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Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

EPRS

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei211ATPBy similarity1
Binding sitei398ATPBy similarity1

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutamate-tRNA ligase activity Source: Reactome
  • GTPase binding Source: UniProtKB
  • proline-tRNA ligase activity Source: GO_Central
  • RNA stem-loop binding Source: UniProtKB

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
  • protein complex assembly Source: ProtInc
  • tRNA aminoacylation for protein translation Source: Reactome
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

Enzyme and pathway databases

BioCyciZFISH:HS06187-MONOMER.
BRENDAi6.1.1.15. 2681.
ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
R-HSA-379716. Cytosolic tRNA aminoacylation.
R-HSA-6782315. tRNA modification in the nucleus and cytosol.
SIGNORiP07814.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional glutamate/proline--tRNA ligase
Alternative name(s):
Bifunctional aminoacyl-tRNA synthetase
Cell proliferation-inducing gene 32 protein
Glutamatyl-prolyl-tRNA synthetase
Including the following 2 domains:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Proline--tRNA ligase (EC:6.1.1.15)
Alternative name(s):
Prolyl-tRNA synthetase
Gene namesi
Name:EPRS
Synonyms:GLNS, PARS, QARS, QPRS
ORF Names:PIG32
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3418. EPRS.

Subcellular locationi

GO - Cellular componenti

  • aminoacyl-tRNA synthetase multienzyme complex Source: Ensembl
  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • GAIT complex Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi886S → A: Abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. Abolishes interaction with SYNCRIP. 1 Publication1
Mutagenesisi886S → D: Not active in translation inhibition (phosphomimetic) and abolishes GAIT complex association with eiF4G. No effect on interaction with SYNCRIP. 1 Publication1
Mutagenesisi999S → A: Not active in translation inhibition, and abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. 1 Publication1
Mutagenesisi999S → D: Active in translation inhibition (phosphomimetic). No effect on GAIT complex association with eiF4G. 1 Publication1

Organism-specific databases

DisGeNETi2058.
OpenTargetsiENSG00000136628.
PharmGKBiPA27837.

Chemistry databases

ChEMBLiCHEMBL3873.
DrugBankiDB00172. L-Proline.

Polymorphism and mutation databases

BioMutaiEPRS.
DMDMi288558855.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001197431 – 1512Bifunctional glutamate/proline--tRNA ligaseAdd BLAST1512

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei300N6-acetyllysine; alternateCombined sources1
Modified residuei300N6-malonyllysine; alternate1 Publication1
Modified residuei355PhosphothreonineCombined sources1
Modified residuei417N6-acetyllysineCombined sources1
Modified residuei434PhosphoserineCombined sources1
Modified residuei498N6-acetyllysineCombined sources1
Modified residuei535N6-acetyllysineCombined sources1
Modified residuei542N6-acetyllysineCombined sources1
Modified residuei637N6-acetyllysineCombined sources1
Modified residuei747PhosphoserineCombined sources1
Modified residuei788N6-acetyllysineCombined sources1
Modified residuei861N6-acetyllysineBy similarity1
Modified residuei872PhosphotyrosineCombined sources1
Modified residuei882PhosphoserineCombined sources1
Modified residuei885PhosphoserineCombined sources1
Modified residuei886Phosphoserine; by CDK5Combined sources2 Publications1
Modified residuei891PhosphoserineCombined sources1
Modified residuei898PhosphothreonineCombined sources1
Modified residuei998PhosphoserineCombined sources1
Modified residuei999Phosphoserine1 Publication1
Modified residuei1000PhosphoserineCombined sources1
Modified residuei1152Omega-N-methylarginineCombined sources1
Modified residuei1350PhosphoserineCombined sources1
Modified residuei1503N6-acetyllysineCombined sources1

Post-translational modificationi

Phosphorylated at Ser-886 by CDK5 and at Ser-999 by an unknown kinase in a IFN-gamma-dependent manner in monocytes; these sequential phosphorylations are causing release from the multisynthetase complex, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition. Phosphorylation at Ser-999 is specifically required for the interaction of GAIT complex-associated RPL13A with eIF4G.2 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP07814.
MaxQBiP07814.
PaxDbiP07814.
PeptideAtlasiP07814.
PRIDEiP07814.

PTM databases

iPTMnetiP07814.
PhosphoSitePlusiP07814.
SwissPalmiP07814.

Expressioni

Gene expression databases

BgeeiENSG00000136628.
CleanExiHS_EPRS.
HS_QARS.
ExpressionAtlasiP07814. baseline and differential.
GenevisibleiP07814. HS.

Organism-specific databases

HPAiHPA026490.
HPA030052.

Interactioni

Subunit structurei

Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43. Interacts with DUS2L. Component of the GAIT complex; in humans the complex assembly seems to be a two-step process in which EPRS first associates with SYNCRIP to form a pre-GAIT complex which is deficient in GAIT element binding.3 Publications

Binary interactionsi

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

GO - Molecular functioni

  • GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108372. 110 interactors.
DIPiDIP-40825N.
IntActiP07814. 32 interactors.
MINTiMINT-141120.
STRINGi9606.ENSP00000355890.

Chemistry databases

BindingDBiP07814.

Structurei

Secondary structure

11512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 12Combined sources3
Helixi15 – 24Combined sources10
Turni25 – 27Combined sources3
Beta strandi30 – 33Combined sources4
Beta strandi39 – 43Combined sources5
Beta strandi46 – 48Combined sources3
Helixi51 – 61Combined sources11
Helixi63 – 65Combined sources3
Helixi72 – 87Combined sources16
Turni88 – 90Combined sources3
Helixi95 – 106Combined sources12
Beta strandi110 – 113Combined sources4
Beta strandi114 – 116Combined sources3
Helixi119 – 129Combined sources11
Helixi132 – 139Combined sources8
Helixi145 – 155Combined sources11
Helixi158 – 167Combined sources10
Helixi750 – 769Combined sources20
Helixi774 – 795Combined sources22
Turni1020 – 1022Combined sources3
Helixi1024 – 1034Combined sources11
Beta strandi1038 – 1040Combined sources3
Beta strandi1042 – 1045Combined sources4
Beta strandi1047 – 1049Combined sources3
Helixi1051 – 1070Combined sources20
Beta strandi1080 – 1083Combined sources4
Helixi1084 – 1087Combined sources4
Turni1088 – 1090Combined sources3
Helixi1095 – 1100Combined sources6
Beta strandi1102 – 1107Combined sources6
Beta strandi1110 – 1118Combined sources9
Beta strandi1120 – 1122Combined sources3
Helixi1123 – 1133Combined sources11
Helixi1137 – 1139Combined sources3
Beta strandi1142 – 1151Combined sources10
Turni1160 – 1162Combined sources3
Beta strandi1165 – 1178Combined sources14
Helixi1179 – 1198Combined sources20
Beta strandi1206 – 1209Combined sources4
Turni1212 – 1214Combined sources3
Beta strandi1219 – 1229Combined sources11
Turni1230 – 1233Combined sources4
Beta strandi1234 – 1245Combined sources12
Helixi1247 – 1252Combined sources6
Beta strandi1255 – 1257Combined sources3
Beta strandi1261 – 1264Combined sources4
Beta strandi1265 – 1267Combined sources3
Beta strandi1269 – 1276Combined sources8
Helixi1278 – 1287Combined sources10
Turni1297 – 1299Combined sources3
Beta strandi1303 – 1308Combined sources6
Beta strandi1313 – 1315Combined sources3
Helixi1317 – 1336Combined sources20
Beta strandi1341 – 1343Combined sources3
Beta strandi1347 – 1349Combined sources3
Helixi1351 – 1360Combined sources10
Beta strandi1364 – 1369Combined sources6
Helixi1371 – 1376Combined sources6
Beta strandi1378 – 1383Combined sources6
Turni1384 – 1386Combined sources3
Beta strandi1389 – 1393Combined sources5
Helixi1394 – 1396Combined sources3
Helixi1397 – 1423Combined sources27
Beta strandi1424 – 1426Combined sources3
Helixi1430 – 1438Combined sources9
Beta strandi1442 – 1447Combined sources6
Helixi1451 – 1462Combined sources12
Beta strandi1477 – 1484Combined sources8
Beta strandi1498 – 1501Combined sources4
Beta strandi1504 – 1509Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FYJNMR-A749-805[»]
4HVCX-ray2.00A/B1003-1512[»]
4K86X-ray2.40A1000-1512[»]
4K87X-ray2.30A1000-1512[»]
4K88X-ray2.62A1000-1512[»]
5A1NX-ray2.10A1-175[»]
5A34X-ray2.60A/C/E/G1-175[»]
5A5HX-ray2.32A/C/E/G1-175[»]
5BMUX-ray2.60B/D/F/H1-175[»]
ProteinModelPortaliP07814.
SMRiP07814.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07814.

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
Regioni959 – 991ChargedAdd BLAST33
Regioni1007 – 1512Proline--tRNA ligaseAdd BLAST506

Motif

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

Domaini

The WHEP-TRS domain is involved in RNA binding.

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1147. Eukaryota.
KOG4163. Eukaryota.
COG0008. LUCA.
COG0442. LUCA.
GeneTreeiENSGT00550000074815.
HOVERGENiHBG017875.
InParanoidiP07814.
KOiK14163.
OMAiVAMLHIK.
OrthoDBiEOG091G04TK.
PhylomeDBiP07814.
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. 3 hits.
PS51185. WHEP_TRS_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07814-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD
60 70 80 90 100
VNSILRYLAR VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSTIN
110 120 130 140 150
ELNHCLSLRT YLVGNSLSLA DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW
160 170 180 190 200
FGFLEAQQAF QSVGTKWDVS TTKARVAPEK 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
AEREQRIDSK HRKNPIEKNL 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 LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG LKPVWYSPKV
560 570 580 590 600
FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKLNLENKD
610 620 630 640 650
YKKTTKVTWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK
660 670 680 690 700
HEELMLGDPC LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCVLI
710 720 730 740 750
YIPDGHTKEM PTSGSKEKTK VEATKNETSA PFKERPTPSL NNNCTTSEDS
760 770 780 790 800
LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA VKQLLSLKAE YKEKTGQEYK
810 820 830 840 850
PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL KAEKSPKAKI
860 870 880 890 900
NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE
910 920 930 940 950
AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY
960 970 980 990 1000
KPVSATGAED KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS
1010 1020 1030 1040 1050
GAGEGQGPKK QTRLGLEAKK EENLADWYSQ VITKSEMIEY HDISGCYILR
1060 1070 1080 1090 1100
PWAYAIWEAI KDFFDAEIKK LGVENCYFPM FVSQSALEKE KTHVADFAPE
1110 1120 1130 1140 1150
VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL PIKLNQWCNV
1160 1170 1180 1190 1200
VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL
1210 1220 1230 1240 1250
LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK
1260 1270 1280 1290 1300
MFEIVFEDPK IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA
1310 1320 1330 1340 1350
CVQVVIIPCG ITNALSEEDK EALIAKCNDY RRRLLSVNIR VRADLRDNYS
1360 1370 1380 1390 1400
PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV AVRRDTGEKL TVAENEAETK
1410 1420 1430 1440 1450
LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG KIVQIPFCGE
1460 1470 1480 1490 1500
IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN
1510
PAKYYTLFGR SY
Length:1,512
Mass (Da):170,591
Last modified:February 9, 2010 - v5
Checksum:i2CE4311076719403
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti532K → R in CAI45949 (PubMed:17974005).Curated1
Sequence conflicti594L → F in CAA38224 (PubMed:1988429).Curated1
Sequence conflicti594L → F in AAS72877 (Ref. 5) Curated1
Sequence conflicti943K → E in CAI45949 (PubMed:17974005).Curated1
Sequence conflicti1177 – 1179ATM → VTV in CAI45949 (PubMed:17974005).Curated3
Sequence conflicti1441K → R in CAI45949 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037288296A → P.Corresponds to variant rs35999099dbSNPEnsembl.1
Natural variantiVAR_037289308D → E.5 PublicationsCorresponds to variant rs2230301dbSNPEnsembl.1
Natural variantiVAR_037290334Q → H.3 PublicationsCorresponds to variant rs1063236dbSNPEnsembl.1
Natural variantiVAR_037291893P → H.Corresponds to variant rs5030751dbSNPEnsembl.1
Natural variantiVAR_057358913E → G.Corresponds to variant rs2230302dbSNPEnsembl.1
Natural variantiVAR_0372921043I → V.1 PublicationCorresponds to variant rs5030752dbSNPEnsembl.1
Natural variantiVAR_0372931107S → F.Corresponds to variant rs12144752dbSNPEnsembl.1
Natural variantiVAR_0372941399T → N.Corresponds to variant rs34559775dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR933648 mRNA. Translation: CAI45949.1.
AC103590 Genomic DNA. No translation available.
BC015494 mRNA. Translation: AAH15494.1. Sequence problems.
BC034797 mRNA. Translation: AAH34797.1. Sequence problems.
BC046156 mRNA. Translation: AAH46156.1. Sequence problems.
BC058921 mRNA. Translation: AAH58921.1. Sequence problems.
BC126275 mRNA. Translation: AAI26276.1.
BC136465 mRNA. Translation: AAI36466.1.
X54326 mRNA. Translation: CAA38224.1. Different initiation.
AY493416 mRNA. Translation: AAS72877.1. Different initiation.
X07466 mRNA. Translation: CAA30354.1. Sequence problems.
CCDSiCCDS31027.1.
PIRiA38663. SYHUQT.
RefSeqiNP_004437.2. NM_004446.2.
UniGeneiHs.497788.

Genome annotation databases

EnsembliENST00000366923; ENSP00000355890; ENSG00000136628.
GeneIDi2058.
KEGGihsa:2058.
UCSCiuc001hly.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR933648 mRNA. Translation: CAI45949.1.
AC103590 Genomic DNA. No translation available.
BC015494 mRNA. Translation: AAH15494.1. Sequence problems.
BC034797 mRNA. Translation: AAH34797.1. Sequence problems.
BC046156 mRNA. Translation: AAH46156.1. Sequence problems.
BC058921 mRNA. Translation: AAH58921.1. Sequence problems.
BC126275 mRNA. Translation: AAI26276.1.
BC136465 mRNA. Translation: AAI36466.1.
X54326 mRNA. Translation: CAA38224.1. Different initiation.
AY493416 mRNA. Translation: AAS72877.1. Different initiation.
X07466 mRNA. Translation: CAA30354.1. Sequence problems.
CCDSiCCDS31027.1.
PIRiA38663. SYHUQT.
RefSeqiNP_004437.2. NM_004446.2.
UniGeneiHs.497788.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FYJNMR-A749-805[»]
4HVCX-ray2.00A/B1003-1512[»]
4K86X-ray2.40A1000-1512[»]
4K87X-ray2.30A1000-1512[»]
4K88X-ray2.62A1000-1512[»]
5A1NX-ray2.10A1-175[»]
5A34X-ray2.60A/C/E/G1-175[»]
5A5HX-ray2.32A/C/E/G1-175[»]
5BMUX-ray2.60B/D/F/H1-175[»]
ProteinModelPortaliP07814.
SMRiP07814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108372. 110 interactors.
DIPiDIP-40825N.
IntActiP07814. 32 interactors.
MINTiMINT-141120.
STRINGi9606.ENSP00000355890.

Chemistry databases

BindingDBiP07814.
ChEMBLiCHEMBL3873.
DrugBankiDB00172. L-Proline.

PTM databases

iPTMnetiP07814.
PhosphoSitePlusiP07814.
SwissPalmiP07814.

Polymorphism and mutation databases

BioMutaiEPRS.
DMDMi288558855.

Proteomic databases

EPDiP07814.
MaxQBiP07814.
PaxDbiP07814.
PeptideAtlasiP07814.
PRIDEiP07814.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366923; ENSP00000355890; ENSG00000136628.
GeneIDi2058.
KEGGihsa:2058.
UCSCiuc001hly.2. human.

Organism-specific databases

CTDi2058.
DisGeNETi2058.
GeneCardsiEPRS.
HGNCiHGNC:3418. EPRS.
HPAiHPA026490.
HPA030052.
MIMi138295. gene.
neXtProtiNX_P07814.
OpenTargetsiENSG00000136628.
PharmGKBiPA27837.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1147. Eukaryota.
KOG4163. Eukaryota.
COG0008. LUCA.
COG0442. LUCA.
GeneTreeiENSGT00550000074815.
HOVERGENiHBG017875.
InParanoidiP07814.
KOiK14163.
OMAiVAMLHIK.
OrthoDBiEOG091G04TK.
PhylomeDBiP07814.
TreeFamiTF300380.

Enzyme and pathway databases

BioCyciZFISH:HS06187-MONOMER.
BRENDAi6.1.1.15. 2681.
ReactomeiR-HSA-2408517. SeMet incorporation into proteins.
R-HSA-379716. Cytosolic tRNA aminoacylation.
R-HSA-6782315. tRNA modification in the nucleus and cytosol.
SIGNORiP07814.

Miscellaneous databases

EvolutionaryTraceiP07814.
GeneWikiiEPRS.
GenomeRNAii2058.
PROiP07814.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136628.
CleanExiHS_EPRS.
HS_QARS.
ExpressionAtlasiP07814. baseline and differential.
GenevisibleiP07814. HS.

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. 3 hits.
PS51185. WHEP_TRS_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYEP_HUMAN
AccessioniPrimary (citable) accession number: P07814
Secondary accession number(s): A0AVA9
, B9EGH3, Q05BP6, Q05DF8, Q5DSM1, Q5H9S5, Q6PD57, Q86X73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 9, 2010
Last modified: November 2, 2016
This is version 200 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

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

Keywords - Technical termi

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

Documents

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

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.