Hmdb loader

Showing Protein Bifunctional glutamate/proline--tRNA ligase (HMDBP00567)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 7 metabolites
Identification
HMDB Protein ID HMDBP00567
Secondary Accession Numbers
  • 5839
Name Bifunctional glutamate/proline--tRNA ligase
Synonyms
  1. Cell proliferation-inducing gene 32 protein
  2. GluRS
  3. Glutamate--tRNA ligase
  4. Glutamyl-tRNA synthetase
  5. Proline--tRNA ligase
  6. Prolyl-tRNA synthetase
  7. Bifunctional aminoacyl-tRNA synthetase
  8. Glutamatyl-prolyl-tRNA synthetase
Gene Name EPRS
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific 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.
Pathways
  • Aminoacyl-tRNA biosynthesis
  • Arginine and proline metabolism
  • Arginine: Glycine Amidinotransferase Deficiency (AGAT Deficiency)
  • Creatine deficiency, guanidinoacetate methyltransferase deficiency
  • Guanidinoacetate Methyltransferase Deficiency (GAMT Deficiency)
  • Hyperornithinemia with gyrate atrophy (HOGA)
  • Hyperornithinemia-hyperammonemia-homocitrullinuria [HHH-syndrome]
  • Hyperprolinemia Type I
  • Hyperprolinemia Type II
  • L-arginine:glycine amidinotransferase deficiency
  • Ornithine Aminotransferase Deficiency (OAT Deficiency)
  • Porphyrin and chlorophyll metabolism
  • Prolidase Deficiency (PD)
  • Prolinemia Type II
Reactions
Adenosine triphosphate + L-Glutamic acid + tRNA(Glu) → Adenosine monophosphate + Pyrophosphate + L-glutamyl-tRNA(Glu) details
Adenosine triphosphate + L-Proline + tRNA(Pro) → Adenosine monophosphate + Pyrophosphate + L-prolyl-tRNA(Pro) details
Adenosine triphosphate + L-Proline + tRNA(Pro) → Adenosine monophosphate + Pyrophosphate + L-Prolyl-tRNA(Pro) details
tRNA(Glu) + L-Glutamic acid + Adenosine triphosphate → L-Glutamyl-tRNA(Glu) + Pyrophosphate + Adenosine monophosphate details
GO Classification
Biological Process
negative regulation of translation
glutamyl-tRNA aminoacylation
prolyl-tRNA aminoacylation
tRNA aminoacylation for protein translation
cellular response to interferon-gamma
protein complex assembly
Cellular Component
cytosol
ribonucleoprotein complex
Component
cell part
intracellular part
cytoplasm
Function
binding
nucleotide binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
proline-trna ligase activity
glutamate-trna ligase activity
ligase activity
ligase activity, forming carbon-oxygen bonds
ligase activity, forming aminoacyl-trna and related compounds
aminoacyl-trna ligase activity
Molecular Function
ATP binding
RNA stem-loop binding
glutamate-tRNA ligase activity
proline-tRNA ligase activity
Process
rna metabolic process
ncrna metabolic process
trna metabolic process
trna aminoacylation
trna aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
prolyl-trna aminoacylation
glutamyl-trna aminoacylation
biosynthetic process
Cellular Location Not Available
Gene Properties
Chromosome Location 1
Locus 1q41
SNPs EPRS
Gene Sequence 
>4539 bp
ATGGCGACGCTCTCTCTGACCGTGAATTCAGGAGACCCTCCGCTAGGAGCTTTGCTGGCA
GTAGAACACGTGAAAGACGATGTCAGCATTTCCGTTGAAGAAGGGAAAGAGAATATTCTT
CATGTTTCTGAAAATGTGATATTCACAGATGTGAATTCTATACTTCGCTACTTGGCTAGA
GTTGCAACTACAGCTGGGTTATATGGCTCTAATCTGATGGAACATACTGAGATTGATCAC
TGGTTGGAGTTCAGTGCTACAAAATTATCTTCATGTGATTCCTTTACTTCTACAATTAAT
GAACTCAATCATTGCCTGTCTCTGAGAACATACTTAGTTGGAAACTCCTTGAGTTTAGCA
GATTTATGTGTTTGGGCCACCCTAAAAGGAAATGCTGCCTGGCAAGAACAGTTGAAACAG
AAGAAAGCTCCAGTTCATGTAAAACGTTGGTTTGGCTTTCTTGAAGCCCAGCAGGCCTTC
CAGTCAGTAGGTACCAAGTGGGATGTTTCAACAACCAAAGCTCGAGTGGCACCTGAGAAA
AAGCAAGATGTTGGGAAATTTGTTGAGCTTCCAGGTGCGGAGATGGGAAAGGTTACCGTC
AGATTTCCTCCAGAGGCCAGTGGTTACTTACACATTGGGCATGCAAAAGCTGCTCTTCTG
AACCAGCACTACCAGGTTAACTTTAAAGGGAAACTGATCATGAGATTTGATGACACAAAT
CCTGAAAAAGAAAAGGAAGATTTTGAGAAGGTTATCTTGGAAGATGTTGCAATGTTGCAT
ATCAAACCAGATCAATTTACTTATACTTCGGATCATTTTGAAACTATAATGAAGTATGCA
GAGAAGCTAATTCAAGAAGGGAAGGCTTATGTGGATGATACTCCTGCTGAACAGATGAAA
GCAGAACGTGAGCAGAGGATAGAATCTAAACATAGAAAAAACCCTATTGAGAAGAATCTA
CAAATGTGGGAAGAAATGAAAAAAGGGAGCCAGTTTGGTCAGTCCTGTTGTTTGCGAGCA
AAAATTGACATGAGTAGTAACAATGGATGCATGAGAGATCCAACCCTTTATCGCTGCAAA
ATTCAACCACATCCAAGAACTGGAAATAAATACAATGTTTATCCAACATATGATTTTGCC
TGCCCCATAGTTGACAGCATCGAAGGTGTTACACATGCCCTGAGAACAACAGAATACCAT
GACAGAGATGAGCAGTTTTACTGGATTATTGAAGCTTTAGGCATAAGAAAACCATATATT
TGGGAATATAGTCGGCTAAATCTCAACAACACAGTGCTATCCAAAAGAAAACTCACATGG
TTTGTCAATGAAGGACTAGTAGATGGATGGGATGACCCAAGATTTCCTACGGTTCGTGGT
GTACTGAGAAGAGGGATGACAGTTGAAGGACTGAAACAGTTTATTGCTGCTCAGGGCTCC
TCACGTTCAGTCGTGAACATGGAGTGGGACAAAATCTGGGCGTTTAACAAAAAGGTTATT
GACCCAGTGGCTCCACGATATGTTGCATTACTGAAGAAAGAAGTGATCCCAGTGAATGTA
CCTGAAGCTCAGGAGGAGATGAAAGAAGTAGCCAGACACCCAAAGAATCCTGAGGTTGGC
TTGAAGCCTGTGTGGTATAGTCCCAAAGTTTTCATTGAAGGTGCTGATGCAGAGACTTTT
TCGGAGGGTGAGATGGTTACATTTATAAATTGGGGCAACCTCAACATTACAAAAATACAC
AAAAATGCAGATGGAAAAATCATATCTCTTGATGCAAAGTTGAATTTGGAAAACAAAGAC
TACAAGAAAACCACTAAGGTCACTTGGCTTGCAGAGACTACACATGCTCTTCCTATTCCA
GTAATCTGTGTCACTTATGAGCACTTGATCACAAAGCCAGTGCTAGGAAAAGACGAGGAC
TTTAAGCAGTATGTCAACAAGAACAGTAAGCATGAAGAGCTAATGCTAGGGGATCCCTGC
CTTAAGGATTTGAAAAAAGGAGATATTATACAACTCCAGAGAAGAGGATTCTTCATATGT
GATCAACCTTATGAACCTGTTAGCCCATATAGTTGCAAGGAAGCCCCGTGTGTTTTGATA
TACATTCCTGATGGGCACACAAAGGAAATGCCAACATCAGGGTCAAAGGAAAAGACCAAA
GTAGAAGCCACAAAAAATGAGACCTCTGCTCCTTTTAAGGAAAGACCAACACCTTCTCTG
AATAATAATTGTACTACATCTGAGGATTCCTTGGTCCTTTACAATAGAGTGGCTGTTCAA
GGAGATGTGGTTCGTGAATTAAAAGCCAAGAAAGCACCAAAGGAAGATGTAGATGCAGCT
GTAAAACAGCTTTTGTCTTTGAAAGCTGAATATAAGGAGAAAACTGGCCAGGAATATAAA
CCTGGAAACCCTCCTGCTGAAATAGGACAGAATATTTCTTCTAATTCCTCAGCAAGTATT
CTGGAAAGTAAATCTCTGTATGATGAAGTTGCTGCACAAGGGGAGGTGGTTCGTAAGCTA
AAAGCTGAAAAATCCCCTAAGGCTAAAATAAATGAAGCTGTAGAATGCTTACTGTCCCTG
AAGGCTCAGTATAAAGAAAAAACTGGGAAGGAGTACATACCTGGTCAGCCCCCATTATCT
CAAAGTTCGGATTCAAGCCCAACCAGAAATTCTGAACCTGCTGGTTTAGAAACACCAGAA
GCGAAAGTACTTTTTGACAAAGTAGCTTCTCAAGGGGAAGTAGTTCGGAAACTTAAAACT
GAAAAAGCCCCTAAGGATCAAGTAGATATAGCTGTTCAAGAACTCCTTCAGCTAAAGGCA
CAGTACGAGTCTTTGATAGGAGTAGAGTATAAGCCTGTGTCGGCCACTGGAGCTGAGGAC
AAAGATAAGAAGAAGAAAGAAAAAGAAAATAAATCTGAAAAGCAGAATAAGCCTCAGAAA
CAAAATGATGGCCAAAGGAAAGACCCTTCTAAAAACCAAGGAGGTGGGCTCTCATCAAGT
GGAGCAGGAGAAGGGCAGGGGCCTAAGAAACAGACCAGGTTGGGTCTTGAGGCAAAAAAA
GAAGAAAATCTTGCTGATTGGTATTCTCAGGTCATCACAAAATCAGAAATGATTGAATAC
CATGACGTAAGTGGCTGTTATATTCTTCGTCCCTGGGCCTATGCCATTTGGGAAGCCATC
AAGGACTTTTTTGATGCTGAGATCAAGAAACTTGGTGTTGAAAACTGCTACTTCCCCATG
TTTGTGTCTCAAAGTGCATTAGAGAAAGAGAAGACTCATGTTGCTGACTTTGCCCCAGAG
GTTGCTTGGGTTACAAGATCTGGCAAAACCGAGCTGGCAGAACCAATTGCCATTCGTCCT
ACTAGTGAAACAGTAATGTATCCTGCATATGCAAAATGGGTACAATCACACAGAGACCTG
CCCATCAAGCTCAATCAGTGGTGCAATGTGGTGCGTTGGGAATTCAAGCATCCTCAGCCT
TTCCTACGTACTCGTGAATTTCTTTGGCAGGAAGGGCACAGTGCTTTTGTTACCGTGGAA
GAGGCAGCGGAAGAGGTCTTGCAGATACTTGACTTATATGCTCAGGTATATGAAGAACTC
CTGGCAATTCCTGTTGTTAAAGGAAGAAAGACGGAAAAGGAAAAATTTGCAGGAGGAGAC
TATACAACTACAATAGAAGCATTTATATCTGCTAGTGGAAGAGCTATCCAGGGAGGAACA
TCACATCATTTAGGGCAGAATTTTTCCAAAATGTTTGAAATCGTTTTTGAAGATCCAAAG
ATACCAGGAGAGAAGCAATTTGCCTATCAAAACTCCTGGGGCCTGACAACTCGAACTATT
GGTGTTATGACCATGGTTCATGGGGACAACATGGGTTTAGTATTACCACCCCGTGTAGCA
TGTGTTCAGGTGGTGATTATTCCTTGTGGCATTACCAATGCACTTTCTGAAGAAGACAAA
GAAGCGCTGATTGCAAAATGCAATGATTATCGAAGGCGATTACTCAGTGTTAACATCCGC
GTTAGAGCTGATTTACGAGATAATTATTCTCCAGGTTGGAAATTCAATCACTGGGAGCTC
AAGGGAGTTCCCATTAGACTTGAAGTTGGGCCACGTGATATGAAGAGCTGTCAGTTTGTA
GCCGTCAGACGAGATACTGGAGAAAAGCTGACAGTTGCTGAAAATGAGGCAGAGACTAAA
CTTCAAGCTATTTTGGAAGACATCCAGGTCACCCTTTTCACAAGGGCTTCTGAAGACCTT
AAGACTCATATGGTTGTGGCTAATACAATGGAAGACTTTCAGAAGATACTAGATTCTGGA
AGGATTGTTCAGATTCCATTCTGTGGGGAAATTGACTGTGAGGACTGGATCAAAAAGACC
ACTGCCAGGGATCAAGATCTTGAACCTGGTGCTCCATCCATGGGAGCTAAAAGCCTTTGC
ATCCCCTTCAAACCACTCTGTGAACTGCAGCCTGGAGCCAAATGTGTCTGTGGCAAGAAC
CCTGCCAAGTACTACACCTTATTTGGTCGCAGCTACTGA
Protein Properties
Number of Residues 1512
Molecular Weight 170589.705
Theoretical pI 7.321
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Bifunctional aminoacyl-tRNA synthetase
MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLAR
VATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLA
DLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEK
KQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTN
PEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMK
AEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCK
IQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYI
WEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGS
SRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVG
LKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKD
YKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPC
LKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTK
VEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAA
VKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKL
KAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPE
AKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAED
KDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKK
EENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPM
FVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDL
PIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEEL
LAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPK
IPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDK
EALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFV
AVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSG
KIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKN
PAKYYTLFGRSY
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P07814
UniProtKB/Swiss-Prot Entry Name SYEP_HUMAN
PDB IDs
GenBank Gene ID CR933648
GeneCard ID EPRS
GenAtlas ID EPRS
HGNC ID HGNC:3418
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  7. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  8. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  9. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: 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. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  11. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  12. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  13. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. doi: 10.1021/pr0705441. Epub 2008 Jan 26. [PubMed:18220336 ]
  14. Molina H, Horn DM, 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. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  15. 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. 2005 Jul 1;65(13):5638-46. [PubMed:15994936 ]
  16. 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. 1991 Jan 25;266(3):1448-55. [PubMed:1988429 ]
  17. Thommes 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. 1988 Jun 24;16(12):5391-406. [PubMed:3290852 ]
  18. 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. 1991 Dec;10(13):4267-77. [PubMed:1756734 ]
  19. Kaiser E, Eberhard D, Knippers R: Exons encoding the highly conserved part of human glutaminyl-tRNA synthetase. J Mol Evol. 1992 Jan;34(1):45-53. [PubMed:1556743 ]
  20. Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS: Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats. Biochemistry. 2000 Dec 26;39(51):15775-82. [PubMed:11123902 ]