Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial  

UniProtKB / Swiss-Prot ID :  ACDSB_HUMAN

Gene Name (Synonyms) : 
ACADSB  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Mitochondrion matrix. 

Protein Function :  Has greatest activity toward short branched chain acyl- CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl- CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent. 

Protein Sequence MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDEEMMIKSSVKK...
Predicted Secondary Structure CHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHH...
Protein Variant
LocationDescription
13R -> K (in dbSNP:rs12263012). VAR_048177
209S -> G (in dbSNP:rs1799823). VAR_014749
255L -> F (in SBCADD). VAR_013010
316I -> V (in dbSNP:rs1131430). VAR_048178
376E -> G (in dbSNP:rs12357783). VAR_048179
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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
70Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SSVKKFAQE
HHHHHHHHH
43.72Phosphositeplus
Link
198PhosphotyrosineKEGDYYVLN
EECCEEEEE
13.31Phosphositeplus
Link
199PhosphotyrosineEGDYYVLNG
ECCEEEEEE
11.82Phosphositeplus
Link
284Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GHGYKYAIG
CCHHHHHHH
32.57Phosphositeplus
Link
284N6-acetyllysineGHGYKYAIG
CCHHHHHHH
32.57HPRD
Link
284N6-acetyllysineGHGYKYAIG
CCHHHHHHH
32.57Phosphositeplus
Link
284N6-acetyllysine.GHGYKYAIG
CCHHHHHHH
32.57UniProtKB
Link
413PhosphotyrosineIGTIYEGAS
CEEECCCCH
14.24Phosphositeplus
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
Kegg disease
OMIM disease
610006Short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD)
Drug Reference
DrugBank
DB00167L-Isoleucine
DB00313Valproic Acid
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-284, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures