Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3  

UniProtKB / Swiss-Prot ID :  NDUA3_BOVIN

Gene Name (Synonyms) : 
NDUFA3  

Species :  Bos taurus (Bovine). 

Subcellular Localization :  Mitochondrion inner membrane; Single-pass membrane protein. 

Protein Function :  Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. 

Transmembrane Topology (topPTM) : NDUA3_BOVIN 

Protein Sequence MAERVAAFLKNVWAKEPVLVASFAIAGLAVILPTLSPYTKYSLMINRATPYNYPVPLRDDGNMPDVPSHP...
Predicted Secondary Structure CHHHHHHHHHHHHCCCCCEEHHHHHHHHHHHHCCCCCCEEEEEEEECCCCCCCCCCCCCCCCCCCCCCCC...
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.---MAERVA
---CHHHHH
17.19UniProtKB
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
"Electrospray ionization mass spectrometric analysis of subunits ofNADH:ubiquinone oxidoreductase (complex I) from bovine heartmitochondria.";
Fearnley I.M., Skehel J.M., Walker J.E.;
Biochem. Soc. Trans. 22:551-555(1994).
Cited for: ACETYLATION AT ALA-2.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures