HUMAN:ACADS

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ACADS
Protein Name(s)	Short-chain specific acyl-CoA dehydrogenase, mitochondrial SCAD Butyryl-CoA dehydrogenase
External Links
UniProt	P16219
EMBL	M26393 Z80345 Z80347 U83992 U83991 BC025963
CCDS	CCDS9207.1
PIR	A30605
RefSeq	NP_000008.1 NP_001289483.1
PDB	2VIG
PDBsum	2VIG
SMR	P16219
BioGrid	106553
IntAct	P16219
MINT	P16219
STRING	9606.ENSP00000242592
DrugBank	DB03059 DB03147 DB00157
SwissLipids	SLP:000001403
iPTMnet	P16219
PhosphoSitePlus	P16219
BioMuta	ACADS
DMDM	113019
DOSAC-COBS-2DPAGE	P16219
SWISS-2DPAGE	P16219
UCD-2DPAGE	P16219
EPD	P16219
jPOST	P16219
MassIVE	P16219
MaxQB	P16219
PaxDb	P16219
PeptideAtlas	P16219
PRIDE	P16219
ProteomicsDB	53323
DNASU	35
Ensembl	ENST00000242592
GeneID	35
KEGG	hsa:35
UCSC	uc001tza.5
CTD	35
DisGeNET	35
GeneCards	ACADS
GeneReviews	ACADS
HGNC	HGNC:90
HPA	CAB019284 HPA004799 HPA022271
MalaCards	ACADS
MIM	201470 606885
neXtProt	NX_P16219
OpenTargets	ENSG00000122971
Orphanet	26792
PharmGKB	PA24426
eggNOG	KOG0139 COG1960
GeneTree	ENSGT00940000158866
HOGENOM	HOG000131659
InParanoid	P16219
KO	K00248
OMA	LYREAPM
OrthoDB	589058at2759
PhylomeDB	P16219
TreeFam	TF105019
BioCyc	MetaCyc:HS04619-MONOMER
Reactome	R-HSA-77350 R-HSA-77352
SABIO-RK	P16219
UniPathway	UPA00660
ChiTaRS	ACADS
EvolutionaryTrace	P16219
GenomeRNAi	35
Pharos	P16219
PRO	PR:P16219
Proteomes	UP000005640
Bgee	ENSG00000122971
ExpressionAtlas	P16219
Genevisible	P16219
GO	GO:0005759 GO:0005739 GO:0005654 GO:0005634 GO:0003995 GO:0004085 GO:0050660 GO:0046359 GO:0006635 GO:0033539
Gene3D	1.10.540.10
InterPro	IPR006089 IPR006091 IPR036250 IPR009075 IPR013786 IPR037069 IPR009100
Pfam	PF00441 PF02770 PF02771
SUPFAM	SSF47203 SSF56645
PROSITE	PS00072 PS00073

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes
involved_in	GO:0006635	fatty acid beta-oxidation	PMID:11134486^[1]	ECO:0000305	curator inference used in manual assertion	GO:0003995	P		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	PMID:11134486^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q3ZBF6	C		Seeded From UniProt
enables	GO:0004085	butyryl-CoA dehydrogenase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q3ZBF6	F		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q3ZBF6	F		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	PMID:3597357^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_in:(UBERON:0002107)	Seeded From UniProt
involved_in	GO:0033539	fatty acid beta-oxidation using acyl-CoA dehydrogenase	PMID:3597357^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(UBERON:0002107) has_input:(CHEBI:15536)\|occurs_in(UBERON:0002107) has_input:(CHEBI:15539)\|occurs_in(UBERON:0002107) has_input:(CHEBI:15517)\|occurs_in(UBERON:0002107) has_input:(CHEBI:27540)	Seeded From UniProt
part_of	GO:0005634	nucleus	PMID:21630459^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt
involved_in	GO:0046359	butyrate catabolic process	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000097838 RGD:620514	P		Seeded From UniProt
enables	GO:0004085	butyryl-CoA dehydrogenase activity	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000097838 RGD:620514	F		Seeded From UniProt
part_of	GO:0005739	mitochondrion	PMID:16729965^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
part_of	GO:0005813	centrosome	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
part_of	GO:0005739	mitochondrion	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006089	F		Seeded From UniProt
enables	GO:0016627	oxidoreductase activity, acting on the CH-CH group of donors	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006091 InterPro:IPR009075 InterPro:IPR009100 InterPro:IPR013786 InterPro:IPR036250 InterPro:IPR037069	F		Seeded From UniProt
enables	GO:0050660	flavin adenine dinucleotide binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013786 InterPro:IPR037069	F		Seeded From UniProt
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006089 InterPro:IPR006091 InterPro:IPR009075 InterPro:IPR009100 InterPro:IPR013786 InterPro:IPR036250 InterPro:IPR037069	P		Seeded From UniProt
enables	GO:0004085	butyryl-CoA dehydrogenase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.3.8.1	F		Seeded From UniProt
involved_in	GO:0006635	fatty acid beta-oxidation	PMID:8276399^[6] Reactome:R-HSA-77352 Reactome:R-HSA-77350	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	PMID:2565344^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt
part_of	GO:0005759	mitochondrial matrix	Reactome:R-HSA-77327 Reactome:R-HSA-77319	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt
involved_in	GO:0006631	fatty acid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0276	P		Seeded From UniProt
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P		Seeded From UniProt
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C		Seeded From UniProt
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P		Seeded From UniProt
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F		Seeded From UniProt
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0170	C		Seeded From UniProt
involved_in	GO:0006635	fatty acid beta-oxidation	PMID:11134486^[1]	ECO:0000305	curator inference used in manual assertion	GO:0003995	P		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	PMID:11134486^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q3ZBF6	C		Seeded From UniProt
enables	GO:0004085	butyryl-CoA dehydrogenase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q3ZBF6	F		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q3ZBF6	F		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	PMID:3597357^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_in:(UBERON:0002107)	Seeded From UniProt
involved_in	GO:0033539	fatty acid beta-oxidation using acyl-CoA dehydrogenase	PMID:3597357^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(UBERON:0002107) has_input:(CHEBI:15536)\|occurs_in(UBERON:0002107) has_input:(CHEBI:15539)\|occurs_in(UBERON:0002107) has_input:(CHEBI:15517)\|occurs_in(UBERON:0002107) has_input:(CHEBI:27540)	Seeded From UniProt
part_of	GO:0005634	nucleus	PMID:21630459^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt
involved_in	GO:0006635	fatty acid beta-oxidation	PMID:8276399^[6] Reactome:R-HSA-77352 Reactome:R-HSA-77350	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	PMID:2565344^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt
involved_in	GO:0046359	butyrate catabolic process	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000097838 RGD:620514	P		Seeded From UniProt
enables	GO:0004085	butyryl-CoA dehydrogenase activity	PMID:21873635^[4]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000097838 RGD:620514	F		Seeded From UniProt
involved_in	GO:0006635	fatty acid beta-oxidation	Reactome:R-HSA-77352	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt
involved_in	GO:0006635	fatty acid beta-oxidation	Reactome:R-HSA-77350	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt
part_of	GO:0005759	mitochondrial matrix	Reactome:R-HSA-77327 Reactome:R-HSA-77319	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt
part_of	GO:0005759	mitochondrial matrix	Reactome:R-HSA-77319	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt
part_of	GO:0005739	mitochondrion	PMID:16729965^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
part_of	GO:0005813	centrosome	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
part_of	GO:0005739	mitochondrion	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt
enables	GO:0003995	acyl-CoA dehydrogenase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006089	F		Seeded From UniProt
enables	GO:0016627	oxidoreductase activity, acting on the CH-CH group of donors	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006091 InterPro:IPR009075 InterPro:IPR009100 InterPro:IPR013786 InterPro:IPR036250 InterPro:IPR037069	F		Seeded From UniProt
enables	GO:0050660	flavin adenine dinucleotide binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013786 InterPro:IPR037069	F		Seeded From UniProt
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR006089 InterPro:IPR006091 InterPro:IPR009075 InterPro:IPR009100 InterPro:IPR013786 InterPro:IPR036250 InterPro:IPR037069	P		Seeded From UniProt
enables	GO:0004085	butyryl-CoA dehydrogenase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.3.8.1	F		Seeded From UniProt
involved_in	GO:0006631	fatty acid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0276	P		Seeded From UniProt
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P		Seeded From UniProt
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C		Seeded From UniProt
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	P		Seeded From UniProt
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F		Seeded From UniProt
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0170	C		Seeded From UniProt
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Corydon, MJ et al. (2001) Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr. Res. 49 18-23 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Finocchiaro, G et al. (1987) Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver. J. Biol. Chem. 262 7982-9 PubMed GONUTS page
↑ ^3.0 ^3.1 de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^5.0 ^5.1 Lamhonwah, AM & Tein, I (2006) Novel localization of OCTN1, an organic cation/carnitine transporter, to mammalian mitochondria. Biochem. Biophys. Res. Commun. 345 1315-25 PubMed GONUTS page
↑ ^6.0 ^6.1 Kelly, CL et al. (1993) Cloning and characterization of the mouse short-chain acyl-CoA dehydrogenase cDNA. Genomics 18 137-40 PubMed GONUTS page
↑ ^7.0 ^7.1 Naito, E et al. (1989) Molecular cloning and nucleotide sequence of complementary DNAs encoding human short chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short chain acyl-coenzyme A dehydrogenase deficiency. J. Clin. Invest. 83 1605-13 PubMed GONUTS page

[PMID:11134486-1] 1.0 ^1.1 ^1.2 ^1.3 Corydon, MJ et al. (2001) Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr. Res. 49 18-23 PubMed GONUTS page

[PMID:3597357-2] 2.0 ^2.1 ^2.2 ^2.3 Finocchiaro, G et al. (1987) Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver. J. Biol. Chem. 262 7982-9 PubMed GONUTS page

[PMID:21630459-3] 3.0 ^3.1 de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page

[PMID:21873635-4] 4.0 ^4.1 ^4.2 ^4.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:16729965-5] 5.0 ^5.1 Lamhonwah, AM & Tein, I (2006) Novel localization of OCTN1, an organic cation/carnitine transporter, to mammalian mitochondria. Biochem. Biophys. Res. Commun. 345 1315-25 PubMed GONUTS page

[PMID:8276399-6] 6.0 ^6.1 Kelly, CL et al. (1993) Cloning and characterization of the mouse short-chain acyl-CoA dehydrogenase cDNA. Genomics 18 137-40 PubMed GONUTS page

[PMID:2565344-7] 7.0 ^7.1 Naito, E et al. (1989) Molecular cloning and nucleotide sequence of complementary DNAs encoding human short chain acyl-coenzyme A dehydrogenase and the study of the molecular basis of human short chain acyl-coenzyme A dehydrogenase deficiency. J. Clin. Invest. 83 1605-13 PubMed GONUTS page

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HUMAN:ACADS

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Annotations

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References

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