GO_REF:0000002
Gene Ontology annotation through association of InterPro records with GO terms
GO_REF:0000024
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
GO_REF:0000033
Annotation inferences using phylogenetic trees
GO_REF:0000044
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
GO_REF:0000052
Gene Ontology annotation based on curation of immunofluorescence data
GO_REF:0000107
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
GO_REF:0000116
Automatic Gene Ontology annotation based on Rhea mapping
GO_REF:0000117
Electronic Gene Ontology annotations created by ARBA machine learning models
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
PMID:16020546
Human acyl-CoA dehydrogenase-9 plays a novel role in the mitochondrial beta-oxidation of unsaturated fatty acids.
PMID:18063578
The layered structure of human mitochondrial DNA nucleoids.
PMID:18227065
Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase.
PMID:21237683
Identification and characterization of new long chain acyl-CoA dehydrogenases.
PMID:21492153
Analysis of proteomic changes induced upon cellular differentiation of the human intestinal cell line Caco-2.
PMID:32296183
A reference map of the human binary protein interactome.
PMID:34800366
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
PMID:7479827
Molecular basis of human mitochondrial very-long-chain acyl-CoA dehydrogenase deficiency causing cardiomyopathy and sudden death in childhood.
PMID:7668252
Cloning of human very-long-chain acyl-coenzyme A dehydrogenase and molecular characterization of its deficiency in two patients.
PMID:8466512
A novel disease with deficiency of mitochondrial very-long-chain acyl-CoA dehydrogenase.
PMID:9461620
Catalytic and FAD-binding residues of mitochondrial very long chain acyl-coenzyme A dehydrogenase.
PMID:9599005
Very-long-chain acyl-CoA dehydrogenase subunit assembles to the dimer form on mitochondrial inner membrane.
Reactome:R-HSA-1791069
Expression of ACADVL
Reactome:R-HSA-77299
palmitoyl-CoA+FAD => trans-Hexadec-2-enoyl-CoA+FADH2
PMID:15639194
Differential induction of genes in liver and brown adipose tissue regulated by peroxisome proliferator-activated receptor-alpha during fasting and cold exposure in acyl-CoA dehydrogenase-deficient mice.
file:human/ACADVL/ACADVL-uniprot.txt
UniProt record for human ACADVL (P49748)