P07814 (SYEP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Glutamate--tRNA ligase
   EC=6.1.1.17
   Alternative name(s):
   Glutamyl-tRNA synthetase
   Short name=GluRS
2. Proline--tRNA ligase
   EC=6.1.1.15
   Alternative name(s):
   Prolyl-tRNA synthetase

Gene names

Name:	EPRS
Synonyms:	GLNS, PARS, QARS, QPRS
ORF Names:	PIG32

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1512 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.9 Ref.24
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
Subunit structure	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. Ref.9 Ref.10 Ref.16
Subcellular location	Cytoplasm Probable.
Domain	The WHEP-TRS domain is involved in RNA binding.
Post-translational modification	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. Ref.16 Ref.22
Sequence similarities	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.
Caution	Was originally thought to be a glutaminyl-tRNA synthetase.
Sequence caution	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 AAS72877.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA30354.1 differs from that shown. Reason: Sequencing errors. The sequence CAA38224.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Protein biosynthesis Translation regulation
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to interferon-gamma Inferred from direct assay Ref.9. Source: UniProtKB glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro negative regulation of translation Inferred from direct assay Ref.24. Source: UniProtKB prolyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro protein complex assembly Traceable author statement PubMed 8188258. Source: ProtInc tRNA aminoacylation for protein translation Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome ribonucleoprotein complex Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA stem-loop binding Inferred from direct assay Ref.9. Source: UniProtKB glutamate-tRNA ligase activity Traceable author statement. Source: Reactome proline-tRNA ligase activity Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IARS	P41252	4	EBI-355315,EBI-355303

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1512

1512

Bifunctional glutamate/proline--tRNA ligase

PRO_0000119743

Regions

Domain

749 – 805

57

WHEP-TRS 1

Domain

822 – 878

57

WHEP-TRS 2

Domain

900 – 956

57

WHEP-TRS 3

Nucleotide binding

432 – 436

5

ATP By similarity

Region

164 – 759

596

Glutamate--tRNA ligase

Region

760 – 956

197

3 X 57 AA approximate repeats

Region

959 – 991

33

Charged

Region

1007 – 1512

506

Proline--tRNA ligase

Motif

204 – 214

11

"HIGH" region

Motif

432 – 436

5

"KMSKS" region

Sites

Binding site

211

1

ATP By similarity

Binding site

398

1

ATP By similarity

Amino acid modifications

Modified residue

300

1

N6-acetyllysine; alternate Ref.18

Modified residue

300

1

N6-malonyllysine; alternate Ref.21

Modified residue

417

1

N6-acetyllysine Ref.18

Modified residue

498

1

N6-acetyllysine Ref.18

Modified residue

535

1

N6-acetyllysine Ref.18

Modified residue

542

1

N6-acetyllysine Ref.18

Modified residue

637

1

N6-acetyllysine Ref.18

Modified residue

788

1

N6-acetyllysine Ref.18

Modified residue

872

1

Phosphotyrosine Ref.15

Modified residue

882

1

Phosphoserine Ref.15 Ref.17

Modified residue

885

1

Phosphoserine Ref.15

Modified residue

886

1

Phosphoserine; by CDK5 Ref.15 Ref.16 Ref.17 Ref.22 Ref.23

Modified residue

891

1

Phosphoserine Ref.17

Modified residue

898

1

Phosphothreonine Ref.12 Ref.15

Modified residue

999

1

Phosphoserine Ref.16

Modified residue

1000

1

Phosphoserine Ref.19

Modified residue

1503

1

N6-acetyllysine Ref.18

Natural variations

Natural variant

296

1

A → P.
Corresponds to variant rs35999099 [ dbSNP | Ensembl ].

VAR_037288

Natural variant

308

1

D → E. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6
Corresponds to variant rs2230301 [ dbSNP | Ensembl ].

VAR_037289

Natural variant

334

1

Q → H. Ref.4 Ref.5 Ref.6
Corresponds to variant rs1063236 [ dbSNP | Ensembl ].

VAR_037290

Natural variant

893

1

P → H.
Corresponds to variant rs5030751 [ dbSNP | Ensembl ].

VAR_037291

Natural variant

913

1

E → G.
Corresponds to variant rs2230302 [ dbSNP | Ensembl ].

VAR_057358

Natural variant

1043

1

I → V. Ref.1
Corresponds to variant rs5030752 [ dbSNP | Ensembl ].

VAR_037292

Natural variant

1107

1

S → F.
Corresponds to variant rs12144752 [ dbSNP | Ensembl ].

VAR_037293

Natural variant

1399

1

T → N.
Corresponds to variant rs34559775 [ dbSNP | Ensembl ].

VAR_037294

Experimental info

Mutagenesis

886

1

S → A: Abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. Abolishes interaction with SYNCRIP. Ref.24

Mutagenesis

886

1

S → D: Not active in translation inhibition (phosphomimetic) and abolishes GAIT complex association with eiF4G. No effect on interaction with SYNCRIP. Ref.24

Mutagenesis

999

1

S → A: Not active in translation inhibition, and abolishes release from multisynthetase complex and association with GAIT complex assembly upon interferon-gamma treatment. Ref.24

Mutagenesis

999

1

S → D: Active in translation inhibition (phosphomimetic). No effect on GAIT complex association with eiF4G. Ref.24

Sequence conflict

532

1

K → R in CAI45949. Ref.1

Sequence conflict

594

1

L → F in CAA38224. Ref.4

Sequence conflict

594

1

L → F in AAS72877. Ref.5

Sequence conflict

943

1

K → E in CAI45949. Ref.1

Sequence conflict

1177 – 1179

3

ATM → VTV in CAI45949. Ref.1

Sequence conflict

1441

1

K → R in CAI45949. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1512

Helix Strand Turn

Details...

Helix

750 – 769

20

Helix

774 – 795

22

Turn

1020 – 1022

3

Helix

1024 – 1034

11

Beta strand

1038 – 1040

3

Beta strand

1047 – 1049

3

Helix

1051 – 1070

20

Beta strand

1080 – 1083

4

Helix

1084 – 1087

4

Helix

1095 – 1100

6

Beta strand

1102 – 1107

6

Beta strand

1110 – 1118

9

Beta strand

1120 – 1122

3

Helix

1123 – 1133

11

Helix

1137 – 1139

3

Beta strand

1142 – 1151

10

Turn

1160 – 1162

3

Beta strand

1165 – 1178

14

Helix

1179 – 1198

20

Beta strand

1206 – 1209

4

Turn

1212 – 1214

3

Beta strand

1219 – 1229

11

Turn

1230 – 1233

4

Beta strand

1234 – 1245

12

Helix

1247 – 1252

6

Beta strand

1255 – 1257

3

Beta strand

1265 – 1267

3

Beta strand

1269 – 1276

8

Helix

1278 – 1287

10

Turn

1297 – 1299

3

Beta strand

1303 – 1308

6

Helix

1317 – 1336

20

Beta strand

1341 – 1343

3

Beta strand

1347 – 1349

3

Helix

1351 – 1360

10

Beta strand

1364 – 1369

6

Helix

1371 – 1376

6

Beta strand

1378 – 1383

6

Turn

1384 – 1386

3

Beta strand

1389 – 1393

5

Helix

1394 – 1396

3

Helix

1397 – 1423

27

Beta strand

1424 – 1426

3

Helix

1430 – 1438

9

Beta strand

1442 – 1447

6

Helix

1451 – 1462

12

Beta strand

1477 – 1484

8

Beta strand

1504 – 1509

6

Sequences

	Sequence		Length	Mass (Da)
	P07814 [UniParc]. Last modified February 9, 2010. Version 5. Checksum: 2CE4311076719403	FASTA	1,512	170,591
	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 AEREQRIDSK HRKNPIEKNL QMWEEMKKGS QFGQSCCLRA 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 DAKLNLENKD 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-872; SER-882; SER-885; SER-886 AND THR-898, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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, MASS SPECTROMETRY.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"The first identification of lysine malonylation substrates and its regulatory enzyme." Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y. Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract] Cited for: MALONYLATION AT LYS-300.
[22]	"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.
[23]	"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, MASS SPECTROMETRY.
[24]	"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.
[25]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00013452.

PIR

SYHUQT. A38663.

RefSeq

NP_004437.2. NM_004446.2.

UniGene

Hs.497788.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FYJ	NMR	-	A	749-805	[»]
4HVC	X-ray	2.00	A/B	1003-1512	[»]

ProteinModelPortal

P07814.

SMR

P07814. Positions 189-689, 749-805, 826-875, 903-952, 1015-1512.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40825N.

IntAct

P07814. 15 interactions.

MINT

MINT-141120.

PTM databases

PhosphoSite

P07814.

Polymorphism databases

DMDM

288558855.

Proteomic databases

PaxDb

P07814.

PRIDE

P07814.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366923; ENSP00000355890; ENSG00000136628.

GeneID

2058.

KEGG

hsa:2058.

UCSC

uc001hly.1. human.

Organism-specific databases

CTD

2058.

GeneCards

GC01M220141.

HGNC

HGNC:3418. EPRS.

HPA

HPA026490.
HPA030052.

MIM

138295. gene.

neXtProt

NX_P07814.

PharmGKB

PA27837.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0442.

HOVERGEN

HBG017875.

InParanoid

P07814.

KO

K14163.

OMA

KAQYKEK.

OrthoDB

EOG4001HD.

Enzyme and pathway databases

Reactome

REACT_71. Gene Expression.

Gene expression databases

Bgee

P07814.

CleanEx

HS_EPRS.
HS_QARS.

Genevestigator

P07814.

GermOnline

ENSG00000136628. Homo sapiens.

Family and domain databases

Gene3D

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.

InterPro

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_Ib_arc/euk.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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.
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]

PANTHER

PTHR10119. PTHR10119. 1 hit.

Pfam

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]

PRINTS

PR00987. TRNASYNTHGLU.

SMART

SM00946. ProRS-C_1. 1 hit.
SM00991. WHEP-TRS. 3 hits.
[Graphical view]

SUPFAM

SSF52954. Anticodon_bd. 1 hit.
SSF47616. GST_C_like. 1 hit.
SSF64586. Pro-tRNA_synth_II_C. 1 hit.
SSF50715. Ribosomal_L25rel. 1 hit.
SSF47060. S15/NS1_bind. 3 hits.

TIGRFAMs

TIGR00463. gltX_arch. 1 hit.
TIGR00408. proS_fam_I. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3873.

DrugBank

DB00142. L-Glutamic Acid.
DB00172. L-Proline.

EvolutionaryTrace

P07814.

GenomeRNAi

2058.

NextBio

8369.

SOURCE

Search...

Entry information

Entry name

SYEP_HUMAN

Accession

Primary (citable) accession number: P07814
Secondary accession number(s): A0AVA9 , B9EGH3, Q05BP6, Q05DF8, Q5DSM1, Q5H9S5, Q6PD57, Q86X73

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	February 9, 2010
Last modified:	May 1, 2013
This is version 162 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.