Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Glyceraldehyde-3-phosphate dehydrogenase A  

UniProtKB / Swiss-Prot ID :  G3P1_ECOLI

Gene Name (Synonyms) : 
gapA b1779, JW1768  

Species :  Escherichia coli (strain K12). 

Subcellular Localization :  Cytoplasm. 

Protein Function :   

Protein Sequence MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGK...
Predicted Secondary Structure CEEEEEEECCCCHHHHHHHHHHHCCCEEEEEEECCCCHHHHHHHHHHHCCCCCCCCEEEECCCEEEECCC...
Protein Variant
LocationDescription
43Y -> I (in strain: ECOR 70).
266G -> D (in strain: E830587).
267E -> A (in strain: E2666-74).
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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
Protein Variant
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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
115N6-succinyllysine.TAGAKKVVM
HCCCCEEEE
45.22UniProtKB
Link
124N6-succinyllysine.TGPSKDNTP
CCCCCCCCC
59.12UniProtKB
Link
132N6-acetyllysine; alternate.PMFVKGANF
CEEEEECCH
40.83UniProtKB
Link
132N6-succinyllysine; alternate.PMFVKGANF
CEEEEECCH
40.83UniProtKB
Link
138N6-acetyllysine.ANFDKYAGQ
CCHHHHCCC
32.63UniProtKB
Link
192N6-acetyllysine; alternate.GPSHKDWRG
CCCCCCCCC
64.42UniProtKB
Link
192N6-succinyllysine; alternate.GPSHKDWRG
CCCCCCCCC
64.42UniProtKB
Link
213N6-succinyllysine.TGAAKAVGK
CCCHHHHHH
42.97UniProtKB
Link
217N6-succinyllysine.KAVGKVLPE
HHHHHHCCC
33.72UniProtKB
Link
225N6-succinyllysine.ELNGKLTGM
CCCCCEEEE
41.63UniProtKB
Link
249Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-...)VRLEKAATY
EEECCCCCH
48.16PupDB
Link
249N6-acetyllysine.VRLEKAATY
EEECCCCCH
48.16UniProtKB
Link
249N6-succinyllysine.VRLEKAATY
EEECCCCCH
48.16UniProtKB
Link
257N6-succinyllysine.YEQIKAAVK
HHHHHHHHH
29.95UniProtKB
Link
261N6-succinyllysine.KAAVKAAAE
HHHHHHHHC
27.81UniProtKB
Link
331N6-malonyllysine; alternate.AHISK
HHHCC
64.85UniProtKB
Link
331N6-succinyllysine; alternate.AHISK
HHHCC
64.85UniProtKB
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-132; LYS-138; LYS-192 ANDLYS-249, AND MASS SPECTROMETRY.
N6-malonyllysine
ReferencePubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme.";
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.;
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
Cited for: MALONYLATION AT LYS-331.
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: SUCCINYLATION AT LYS-115; LYS-124; LYS-132; LYS-192; LYS-213; LYS-217;LYS-225; LYS-249; LYS-257; LYS-261 AND LYS-331.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures