. 34:45-53(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE STRUCTURE.
    9. "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation."
      Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.
      Cell 119:195-208(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE GAIT COMPLEX.
    10. "A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis."
      Kato T., Daigo Y., Hayama S., Ishikawa N., Yamabuki T., Ito T., Miyamoto M., Kondo S., Nakamura Y.
      Cancer Res. 65:5638-5646(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DUS2L.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-898, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-872; SER-882; SER-885; SER-886 AND THR-898, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity."
      Arif A., Jia J., Mukhopadhyay R., Willard B., Kinter M., Fox P.L.
      Mol. Cell 35:164-180(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-886 AND SER-999, INTERACTION WITH SYNCRIP.
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-886 AND SER-891, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-300; LYS-417; LYS-498; LYS-535; LYS-542; LYS-637; LYS-788 AND LYS-1503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: MALONYLATION AT LYS-300.
    23. "Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-dependent kinase 5 dictates transcript-selective translational control."
      Arif A., Jia J., Moodt R.A., DiCorleto P.E., Fox P.L.
      Proc. Natl. Acad. Sci. U.S.A. 108:1415-1420(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-886.
    24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
      Arif A., Chatterjee P., Moodt R.A., Fox P.L.
      Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RECONSTITUTION OF THE GAIT COMPLEX, MUTAGENESIS OF SER-886 AND SER-999.
    26. "Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats."
      Jeong E.-J., Hwang G.-S., Kim K.H., Kim M.J., Kim S., Kim K.-S.
      Biochemistry 39:15775-15782(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 749-805, RNA-BINDING.

    Entry informationi

    Entry nameiSYEP_HUMAN
    AccessioniPrimary (citable) accession number: P07814
    Secondary accession number(s): A0AVA9
    , B9EGH3, Q05BP6, Q05DF8, Q5DSM1, Q5H9S5, Q6PD57, Q86X73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 176 of the entry and version 5 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Caution

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3