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SWISS-2DPAGE 
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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: SYL_ECOLI




SWISS-2DPAGE:  SYL_ECOLI


SYL_ECOLI


General information about the entry
View entry in simple text format
Entry nameSYL_ECOLI
Primary accession numberP07813
integrated into SWISS-2DPAGE on August 1, 1995 (release 2)
2D Annotations were last modified onOctober 1, 2001 (version 1)
General Annotations were last modified on May 19, 2011 (version 11)
Name and origin of the protein
DescriptionRecName: Full=Leucyl-tRNA synthetase; EC=6.1.1.4; AltName: Full=Leucine--tRNA ligase; Short=LeuRS;.
Gene nameName=leuS
OrderedLocusNames=b0642, JW0637
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   MAPPING ON GEL
MEDLINE=96314059; PubMed=8740179; [NCBI, ExPASy, EBI, Israel, Japan]
Pasquali C., Frutiger S., Wilkins M.R., Hughes G.J., Appel R.D., Bairoch A., Schaller D., Sanchez J.-C., Hochstrasser D.F.
''''''Two-dimensional gel electrophoresis of Escherichia coli homogenates: the Escherichia coli SWISS-2DPAGE database'';'';''
Electrophoresis 17(1):547-555(1996)
[2]   MAPPING ON GEL
Vanbogelen R.A., Abshire K.Z., Pertsemlidis A., Clark R.L., Neidhardt F.C.
''''''Gene-protein database of Escherichia coli K-12, edition 6'';'';''
(IN) Neidhardt et al. (eds.)Escherichia coli and Salmonella: Cellular and Molecular Biology (2nd ed.), pp.2067-2117, ASM Press, Washington DC (1996)
[3]   MAPPING ON GEL
MEDLINE=80159887; PubMed=6988414; [NCBI, ExPASy, EBI, Israel, Japan]
Bloch P.L., Phillips T.A., Neidhardt F.C.
''''''Protein identifications of O'Farrell two-dimensional gels: locations of 81 Escherichia coli proteins'';'';''
J. Bacteriol. 141(1):1409-1420(1980)
[4]   PROTEIN EXPRESSION
MEDLINE=79216190; PubMed=156716; [NCBI, ExPASy, EBI, Israel, Japan]
Herendeen S.L., Vanbogelen R.A., Neidhardt F.C.
''''''Levels of major proteins of Escherichia coli during growth at different temperatures'';'';''
J. Bacteriol. 139(1):185-194(1979)
[5]   PROTEIN EXPRESSION
MEDLINE=78212912; PubMed=352533; [NCBI, ExPASy, EBI, Israel, Japan]
Pedersen S., Bloch P.L., Reeh S., Neidhardt F.C.
''''''Patterns of protein synthesis in E. coli: a catalog of the amount of 140 individual proteins at different growth rates'';'';''
Cell 14(1):179-190(1978)
Comments
  • SUBUNIT: MONOMER
2D PAGE maps for identified proteins
How to interpret a protein

ECOLI {Escherichia coli}
Escherichia coli
ECOLI
  map experimental info
  protein estimated location
 
ECOLI

MAP LOCATIONS:
pI=5.11; Mw=98803

EXPRESSION:
CHANGED VERY LITTLE THROUGHOUT THE NORMAL ARRHENIUS TEMPERATURE RANGE (23 TO 37C) [4]; INCREASED IN LEVEL WITH INCREASING GROWTH RATE [5].

MAPPING (identification):
GEL MATCHING [1] AND IDENTIFIED ON 2-D GELS BY VANBOGELEN [2] AND BLOCH [3].

Copyright
This SWISS-2DPAGE entry is copyright the Swiss Institute of Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://world-2dpage.expasy.org/swiss-2dpage/docs/license.html or send email from legal@sib.swiss).
Cross-references
ECO2DBASED100.0; 6TH EDITION.
UniProtKB/Swiss-ProtP07813; SYL_ECOLI.
2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 2011_10
Entry nameSYL_ECOLI
Primary accession numberP07813
Secondary accession number(s) P77110 P78292
Sequence was last modified on November 1, 1997 (version 2)
Annotations were last modified on October 19, 2011 (version 116)
Name and origin of the protein
DescriptionRecName: Full=Leucyl-tRNA synthetase; EC=6.1.1.4; AltName: Full=Leucine--tRNA ligase; Short=LeuRS;
Gene nameName=leuS
OrderedLocusNames=b0642, JW0637
Encoded onName=leuS; OrderedLocusNames=b0642, JW0637
Keywords3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX06331; CAA29642.1; -; Genomic_DNA
EMBLU82598; AAB40843.1; ALT_INIT; Genomic_DNA
EMBLU00096; AAC73743.1; -; Genomic_DNA
EMBLAP009048; BAA35289.1; -; Genomic_DNA
PIRH64798; SYECL; .
RefSeqNP_415175.1; NC_000913.2; .
PDB2AJG; X-ray; 2.00 A; A/B=228-413
PDB2AJH; X-ray; 2.40 A; A/B=228-413
PDB2AJI; X-ray; 3.20 A; A/B=228-413
PDBsum2AJG; -; .
PDBsum2AJH; -; .
PDBsum2AJI; -; .
ProteinModelPortalP07813; -; .
SMRP07813; 3-859; .
DIPDIP-10095N; -; .
IntActP07813; 18; .
MINTMINT-1226410; -; .
SWISS-2DPAGEP07813; -; .
ECO2DBASED100.0; 6TH EDITION; .
EnsemblBacteriaEBESCT00000002149; EBESCP00000002149; EBESCG00000001760; .
EnsemblBacteriaEBESCT00000017570; EBESCP00000016861; EBESCG00000016626; .
GeneID947497; -; .
GenomeReviewsAP009048_GR; JW0637; .
GenomeReviewsU00096_GR; b0642; .
KEGGecj:JW0637; -; .
KEGGeco:b0642; -; .
EchoBASEEB0527; -; .
EcoGeneEG10532; leuS; .
eggNOGCOG0495; -; .
GeneTreeEBGT00050000010349; -; .
HOGENOMHBG693845; -; .
OMAYARYCSP; -; .
ProtClustDBPRK00390; -; .
BioCycEcoCyc:LEUS-MONOMER; -; .
BioCycMetaCyc:LEUS-MONOMER; -; .
GenevestigatorP07813; -; .
GOGO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell; .
GOGO:0005524; F:ATP binding; IEA:UniProtKB-KW; .
GOGO:0004823; F:leucine-tRNA ligase activity; IDA:EcoCyc; .
GOGO:0006429; P:leucyl-tRNA aminoacylation; IDA:EcoCyc; .
HAMAPMF_00049_B; Leu_tRNA_synth_B; 1; -
InterProIPR001412; aa-tRNA-synth_I_CS; .
InterProIPR002300; aa-tRNA-synth_Ia; .
InterProIPR002302; Leu-tRNA-synth_Ia_bac/mito; .
InterProIPR014729; Rossmann-like_a/b/a_fold; .
InterProIPR009080; tRNAsynth_1a_anticodon-bd; .
InterProIPR013155; V/L/I-tRNA-synth_anticodon-bd; .
InterProIPR009008; Val/Leu/Ile-tRNA-synth_edit; .
Gene3DG3DSA:3.90.740.10; G3DSA:3.90.740.10; 1; .
Gene3DG3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 3; .
PfamPF08264; Anticodon_1; 1; .
PfamPF00133; tRNA-synt_1; 5; .
PRINTSPR00985; TRNASYNTHLEU; .
SUPFAMSSF47323; tRNAsyn_1a_bind; 1; .
SUPFAMSSF50677; ValRS_IleRS_edit; 1; .
TIGRFAMsTIGR00396; LeuS_bact; 1; .
PROSITEPS00178; AA_TRNA_LIGASE_I; 1; .



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Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server