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Database: UniProt/SWISS-PROT
Entry: SYEP_HUMAN
LinkDB: SYEP_HUMAN
Original site: SYEP_HUMAN 
ID   SYEP_HUMAN              Reviewed;        1512 AA.
AC   P07814; A0AVA9; B9EGH3; Q05BP6; Q05DF8; Q5DSM1; Q5H9S5; Q6PD57;
AC   Q86X73;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 5.
DT   03-SEP-2014, entry version 175.
DE   RecName: Full=Bifunctional glutamate/proline--tRNA ligase;
DE   AltName: Full=Bifunctional aminoacyl-tRNA synthetase;
DE   AltName: Full=Cell proliferation-inducing gene 32 protein;
DE   AltName: Full=Glutamatyl-prolyl-tRNA synthetase;
DE   Includes:
DE     RecName: Full=Glutamate--tRNA ligase;
DE              EC=6.1.1.17;
DE     AltName: Full=Glutamyl-tRNA synthetase;
DE              Short=GluRS;
DE   Includes:
DE     RecName: Full=Proline--tRNA ligase;
DE              EC=6.1.1.15;
DE     AltName: Full=Prolyl-tRNA synthetase;
GN   Name=EPRS; Synonyms=GLNS, PARS, QARS, QPRS; ORFNames=PIG32;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-308 AND
RP   VAL-1043.
RC   TISSUE=Bone marrow;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-308.
RC   TISSUE=Brain, Duodenum, Eye, Lung, Placenta, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 54-1512, AND VARIANTS GLU-308 AND
RP   HIS-334.
RX   PubMed=1988429;
RA   Fett R., Knippers R.;
RT   "The primary structure of human glutaminyl-tRNA synthetase. A highly
RT   conserved core, amino acid repeat regions, and homologies with
RT   translation elongation factors.";
RL   J. Biol. Chem. 266:1448-1455(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-1512, AND VARIANTS
RP   GLU-308 AND HIS-334.
RA   Kim J.W.;
RT   "Identification of a proliferation inducing gene.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 168-959, AND VARIANTS
RP   GLU-308 AND HIS-334.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=3290852; DOI=10.1093/nar/16.12.5391;
RA   Thoemmes P., Fett R., Schray B., Kunze N., Knippers R.;
RT   "The core region of human glutaminyl-tRNA synthetase homologies with
RT   the Escherichia coli and yeast enzymes.";
RL   Nucleic Acids Res. 16:5391-5406(1988).
RN   [7]
RP   FUNCTION.
RX   PubMed=1756734;
RA   Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M.;
RT   "A component of the multisynthetase complex is a multifunctional
RT   aminoacyl-tRNA synthetase.";
RL   EMBO J. 10:4267-4277(1991).
RN   [8]
RP   GENE STRUCTURE.
RX   PubMed=1556743; DOI=10.1007/BF00163851;
RA   Kaiser E., Eberhard D., Knippers R.;
RT   "Exons encoding the highly conserved part of human glutaminyl-tRNA
RT   synthetase.";
RL   J. Mol. Evol. 34:45-53(1992).
RN   [9]
RP   FUNCTION, AND IDENTIFICATION IN THE GAIT COMPLEX.
RX   PubMed=15479637; DOI=10.1016/j.cell.2004.09.030;
RA   Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L.,
RA   Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
RT   "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-
RT   specific silencing of translation.";
RL   Cell 119:195-208(2004).
RN   [10]
RP   INTERACTION WITH DUS2L.
RX   PubMed=15994936; DOI=10.1158/0008-5472.CAN-05-0600;
RA   Kato T., Daigo Y., Hayama S., Ishikawa N., Yamabuki T., Ito T.,
RA   Miyamoto M., Kondo S., Nakamura Y.;
RT   "A novel human tRNA-dihydrouridine synthase involved in pulmonary
RT   carcinogenesis.";
RL   Cancer Res. 65:5638-5646(2005).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-898, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-872; SER-882; SER-885;
RP   SER-886 AND THR-898, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [17]
RP   PHOSPHORYLATION AT SER-886 AND SER-999, AND INTERACTION WITH SYNCRIP.
RX   PubMed=19647514; DOI=10.1016/j.molcel.2009.05.028;
RA   Arif A., Jia J., Mukhopadhyay R., Willard B., Kinter M., Fox P.L.;
RT   "Two-site phosphorylation of EPRS coordinates multimodal regulation of
RT   noncanonical translational control activity.";
RL   Mol. Cell 35:164-180(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-886 AND
RP   SER-891, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-300; LYS-417; LYS-498;
RP   LYS-535; LYS-542; LYS-637; LYS-788 AND LYS-1503, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [21]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [22]
RP   MALONYLATION AT LYS-300.
RX   PubMed=21908771; DOI=10.1074/mcp.M111.012658;
RA   Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
RA   He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA   Dai J., Verdin E., Ye Y., Zhao Y.;
RT   "The first identification of lysine malonylation substrates and its
RT   regulatory enzyme.";
RL   Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN   [23]
RP   PHOSPHORYLATION AT SER-886.
RX   PubMed=21220307; DOI=10.1073/pnas.1011275108;
RA   Arif A., Jia J., Moodt R.A., DiCorleto P.E., Fox P.L.;
RT   "Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-
RT   dependent kinase 5 dictates transcript-selective translational
RT   control.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:1415-1420(2011).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [25]
RP   FUNCTION, RECONSTITUTION OF THE GAIT COMPLEX, AND MUTAGENESIS OF
RP   SER-886 AND SER-999.
RX   PubMed=23071094; DOI=10.1128/MCB.01168-12;
RA   Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
RT   "Heterotrimeric GAIT complex drives transcript-selective translation
RT   inhibition in murine macrophages.";
RL   Mol. Cell. Biol. 32:5046-5055(2012).
RN   [26]
RP   STRUCTURE BY NMR OF 749-805, AND RNA-BINDING.
RX   PubMed=11123902; DOI=10.1021/bi001393h;
RA   Jeong E.-J., Hwang G.-S., Kim K.H., Kim M.J., Kim S., Kim K.-S.;
RT   "Structural analysis of multifunctional peptide motifs in human
RT   bifunctional tRNA synthetase: identification of RNA-binding residues
RT   and functional implications for tandem repeats.";
RL   Biochemistry 39:15775-15782(2000).
CC   -!- FUNCTION: Catalyzes the attachment of the cognate amino acid to
CC       the corresponding tRNA in a two-step reaction: the amino acid is
CC       first activated by ATP to form a covalent intermediate with AMP
CC       and is then transferred to the acceptor end of the cognate tRNA.
CC       Component of the GAIT (gamma interferon-activated inhibitor of
CC       translation) complex which mediates interferon-gamma-induced
CC       transcript-selective translation inhibition in inflammation
CC       processes. Upon interferon-gamma activation and subsequent
CC       phosphorylation dissociates from the multisynthetase complex and
CC       assembles into the GAIT complex which binds to stem loop-
CC       containing GAIT elements in the 3'-UTR of diverse inflammatory
CC       mRNAs (such as ceruplasmin) and suppresses their translation.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu).
CC   -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
CC       diphosphate + L-prolyl-tRNA(Pro).
CC   -!- SUBUNIT: Component of the multisynthetase complex which is
CC       comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the
CC       monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl,
CC       arginyl, and aspartyl-tRNA synthetases as well as three auxiliary
CC       proteins, p18, p48 and p43. Interacts with DUS2L. Component of the
CC       GAIT complex; in humans the complex assembly seems to be a two-
CC       step process in which EPRS first associates with SYNCRIP to form a
CC       pre-GAIT complex which is deficient in GAIT element binding.
CC   -!- INTERACTION:
CC       P41252:IARS; NbExp=5; IntAct=EBI-355315, EBI-355303;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- DOMAIN: The WHEP-TRS domain is involved in RNA binding.
CC   -!- PTM: Phosphorylated at Ser-886 by CDK5 and at Ser-999 by an
CC       unknown kinase in a IFN-gamma-dependent manner in monocytes; these
CC       sequential phosphorylations are causing release from the
CC       multisynthetase complex, association with the GAIT complex and
CC       subsequent involvement in transcript-selective translation
CC       inhibition. Phosphorylation at Ser-999 is specifically required
CC       for the interaction of GAIT complex-associated RPL13A with eIF4G.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the class-I
CC       aminoacyl-tRNA synthetase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC       aminoacyl-tRNA synthetase family.
CC   -!- SIMILARITY: Contains 3 WHEP-TRS domains.
CC   -!- CAUTION: Was originally thought to be a glutaminyl-tRNA
CC       synthetase.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH15494.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH34797.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH46156.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH58921.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAS72877.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=CAA30354.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
CC       Sequence=CAA38224.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; CR933648; CAI45949.1; -; mRNA.
DR   EMBL; AC103590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC015494; AAH15494.1; ALT_SEQ; mRNA.
DR   EMBL; BC034797; AAH34797.1; ALT_SEQ; mRNA.
DR   EMBL; BC046156; AAH46156.1; ALT_SEQ; mRNA.
DR   EMBL; BC058921; AAH58921.1; ALT_SEQ; mRNA.
DR   EMBL; BC126275; AAI26276.1; -; mRNA.
DR   EMBL; BC136465; AAI36466.1; -; mRNA.
DR   EMBL; X54326; CAA38224.1; ALT_INIT; mRNA.
DR   EMBL; AY493416; AAS72877.1; ALT_INIT; mRNA.
DR   EMBL; X07466; CAA30354.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS31027.1; -.
DR   PIR; A38663; SYHUQT.
DR   RefSeq; NP_004437.2; NM_004446.2.
DR   UniGene; Hs.497788; -.
DR   PDB; 1FYJ; NMR; -; A=749-805.
DR   PDB; 4HVC; X-ray; 2.00 A; A/B=1003-1512.
DR   PDB; 4K86; X-ray; 2.40 A; A=1000-1512.
DR   PDB; 4K87; X-ray; 2.30 A; A=1000-1512.
DR   PDB; 4K88; X-ray; 2.62 A; A=1000-1512.
DR   PDBsum; 1FYJ; -.
DR   PDBsum; 4HVC; -.
DR   PDBsum; 4K86; -.
DR   PDBsum; 4K87; -.
DR   PDBsum; 4K88; -.
DR   ProteinModelPortal; P07814; -.
DR   SMR; P07814; 189-696, 749-805, 826-875, 903-952, 1016-1512.
DR   BioGrid; 108372; 73.
DR   DIP; DIP-40825N; -.
DR   IntAct; P07814; 20.
DR   MINT; MINT-141120; -.
DR   ChEMBL; CHEMBL3873; -.
DR   DrugBank; DB00142; L-Glutamic Acid.
DR   DrugBank; DB00172; L-Proline.
DR   PhosphoSite; P07814; -.
DR   DMDM; 288558855; -.
DR   MaxQB; P07814; -.
DR   PaxDb; P07814; -.
DR   PRIDE; P07814; -.
DR   Ensembl; ENST00000366923; ENSP00000355890; ENSG00000136628.
DR   GeneID; 2058; -.
DR   KEGG; hsa:2058; -.
DR   UCSC; uc001hly.1; human.
DR   CTD; 2058; -.
DR   GeneCards; GC01M220141; -.
DR   HGNC; HGNC:3418; EPRS.
DR   HPA; HPA026490; -.
DR   HPA; HPA030052; -.
DR   MIM; 138295; gene.
DR   neXtProt; NX_P07814; -.
DR   PharmGKB; PA27837; -.
DR   eggNOG; COG0442; -.
DR   HOVERGEN; HBG017875; -.
DR   InParanoid; P07814; -.
DR   KO; K14163; -.
DR   OMA; VAMLHIK; -.
DR   OrthoDB; EOG754HNH; -.
DR   PhylomeDB; P07814; -.
DR   TreeFam; TF300380; -.
DR   Reactome; REACT_15306; Cytosolic tRNA aminoacylation.
DR   EvolutionaryTrace; P07814; -.
DR   GeneWiki; EPRS; -.
DR   GenomeRNAi; 2058; -.
DR   NextBio; 8369; -.
DR   PRO; PR:P07814; -.
DR   Bgee; P07814; -.
DR   CleanEx; HS_EPRS; -.
DR   CleanEx; HS_QARS; -.
DR   Genevestigator; P07814; -.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; TAS:Reactome.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; TAS:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0035613; F:RNA stem-loop binding; IDA:UniProtKB.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
DR   GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR   Gene3D; 1.10.1160.10; -; 1.
DR   Gene3D; 1.10.287.10; -; 3.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 2.40.240.10; -; 2.
DR   Gene3D; 3.30.110.30; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR   InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR   InterPro; IPR017449; Pro-tRNA_synth_II.
DR   InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009068; S15_NS1_RNA-bd.
DR   InterPro; IPR000738; WHEP-TRS.
DR   PANTHER; PTHR10119; PTHR10119; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   Pfam; PF03950; tRNA-synt_1c_C; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF00458; WHEP-TRS; 3.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   SMART; SM00991; WHEP-TRS; 3.
DR   SUPFAM; SSF47060; SSF47060; 3.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF50715; SSF50715; 1.
DR   SUPFAM; SSF52954; SSF52954; 1.
DR   SUPFAM; SSF64586; SSF64586; 1.
DR   TIGRFAMs; TIGR00463; gltX_arch; 1.
DR   TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS00762; WHEP_TRS_1; 3.
DR   PROSITE; PS51185; WHEP_TRS_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW   Complete proteome; Cytoplasm; Ligase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism;
KW   Protein biosynthesis; Reference proteome; Repeat; RNA-binding;
KW   Translation regulation.
FT   CHAIN         1   1512       Bifunctional glutamate/proline--tRNA
FT                                ligase.
FT                                /FTId=PRO_0000119743.
FT   DOMAIN      749    805       WHEP-TRS 1.
FT   DOMAIN      822    878       WHEP-TRS 2.
FT   DOMAIN      900    956       WHEP-TRS 3.
FT   NP_BIND     432    436       ATP (By similarity).
FT   REGION      164    759       Glutamate--tRNA ligase.
FT   REGION      760    956       3 X 57 AA approximate repeats.
FT   REGION      959    991       Charged.
FT   REGION     1007   1512       Proline--tRNA ligase.
FT   MOTIF       204    214       "HIGH" region.
FT   MOTIF       432    436       "KMSKS" region.
FT   BINDING     211    211       ATP (By similarity).
FT   BINDING     398    398       ATP (By similarity).
FT   MOD_RES     300    300       N6-acetyllysine; alternate.
FT   MOD_RES     300    300       N6-malonyllysine; alternate.
FT   MOD_RES     417    417       N6-acetyllysine.
FT   MOD_RES     498    498       N6-acetyllysine.
FT   MOD_RES     535    535       N6-acetyllysine.
FT   MOD_RES     542    542       N6-acetyllysine.
FT   MOD_RES     637    637       N6-acetyllysine.
FT   MOD_RES     788    788       N6-acetyllysine.
FT   MOD_RES     861    861       N6-acetyllysine (By similarity).
FT   MOD_RES     872    872       Phosphotyrosine.
FT   MOD_RES     882    882       Phosphoserine.
FT   MOD_RES     885    885       Phosphoserine.
FT   MOD_RES     886    886       Phosphoserine; by CDK5.
FT   MOD_RES     891    891       Phosphoserine.
FT   MOD_RES     898    898       Phosphothreonine.
FT   MOD_RES     999    999       Phosphoserine.
FT   MOD_RES    1000   1000       Phosphoserine.
FT   MOD_RES    1503   1503       N6-acetyllysine.
FT   VARIANT     296    296       A -> P (in dbSNP:rs35999099).
FT                                /FTId=VAR_037288.
FT   VARIANT     308    308       D -> E (in dbSNP:rs2230301).
FT                                /FTId=VAR_037289.
FT   VARIANT     334    334       Q -> H (in dbSNP:rs1063236).
FT                                /FTId=VAR_037290.
FT   VARIANT     893    893       P -> H (in dbSNP:rs5030751).
FT                                /FTId=VAR_037291.
FT   VARIANT     913    913       E -> G (in dbSNP:rs2230302).
FT                                /FTId=VAR_057358.
FT   VARIANT    1043   1043       I -> V (in dbSNP:rs5030752).
FT                                /FTId=VAR_037292.
FT   VARIANT    1107   1107       S -> F (in dbSNP:rs12144752).
FT                                /FTId=VAR_037293.
FT   VARIANT    1399   1399       T -> N (in dbSNP:rs34559775).
FT                                /FTId=VAR_037294.
FT   MUTAGEN     886    886       S->A: Abolishes release from
FT                                multisynthetase complex and association
FT                                with GAIT complex assembly upon
FT                                interferon-gamma treatment. Abolishes
FT                                interaction with SYNCRIP.
FT   MUTAGEN     886    886       S->D: Not active in translation
FT                                inhibition (phosphomimetic) and abolishes
FT                                GAIT complex association with eiF4G. No
FT                                effect on interaction with SYNCRIP.
FT   MUTAGEN     999    999       S->A: Not active in translation
FT                                inhibition, and abolishes release from
FT                                multisynthetase complex and association
FT                                with GAIT complex assembly upon
FT                                interferon-gamma treatment.
FT   MUTAGEN     999    999       S->D: Active in translation inhibition
FT                                (phosphomimetic). No effect on GAIT
FT                                complex association with eiF4G.
FT   CONFLICT    532    532       K -> R (in Ref. 1; CAI45949).
FT   CONFLICT    594    594       L -> F (in Ref. 4; CAA38224 and 5;
FT                                AAS72877).
FT   CONFLICT    943    943       K -> E (in Ref. 1; CAI45949).
FT   CONFLICT   1177   1179       ATM -> VTV (in Ref. 1; CAI45949).
FT   CONFLICT   1441   1441       K -> R (in Ref. 1; CAI45949).
FT   HELIX       750    769
FT   HELIX       774    795
FT   TURN       1020   1022
FT   HELIX      1024   1034
FT   STRAND     1038   1040
FT   STRAND     1042   1045
FT   STRAND     1047   1049
FT   HELIX      1051   1070
FT   STRAND     1080   1083
FT   HELIX      1084   1087
FT   TURN       1088   1090
FT   HELIX      1095   1100
FT   STRAND     1102   1107
FT   STRAND     1110   1118
FT   STRAND     1120   1122
FT   HELIX      1123   1133
FT   HELIX      1137   1139
FT   STRAND     1142   1151
FT   TURN       1160   1162
FT   STRAND     1165   1178
FT   HELIX      1179   1198
FT   STRAND     1206   1209
FT   TURN       1212   1214
FT   STRAND     1219   1229
FT   TURN       1230   1233
FT   STRAND     1234   1245
FT   HELIX      1247   1252
FT   STRAND     1255   1257
FT   STRAND     1261   1264
FT   STRAND     1265   1267
FT   STRAND     1269   1276
FT   HELIX      1278   1287
FT   TURN       1297   1299
FT   STRAND     1303   1308
FT   STRAND     1313   1315
FT   HELIX      1317   1336
FT   STRAND     1341   1343
FT   STRAND     1347   1349
FT   HELIX      1351   1360
FT   STRAND     1364   1369
FT   HELIX      1371   1376
FT   STRAND     1378   1383
FT   TURN       1384   1386
FT   STRAND     1389   1393
FT   HELIX      1394   1396
FT   HELIX      1397   1423
FT   STRAND     1424   1426
FT   HELIX      1430   1438
FT   STRAND     1442   1447
FT   HELIX      1451   1462
FT   STRAND     1477   1484
FT   STRAND     1498   1501
FT   STRAND     1504   1509
SQ   SEQUENCE   1512 AA;  170591 MW;  2CE4311076719403 CRC64;
     MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD VNSILRYLAR
     VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSTIN ELNHCLSLRT YLVGNSLSLA
     DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW FGFLEAQQAF QSVGTKWDVS TTKARVAPEK
     KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN
     PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
     AEREQRIDSK HRKNPIEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC MRDPTLYRCK
     IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI
     WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS
     SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG
     LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKLNLENKD
     YKKTTKVTWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK HEELMLGDPC
     LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCVLI YIPDGHTKEM PTSGSKEKTK
     VEATKNETSA PFKERPTPSL NNNCTTSEDS LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA
     VKQLLSLKAE YKEKTGQEYK PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL
     KAEKSPKAKI NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE
     AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY KPVSATGAED
     KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS GAGEGQGPKK QTRLGLEAKK
     EENLADWYSQ VITKSEMIEY HDISGCYILR PWAYAIWEAI KDFFDAEIKK LGVENCYFPM
     FVSQSALEKE KTHVADFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL
     PIKLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL
     LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK MFEIVFEDPK
     IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA CVQVVIIPCG ITNALSEEDK
     EALIAKCNDY RRRLLSVNIR VRADLRDNYS PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV
     AVRRDTGEKL TVAENEAETK LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG
     KIVQIPFCGE IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN
     PAKYYTLFGR SY
//
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