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Sample Preparation and Post-separation Analysis

Searching in 'SWISS-2DPAGE' for entry matching: P0A9Q9



General information about the entry
View entry in simple text format
Entry nameDHAS_ECOLI
Primary accession numberP0A9Q9
Secondary accession number(s) P00353
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 November 9, 2011 (version 10)
Name and origin of the protein
DescriptionRecName: Full=Aspartate-semialdehyde dehydrogenase; Short=ASA dehydrogenase; Short=ASADH; EC=; AltName: Full=Aspartate-beta-semialdehyde dehydrogenase;.
Gene nameName=asd
OrderedLocusNames=b3433, JW3396
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
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

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

pI=5.20; Mw=50339  [identification data]

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

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 or send email from
2DBase-EcoliP0A9Q9; DHAS_ECOLI.
UniProtKB/Swiss-ProtP0A9Q9; DHAS_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 nameDHAS_ECOLI
Primary accession numberP0A9Q9
Secondary accession number(s) P00353 Q2M797
Sequence was last modified on July 21, 1986 (version 1)
Annotations were last modified on October 19, 2011 (version 65)
Name and origin of the protein
DescriptionRecName: Full=Aspartate-semialdehyde dehydrogenase; Short=ASA dehydrogenase; Short=ASADH; EC=; AltName: Full=Aspartate-beta-semialdehyde dehydrogenase;
Gene nameName=asd
OrderedLocusNames=b3433, JW3396
Encoded onName=asd; Synonyms=hom; OrderedLocusNames=b3433, JW3396
Keywords3D-structure; Amino-acid biosynthesis; Complete proteome; Diaminopimelate biosynthesis; Direct protein sequencing; Lysine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome; Threonine biosynthesis.
Copyrighted by the UniProt Consortium, see Distributed under the Creative Commons Attribution-NoDerivs License
EMBLV00262; CAA23511.1; -; Genomic_DNA
EMBLU18997; AAA58231.1; -; Genomic_DNA
EMBLU00096; AAC76458.1; -; Genomic_DNA
EMBLAP009048; BAE77859.1; -; Genomic_DNA
PIRA00364; DEECDA; .
RefSeqNP_417891.1; NC_000913.2; .
PDB1BRM; X-ray; 2.50 A; A/B/C=1-367
PDB1GL3; X-ray; 2.60 A; A/B=1-367
PDB1T4B; X-ray; 1.60 A; A/B=1-367
PDB1T4D; X-ray; 1.95 A; A/B/C=1-367
PDBsum1BRM; -; .
PDBsum1GL3; -; .
PDBsum1T4B; -; .
PDBsum1T4D; -; .
ProteinModelPortalP0A9Q9; -; .
SMRP0A9Q9; 1-367; .
IntActP0A9Q9; 1; .
PhosSiteP0A9Q9; -; .
2DBase-EcoliP0A9Q9; -; .
EnsemblBacteriaEBESCT00000001309; EBESCP00000001309; EBESCG00000001084; .
EnsemblBacteriaEBESCT00000015935; EBESCP00000015226; EBESCG00000014995; .
GeneID947939; -; .
GenomeReviewsAP009048_GR; JW3396; .
GenomeReviewsU00096_GR; b3433; .
KEGGecj:JW3396; -; .
KEGGeco:b3433; -; .
EchoBASEEB0086; -; .
EcoGeneEG10088; asd; .
eggNOGCOG0136; -; .
GeneTreeEBGT00050000010426; -; .
HOGENOMHBG289760; -; .
ProtClustDBPRK06598; -; .
GenevestigatorP0A9Q9; -; .
GOGO:0005737; C:cytoplasm; IEA:InterPro; .
GOGO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:EC; .
GOGO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro; .
GOGO:0051287; F:NAD binding; IEA:InterPro; .
GOGO:0050661; F:NADP binding; IEA:InterPro; .
GOGO:0046983; F:protein dimerization activity; IEA:InterPro; .
GOGO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW; .
GOGO:0009097; P:isoleucine biosynthetic process; IEA:InterPro; .
GOGO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW; .
GOGO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-KW; .
HAMAPMF_02121; ASADH; 1; -
InterProIPR000319; Asp-semialdehyde_DH_CS; .
InterProIPR011534; Asp_ADH_proteob; .
InterProIPR012080; Asp_semialdehyde_DH; .
InterProIPR016040; NAD(P)-bd_dom; .
InterProIPR000534; Semialdehyde_DH_NAD-bd; .
InterProIPR012280; Semialdhyde_DH_dimer_dom; .
Gene3DG3DSA:; NAD(P)-bd; 1; .
PfamPF01118; Semialdhyde_dh; 1; .
PfamPF02774; Semialdhyde_dhC; 1; .
PIRSFPIRSF000148; ASA_dh; 1; .
SMARTSM00859; Semialdhyde_dh; 1; .
TIGRFAMsTIGR01745; Asd_gamma; 1; .
PROSITEPS01103; ASD; 1; .


SWISS-2DPAGE (search AC)

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