Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Bifunctional glutamate/proline--tRNA ligase  

UniProtKB / Swiss-Prot ID :  SYEP_HUMAN

Gene Name (Synonyms) : 
EPRS, GLNS, PARS, QARS, QPRS PIG32  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein 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 (By similarity). 

Protein Sequence MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLARVATTAGLYGS...
Predicted Secondary Structure CCHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHCCHHHHHHHHHHHHHCCHHHHHHHHHCC...
Protein Variant
LocationDescription
296A -> P (in dbSNP:rs35999099). VAR_037288
308D -> E (in dbSNP:rs2230301). VAR_037289
334Q -> H (in dbSNP:rs1063236). VAR_037290
893P -> H (in dbSNP:rs5030751). VAR_037291
913E -> G (in dbSNP:rs2230302). VAR_057358
1043I -> V (in dbSNP:rs5030752). VAR_037292
1107S -> F (in dbSNP:rs12144752). VAR_037293
1399T -> N (in dbSNP:rs34559775). VAR_037294
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
92S-nitrosocysteineKLSSCDSFT
HHHHHHCCC
4.58dbSNO
Link-
105S-nitrosocysteineELNHCLSLR
HHHCCHHHH
2.41dbSNO
Link-
139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QEQLKQKKA
CCCCCHHHH
60.82Phosphositeplus
Link-
229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QVNFKGKLI
HHHHHHHHH
50.35Phosphositeplus
Link-
288Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IQEGKAYVD
EEEEEECCC
35.47Phosphositeplus
Link-
300N6-acetyllysineAEQMKAERE
EEEECCCCH
46.95HPRD
Link-
300N6-acetyllysineAEQMKAERE
EEEECCCCH
46.95Phosphositeplus
Link-
300N6-acetyllysine; alternate.AEQMKAERE
EEEECCCCH
46.95UniProtKB
Link-
300N6-malonyllysine; alternate.AEQMKAERE
EEEECCCCH
46.95UniProtKB
Link-
318Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)NPIEKNLQM
HHCCCCEEE
64.77Phosphositeplus
Link-
346PhosphoserineIDMSSNNGC
CCCCCEEEE
27.90Phosphositeplus
Link-
357PhosphotyrosineDPTLYRCKI
EECCCCCEE
19.22Phosphositeplus
Link-
377PhosphotyrosineVYPTYDFAC
HHHCCCCCH
12.45Phosphositeplus
Link-
417N6-acetyllysineLGIRKPYIW
CEECHHHHH
40.01HPRD
Link-
417N6-acetyllysineLGIRKPYIW
CEECHHHHH
40.01Phosphositeplus
Link-
417N6-acetyllysine.LGIRKPYIW
CEECHHHHH
40.01UniProtKB
Link-
434PhosphoserineNTVLSKRKL
CCCHHHHHH
26.52HPRD
Link-
434PhosphoserineNTVLSKRKL
CCCHHHHHH
26.52Phosphositeplus
Link-
435Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TVLSKRKLT
CCHHHHHHH
49.76Phosphositeplus
Link-
472Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VEGLKQFIA
CEEEEEECC
54.76Phosphositeplus
Link-
497N6-acetyllysineWAFNKKVID
EEEEECCEE
41.80HPRD
Link-
497N6-acetyllysineWAFNKKVID
EEEEECCEE
41.80Phosphositeplus
Link-
498N6-acetyllysineAFNKKVIDP
EEEECCEEE
45.59HPRD
Link-
498N6-acetyllysineAFNKKVIDP
EEEECCEEE
45.59Phosphositeplus
Link-
498N6-acetyllysine.AFNKKVIDP
EEEECCEEE
45.59UniProtKB
Link-
535Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AKHPKNPEV
CCCEEEEEE
82.14Phosphositeplus
Link-
535N6-acetyllysineAKHPKNPEV
CCCEEEEEE
82.14HPRD
Link-
535N6-acetyllysineAKHPKNPEV
CCCEEEEEE
82.14Phosphositeplus
Link-
535N6-acetyllysine.AKHPKNPEV
CCCEEEEEE
82.14UniProtKB
Link-
542N6-acetyllysineEVGLKPVWY
EECCCCCCE
31.43HPRD
Link-
542N6-acetyllysineEVGLKPVWY
EECCCCCCE
31.43Phosphositeplus
Link-
542N6-acetyllysine.EVGLKPVWY
EECCCCCCE
31.43UniProtKB
Link-
546PhosphotyrosineKPVWYSPKV
CCCCEEEEE
18.48Phosphositeplus
Link-
547PhosphoserinePVWYSPKVF
CCCEEEEEE
11.52Phosphositeplus
Link-
637N6-acetyllysinePVLGKDEDF
CCCCCCCCC
54.50HPRD
Link-
637N6-acetyllysinePVLGKDEDF
CCCCCCCCC
54.50Phosphositeplus
Link-
637N6-acetyllysine.PVLGKDEDF
CCCCCCCCC
54.50UniProtKB
Link-
690PhosphotyrosinePVSPYSCKE
CCCHHHHHH
21.13Phosphositeplus
Link
713PhosphoserineEMPTSGSKE
HHHHHHHHH
34.89HPRD
Link
782Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DAAVKQLLS
HHHHHHHHH
30.42Phosphositeplus
Link-
788N6-acetyllysineLLSLKAEYK
HHHHHHHHH
35.48HPRD
Link-
788N6-acetyllysineLLSLKAEYK
HHHHHHHHH
35.48Phosphositeplus
Link-
788N6-acetyllysine.LLSLKAEYK
HHHHHHHHH
35.48UniProtKB
Link-
813PhosphoserineGQNISSNSS
CCCCCCCCC
30.89HPRD
Link-
813PhosphoserineGQNISSNSS
CCCCCCCCC
30.89PhosphoELM
Link-
813PhosphoserineGQNISSNSS
CCCCCCCCC
30.89PhosphoELM
Link-
813PhosphoserineGQNISSNSS
CCCCCCCCC
30.89Phosphositeplus
Link-
814PhosphoserineQNISSNSSA
CCCCCCCCC
36.61PhosphoELM
Link-
819PhosphoserineNSSASILES
CCCCCCCCC
29.65PhosphoELM
Link-
827PhosphotyrosineSKSLYDEVA
CCCCHHHHH
19.69Phosphositeplus
Link-
845PhosphoserineKAEKSPKAK
HHHHHHHHC
24.12HPRD
Link-
845PhosphoserineKAEKSPKAK
HHHHHHHHC
24.12Phosphositeplus
Link-
856S-nitrosocysteineEAVECLLSL
CHHHHHHHH
3.58dbSNO
Link-
859PhosphoserineECLLSLKAQ
HHHHHHHHH
18.18Phosphositeplus
Link-
861Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LLSLKAQYK
HHHHHHHHH
30.02Phosphositeplus
Link-
872PhosphotyrosineTGKEYIPGQ
HHHHHHHCC
18.85HPRD
Link-
872PhosphotyrosineTGKEYIPGQ
HHHHHHHCC
18.85PhosphoELM
Link-
872PhosphotyrosineTGKEYIPGQ
HHHHHHHCC
18.85Phosphositeplus
Link-
872PhosphotyrosineTGKEYIPGQ
HHHHHHHCC
18.85SysPTM
Link-
872Phosphotyrosine.TGKEYIPGQ
HHHHHHHCC
18.85UniProtKB
Link-
880PhosphoserineQPPLSQSSD
CCCCCCCCC
33.52HPRD
Link-
880PhosphoserineQPPLSQSSD
CCCCCCCCC
33.52PhosphoELM
Link-
880PhosphoserineQPPLSQSSD
CCCCCCCCC
33.52Phosphositeplus
Link-
880PhosphoserineQPPLSQSSD
CCCCCCCCC
33.52SysPTM
Link-
880Phosphoserine.QPPLSQSSD
CCCCCCCCC
33.52UniProtKB
Link-
882PhosphoserinePLSQSSDSS
CCCCCCCCC
32.51HPRD
Link-
882PhosphoserinePLSQSSDSS
CCCCCCCCC
32.51PhosphoELM
Link-
882PhosphoserinePLSQSSDSS
CCCCCCCCC
32.51Phosphositeplus
Link-
882PhosphoserinePLSQSSDSS
CCCCCCCCC
32.51SysPTM
Link-
882Phosphoserine.PLSQSSDSS
CCCCCCCCC
32.51UniProtKB
Link-
883PhosphoserineLSQSSDSSP
CCCCCCCCC
33.60HPRD
Link-
883PhosphoserineLSQSSDSSP
CCCCCCCCC
33.60PhosphoELM
Link-
883PhosphoserineLSQSSDSSP
CCCCCCCCC
33.60Phosphositeplus
Link-
883PhosphoserineLSQSSDSSP
CCCCCCCCC
33.60SysPTM
Link-
883Phosphoserine.LSQSSDSSP
CCCCCCCCC
33.60UniProtKB
Link-
885PhosphoserineQSSDSSPTR
CCCCCCCCC
39.92HPRD
Link-
885PhosphoserineQSSDSSPTR
CCCCCCCCC
39.92Phosphositeplus
Link-
885PhosphoserineQSSDSSPTR
CCCCCCCCC
39.92SysPTM
Link-
885Phosphoserine.QSSDSSPTR
CCCCCCCCC
39.92UniProtKB
Link-
886PhosphoserineSSDSSPTRN
CCCCCCCCH
34.97HPRD
Link-
886PhosphoserineSSDSSPTRN
CCCCCCCCH
34.97Phosphositeplus
Link-
886PhosphoserineSSDSSPTRN
CCCCCCCCH
34.97SysPTM
Link-
886Phosphoserine; by CDK5.SSDSSPTRN
CCCCCCCCH
34.97UniProtKB
Link-
888PhosphothreonineDSSPTRNSE
CCCCCCHHH
44.42HPRD
Link-
888PhosphothreonineDSSPTRNSE
CCCCCCHHH
44.42PhosphoELM
Link-
888PhosphothreonineDSSPTRNSE
CCCCCCHHH
44.42Phosphositeplus
Link-
888PhosphothreonineDSSPTRNSE
CCCCCCHHH
44.42SysPTM
Link-
888Phosphothreonine.DSSPTRNSE
CCCCCCHHH
44.42UniProtKB
Link-
891PhosphoserinePTRNSEPAG
CCCHHHHHH
41.48HPRD
Link-
891PhosphoserinePTRNSEPAG
CCCHHHHHH
41.48Phosphositeplus
Link-
891PhosphoserinePTRNSEPAG
CCCHHHHHH
41.48SysPTM
Link-
891Phosphoserine.PTRNSEPAG
CCCHHHHHH
41.48UniProtKB
Link-
898PhosphothreonineAGLETPEAK
HHHHCCCCC
31.32HPRD
Link-
898PhosphothreonineAGLETPEAK
HHHHCCCCC
31.32PhosphoELM
Link-
898PhosphothreonineAGLETPEAK
HHHHCCCCC
31.32Phosphositeplus
Link-
898PhosphothreonineAGLETPEAK
HHHHCCCCC
31.32SysPTM
Link-
898Phosphothreonine.AGLETPEAK
HHHHCCCCC
31.32UniProtKB
Link-
910PhosphoserineDKVASQGEV
CCHHHHCCC
41.53Phosphositeplus
Link-
943Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KAQYKSLIG
HHHHCCCCC
27.06Phosphositeplus
Link-
991Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KDPSKNQGG
HHHHHHHHH
59.69Phosphositeplus
Link-
999PhosphoserineGGLSSSGAG
HHHHCCCCE
37.52HPRD
Link-
999PhosphoserineGGLSSSGAG
HHHHCCCCE
37.52Phosphositeplus
Link-
999Phosphoserine.GGLSSSGAG
HHHHCCCCE
37.52UniProtKB
Link-
1000PhosphoserineGLSSSGAGE
HHHCCCCEE
29.32HPRD
Link-
1000PhosphoserineGLSSSGAGE
HHHCCCCEE
29.32PhosphoELM
Link-
1000PhosphoserineGLSSSGAGE
HHHCCCCEE
29.32Phosphositeplus
Link-
1000PhosphoserineGLSSSGAGE
HHHCCCCEE
29.32SysPTM
Link-
1000Phosphoserine.GLSSSGAGE
HHHCCCCEE
29.32UniProtKB
Link-
1009Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GQGPKKQTR
ECCCCCCHH
65.42Phosphositeplus
Link-
1012PhosphothreoninePKKQTRLGL
CCCCHHHHH
36.42HPRD
Link-
1012PhosphothreoninePKKQTRLGL
CCCCHHHHH
36.42Phosphositeplus
Link-
1070Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AEIKKLGVE
HHHCHHEEE
57.02Phosphositeplus
Link-
1109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TRSGKTELA
CCHHHHHHH
39.82Phosphositeplus
Link-
1121PhosphothreonineAIRPTSETV
HHHHHHHHH
29.37HPRD
Link-
1132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PAYAKWVQS
HCCCEEEEE
34.91Phosphositeplus
Link-
1156N6-acetyllysineRWEFKHPQP
CCHHHHHHH
42.75HPRD
Link-
1156N6-acetyllysineRWEFKHPQP
CCHHHHHHH
42.75Phosphositeplus
Link-
1156N6-acetyllysine.RWEFKHPQP
CCHHHHHHH
42.75UniProtKB
Link-
1336PhosphoserineRRLLSVNIR
HHHHHHHHH
20.08HPRD
Link-
1336PhosphoserineRRLLSVNIR
HHHHHHHHH
20.08Phosphositeplus
Link-
1361Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HWELKGVPI
CHHHHHHHH
46.47Phosphositeplus
Link-
1375Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PRDMKSCQF
EEEEECCCH
52.98Phosphositeplus
Link-
1389Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DTGEKLTVA
HHHHHHCHH
51.29Phosphositeplus
Link-
1435Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EDFQKILDS
CEEEEEEEE
45.27Phosphositeplus
Link-
1503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KNPAKYYTL
39.79Phosphositeplus
Link-
1503N6-acetyllysineKNPAKYYTL
39.79HPRD
Link-
1503N6-acetyllysineKNPAKYYTL
39.79Phosphositeplus
Link-
1503N6-acetyllysine.KNPAKYYTL
39.79UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IKKB_HUMANphysical interactionMINT-48073MINT14743216
HS90A_HUMANphysical interactionMINT-13695MINT10913161
HS90A_HUMANphysical interactionMINT-13696MINT10913161
SYIC_HUMANphysical interactionMINT-15365MINT10913161
SYIC_HUMANphysical interactionMINT-15364MINT10913161
1433Z_HUMANphysical interactionMINT-3297276MINT15161933
NFKB2_HUMANphysical interactionMINT-48714MINT14743216
NELFD_HUMANphysical interactionMINT-64854MINT16169070
RIPK3_HUMANphysical interactionMINT-49098MINT14743216
CRCM_HUMANphysical interactionEBI-1066507
intact17353931
IKKE_HUMANphysical interactionEBI-1083295
intact17353931
SYRC_HUMANyeast 2-hybridHPRD:00703HPRD9556618
HNRPQ_HUMANin vivoHPRD:00703HPRD15479637
NELFD_HUMANyeast 2-hybridHPRD:00703HPRD16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00172L-Proline
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-300; LYS-417; LYS-498;LYS-535; LYS-542; LYS-637; LYS-788; LYS-1156 AND LYS-1503, AND MASSSPECTROMETRY.
N6-malonyllysine
ReferencePubMed
"The first identification of lysine malonylation substrates and itsregulatory 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).
Cited for: MALONYLATION AT LYS-300.
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-898, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-885; SER-886 ANDSER-891, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886 AND THR-888, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-872; SER-882; SER-883;SER-885; SER-886; SER-891 AND THR-898, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-880; SER-882; SER-883;SER-885; SER-886; THR-888; SER-999 AND SER-1000, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-885 ANDSER-886, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-886 ANDSER-891, AND MASS SPECTROMETRY.
"Phosphorylation of glutamyl-prolyl tRNA synthetase by cyclin-dependent kinase 5 dictates transcript-selective translationalcontrol.";
Arif A., Jia J., Moodt R.A., DiCorleto P.E., Fox P.L.;
Proc. Natl. Acad. Sci. U.S.A. 108:1415-1420(2011).
Cited for: PHOSPHORYLATION AT SER-886.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-898 AND SER-1000, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures