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UniProtKB/Swiss-Prot entry P07814


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SYEP_HUMAN
Primary accession number P07814
Secondary accession numbers A0AVA9 Q05BP6 Q05DF8 Q5DSM1 Q5H9S5 Q6PD57 Q86X73
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on December 4, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 112)
Name and origin of the protein
Protein name Bifunctional aminoacyl-tRNA synthetase
Synonym Proliferation-inducing gene 32 protein
Includes Glutamyl-tRNA synthetase
     (EC 6.1.1.17)
     (Glutamate--tRNA ligase)
Prolyl-tRNA synthetase
     (EC 6.1.1.15)
     (Proline--tRNA ligase)
Gene name
Name: EPRS
Synonyms: GLNS, PARS, QARS, QPRS
ORFNames: PIG32
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLN-334 AND VAL-1043.
TISSUE=Bone marrow;
The German cDNA consortium;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-308 AND GLN-334.
TISSUE=Brain, Duodenum, Eye, Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 54-1512.
PubMed=1988429 [NCBI, ExPASy, EBI, Israel, Japan]
Fett R., Knippers R.;
"The primary structure of human glutaminyl-tRNA synthetase. A highly conserved core, amino acid repeat regions, and homologies with translation elongation factors.";
J. Biol. Chem. 266:1448-1455(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-1512.
Kim J.W.;
"Identification of a proliferation inducing gene.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[5]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 168-959.
TISSUE=Cervix carcinoma;
DOI=10.1093/nar/16.12.5391; PubMed=3290852 [NCBI, ExPASy, EBI, Israel, Japan]
Thoemmes P., Fett R., Schray B., Kunze N., Knippers R.;
"The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coli and yeast enzymes.";
Nucleic Acids Res. 16:5391-5406(1988).
[6]
FUNCTION.
PubMed=1756734 [NCBI, ExPASy, EBI, Israel, Japan]
Cerini C., Kerjan P., Astier M., Gratecos D., Mirande M., Semeriva M.;
"A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase.";
EMBO J. 10:4267-4277(1991).
[7]
GENE STRUCTURE.
DOI=10.1007/BF00163851; PubMed=1556743 [NCBI, ExPASy, EBI, Israel, Japan]
Kaiser E., Eberhard D., Knippers R.;
"Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase.";
J. Mol. Evol. 34:45-53(1992).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-898 AND SER-1000, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[9]
INTERACTION WITH DUS2L.
DOI=10.1158/0008-5472.CAN-05-0600; PubMed=15994936 [NCBI, ExPASy, EBI, Israel, Japan]
Kato T., Daigo Y., Hayama S., Ishikawa N., Yamabuki T., Ito T., Miyamoto M., Kondo S., Nakamura Y.;
"A novel human tRNA-dihydrouridine synthase involved in pulmonary carcinogenesis.";
Cancer Res. 65:5638-5646(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-898, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-885; SER-886 AND SER-891, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886 AND THR-888, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
STRUCTURE BY NMR OF 749-805, AND RNA-BINDING.
DOI=10.1021/bi001393h; PubMed=11123902 [NCBI, ExPASy, EBI, Israel, Japan]
Jeong E.-J., Hwang G.-S., Kim K.H., Kim M.J., Kim S., Kim K.-S.;
"Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats.";
Biochemistry 39:15775-15782(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CR933648; CAI45949.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015494; AAH15494.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034797; AAH34797.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC046156; AAH46156.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058921; AAH58921.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126275; AAI26276.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54326; CAA38224.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY493416; AAS72877.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07466; CAA30354.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38663; SYHUQT.
RefSeq NP_004437.2; -.
UniGene Hs.497788
3D structure databases
PDB
1FYJ; NMR; -; A=677-733.[ExPASy / RCSB / EBI]
PDBsum 1FYJ; -.
SMR P07814; 677-733.
ModBase P07814.
Protein-protein interaction databases
IntAct P07814; -.
PTM databases
PhosphoSite P07814; -.
Organism-specific databases
HGNC HGNC:3418; EPRS.
GenAtlas EPRS.
MIM 138295; gene. [NCBI / EBI]
PharmGKB PA27837; -.
GeneCards P07814.
Gene expression databases
ArrayExpress P07814; -.
CleanEx HS_EPRS; -.
HS_QARS; -.
GermOnline ENSG00000136628; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006461; Biological process: protein complex assembly (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002314; aa-tRNA-synt_IIb.
IPR001412; aa-tRNA-synth_I_CS.
IPR006195; aa-tRNA-synth_II.
IPR004154; Anticodon_bd.
IPR004526; Glu-tRNA-synth_Ic_arc/euk.
IPR000924; Glu/Gln-tRNA-synth_Ic.
IPR010987; Glutathione-S-Trfase_C-like.
IPR002316; Pro-tRNA-synth_IIa.
IPR004499; Pro-tRNA-synth_IIa_pro-type.
IPR016061; Pro-tRNA_synth_II_C.
IPR009068; S15_NS1_RNA_bd.
IPR000738; WHEP-TRS.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.800; Anticodon_bd; 2.
G3DSA:1.20.1050.10; GST_C_like; 2.
G3DSA:3.30.110.30; Pro-tRNA-synth_II_C_arc/euk; 2.
G3DSA:1.10.287.10; S15_NS1_RNA_bd; 6.
PANTHER PTHR10119; Glu_tRNA-synt_1c; 2.
Pfam PF03129; HGTP_anticodon; 2.
PF09180; ProRS-C_1; 2.
PF00749; tRNA-synt_1c; 2.
PF03950; tRNA-synt_1c_C; 2.
PF00587; tRNA-synt_2b; 2.
PF00458; WHEP-TRS; 6.
Pfam graphical view of domain structure.
PRINTS PR00987; TRNASYNTHGLU.
PR01046; TRNASYNTHPRO.
TIGRFAMs TIGR00463; gltX_arch; 1.
TIGR00408; proS_fam_I; 1.
PROSITE PS00178; AA_TRNA_LIGASE_I; 1.
PS50862; AA_TRNA_LIGASE_II; 1.
PS00762; WHEP_TRS_1; 3.
PS51185; WHEP_TRS_2; 3.
PROSITE graphical view of domain structure (profiles).
BLOCKS P07814.
ProtoNet P07814.
Genome annotation databases
Ensembl ENSG00000136628; Homo sapiens. [Contig view]
GeneID 2058; -.
KEGG hsa:2058; -.
Phylogenomic databases
HOVERGEN P07814; -.
Other
DrugBank DB00142; L-Glutamic Acid.
DB00172; L-Proline.
NextBio 8369; -.
SOURCE EPRS; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; Polymorphism; Protein biosynthesis; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1512  1512     Bifunctional aminoacyl-tRNA synthetase. PRO_0000119743
DOMAIN   749    805  57     WHEP-TRS 1. 
DOMAIN   822    878  57     WHEP-TRS 2. 
DOMAIN   900    956  57     WHEP-TRS 3. 
REGION   164    759  596     Glutamyl-tRNA synthetase. 
REGION   760    956  197     3 X 57 AA approximate repeats. 
REGION   959    991  33     Charged. 
REGION   1007   1512  506     Prolyl-tRNA synthetase. 
MOTIF   204    214  11     "HIGH" region. 
MOTIF   432    436  5     "KMSKS" region. 
BINDING   435    435        ATP (By similarity). 
MOD_RES   885    885        Phosphoserine. 
MOD_RES   886    886        Phosphoserine. 
MOD_RES   888    888        Phosphothreonine. 
MOD_RES   891    891        Phosphoserine. 
MOD_RES   898    898        Phosphothreonine. 
MOD_RES   1000   1000        Phosphoserine. 
VARIANT   296    296  1     A -> P (in dbSNP:rs35999099 [NCBI]). VAR_037288 
VARIANT   308    308  1     E -> D (in dbSNP:rs2230301 [NCBI]). VAR_037289 
VARIANT   334    334  1     H -> Q (in dbSNP:rs1063236 [NCBI]). VAR_037290 
VARIANT   893    893  1     P -> H (in dbSNP:rs5030751 [NCBI]). VAR_037291 
VARIANT   1043   1043  1     I -> V (in dbSNP:rs5030752 [NCBI]). VAR_037292 
VARIANT   1107   1107  1     S -> F (in dbSNP:rs12144752 [NCBI]). VAR_037293 
VARIANT   1399   1399  1     T -> N (in dbSNP:rs34559775 [NCBI]). VAR_037294 
CONFLICT   532    532        K -> R (in Ref. 1; CAI45949). 
CONFLICT   594    594        F -> L (in Ref. 1; CAI45949 and 2; AAH58921/AAH34797/AAI26276). 
CONFLICT   943    943        K -> E (in Ref. 1; CAI45949). 
CONFLICT   1177   1179        ATM -> VTV (in Ref. 1; CAI45949). 
CONFLICT   1441   1441        K -> R (in Ref. 1; CAI45949). 
HELIX   750    769  20      
HELIX   774    795  22      
Sequence information
Length: 1512 AA [This is the length of the unprocessed precursor] Molecular weight: 170648 Da [This is the MW of the unprocessed precursor] CRC64: 89402F1C51BECD31 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATLSLTVNS GDPPLGALLA VEHVKDDVSI SVEEGKENIL HVSENVIFTD VNSILRYLAR 

        70         80         90        100        110        120 
VATTAGLYGS NLMEHTEIDH WLEFSATKLS SCDSFTSTIN ELNHCLSLRT YLVGNSLSLA 

       130        140        150        160        170        180 
DLCVWATLKG NAAWQEQLKQ KKAPVHVKRW FGFLEAQQAF QSVGTKWDVS TTKARVAPEK 

       190        200        210        220        230        240 
KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN 

       250        260        270        280        290        300 
PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK 

       310        320        330        340        350        360 
AEREQRIESK HRKNPIEKNL QMWEEMKKGS QFGHSCCLRA KIDMSSNNGC MRDPTLYRCK 

       370        380        390        400        410        420 
IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI 

       430        440        450        460        470        480 
WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS 

       490        500        510        520        530        540 
SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVIPVNV PEAQEEMKEV AKHPKNPEVG 

       550        560        570        580        590        600 
LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNLNITKIH KNADGKIISL DAKFNLENKD 

       610        620        630        640        650        660 
YKKTTKVTWL AETTHALPIP VICVTYEHLI TKPVLGKDED FKQYVNKNSK HEELMLGDPC 

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

       730        740        750        760        770        780 
VEATKNETSA PFKERPTPSL NNNCTTSEDS LVLYNRVAVQ GDVVRELKAK KAPKEDVDAA 

       790        800        810        820        830        840 
VKQLLSLKAE YKEKTGQEYK PGNPPAEIGQ NISSNSSASI LESKSLYDEV AAQGEVVRKL 

       850        860        870        880        890        900 
KAEKSPKAKI NEAVECLLSL KAQYKEKTGK EYIPGQPPLS QSSDSSPTRN SEPAGLETPE 

       910        920        930        940        950        960 
AKVLFDKVAS QGEVVRKLKT EKAPKDQVDI AVQELLQLKA QYKSLIGVEY KPVSATGAED 

       970        980        990       1000       1010       1020 
KDKKKKEKEN KSEKQNKPQK QNDGQRKDPS KNQGGGLSSS GAGEGQGPKK QTRLGLEAKK 

      1030       1040       1050       1060       1070       1080 
EENLADWYSQ VITKSEMIEY HDISGCYILR PWAYAIWEAI KDFFDAEIKK LGVENCYFPM 

      1090       1100       1110       1120       1130       1140 
FVSQSALEKE KTHVADFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL 

      1150       1160       1170       1180       1190       1200 
PIKLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATME EAAEEVLQIL DLYAQVYEEL 

      1210       1220       1230       1240       1250       1260 
LAIPVVKGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGGT SHHLGQNFSK MFEIVFEDPK 

      1270       1280       1290       1300       1310       1320 
IPGEKQFAYQ NSWGLTTRTI GVMTMVHGDN MGLVLPPRVA CVQVVIIPCG ITNALSEEDK 

      1330       1340       1350       1360       1370       1380 
EALIAKCNDY RRRLLSVNIR VRADLRDNYS PGWKFNHWEL KGVPIRLEVG PRDMKSCQFV 

      1390       1400       1410       1420       1430       1440 
AVRRDTGEKL TVAENEAETK LQAILEDIQV TLFTRASEDL KTHMVVANTM EDFQKILDSG 

      1450       1460       1470       1480       1490       1500 
KIVQIPFCGE IDCEDWIKKT TARDQDLEPG APSMGAKSLC IPFKPLCELQ PGAKCVCGKN 

      1510 
PAKYYTLFGR SY 

P07814 in FASTA format

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