Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  N(G),N(G)-dimethylarginine dimethylaminohydrolase 1  

UniProtKB / Swiss-Prot ID :  DDAH1_BOVIN

Gene Name (Synonyms) : 
DDAH1  

Species :  Bos taurus (Bovine). 

Subcellular Localization :   

Protein Function :  Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation. 

Protein Sequence MASLGHPATFGRATHVVVRALPESLAQQALRRTKGDEVDFARAERQHQLYVGVLGSKLGLQVVQLPADES...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCHHHHHHHHHHHHHHHHHHCCCEEEEECCCCC...
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
2N-acetylalanine.---MASLGH
---CCCCCC
17.29UniProtKB
Link-
222S-nitrosocysteineTAANCIYLN
HHHHHHHHC
1.53dbSNO
Link
222S-nitrosocysteine.TAANCIYLN
HHHHHHHHC
1.53UniProtKB
Link
274S-nitrosocysteineGLLTCSSVL
CCCEEEEEE
2.62dbSNO
Link
274S-nitrosocysteine.GLLTCSSVL
CCCEEEEEE
2.62UniProtKB
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
"Zn(II)-free dimethylargininase-1 (DDAH-1) is inhibited upon specificCysS-nitrosylation.";
Knipp M., Braun O., Gehrig P.M., Sack R., Vasak M.;
J. Biol. Chem. 278:3410-3416(2003).
Cited for: PROTEIN SEQUENCE OF 2-285, MASS SPECTROMETRY, ACETYLATION AT ALA-2,S-NITROSYLATION AT CYS-222 AND CYS-274, ENZYME REGULATION, AND3D-STRUCTURE MODELING.
S-nitrosylation
ReferencePubMed
"Zn(II)-free dimethylargininase-1 (DDAH-1) is inhibited upon specificCysS-nitrosylation.";
Knipp M., Braun O., Gehrig P.M., Sack R., Vasak M.;
J. Biol. Chem. 278:3410-3416(2003).
Cited for: PROTEIN SEQUENCE OF 2-285, MASS SPECTROMETRY, ACETYLATION AT ALA-2,S-NITROSYLATION AT CYS-222 AND CYS-274, ENZYME REGULATION, AND3D-STRUCTURE MODELING.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures