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Q8CGC7 (SYEP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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

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
    Short name=ProRS
Gene names
Name:Eprs
Synonyms:Qprs
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity. 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.6

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 By similarity. Component of the GAIT complex. Ref.6

Domain

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

Post-translational modification

Phosphorylated at Ser-999 in macrophages in a IFN-gamma-dependent manner; the phosphorylation is involving CDK5 and is 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 By similarity. Ref.6

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.

Sequence caution

The sequence AAH40802.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15121512Bifunctional glutamate/proline--tRNA ligase HAMAP-Rule MF_01571
PRO_0000119744

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
Region1007 – 1512506Proline--tRNA ligase HAMAP-Rule MF_01571
Motif204 – 21411"HIGH" region HAMAP-Rule MF_01571
Motif432 – 4365"KMSKS" region HAMAP-Rule MF_01571
Compositional bias959 – 99133Asp/Glu/Lys-rich HAMAP-Rule MF_01571

Sites

Binding site2111ATP By similarity
Binding site3981ATP By similarity

Amino acid modifications

Modified residue3001N6-acetyllysine; alternate Ref.7
Modified residue3001N6-malonyllysine; alternate By similarity
Modified residue4171N6-acetyllysine By similarity
Modified residue4981N6-acetyllysine By similarity
Modified residue5351N6-acetyllysine By similarity
Modified residue5421N6-acetyllysine By similarity
Modified residue6371N6-acetyllysine By similarity
Modified residue7881N6-acetyllysine Ref.7
Modified residue8611N6-acetyllysine Ref.7
Modified residue8721Phosphotyrosine By similarity
Modified residue8851Phosphoserine By similarity
Modified residue9991Phosphoserine Ref.6
Modified residue15031N6-acetyllysine By similarity

Natural variations

Natural variant8711D → E.

Experimental info

Mutagenesis9991S → A: Not active in translation inhibition. Ref.6
Mutagenesis9991S → D: Active in translation inhibition (phosphomimetic). Ref.6
Sequence conflict941R → G in AAH40802. Ref.2
Sequence conflict1721N → S in AAH40802. Ref.2
Sequence conflict6181S → P in AAH40802. Ref.2
Sequence conflict9861G → R in X54327. Ref.4
Sequence conflict12901N → S in AAH94679. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CGC7 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: D14F6EA015B1BB6A

FASTA1,512170,079
        10         20         30         40         50         60 
MAALCLTVNA GNPPLEALLA VEHVKGDVSI SVEEGKENLL RVSETVAFTD VNSILRYLAR 

        70         80         90        100        110        120 
IATTSGLYGT NLMEHTEIDH WLEFSATKLS SCDRLTSAIN ELNHCLSLRT YLVGNSLTLA 

       130        140        150        160        170        180 
DLCVWATLKG SAAWQEHLKQ NKTLVHVKRW FGFLEAQQAF RSVGTKWDVS GNRATVAPDK 

       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 
AEREQRTESK HRKNSVEKNL 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 LKKEVVPVNV LDAQEEMKEV ARHPKNPDVG 

       550        560        570        580        590        600 
LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNINITKIH KNADGKITSL DAKLNLENKD 

       610        620        630        640        650        660 
YKKTTKITWL AESTHALSIP AVCVTYEHLI TKPVLGKDED FKQYINKDSK HEELMLGDPC 

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

       730        740        750        760        770        780 
VEISKKETSS APKERPAPAV SSTCATAEDS SVLYSRVAVQ GDVVRELKAK KAPKEDIDAA 

       790        800        810        820        830        840 
VKQLLTLKAE YKEKTGQEYK PGNPSAAAVQ TVSTKSSSNT VESTSLYNKV AAQGEVVRKL 

       850        860        870        880        890        900 
KAEKAPKAKV TEAVECLLSL KAEYKEKTGK DYVPGQPPAS QNSHSNPVSN AQPAGAEKPE 

       910        920        930        940        950        960 
AKVLFDRVAC QGEVVRKLKA EKASKDQVDS AVQELLQLKA QYKSLTGIEY KPVSATGAED 

       970        980        990       1000       1010       1020 
KDKKKKEKEN KSEKQNKPQK QNDGQGKDSS KSQGSGLSSG GAGEGQGPKK QTRLGLEAKK 

      1030       1040       1050       1060       1070       1080 
EENLAEWYSQ VITKSEMIEY YDVSGCYILR PWSYSIWESI KDFFDAEIKK LGVENCYFPI 

      1090       1100       1110       1120       1130       1140 
FVSQAALEKE KNHIEDFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL 

      1150       1160       1170       1180       1190       1200 
PVRLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATFE EAADEVLQIL ELYARVYEEL 

      1210       1220       1230       1240       1250       1260 
LAIPVVRGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGAT SHHLGQNFSK MCEIVFEDPK 

      1270       1280       1290       1300       1310       1320 
TPGEKQFAYQ CSWGLTTRTI GVMVMVHGDN MGLVLPPRVA SVQVVVIPCG ITNALSEEDR 

      1330       1340       1350       1360       1370       1380 
EALMAKCNEY RRRLLGANIR VRVDLRDNYS PGWKFNHWEL KGVPVRLEVG PRDMKSCQFV 

      1390       1400       1410       1420       1430       1440 
AVRRDTGEKL TIAEKEAEAK LEKVLEDIQL NLFTRASEDL KTHMVVSNTL EDFQKVLDAG 

      1450       1460       1470       1480       1490       1500 
KVAQIPFCGE IDCEDWIKKM TARDQDVEPG APSMGAKSLC IPFNPLCELQ PGAMCVCGKN 

      1510 
PAKFYTLFGR SY 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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].
Strain: C57BL/6 and FVB/N.
Tissue: Eye and Mammary tumor.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-962.
Strain: C57BL/6J.
Tissue: Pancreas.
[4]"M.musculus mRNA for glutamyl-tRNA synthetase."
Knippers R.
Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 406-1512.
[5]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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, PHOSPHORYLATION AT SER-999, SUBUNIT, RECONSTITUTION OF THE GAIT COMPLEX, MUTAGENESIS OF SER-999.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-300; LYS-788 AND LYS-861, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC129195 Genomic DNA. No translation available.
AC131980 Genomic DNA. No translation available.
BC040802 mRNA. Translation: AAH40802.1. Sequence problems.
BC094679 mRNA. Translation: AAH94679.1.
AK148463 mRNA. Translation: BAE28568.1.
X54327 mRNA. No translation available.
RefSeqNP_084011.1. NM_029735.1.
UniGeneMm.154511.
Mm.490980.

3D structure databases

ProteinModelPortalQ8CGC7.
SMRQ8CGC7. Positions 749-804, 826-875, 900-952, 1016-1512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid223350. 10 interactions.
IntActQ8CGC7. 3 interactions.
MINTMINT-1869828.

PTM databases

PhosphoSiteQ8CGC7.

Proteomic databases

PaxDbQ8CGC7.
PRIDEQ8CGC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046514; ENSMUSP00000045841; ENSMUSG00000026615.
GeneID107508.
KEGGmmu:107508.
UCSCuc007dze.1. mouse.

Organism-specific databases

CTD2058.
MGIMGI:97838. Eprs.

Phylogenomic databases

eggNOGCOG0442.
GeneTreeENSGT00550000074815.
HOGENOMHOG000022047.
HOVERGENHBG017875.
InParanoidQ8CGC7.
KOK14163.
OMAVAMLHIK.
OrthoDBEOG754HNH.
TreeFamTF300380.

Gene expression databases

ArrayExpressQ8CGC7.
BgeeQ8CGC7.
CleanExMM_EPRS.
GenevestigatorQ8CGC7.

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.
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.
PfamPF03129. 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. 2 hits.
PS51185. WHEP_TRS_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio358934.
PROQ8CGC7.
SOURCESearch...

Entry information

Entry nameSYEP_MOUSE
AccessionPrimary (citable) accession number: Q8CGC7
Secondary accession number(s): E9QKC4, Q3UFJ2, Q4VC16
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 27, 2011
Last modified: March 19, 2014
This is version 100 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries