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SWISS-2DPAGE 
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Sample Preparation and Post-separation Analysis



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




SWISS-2DPAGE:  THIO_ECOLI


THIO_ECOLI


General information about the entry
View entry in simple text format
Entry nameTHIO_ECOLI
Primary accession numberP0AA25
Secondary accession number(s) P00274
integrated into SWISS-2DPAGE on August 1, 1995 (release 2)
2D Annotations were last modified onMarch 31, 2004 (version 3)
General Annotations were last modified on May 19, 2011 (version 16)
Name and origin of the protein
DescriptionRecName: Full=Thioredoxin-1; Short=Trx-1;.
Gene nameName=trxA
Synonyms=fipA, tsnC
OrderedLocusNames=b3781, JW5856
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]   MAPPING ON GEL
PubMed=11680886; [NCBI, ExPASy, EBI, Israel, Japan]
Tonella L., Hoogland C., Binz P.-A., Appel R.D., Hochstrasser D.F., Sanchez J.-C.
''''''New perspectives in the Escherichia coli proteome investigation'';'';''
Proteomics 1(1):409-423(2001)
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=4.67; Mw=11675

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



ECOLI4-5 {Escherichia coli(4-5)}
Escherichia coli
ECOLI4-5
  map experimental info
  protein estimated location
 
ECOLI4-5

MAP LOCATIONS:
pI=4.80; Mw=9699  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [4].



ECOLI4.5-5.5 {Escherichia coli(4.5-5.5)}
Escherichia coli
ECOLI4.5-5.5
  map experimental info
  protein estimated location
 
ECOLI4.5-5.5

MAP LOCATIONS:
pI=4.95; Mw=9553  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [4].

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
ECO2DBASEB012.0; 6TH EDITION.
UniProtKB/Swiss-ProtP0AA25; THIO_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 nameTHIO_ECOLI
Primary accession numberP0AA25
Secondary accession number(s) P00274 P76750 Q2M889 Q47674 Q8XAT2
Sequence was last modified on January 23, 2007 (version 2)
Annotations were last modified on October 19, 2011 (version 67)
Name and origin of the protein
DescriptionRecName: Full=Thioredoxin-1; Short=Trx-1;
Gene nameName=trxA
Synonyms=fipA, tsnC
OrderedLocusNames=b3781, JW5856
Encoded onName=trxA; Synonyms=fipA, tsnC; OrderedLocusNames=b3781, JW5856
Keywords3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Disulfide bond; Electron transport; Host-virus interaction; Redox-active center; Reference proteome; Transport.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLM26133; AAA24693.1; -; Genomic_DNA
EMBLK02845; AAA24534.1; ALT_INIT; Genomic_DNA
EMBLM10424; AAA24533.1; -; Genomic_DNA
EMBLM54881; AAA24696.1; -; Genomic_DNA
EMBLM12779; AAA24694.1; -; Genomic_DNA
EMBLM87049; AAA67582.1; ALT_INIT; Genomic_DNA
EMBLU00096; AAC76786.2; -; Genomic_DNA
EMBLAP009048; BAE77517.1; -; Genomic_DNA
PIRA91519; TXEC; .
RefSeqNP_418228.2; NC_000913.2; .
PDB1F6M; X-ray; 2.95 A; C/D/G/H=2-109
PDB1KEB; X-ray; 1.80 A; A/B=2-108
PDB1M7T; NMR; -; A=68-108
PDB1OAZ; X-ray; 2.77 A; A/B=1-109
PDB1SKR; X-ray; 2.40 A; B=2-108
PDB1SKS; X-ray; 2.30 A; B=2-108
PDB1SKW; X-ray; 2.30 A; B=2-108
PDB1SL0; X-ray; 3.20 A; B/D=2-108
PDB1SL1; X-ray; 2.20 A; B=2-108
PDB1SL2; X-ray; 2.30 A; B=2-108
PDB1SRX; X-ray; 2.80 A; A=2-109
PDB1T7P; X-ray; 2.20 A; B=2-108
PDB1T8E; X-ray; 2.54 A; B=2-108
PDB1THO; X-ray; 2.30 A; A=2-108
PDB1TK0; X-ray; 2.30 A; B=2-108
PDB1TK5; X-ray; 2.20 A; B=2-108
PDB1TK8; X-ray; 2.50 A; B=2-108
PDB1TKD; X-ray; 2.49 A; B=2-108
PDB1TXX; X-ray; 2.20 A; A=2-109
PDB1X9M; X-ray; 2.10 A; B=2-108
PDB1X9S; X-ray; 2.70 A; B=2-108
PDB1X9W; X-ray; 2.30 A; B=2-108
PDB1XOA; NMR; -; A=2-109
PDB1XOB; NMR; -; A=2-109
PDB1ZCP; X-ray; 2.30 A; A/B/C/D=2-108
PDB1ZYQ; X-ray; 2.70 A; B=2-108
PDB1ZZY; X-ray; 2.50 A; A/B=1-109
PDB2AJQ; X-ray; 2.60 A; B/I=2-108
PDB2BTO; X-ray; 2.50 A; T=2-109
PDB2EIO; X-ray; 2.60 A; A/B/C/D=2-109
PDB2EIQ; X-ray; 1.90 A; A/B=2-109
PDB2EIR; X-ray; 2.50 A; A/B/C/D=2-109
PDB2FCH; X-ray; 2.60 A; A/B/C/D/E/F/G=2-108
PDB2FD3; X-ray; 2.45 A; A/B=2-108
PDB2H6X; X-ray; 2.60 A; A/B=2-109
PDB2H6Y; X-ray; 2.40 A; A/B=2-109
PDB2H6Z; X-ray; 2.25 A; A/B=2-109
PDB2H70; X-ray; 2.70 A; A/B=2-109
PDB2H71; X-ray; 2.20 A; A/B=2-109
PDB2H72; X-ray; 2.25 A; A/B=2-109
PDB2H73; X-ray; 2.45 A; A/B=2-109
PDB2H74; X-ray; 2.40 A; A/B=4-109
PDB2H75; X-ray; 2.20 A; A/B=2-109
PDB2H76; X-ray; 2.25 A; A/B=2-109
PDB2O8V; X-ray; 3.00 A; B=2-109
PDB2TIR; X-ray; 2.00 A; A=2-109
PDB2TRX; X-ray; 1.68 A; A/B=2-109
PDB3DYR; X-ray; 2.00 A; A/B=2-109
PDBsum1F6M; -; .
PDBsum1KEB; -; .
PDBsum1M7T; -; .
PDBsum1OAZ; -; .
PDBsum1SKR; -; .
PDBsum1SKS; -; .
PDBsum1SKW; -; .
PDBsum1SL0; -; .
PDBsum1SL1; -; .
PDBsum1SL2; -; .
PDBsum1SRX; -; .
PDBsum1T7P; -; .
PDBsum1T8E; -; .
PDBsum1THO; -; .
PDBsum1TK0; -; .
PDBsum1TK5; -; .
PDBsum1TK8; -; .
PDBsum1TKD; -; .
PDBsum1TXX; -; .
PDBsum1X9M; -; .
PDBsum1X9S; -; .
PDBsum1X9W; -; .
PDBsum1XOA; -; .
PDBsum1XOB; -; .
PDBsum1ZCP; -; .
PDBsum1ZYQ; -; .
PDBsum1ZZY; -; .
PDBsum2AJQ; -; .
PDBsum2BTO; -; .
PDBsum2EIO; -; .
PDBsum2EIQ; -; .
PDBsum2EIR; -; .
PDBsum2FCH; -; .
PDBsum2FD3; -; .
PDBsum2H6X; -; .
PDBsum2H6Y; -; .
PDBsum2H6Z; -; .
PDBsum2H70; -; .
PDBsum2H71; -; .
PDBsum2H72; -; .
PDBsum2H73; -; .
PDBsum2H74; -; .
PDBsum2H75; -; .
PDBsum2H76; -; .
PDBsum2O8V; -; .
PDBsum2TIR; -; .
PDBsum2TRX; -; .
PDBsum3DYR; -; .
ProteinModelPortalP0AA25; -; .
SMRP0AA25; 2-109; .
DIPDIP-31856N; -; .
IntActP0AA25; 91; .
SWISS-2DPAGEP0AA25; -; .
ECO2DBASEB012.0; 6TH EDITION; .
PRIDEP0AA25; -; .
EnsemblBacteriaEBESCT00000004349; EBESCP00000004349; EBESCG00000003545; .
EnsemblBacteriaEBESCT00000004350; EBESCP00000004350; EBESCG00000003545; .
EnsemblBacteriaEBESCT00000017819; EBESCP00000017110; EBESCG00000016875; .
GeneID948289; -; .
GenomeReviewsAP009048_GR; JW5856; .
GenomeReviewsU00096_GR; b3781; .
KEGGecj:JW5856; -; .
KEGGeco:b3781; -; .
EchoBASEEB1024; -; .
EcoGeneEG11031; trxA; .
eggNOGCOG0526; -; .
GeneTreeEBGT00050000008978; -; .
HOGENOMHBG493509; -; .
OMATLMLFKG; -; .
ProtClustDBPRK09381; -; .
BioCycEcoCyc:RED-THIOREDOXIN-MONOMER; -; .
GenevestigatorP0AA25; -; .
GOGO:0009055; F:electron carrier activity; IEA:InterPro; .
GOGO:0005515; F:protein binding; IPI:IntAct; .
GOGO:0015035; F:protein disulfide oxidoreductase activity; IDA:EcoCyc; .
GOGO:0045454; P:cell redox homeostasis; IMP:EcoCyc; .
GOGO:0022900; P:electron transport chain; IEA:UniProtKB-KW; .
GOGO:0006662; P:glycerol ether metabolic process; IEA:InterPro; .
GOGO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW; .
GOGO:0006810; P:transport; IEA:UniProtKB-KW; .
InterProIPR005746; Thioredoxin; .
InterProIPR012336; Thioredoxin-like_fold; .
InterProIPR017937; Thioredoxin_CS; .
InterProIPR013766; Thioredoxin_domain; .
Gene3DG3DSA:3.40.30.10; Thioredoxin_fold; 1; .
PANTHERPTHR10438; Trx; 1; .
PfamPF00085; Thioredoxin; 1; .
PIRSFPIRSF000077; Thioredoxin; 1; .
PRINTSPR00421; THIOREDOXIN; .
SUPFAMSSF52833; Thiordxn-like_fd; 1; .
TIGRFAMsTIGR01068; Thioredoxin; 1; .
PROSITEPS00194; THIOREDOXIN_1; 1; .
PROSITEPS51352; THIOREDOXIN_2; 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