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Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

Eprs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (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.By similarity1 Publication

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)DescriptionActionsGraphical viewLength
Binding sitei211ATPBy similarity1
Binding sitei398ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi432 – 436ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

  • cellular response to interferon-gamma Source: UniProtKB
  • glutamyl-tRNA aminoacylation Source: InterPro
  • negative regulation of translation Source: UniProtKB
  • prolyl-tRNA aminoacylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional glutamate/proline--tRNA ligase
Alternative name(s):
Bifunctional aminoacyl-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
Short name:
ProRS
Gene namesi
Name:Eprs
Synonyms:Qprs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97838. Eprs.

Subcellular locationi

GO - Cellular componenti

  • aminoacyl-tRNA synthetase multienzyme complex Source: MGI
  • cytoplasm Source: GO_Central
  • GAIT complex Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: MGI
  • membrane Source: MGI
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi999S → A: Not active in translation inhibition. 1 Publication1
Mutagenesisi999S → D: Active in translation inhibition (phosphomimetic). 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001197441 – 1512Bifunctional glutamate/proline--tRNA ligaseAdd BLAST1512

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei300N6-acetyllysine; alternateCombined sources1
Modified residuei300N6-malonyllysine; alternateBy similarity1
Modified residuei355PhosphothreonineBy similarity1
Modified residuei417N6-acetyllysineBy similarity1
Modified residuei434PhosphoserineBy similarity1
Modified residuei498N6-acetyllysineBy similarity1
Modified residuei535N6-acetyllysineBy similarity1
Modified residuei542N6-acetyllysineBy similarity1
Modified residuei637N6-acetyllysineBy similarity1
Modified residuei788N6-acetyllysineCombined sources1
Modified residuei861N6-acetyllysineCombined sources1
Modified residuei872PhosphotyrosineBy similarity1
Modified residuei885PhosphoserineBy similarity1
Modified residuei998PhosphoserineBy similarity1
Modified residuei999Phosphoserine1 Publication1
Modified residuei1152Omega-N-methylarginineBy similarity1
Modified residuei1350PhosphoserineBy similarity1
Modified residuei1503N6-acetyllysineBy similarity1

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ8CGC7.
MaxQBiQ8CGC7.
PaxDbiQ8CGC7.
PeptideAtlasiQ8CGC7.
PRIDEiQ8CGC7.

PTM databases

iPTMnetiQ8CGC7.
PhosphoSitePlusiQ8CGC7.
SwissPalmiQ8CGC7.

Expressioni

Gene expression databases

BgeeiENSMUSG00000026615.
CleanExiMM_EPRS.
ExpressionAtlasiQ8CGC7. baseline and differential.
GenevisibleiQ8CGC7. MM.

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 (By similarity). Component of the GAIT complex.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi223350. 4 interactors.
IntActiQ8CGC7. 5 interactors.
MINTiMINT-1869828.
STRINGi10090.ENSMUSP00000045841.

Structurei

3D structure databases

ProteinModelPortaliQ8CGC7.
SMRiQ8CGC7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini749 – 805WHEP-TRS 1Add BLAST57
Domaini822 – 878WHEP-TRS 2Add BLAST57
Domaini900 – 956WHEP-TRS 3Add BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni164 – 759Glutamate--tRNA ligaseAdd BLAST596
Regioni760 – 9563 X 57 AA approximate repeatsAdd BLAST197
Regioni1007 – 1512Proline--tRNA ligaseAdd BLAST506

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi204 – 214"HIGH" regionAdd BLAST11
Motifi432 – 436"KMSKS" region5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi959 – 991Asp/Glu/Lys-richAdd BLAST33

Domaini

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

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

eggNOGiKOG1147. Eukaryota.
KOG4163. Eukaryota.
COG0008. LUCA.
COG0442. LUCA.
GeneTreeiENSGT00550000074815.
HOGENOMiHOG000022047.
HOVERGENiHBG017875.
InParanoidiQ8CGC7.
KOiK14163.
OMAiVAMLHIK.
OrthoDBiEOG091G04TK.
TreeFamiTF300380.

Family and domain databases

CDDicd00778. ProRS_core_arch_euk. 1 hit.
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. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
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.
IPR033721. ProRS_core_arch_euk.
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_dom.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF00458. WHEP-TRS. 3 hits.
[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. 2 hits.
PS51185. WHEP_TRS_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CGC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALCLTVNA GNPPLEALLA VEHVKGDVSI SVEEGKENLL RVSETVAFTD
60 70 80 90 100
VNSILRYLAR IATTSGLYGT NLMEHTEIDH WLEFSATKLS SCDRLTSAIN
110 120 130 140 150
ELNHCLSLRT YLVGNSLTLA DLCVWATLKG SAAWQEHLKQ NKTLVHVKRW
160 170 180 190 200
FGFLEAQQAF RSVGTKWDVS GNRATVAPDK KQDVGKFVEL PGAEMGKVTV
210 220 230 240 250
RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN PEKEKEDFEK
260 270 280 290 300
VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
310 320 330 340 350
AEREQRTESK HRKNSVEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC
360 370 380 390 400
MRDPTLYRCK IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH
410 420 430 440 450
DRDEQFYWII EALGIRKPYI WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW
460 470 480 490 500
DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS SRSVVNMEWD KIWAFNKKVI
510 520 530 540 550
DPVAPRYVAL LKKEVVPVNV LDAQEEMKEV ARHPKNPDVG LKPVWYSPKV
560 570 580 590 600
FIEGADAETF SEGEMVTFIN WGNINITKIH KNADGKITSL DAKLNLENKD
610 620 630 640 650
YKKTTKITWL AESTHALSIP AVCVTYEHLI TKPVLGKDED FKQYINKDSK
660 670 680 690 700
HEELMLGDPC LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCREAPCILI
710 720 730 740 750
YIPDGHTKEM PTSGSKEKTK VEISKKETSS APKERPAPAV SSTCATAEDS
760 770 780 790 800
SVLYSRVAVQ GDVVRELKAK KAPKEDIDAA VKQLLTLKAE YKEKTGQEYK
810 820 830 840 850
PGNPSAAAVQ TVSTKSSSNT VESTSLYNKV AAQGEVVRKL KAEKAPKAKV
860 870 880 890 900
TEAVECLLSL KAEYKEKTGK DYVPGQPPAS QNSHSNPVSN AQPAGAEKPE
910 920 930 940 950
AKVLFDRVAC QGEVVRKLKA EKASKDQVDS AVQELLQLKA QYKSLTGIEY
960 970 980 990 1000
KPVSATGAED KDKKKKEKEN KSEKQNKPQK QNDGQGKDSS KSQGSGLSSG
1010 1020 1030 1040 1050
GAGEGQGPKK QTRLGLEAKK EENLAEWYSQ VITKSEMIEY YDVSGCYILR
1060 1070 1080 1090 1100
PWSYSIWESI KDFFDAEIKK LGVENCYFPI FVSQAALEKE KNHIEDFAPE
1110 1120 1130 1140 1150
VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL PVRLNQWCNV
1160 1170 1180 1190 1200
VRWEFKHPQP FLRTREFLWQ EGHSAFATFE EAADEVLQIL ELYARVYEEL
1210 1220 1230 1240 1250
LAIPVVRGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGAT SHHLGQNFSK
1260 1270 1280 1290 1300
MCEIVFEDPK TPGEKQFAYQ CSWGLTTRTI GVMVMVHGDN MGLVLPPRVA
1310 1320 1330 1340 1350
SVQVVVIPCG ITNALSEEDR EALMAKCNEY RRRLLGANIR VRVDLRDNYS
1360 1370 1380 1390 1400
PGWKFNHWEL KGVPVRLEVG PRDMKSCQFV AVRRDTGEKL TIAEKEAEAK
1410 1420 1430 1440 1450
LEKVLEDIQL NLFTRASEDL KTHMVVSNTL EDFQKVLDAG KVAQIPFCGE
1460 1470 1480 1490 1500
IDCEDWIKKM TARDQDVEPG APSMGAKSLC IPFNPLCELQ PGAMCVCGKN
1510
PAKFYTLFGR SY
Length:1,512
Mass (Da):170,079
Last modified:July 27, 2011 - v4
Checksum:iD14F6EA015B1BB6A
GO

Sequence cautioni

The sequence AAH40802 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti94R → G in AAH40802 (PubMed:15489334).Curated1
Sequence conflicti172N → S in AAH40802 (PubMed:15489334).Curated1
Sequence conflicti618S → P in AAH40802 (PubMed:15489334).Curated1
Sequence conflicti986G → R in X54327 (Ref. 4) Curated1
Sequence conflicti1290N → S in AAH94679 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti871D → E.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35818.1.
RefSeqiNP_084011.1. NM_029735.1.
UniGeneiMm.154511.
Mm.490980.

Genome annotation databases

EnsembliENSMUST00000046514; ENSMUSP00000045841; ENSMUSG00000026615.
GeneIDi107508.
KEGGimmu:107508.
UCSCiuc007dze.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35818.1.
RefSeqiNP_084011.1. NM_029735.1.
UniGeneiMm.154511.
Mm.490980.

3D structure databases

ProteinModelPortaliQ8CGC7.
SMRiQ8CGC7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223350. 4 interactors.
IntActiQ8CGC7. 5 interactors.
MINTiMINT-1869828.
STRINGi10090.ENSMUSP00000045841.

PTM databases

iPTMnetiQ8CGC7.
PhosphoSitePlusiQ8CGC7.
SwissPalmiQ8CGC7.

Proteomic databases

EPDiQ8CGC7.
MaxQBiQ8CGC7.
PaxDbiQ8CGC7.
PeptideAtlasiQ8CGC7.
PRIDEiQ8CGC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046514; ENSMUSP00000045841; ENSMUSG00000026615.
GeneIDi107508.
KEGGimmu:107508.
UCSCiuc007dze.1. mouse.

Organism-specific databases

CTDi2058.
MGIiMGI:97838. Eprs.

Phylogenomic databases

eggNOGiKOG1147. Eukaryota.
KOG4163. Eukaryota.
COG0008. LUCA.
COG0442. LUCA.
GeneTreeiENSGT00550000074815.
HOGENOMiHOG000022047.
HOVERGENiHBG017875.
InParanoidiQ8CGC7.
KOiK14163.
OMAiVAMLHIK.
OrthoDBiEOG091G04TK.
TreeFamiTF300380.

Miscellaneous databases

ChiTaRSiEprs. mouse.
PROiQ8CGC7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026615.
CleanExiMM_EPRS.
ExpressionAtlasiQ8CGC7. baseline and differential.
GenevisibleiQ8CGC7. MM.

Family and domain databases

CDDicd00778. ProRS_core_arch_euk. 1 hit.
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. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
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.
IPR033721. ProRS_core_arch_euk.
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_dom.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF00458. WHEP-TRS. 3 hits.
[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. 2 hits.
PS51185. WHEP_TRS_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYEP_MOUSE
AccessioniPrimary (citable) accession number: Q8CGC7
Secondary accession number(s): E9QKC4, Q3UFJ2, Q4VC16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 123 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.