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P07814

- SYEP_HUMAN

UniProt

P07814 - SYEP_HUMAN

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Protein

Bifunctional glutamate/proline--tRNA ligase

Gene
EPRS, GLNS, PARS, QARS, QPRS, PIG32
Organism
Homo sapiens (Human)
Status
Reviewed - 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).UniRule annotation
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei211 – 2111ATP By similarity
Binding sitei398 – 3981ATP By similarity

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-tRNA ligase activity Source: Reactome
  3. proline-tRNA ligase activity Source: Reactome
  4. protein binding Source: IntAct
  5. RNA stem-loop binding Source: UniProtKB

GO - Biological processi

  1. cellular response to interferon-gamma Source: UniProtKB
  2. gene expression Source: Reactome
  3. glutamyl-tRNA aminoacylation Source: InterPro
  4. negative regulation of translation Source: UniProtKB
  5. prolyl-tRNA aminoacylation Source: InterPro
  6. protein complex assembly Source: ProtInc
  7. 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

ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3418. EPRS.

Subcellular locationi

Cytoplasm Inferred UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. GAIT complex Source: UniProtKB
  4. ribonucleoprotein complex 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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15121512Bifunctional glutamate/proline--tRNA ligaseUniRule annotationPRO_0000119743Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei300 – 3001N6-acetyllysine; alternate1 Publication
Modified residuei300 – 3001N6-malonyllysine; alternate1 Publication
Modified residuei417 – 4171N6-acetyllysine1 Publication
Modified residuei498 – 4981N6-acetyllysine1 Publication
Modified residuei535 – 5351N6-acetyllysine1 Publication
Modified residuei542 – 5421N6-acetyllysine1 Publication
Modified residuei637 – 6371N6-acetyllysine1 Publication
Modified residuei788 – 7881N6-acetyllysine1 Publication
Modified residuei861 – 8611N6-acetyllysine By similarity
Modified residuei872 – 8721Phosphotyrosine1 Publication
Modified residuei882 – 8821Phosphoserine2 Publications
Modified residuei885 – 8851Phosphoserine1 Publication
Modified residuei886 – 8861Phosphoserine; by CDK55 Publications
Modified residuei891 – 8911Phosphoserine1 Publication
Modified residuei898 – 8981Phosphothreonine2 Publications
Modified residuei999 – 9991Phosphoserine1 Publication
Modified residuei1000 – 10001Phosphoserine1 Publication
Modified residuei1503 – 15031N6-acetyllysine1 Publication

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

MaxQBiP07814.
PaxDbiP07814.
PRIDEiP07814.

PTM databases

PhosphoSiteiP07814.

Expressioni

Gene expression databases

BgeeiP07814.
CleanExiHS_EPRS.
HS_QARS.
GenevestigatoriP07814.

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

Protein-protein interaction databases

BioGridi108372. 73 interactions.
DIPiDIP-40825N.
IntActiP07814. 20 interactions.
MINTiMINT-141120.

Structurei

Secondary structure

1
1512
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi750 – 76920
Helixi774 – 79522
Turni1020 – 10223
Helixi1024 – 103411
Beta strandi1038 – 10403
Beta strandi1042 – 10454
Beta strandi1047 – 10493
Helixi1051 – 107020
Beta strandi1080 – 10834
Helixi1084 – 10874
Turni1088 – 10903
Helixi1095 – 11006
Beta strandi1102 – 11076
Beta strandi1110 – 11189
Beta strandi1120 – 11223
Helixi1123 – 113311
Helixi1137 – 11393
Beta strandi1142 – 115110
Turni1160 – 11623
Beta strandi1165 – 117814
Helixi1179 – 119820
Beta strandi1206 – 12094
Turni1212 – 12143
Beta strandi1219 – 122911
Turni1230 – 12334
Beta strandi1234 – 124512
Helixi1247 – 12526
Beta strandi1255 – 12573
Beta strandi1261 – 12644
Beta strandi1265 – 12673
Beta strandi1269 – 12768
Helixi1278 – 128710
Turni1297 – 12993
Beta strandi1303 – 13086
Beta strandi1313 – 13153
Helixi1317 – 133620
Beta strandi1341 – 13433
Beta strandi1347 – 13493
Helixi1351 – 136010
Beta strandi1364 – 13696
Helixi1371 – 13766
Beta strandi1378 – 13836
Turni1384 – 13863
Beta strandi1389 – 13935
Helixi1394 – 13963
Helixi1397 – 142327
Beta strandi1424 – 14263
Helixi1430 – 14389
Beta strandi1442 – 14476
Helixi1451 – 146212
Beta strandi1477 – 14848
Beta strandi1498 – 15014
Beta strandi1504 – 15096

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP07814.
SMRiP07814. Positions 189-696, 749-805, 826-875, 903-952, 1016-1512.

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 ligaseUniRule annotationAdd
BLAST
Regioni760 – 9561973 X 57 AA approximate repeatsUniRule annotationAdd
BLAST
Regioni959 – 99133ChargedUniRule annotationAdd
BLAST
Regioni1007 – 1512506Proline--tRNA ligaseUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi204 – 21411"HIGH" regionUniRule annotationAdd
BLAST
Motifi432 – 4365"KMSKS" regionUniRule annotation

Domaini

The WHEP-TRS domain is involved in RNA binding.UniRule annotation

Sequence similaritiesi

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.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0442.
HOVERGENiHBG017875.
InParanoidiP07814.
KOiK14163.
OMAiVAMLHIK.
OrthoDBiEOG754HNH.
PhylomeDBiP07814.
TreeFamiTF300380.

Family and domain databases

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.
InterProiIPR002314. 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]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF14497. 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]
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

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MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD     50
VNSILRYLAR VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSTIN 100
ELNHCLSLRT YLVGNSLSLA DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW 150
FGFLEAQQAF QSVGTKWDVS TTKARVAPEK KQDVGKFVEL PGAEMGKVTV 200
RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN PEKEKEDFEK 250
VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK 300
AEREQRIDSK HRKNPIEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC 350
MRDPTLYRCK IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH 400
DRDEQFYWII EALGIRKPYI WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW 450
DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS SRSVVNMEWD KIWAFNKKVI 500
DPVAPRYVAL LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG LKPVWYSPKV 550
FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKLNLENKD 600
YKKTTKVTWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK 650
HEELMLGDPC LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCKEAPCVLI 700
YIPDGHTKEM PTSGSKEKTK VEATKNETSA PFKERPTPSL NNNCTTSEDS 750
LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA VKQLLSLKAE YKEKTGQEYK 800
PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL KAEKSPKAKI 850
NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE 900
AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY 950
KPVSATGAED KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS 1000
GAGEGQGPKK QTRLGLEAKK EENLADWYSQ VITKSEMIEY HDISGCYILR 1050
PWAYAIWEAI KDFFDAEIKK LGVENCYFPM FVSQSALEKE KTHVADFAPE 1100
VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL PIKLNQWCNV 1150
VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL 1200
LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK 1250
MFEIVFEDPK IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA 1300
CVQVVIIPCG ITNALSEEDK EALIAKCNDY RRRLLSVNIR VRADLRDNYS 1350
PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV AVRRDTGEKL TVAENEAETK 1400
LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG KIVQIPFCGE 1450
IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN 1500
PAKYYTLFGR SY 1512
Length:1,512
Mass (Da):170,591
Last modified:February 9, 2010 - v5
Checksum:i2CE4311076719403
GO

Sequence cautioni

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 CAA30354.1 differs from that shown. Reason: Sequencing errors.
The sequence AAS72877.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAA38224.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti532 – 5321K → R in CAI45949. 1 Publication
Sequence conflicti594 – 5941L → F in CAA38224. 1 Publication
Sequence conflicti594 – 5941L → F in AAS72877. 1 Publication
Sequence conflicti943 – 9431K → E in CAI45949. 1 Publication
Sequence conflicti1177 – 11793ATM → VTV in CAI45949. 1 Publication
Sequence conflicti1441 – 14411K → R in CAI45949. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.1. human.

Polymorphism databases

DMDMi288558855.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS31027.1.
PIRi A38663. SYHUQT.
RefSeqi NP_004437.2. NM_004446.2.
UniGenei Hs.497788.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FYJ NMR - A 749-805 [» ]
4HVC X-ray 2.00 A/B 1003-1512 [» ]
4K86 X-ray 2.40 A 1000-1512 [» ]
4K87 X-ray 2.30 A 1000-1512 [» ]
4K88 X-ray 2.62 A 1000-1512 [» ]
ProteinModelPortali P07814.
SMRi P07814. Positions 189-696, 749-805, 826-875, 903-952, 1016-1512.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108372. 73 interactions.
DIPi DIP-40825N.
IntActi P07814. 20 interactions.
MINTi MINT-141120.

Chemistry

ChEMBLi CHEMBL3873.
DrugBanki DB00142. L-Glutamic Acid.
DB00172. L-Proline.

PTM databases

PhosphoSitei P07814.

Polymorphism databases

DMDMi 288558855.

Proteomic databases

MaxQBi P07814.
PaxDbi P07814.
PRIDEi P07814.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366923 ; ENSP00000355890 ; ENSG00000136628 .
GeneIDi 2058.
KEGGi hsa:2058.
UCSCi uc001hly.1. human.

Organism-specific databases

CTDi 2058.
GeneCardsi GC01M220141.
HGNCi HGNC:3418. EPRS.
HPAi HPA026490.
HPA030052.
MIMi 138295. gene.
neXtProti NX_P07814.
PharmGKBi PA27837.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0442.
HOVERGENi HBG017875.
InParanoidi P07814.
KOi K14163.
OMAi VAMLHIK.
OrthoDBi EOG754HNH.
PhylomeDBi P07814.
TreeFami TF300380.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

EvolutionaryTracei P07814.
GeneWikii EPRS.
GenomeRNAii 2058.
NextBioi 8369.
PROi P07814.
SOURCEi Search...

Gene expression databases

Bgeei P07814.
CleanExi HS_EPRS.
HS_QARS.
Genevestigatori P07814.

Family and domain databases

Gene3Di 1.10.1160.10. 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.
HAMAPi MF_01571. Pro_tRNA_synth_type3.
InterProi IPR002314. 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 ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF14497. 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 ]
PRINTSi PR00987. TRNASYNTHGLU.
SMARTi SM00946. ProRS-C_1. 1 hit.
SM00991. WHEP-TRS. 3 hits.
[Graphical view ]
SUPFAMi SSF47060. SSF47060. 3 hits.
SSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
SSF52954. SSF52954. 1 hit.
SSF64586. SSF64586. 1 hit.
TIGRFAMsi TIGR00463. gltX_arch. 1 hit.
TIGR00408. proS_fam_I. 1 hit.
PROSITEi PS00178. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. 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.

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 3, 2014
This is version 175 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.

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

External Data

Dasty 3

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