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P07814 (SYEP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Glutamate--tRNA ligase
    EC=6.1.1.17
    Alternative name(s):
    Glutamyl-tRNA synthetase
    Short name=GluRS
  2. Proline--tRNA ligase
    EC=6.1.1.15
    Alternative name(s):
    Prolyl-tRNA synthetase
Gene names
Name:EPRS
Synonyms:GLNS, PARS, QARS, QPRS
ORF Names:PIG32
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1512 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.9 Ref.25

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_01571

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01571

Subunit structure

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. Ref.9 Ref.10 Ref.17

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_01571.

Domain

The WHEP-TRS domain is involved in RNA binding. HAMAP-Rule MF_01571

Post-translational modification

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. Ref.17 Ref.23

Sequence similarities

In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family.

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

Contains 3 WHEP-TRS domains.

Caution

Was originally thought to be a glutaminyl-tRNA synthetase.

Sequence caution

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 AAS72877.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA30354.1 differs from that shown. Reason: Sequencing errors.

The sequence CAA38224.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processProtein biosynthesis
Translation regulation
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to interferon-gamma

Inferred from direct assay Ref.9. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

glutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

negative regulation of translation

Inferred from direct assay Ref.25. Source: UniProtKB

prolyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

protein complex assembly

Traceable author statement PubMed 8188258. Source: ProtInc

tRNA aminoacylation for protein translation

Traceable author statement. Source: Reactome

   Cellular_componentGAIT complex

Inferred from direct assay Ref.9Ref.25. Source: UniProtKB

cytoplasm

Traceable author statement PubMed 8188258. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

ribonucleoprotein complex

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA stem-loop binding

Inferred from direct assay Ref.9. Source: UniProtKB

glutamate-tRNA ligase activity

Traceable author statement. Source: Reactome

proline-tRNA ligase activity

Traceable author statement. Source: Reactome

protein binding

Inferred from physical interaction PubMed 10913161PubMed 9556618. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IARSP412525EBI-355315,EBI-355303

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15121512Bifunctional glutamate/proline--tRNA ligase HAMAP-Rule MF_01571
PRO_0000119743

Regions

Domain749 – 80557WHEP-TRS 1
Domain822 – 87857WHEP-TRS 2
Domain900 – 95657WHEP-TRS 3
Nucleotide binding432 – 4365ATP By similarity
Region164 – 759596Glutamate--tRNA ligase HAMAP-Rule MF_01571
Region760 – 9561973 X 57 AA approximate repeats HAMAP-Rule MF_01571
Region959 – 99133Charged HAMAP-Rule MF_01571
Region1007 – 1512506Proline--tRNA ligase HAMAP-Rule MF_01571
Motif204 – 21411"HIGH" region HAMAP-Rule MF_01571
Motif432 – 4365"KMSKS" region HAMAP-Rule MF_01571

Sites

Binding site2111ATP By similarity
Binding site3981ATP By similarity

Amino acid modifications

Modified residue3001N6-acetyllysine; alternate Ref.19
Modified residue3001N6-malonyllysine; alternate Ref.22
Modified residue4171N6-acetyllysine Ref.19
Modified residue4981N6-acetyllysine Ref.19
Modified residue5351N6-acetyllysine Ref.19
Modified residue5421N6-acetyllysine Ref.19
Modified residue6371N6-acetyllysine Ref.19
Modified residue7881N6-acetyllysine Ref.19
Modified residue8611N6-acetyllysine By similarity
Modified residue8721Phosphotyrosine Ref.15
Modified residue8821Phosphoserine Ref.15 Ref.18
Modified residue8851Phosphoserine Ref.15
Modified residue8861Phosphoserine; by CDK5 Ref.15 Ref.17 Ref.18 Ref.23 Ref.24
Modified residue8911Phosphoserine Ref.18
Modified residue8981Phosphothreonine Ref.12 Ref.15
Modified residue9991Phosphoserine Ref.17
Modified residue10001Phosphoserine Ref.20
Modified residue15031N6-acetyllysine Ref.19

Natural variations

Natural variant2961A → P.
Corresponds to variant rs35999099 [ dbSNP | Ensembl ].
VAR_037288
Natural variant3081D → E. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6
Corresponds to variant rs2230301 [ dbSNP | Ensembl ].
VAR_037289
Natural variant3341Q → H. Ref.4 Ref.5 Ref.6
Corresponds to variant rs1063236 [ dbSNP | Ensembl ].
VAR_037290
Natural variant8931P → H.
Corresponds to variant rs5030751 [ dbSNP | Ensembl ].
VAR_037291
Natural variant9131E → G.
Corresponds to variant rs2230302 [ dbSNP | Ensembl ].
VAR_057358
Natural variant10431I → V. Ref.1
Corresponds to variant rs5030752 [ dbSNP | Ensembl ].
VAR_037292
Natural variant11071S → F.
Corresponds to variant rs12144752 [ dbSNP | Ensembl ].
VAR_037293
Natural variant13991T → N.
Corresponds to variant rs34559775 [ dbSNP | Ensembl ].
VAR_037294

Experimental info

Mutagenesis8861S → A: Abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. Abolishes interaction with SYNCRIP. Ref.25
Mutagenesis8861S → D: Not active in translation inhibition (phosphomimetic) and abolishes GAIT complex association with eiF4G. No effect on interaction with SYNCRIP. Ref.25
Mutagenesis9991S → A: Not active in translation inhibition, and abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. Ref.25
Mutagenesis9991S → D: Active in translation inhibition (phosphomimetic). No effect on GAIT complex association with eiF4G. Ref.25
Sequence conflict5321K → R in CAI45949. Ref.1
Sequence conflict5941L → F in CAA38224. Ref.4
Sequence conflict5941L → F in AAS72877. Ref.5
Sequence conflict9431K → E in CAI45949. Ref.1
Sequence conflict1177 – 11793ATM → VTV in CAI45949. Ref.1
Sequence conflict14411K → R in CAI45949. Ref.1

Secondary structure

................................................................................................ 1512
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07814 [UniParc].

Last modified February 9, 2010. Version 5.
Checksum: 2CE4311076719403

FASTA1,512170,591
        10         20         30         40         50         60 
MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD VNSILRYLAR 

        70         80         90        100        110        120 
VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSTIN ELNHCLSLRT YLVGNSLSLA 

       130        140        150        160        170        180 
DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW FGFLEAQQAF QSVGTKWDVS TTKARVAPEK 

       190        200        210        220        230        240 
KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN 

       250        260        270        280        290        300 
PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK 

       310        320        330        340        350        360 
AEREQRIDSK HRKNPIEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC MRDPTLYRCK 

       370        380        390        400        410        420 
IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI 

       430        440        450        460        470        480 
WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS 

       490        500        510        520        530        540 
SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG 

       550        560        570        580        590        600 
LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKLNLENKD 

       610        620        630        640        650        660 
YKKTTKVTWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK HEELMLGDPC 

       670        680        690        700        710        720 
LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCVLI YIPDGHTKEM PTSGSKEKTK 

       730        740        750        760        770        780 
VEATKNETSA PFKERPTPSL NNNCTTSEDS LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA 

       790        800        810        820        830        840 
VKQLLSLKAE YKEKTGQEYK PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL 

       850        860        870        880        890        900 
KAEKSPKAKI NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE 

       910        920        930        940        950        960 
AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY KPVSATGAED 

       970        980        990       1000       1010       1020 
KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS GAGEGQGPKK QTRLGLEAKK 

      1030       1040       1050       1060       1070       1080 
EENLADWYSQ VITKSEMIEY HDISGCYILR PWAYAIWEAI KDFFDAEIKK LGVENCYFPM 

      1090       1100       1110       1120       1130       1140 
FVSQSALEKE KTHVADFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL 

      1150       1160       1170       1180       1190       1200 
PIKLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL 

      1210       1220       1230       1240       1250       1260 
LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK MFEIVFEDPK 

      1270       1280       1290       1300       1310       1320 
IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA CVQVVIIPCG ITNALSEEDK 

      1330       1340       1350       1360       1370       1380 
EALIAKCNDY RRRLLSVNIR VRADLRDNYS PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV 

      1390       1400       1410       1420       1430       1440 
AVRRDTGEKL TVAENEAETK LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG 

      1450       1460       1470       1480       1490       1500 
KIVQIPFCGE IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN 

      1510 
PAKYYTLFGR SY 

« Hide

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31027.1.
PIRSYHUQT. A38663.
RefSeqNP_004437.2. NM_004446.2.
UniGeneHs.497788.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FYJNMR-A749-805[»]
4HVCX-ray2.00A/B1003-1512[»]
4K86X-ray2.40A1000-1512[»]
4K87X-ray2.30A1000-1512[»]
4K88X-ray2.62A1000-1512[»]
ProteinModelPortalP07814.
SMRP07814. Positions 189-696, 749-805, 826-875, 903-952, 1016-1512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108372. 77 interactions.
DIPDIP-40825N.
IntActP07814. 20 interactions.
MINTMINT-141120.

Chemistry

ChEMBLCHEMBL3873.
DrugBankDB00142. L-Glutamic Acid.
DB00172. L-Proline.

PTM databases

PhosphoSiteP07814.

Polymorphism databases

DMDM288558855.

Proteomic databases

MaxQBP07814.
PaxDbP07814.
PRIDEP07814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366923; ENSP00000355890; ENSG00000136628.
GeneID2058.
KEGGhsa:2058.
UCSCuc001hly.1. human.

Organism-specific databases

CTD2058.
GeneCardsGC01M220141.
HGNCHGNC:3418. EPRS.
HPAHPA026490.
HPA030052.
MIM138295. gene.
neXtProtNX_P07814.
PharmGKBPA27837.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0442.
HOVERGENHBG017875.
InParanoidP07814.
KOK14163.
OMAVAMLHIK.
OrthoDBEOG754HNH.
PhylomeDBP07814.
TreeFamTF300380.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

BgeeP07814.
CleanExHS_EPRS.
HS_QARS.
GenevestigatorP07814.

Family and domain databases

Gene3D1.10.1160.10. 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.
HAMAPMF_01571. Pro_tRNA_synth_type3.
InterProIPR002314. 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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF14497. 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]
PRINTSPR00987. TRNASYNTHGLU.
SMARTSM00946. ProRS-C_1. 1 hit.
SM00991. WHEP-TRS. 3 hits.
[Graphical view]
SUPFAMSSF47060. SSF47060. 3 hits.
SSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
SSF52954. SSF52954. 1 hit.
SSF64586. SSF64586. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
TIGR00408. proS_fam_I. 1 hit.
PROSITEPS00178. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP07814.
GeneWikiEPRS.
GenomeRNAi2058.
NextBio8369.
PROP07814.
SOURCESearch...

Entry information

Entry nameSYEP_HUMAN
AccessionPrimary (citable) accession number: P07814
Secondary accession number(s): A0AVA9 expand/collapse secondary AC list , B9EGH3, Q05BP6, Q05DF8, Q5DSM1, Q5H9S5, Q6PD57, Q86X73
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 9, 2010
Last modified: July 9, 2014
This is version 174 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries