Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Isocitrate dehydrogenase [NADP]  

UniProtKB / Swiss-Prot ID :  IDH_ECOLI

Gene Name (Synonyms) : 
icd, icdA, icdE b1136, JW1122  

Species :  Escherichia coli (strain K12). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGERKISWMEIYT...
Predicted Secondary Structure CCCCCCCCCCCCEEEEECCCEECCCCCEEEEEECCCCCHHHHHHHHHHHHHHHHHHCCCCCEEEEEEEEC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
4Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-...)-MESKVVVP
-CCCCCCCC
26.24PupDB
Link
100N6-succinyllysine.RVAIKGPLT
CCEEEECCC
44.75UniProtKB
Link
113Phosphoserine.GGIRSLNVA
CCCHHHHHH
23.52UniProtKB
Link
142N6-acetyllysine.PSPVKHPEL
CCCCCCCCC
57.75UniProtKB
Link
242N6-succinyllysine.EGAFKDWGY
HHHHHHHHH
52.62UniProtKB
Link
273Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-...)PNTGKEIVI
CCCCCCEEE
42.08PupDB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation is a highly abundant and evolutionarily conservedmodification in Escherichia coli.";
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,Grishin N.V., Zhao Y.;
Mol. Cell. Proteomics 8:215-225(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND MASS SPECTROMETRY.
N6-succinyllysine
ReferencePubMed
"Identification of lysine succinylation as a new post-translationalmodification.";
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
Nat. Chem. Biol. 7:58-63(2011).
Cited for: CATALYTIC ACTIVITY, SUCCINYLATION AT LYS-100 AND LYS-242, ANDMUTAGENESIS OF LYS-100 AND LYS-242.
Phosphorylation
ReferencePubMed
"Regulation of an enzyme by phosphorylation at the active site.";
Hurley J.H., Dean A.M., Sohl J.L., Koshland D.E. Jr., Stroud R.M.;
Science 249:1012-1016(1990).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ISOCITRATE ANDMAGNESIUM, PHOSPHORYLATION AT SER-113, AND MUTAGENESIS OF SER-113.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures