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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei211 – 2111ATPBy similarity
Binding sitei398 – 3981ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi432 – 4365ATPBy similarity

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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi886 – 8861S → A: Abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. Abolishes interaction with SYNCRIP. 1 Publication
Mutagenesisi886 – 8861S → D: Not active in translation inhibition (phosphomimetic) and abolishes GAIT complex association with eiF4G. No effect on interaction with SYNCRIP. 1 Publication
Mutagenesisi999 – 9991S → A: Not active in translation inhibition, and abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. 1 Publication
Mutagenesisi999 – 9991S → D: Active in translation inhibition (phosphomimetic). No effect on GAIT complex association with eiF4G. 1 Publication

Organism-specific databases

PharmGKBiPA27837.

Chemistry

ChEMBLiCHEMBL3873.
DrugBankiDB00172. L-Proline.

Polymorphism and mutation databases

BioMutaiEPRS.
DMDMi288558855.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15121512Bifunctional glutamate/proline--tRNA ligasePRO_0000119743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei300 – 3001N6-acetyllysine; alternateCombined sources
Modified residuei300 – 3001N6-malonyllysine; alternate1 Publication
Modified residuei355 – 3551PhosphothreonineCombined sources
Modified residuei417 – 4171N6-acetyllysineCombined sources
Modified residuei434 – 4341PhosphoserineCombined sources
Modified residuei498 – 4981N6-acetyllysineCombined sources
Modified residuei535 – 5351N6-acetyllysineCombined sources
Modified residuei542 – 5421N6-acetyllysineCombined sources
Modified residuei637 – 6371N6-acetyllysineCombined sources
Modified residuei747 – 7471PhosphoserineCombined sources
Modified residuei788 – 7881N6-acetyllysineCombined sources
Modified residuei861 – 8611N6-acetyllysineBy similarity
Modified residuei872 – 8721PhosphotyrosineCombined sources
Modified residuei882 – 8821PhosphoserineCombined sources
Modified residuei885 – 8851PhosphoserineCombined sources
Modified residuei886 – 8861Phosphoserine; by CDK5Combined sources2 Publications
Modified residuei891 – 8911PhosphoserineCombined sources
Modified residuei898 – 8981PhosphothreonineCombined sources
Modified residuei998 – 9981PhosphoserineCombined sources
Modified residuei999 – 9991Phosphoserine1 Publication
Modified residuei1000 – 10001PhosphoserineCombined sources
Modified residuei1350 – 13501PhosphoserineCombined sources
Modified residuei1503 – 15031N6-acetyllysineCombined sources

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, Phosphoprotein

Proteomic databases

EPDiP07814.
MaxQBiP07814.
PaxDbiP07814.
PeptideAtlasiP07814.
PRIDEiP07814.

PTM databases

iPTMnetiP07814.
PhosphoSiteiP07814.
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 interactions.
DIPiDIP-40825N.
IntActiP07814. 32 interactions.
MINTiMINT-141120.
STRINGi9606.ENSP00000355890.

Chemistry

BindingDBiP07814.

Structurei

Secondary structure

1
1512
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi10 – 123Combined sources
Helixi15 – 2410Combined sources
Turni25 – 273Combined sources
Beta strandi30 – 334Combined sources
Beta strandi39 – 435Combined sources
Beta strandi46 – 483Combined sources
Helixi51 – 6111Combined sources
Turni63 – 686Combined sources
Helixi72 – 8615Combined sources
Turni87 – 893Combined sources
Helixi95 – 10511Combined sources
Turni106 – 1083Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi114 – 1163Combined sources
Helixi119 – 12911Combined sources
Helixi132 – 1409Combined sources
Helixi145 – 15511Combined sources
Helixi158 – 16710Combined sources
Helixi750 – 76920Combined sources
Helixi774 – 79522Combined sources
Turni1020 – 10223Combined sources
Helixi1024 – 103411Combined sources
Beta strandi1038 – 10403Combined sources
Beta strandi1042 – 10454Combined sources
Beta strandi1047 – 10493Combined sources
Helixi1051 – 107020Combined sources
Beta strandi1080 – 10834Combined sources
Helixi1084 – 10874Combined sources
Turni1088 – 10903Combined sources
Helixi1095 – 11006Combined sources
Beta strandi1102 – 11076Combined sources
Beta strandi1110 – 11189Combined sources
Beta strandi1120 – 11223Combined sources
Helixi1123 – 113311Combined sources
Helixi1137 – 11393Combined sources
Beta strandi1142 – 115110Combined sources
Turni1160 – 11623Combined sources
Beta strandi1165 – 117814Combined sources
Helixi1179 – 119820Combined sources
Beta strandi1206 – 12094Combined sources
Turni1212 – 12143Combined sources
Beta strandi1219 – 122911Combined sources
Turni1230 – 12334Combined sources
Beta strandi1234 – 124512Combined sources
Helixi1247 – 12526Combined sources
Beta strandi1255 – 12573Combined sources
Beta strandi1261 – 12644Combined sources
Beta strandi1265 – 12673Combined sources
Beta strandi1269 – 12768Combined sources
Helixi1278 – 128710Combined sources
Turni1297 – 12993Combined sources
Beta strandi1303 – 13086Combined sources
Beta strandi1313 – 13153Combined sources
Helixi1317 – 133620Combined sources
Beta strandi1341 – 13433Combined sources
Beta strandi1347 – 13493Combined sources
Helixi1351 – 136010Combined sources
Beta strandi1364 – 13696Combined sources
Helixi1371 – 13766Combined sources
Beta strandi1378 – 13836Combined sources
Turni1384 – 13863Combined sources
Beta strandi1389 – 13935Combined sources
Helixi1394 – 13963Combined sources
Helixi1397 – 142327Combined sources
Beta strandi1424 – 14263Combined sources
Helixi1430 – 14389Combined sources
Beta strandi1442 – 14476Combined sources
Helixi1451 – 146212Combined sources
Beta strandi1477 – 14848Combined sources
Beta strandi1498 – 15014Combined sources
Beta strandi1504 – 15096Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5BMUX-ray2.60B/D/F/H1-175[»]
ProteinModelPortaliP07814.
SMRiP07814. Positions 176-696, 749-805, 826-875, 903-952, 1016-1512.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07814.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini749 – 80557WHEP-TRS 1Add
BLAST
Domaini822 – 87857WHEP-TRS 2Add
BLAST
Domaini900 – 95657WHEP-TRS 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 759596Glutamate--tRNA ligaseAdd
BLAST
Regioni760 – 9561973 X 57 AA approximate repeatsAdd
BLAST
Regioni959 – 99133ChargedAdd
BLAST
Regioni1007 – 1512506Proline--tRNA ligaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi204 – 21411"HIGH" regionAdd
BLAST
Motifi432 – 4365"KMSKS" region

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti532 – 5321K → R in CAI45949 (PubMed:17974005).Curated
Sequence conflicti594 – 5941L → F in CAA38224 (PubMed:1988429).Curated
Sequence conflicti594 – 5941L → F in AAS72877 (Ref. 5) Curated
Sequence conflicti943 – 9431K → E in CAI45949 (PubMed:17974005).Curated
Sequence conflicti1177 – 11793ATM → VTV in CAI45949 (PubMed:17974005).Curated
Sequence conflicti1441 – 14411K → R in CAI45949 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti296 – 2961A → P.
Corresponds to variant rs35999099 [ dbSNP | Ensembl ].
VAR_037288
Natural varianti308 – 3081D → E.5 Publications
Corresponds to variant rs2230301 [ dbSNP | Ensembl ].
VAR_037289
Natural varianti334 – 3341Q → H.3 Publications
Corresponds to variant rs1063236 [ dbSNP | Ensembl ].
VAR_037290
Natural varianti893 – 8931P → H.
Corresponds to variant rs5030751 [ dbSNP | Ensembl ].
VAR_037291
Natural varianti913 – 9131E → G.
Corresponds to variant rs2230302 [ dbSNP | Ensembl ].
VAR_057358
Natural varianti1043 – 10431I → V.1 Publication
Corresponds to variant rs5030752 [ dbSNP | Ensembl ].
VAR_037292
Natural varianti1107 – 11071S → F.
Corresponds to variant rs12144752 [ dbSNP | Ensembl ].
VAR_037293
Natural varianti1399 – 13991T → N.
Corresponds to variant rs34559775 [ dbSNP | Ensembl ].
VAR_037294

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
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[»]
5BMUX-ray2.60B/D/F/H1-175[»]
ProteinModelPortaliP07814.
SMRiP07814. Positions 176-696, 749-805, 826-875, 903-952, 1016-1512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP07814.
ChEMBLiCHEMBL3873.
DrugBankiDB00172. L-Proline.

PTM databases

iPTMnetiP07814.
PhosphoSiteiP07814.
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.
GeneCardsiEPRS.
HGNCiHGNC:3418. EPRS.
HPAiHPA026490.
HPA030052.
MIMi138295. gene.
neXtProtiNX_P07814.
PharmGKBiPA27837.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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: September 7, 2016
This is version 198 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.