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SWISS-2DPAGE

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SWISS-2DPAGE 
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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: P0AE67




SWISS-2DPAGE:  P0AE67


P0AE67


General information about the entry
View entry in simple text format
Entry nameCHEY_ECOLI
Primary accession numberP0AE67
Secondary accession number(s) P06143
integrated into SWISS-2DPAGE on April 1, 2000 (release 12)
2D Annotations were last modified onMarch 31, 2004 (version 1)
General Annotations were last modified on May 19, 2011 (version 10)
Name and origin of the protein
DescriptionRecName: Full=Chemotaxis protein CheY;.
Gene nameName=cheY
OrderedLocusNames=b1882, JW1871
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   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

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

MAP LOCATIONS:
pI=4.95; Mw=9749  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [1].

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
ECO2DBASEB014.1; 6TH EDITION.
UniProtKB/Swiss-ProtP0AE67; CHEY_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 nameCHEY_ECOLI
Primary accession numberP0AE67
Secondary accession number(s) P06143
Sequence was last modified on January 23, 2007 (version 2)
Annotations were last modified on October 19, 2011 (version 68)
Name and origin of the protein
DescriptionRecName: Full=Chemotaxis protein CheY;
Gene nameName=cheY
OrderedLocusNames=b1882, JW1871
Encoded onName=cheY; OrderedLocusNames=b1882, JW1871
Keywords3D-structure; Acetylation; Chemotaxis; Complete proteome; Cytoplasm; Direct protein sequencing; Flagellar rotation; Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Two-component regulatory system.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLK02175; AAA23577.1; -; Genomic_DNA
EMBLM13463; AAA23570.1; -; Genomic_DNA
EMBLU00096; AAC74952.1; -; Genomic_DNA
EMBLAP009048; BAA15698.1; -; Genomic_DNA
PIRE25195; QRECCY; .
RefSeqNP_416396.1; NC_000913.2; .
PDB1A0O; X-ray; 2.95 A; A/C/E/G=2-129
PDB1AB5; X-ray; 2.40 A; A/B=5-129
PDB1AB6; X-ray; 2.20 A; A/B=5-129
PDB1BDJ; X-ray; 2.68 A; A=1-129
PDB1C4W; X-ray; 1.84 A; A=1-129
PDB1CEY; NMR; -; A=2-129
PDB1CHN; X-ray; 1.76 A; A=2-129
PDB1CYE; NMR; -; A=2-129
PDB1D4Z; X-ray; 1.90 A; A=2-129
PDB1DJM; NMR; -; A=1-129
PDB1E6K; X-ray; 2.00 A; A=3-129
PDB1E6L; X-ray; 1.90 A; A=3-129
PDB1E6M; X-ray; 1.70 A; A=3-129
PDB1EAY; X-ray; 2.00 A; A/B=2-129
PDB1EHC; X-ray; 2.26 A; A=2-129
PDB1F4V; X-ray; 2.22 A; A/B/C=1-129
PDB1FFG; X-ray; 2.10 A; A/C=1-129
PDB1FFS; X-ray; 2.40 A; A/C=1-129
PDB1FFW; X-ray; 2.70 A; A/C=2-129
PDB1FQW; X-ray; 2.37 A; A/B=1-129
PDB1HEY; X-ray; 2.24 A; A=2-129
PDB1JBE; X-ray; 1.08 A; A=1-129
PDB1KMI; X-ray; 2.90 A; Y=1-129
PDB1MIH; X-ray; 2.70 A; A/B=1-129
PDB1U8T; X-ray; 1.50 A; A/B/C/D=1-129
PDB1UDR; X-ray; 1.90 A; A/B/C/D=3-129
PDB1VLZ; X-ray; 2.05 A; A/B=1-129
PDB1YMU; X-ray; 2.30 A; A/B=3-129
PDB1YMV; X-ray; 1.90 A; A=3-129
PDB1ZDM; X-ray; 2.40 A; A/B=1-129
PDB2B1J; X-ray; 2.40 A; A/B=2-128
PDB2ID7; X-ray; 1.75 A; A=2-128
PDB2ID9; X-ray; 1.75 A; A=2-129
PDB2IDM; X-ray; 2.00 A; A=2-129
PDB3CHY; X-ray; 1.66 A; A=2-129
PDB3F7N; X-ray; 2.00 A; A/B=2-129
PDB3FFT; X-ray; 2.21 A; A/B=2-129
PDB3FFW; X-ray; 2.00 A; A/B=2-129
PDB3FFX; X-ray; 2.01 A; A/B=2-129
PDB3FGZ; X-ray; 2.00 A; A/B=2-129
PDB3MYY; X-ray; 2.10 A; A/B=2-129
PDB3OLV; X-ray; 1.70 A; A/B=1-129
PDB3OLW; X-ray; 2.30 A; A/B=1-129
PDB3OLX; X-ray; 2.10 A; A/B=1-129
PDB3OLY; X-ray; 2.05 A; A/B=1-129
PDB3OO0; X-ray; 1.55 A; A/B=1-129
PDB3OO1; X-ray; 1.70 A; A/B=1-129
PDB5CHY; X-ray; 2.00 A; A=2-129
PDB6CHY; X-ray; 2.33 A; A/B=2-129
PDBsum1A0O; -; .
PDBsum1AB5; -; .
PDBsum1AB6; -; .
PDBsum1BDJ; -; .
PDBsum1C4W; -; .
PDBsum1CEY; -; .
PDBsum1CHN; -; .
PDBsum1CYE; -; .
PDBsum1D4Z; -; .
PDBsum1DJM; -; .
PDBsum1E6K; -; .
PDBsum1E6L; -; .
PDBsum1E6M; -; .
PDBsum1EAY; -; .
PDBsum1EHC; -; .
PDBsum1F4V; -; .
PDBsum1FFG; -; .
PDBsum1FFS; -; .
PDBsum1FFW; -; .
PDBsum1FQW; -; .
PDBsum1HEY; -; .
PDBsum1JBE; -; .
PDBsum1KMI; -; .
PDBsum1MIH; -; .
PDBsum1U8T; -; .
PDBsum1UDR; -; .
PDBsum1VLZ; -; .
PDBsum1YMU; -; .
PDBsum1YMV; -; .
PDBsum1ZDM; -; .
PDBsum2B1J; -; .
PDBsum2ID7; -; .
PDBsum2ID9; -; .
PDBsum2IDM; -; .
PDBsum3CHY; -; .
PDBsum3F7N; -; .
PDBsum3FFT; -; .
PDBsum3FFW; -; .
PDBsum3FFX; -; .
PDBsum3FGZ; -; .
PDBsum3MYY; -; .
PDBsum3OLV; -; .
PDBsum3OLW; -; .
PDBsum3OLX; -; .
PDBsum3OLY; -; .
PDBsum3OO0; -; .
PDBsum3OO1; -; .
PDBsum5CHY; -; .
PDBsum6CHY; -; .
ProteinModelPortalP0AE67; -; .
SMRP0AE67; 2-129; .
DIPDIP-48237N; -; .
IntActP0AE67; 12; .
SWISS-2DPAGEP0AE67; -; .
ECO2DBASEB014.1; 6TH EDITION; .
EnsemblBacteriaEBESCT00000000750; EBESCP00000000750; EBESCG00000000624; .
EnsemblBacteriaEBESCT00000017790; EBESCP00000017081; EBESCG00000016846; .
GeneID946393; -; .
GenomeReviewsAP009048_GR; JW1871; .
GenomeReviewsU00096_GR; b1882; .
KEGGecj:JW1871; -; .
KEGGeco:b1882; -; .
EchoBASEEB0148; -; .
EcoGeneEG10150; cheY; .
eggNOGCOG0784; -; .
GeneTreeEBGT00050000008654; -; .
HOGENOMHBG753323; -; .
OMAGFTNTSE; -; .
ProtClustDBPRK10610; -; .
BioCycEcoCyc:CHEY-MONOMER; -; .
GenevestigatorP0AE67; -; .
GOGO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell; .
GOGO:0046872; F:metal ion binding; IEA:UniProtKB-KW; .
GOGO:0000156; F:two-component response regulator activity; IEA:InterPro; .
GOGO:0006935; P:chemotaxis; IEA:UniProtKB-KW; .
GOGO:0001539; P:ciliary or flagellar motility; IEA:UniProtKB-KW; .
GOGO:0006355; P:regulation of transcription; DNA-dependent; IEA:InterPro
InterProIPR011006; CheY-like_superfamily; .
InterProIPR001789; Sig_transdc_resp-reg_receiver; .
PfamPF00072; Response_reg; 1; .
SMARTSM00448; REC; 1; .
SUPFAMSSF52172; CheY_like; 1; .
PROSITEPS50110; RESPONSE_REGULATORY; 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