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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: P69441




SWISS-2DPAGE:  P69441


P69441


General information about the entry
View entry in simple text format
Entry nameKAD_ECOLI
Primary accession numberP69441
Secondary accession number(s) P05082
integrated into SWISS-2DPAGE on August 1, 1995 (release 2)
2D Annotations were last modified onOctober 1, 2001 (version 3)
General Annotations were last modified on May 19, 2011 (version 10)
Name and origin of the protein
DescriptionRecName: Full=Adenylate kinase; Short=AK; EC=2.7.4.3; AltName: Full=ATP-AMP transphosphorylase;.
Gene nameName=adk
Synonyms=dnaW, plsA
OrderedLocusNames=b0474, JW0463
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
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)
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=5.49; Mw=28491
pI=5.60; Mw=22509

MAPPING (identification):
MICROSEQUENCE ANALYSIS [1] AND IDENTIFIED ON 2-D GELS BY VANBOGELEN [2].



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

MAP LOCATIONS:
pI=5.00; Mw=9979  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [3].



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=4.99; Mw=10074

MAPPING (identification):
MICROSEQUENCING (MRIIL) [3].



ECOLI5-6 {Escherichia coli(5-6)}
Escherichia coli
ECOLI5-6
  map experimental info
  protein estimated location
 
ECOLI5-6

MAP LOCATIONS:
pI=5.48; Mw=31661  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [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 license@isb-sib.ch).
Cross-references
ECO2DBASEF026.0; 6TH EDITION.
UniProtKB/Swiss-ProtP69441; KAD_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 nameKAD_ECOLI
Primary accession numberP69441
Secondary accession number(s) P05082 P77123 Q2MBV3
Sequence was last modified on August 13, 1987 (version 1)
Annotations were last modified on October 19, 2011 (version 76)
Name and origin of the protein
DescriptionRecName: Full=Adenylate kinase; Short=AK; EC=2.7.4.3; AltName: Full=ATP-AMP transphosphorylase;
Gene nameName=adk
Synonyms=dnaW, plsA
OrderedLocusNames=b0474, JW0463
Encoded onName=adk; Synonyms=dnaW, plsA; OrderedLocusNames=b0474, JW0463
Keywords3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; Transferase.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX03038; CAA26840.1; -; Genomic_DNA
EMBLU82664; AAB40228.1; ALT_INIT; Genomic_DNA
EMBLU00096; AAC73576.1; -; Genomic_DNA
EMBLAP009048; BAE76253.1; -; Genomic_DNA
EMBLM38777; AAA23461.1; -; Genomic_DNA
EMBLD90259; BAA14303.1; -; Genomic_DNA
PIRA24275; KIECA; .
RefSeqNP_415007.1; NC_000913.2; .
PDB1AKE; X-ray; 2.00 A; A/B=1-214
PDB1ANK; X-ray; 2.00 A; A/B=1-214
PDB1E4V; X-ray; 1.85 A; A/B=1-214
PDB1E4Y; X-ray; 1.85 A; A/B=1-214
PDB2ECK; X-ray; 2.80 A; A/B=1-214
PDB3HPQ; X-ray; 2.00 A; A/B=1-214
PDB3HPR; X-ray; 2.00 A; A/B=1-214
PDB4AKE; X-ray; 2.20 A; A/B=1-214
PDBsum1AKE; -; .
PDBsum1ANK; -; .
PDBsum1E4V; -; .
PDBsum1E4Y; -; .
PDBsum2ECK; -; .
PDBsum3HPQ; -; .
PDBsum3HPR; -; .
PDBsum4AKE; -; .
ProteinModelPortalP69441; -; .
SMRP69441; 1-214; .
DIPDIP-47903N; -; .
IntActP69441; 13; .
PhosSiteP69441; -; .
SWISS-2DPAGEP69441; -; .
ECO2DBASEF026.0; 6TH EDITION; .
GeneID945097; -; .
GenomeReviewsAP009048_GR; JW0463; .
GenomeReviewsU00096_GR; b0474; .
KEGGecj:JW0463; -; .
KEGGeco:b0474; -; .
EchoBASEEB0031; -; .
EcoGeneEG10032; adk; .
eggNOGCOG0563; -; .
GeneTreeEBGT00050000010912; -; .
HOGENOMHBG630208; -; .
OMACANGFLF; -; .
ProtClustDBPRK00279; -; .
BioCycEcoCyc:ADENYL-KIN-MONOMER; -; .
BioCycMetaCyc:ADENYL-KIN-MONOMER; -; .
DrugBankDB00131; Adenosine monophosphate; .
GenevestigatorP69441; -; .
GOGO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell; .
GOGO:0004017; F:adenylate kinase activity; IDA:EcoCyc; .
GOGO:0016208; F:AMP binding; IDA:EcoCyc; .
GOGO:0005524; F:ATP binding; IDA:EcoCyc; .
GOGO:0000287; F:magnesium ion binding; IDA:EcoCyc; .
GOGO:0009152; P:purine ribonucleotide biosynthetic process; IMP:EcoCyc; .
GOGO:0015951; P:purine ribonucleotide interconversion; IMP:EcoCyc; .
HAMAPMF_00235; Adenylate_kinase_Adk; 1; -
InterProIPR006259; Adenyl_kin_sub; .
InterProIPR000850; Adenylate_kin; .
InterProIPR007862; Adenylate_kinase_lid-dom; .
PANTHERPTHR23359; Adenylate_kin; 1; .
PfamPF00406; ADK; 1; .
PfamPF05191; ADK_lid; 1; .
PRINTSPR00094; ADENYLTKNASE; .
TIGRFAMsTIGR01351; Adk; 1; .
PROSITEPS00113; ADENYLATE_KINASE; 1; .



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