HUMAN:ACOT8

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ACOT8 (synonyms: ACTEIII, PTE1, PTE2)
Protein Name(s)	Acyl-coenzyme A thioesterase 8 Acyl-CoA thioesterase 8 Choloyl-coenzyme A thioesterase HIV-Nef-associated acyl-CoA thioesterase PTE-2 Peroxisomal acyl-coenzyme A thioester hydrolase 1 PTE-1 Peroxisomal long-chain acyl-CoA thioesterase 1 Thioesterase II hACTE-III hACTEIII hTE
External Links
UniProt	O14734
EMBL	AF014404 X86032 AF124264 AL008726 BC117155 BC117157
CCDS	CCDS13378.1
PIR	JC5644
RefSeq	NP_005460.2
UniGene	Hs.444776
ProteinModelPortal	O14734
SMR	O14734
BioGrid	115323
IntAct	O14734
MINT	MINT-2998229
STRING	9606.ENSP00000217455
PhosphoSite	O14734
MaxQB	O14734
PaxDb	O14734
PRIDE	O14734
DNASU	10005
Ensembl	ENST00000217455
GeneID	10005
KEGG	hsa:10005
UCSC	uc002xqa.2
CTD	10005
GeneCards	GC20M044470
HGNC	HGNC:15919
HPA	CAB010261
MIM	608123
neXtProt	NX_O14734
PharmGKB	PA33941
eggNOG	COG1946
GeneTree	ENSGT00390000004207
HOGENOM	HOG000246495
HOVERGEN	HBG019167
InParanoid	O14734
KO	K11992
OMA	AKEVPIE
OrthoDB	EOG7VTDNQ
PhylomeDB	O14734
TreeFam	TF315124
BRENDA	3.1.2.2
Reactome	REACT_11041 REACT_121147 REACT_17017 REACT_17062
GeneWiki	ACOT8
GenomeRNAi	10005
NextBio	37789
PRO	PR:O14734
Proteomes	UP000005640
Bgee	O14734
CleanEx	HS_ACOT8
ExpressionAtlas	O14734
Genevestigator	O14734
GO	GO:0005739 GO:0005782 GO:0047617 GO:0052689 GO:0033882 GO:0052815 GO:0016290 GO:0005102 GO:0006637 GO:0036109 GO:0006699 GO:0008206 GO:0044255 GO:0043649 GO:0033540 GO:0016559 GO:0044281 GO:0033559 GO:0016032
Gene3D	3.10.129.10
InterPro	IPR003703 IPR029069
PANTHER	PTHR11066
SUPFAM	SSF54637
TIGRFAMs	TIGR00189

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0006637	acyl-CoA metabolic process	PMID:9153233^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045225	negative regulation of CD4 biosynthetic process	PMID:9153233^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
NOT\|enables	GO:0052816	long-chain acyl-CoA hydrolase activity	PMID:9153233^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0052815	medium-chain acyl-CoA hydrolase activity	PMID:9153233^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0052815	medium-chain acyl-CoA hydrolase activity	PMID:9299485^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0047617	acyl-CoA hydrolase activity	PMID:15194431^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0047617	acyl-CoA hydrolase activity	PMID:10092594^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0043649	dicarboxylic acid catabolic process	PMID:16141203^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016559	peroxisome fission	PMID:15194431^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016290	palmitoyl-CoA hydrolase activity	PMID:9299485^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006637	acyl-CoA metabolic process	PMID:9299485^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005782	peroxisomal matrix	PMID:14709540^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005782	peroxisomal matrix	PMID:10092594^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	PMID:20178365^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P50542	F	Seeded From UniProt	complete
enables	GO:0047617	acyl-CoA hydrolase activity	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10995 MGI:MGI:2158201 PANTHER:PTN000115911 SGD:S000003780 UniProtKB:O14734	F	Seeded From UniProt	complete
involved_in	GO:0009062	fatty acid catabolic process	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10995 PANTHER:PTN000115911	P	Seeded From UniProt	complete
involved_in	GO:0006637	acyl-CoA metabolic process	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2158201 PANTHER:PTN000115911 UniProtKB:O14734	P	Seeded From UniProt	complete
part_of	GO:0005782	peroxisomal matrix	PMID:21873635^[8]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000115913 UniProtKB:O14734	C	Seeded From UniProt	complete
enables	GO:0047617	acyl-CoA hydrolase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P58137 ensembl:ENSMUSP00000099383	F	Seeded From UniProt	complete
involved_in	GO:0006637	acyl-CoA metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P58137 ensembl:ENSMUSP00000099383	P	Seeded From UniProt	complete
part_of	GO:0005777	peroxisome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P58137 ensembl:ENSMUSP00000099383	C	Seeded From UniProt	complete
involved_in	GO:0006637	acyl-CoA metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003703	P	Seeded From UniProt	complete
enables	GO:0047617	acyl-CoA hydrolase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003703	F	Seeded From UniProt	complete
enables	GO:0033882	choloyl-CoA hydrolase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.2.27	F	Seeded From UniProt	complete
involved_in	GO:0036109	alpha-linolenic acid metabolic process	Reactome:R-HSA-2046106	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0033540	fatty acid beta-oxidation using acyl-CoA oxidase	Reactome:R-HSA-389887	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016289	CoA hydrolase activity	Reactome:R-HSA-193385	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006699	bile acid biosynthetic process	Reactome:R-HSA-193368	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006637	acyl-CoA metabolic process	Reactome:R-HSA-5690042	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006625	protein targeting to peroxisome	Reactome:R-HSA-9033241	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-9033236 Reactome:R-HSA-9033235	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005782	peroxisomal matrix	Reactome:R-HSA-9033235 Reactome:R-HSA-5690042 Reactome:R-HSA-390304 Reactome:R-HSA-2066779 Reactome:R-HSA-193385	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003986	acetyl-CoA hydrolase activity	Reactome:R-HSA-390304 Reactome:R-HSA-2066779	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P	Seeded From UniProt	complete
part_of	GO:0005777	peroxisome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0576	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
involved_in	GO:0007031	peroxisome organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0962	P	Seeded From UniProt	complete
enables	GO:0052689	carboxylic ester hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0719	F	Seeded From UniProt	complete
part_of	GO:0005782	peroxisomal matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0202	C	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 Liu, LX et al. (1997) Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J. Biol. Chem. 272 13779-85 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Watanabe, H et al. (1997) A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem. Biophys. Res. Commun. 238 234-9 PubMed GONUTS page
↑ ^3.0 ^3.1 Ishizuka, M et al. (2004) Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. Exp. Cell Res. 297 127-41 PubMed GONUTS page
↑ ^4.0 ^4.1 Jones, JM et al. (1999) Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J. Biol. Chem. 274 9216-23 PubMed GONUTS page
↑ Westin, MA et al. (2005) The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes. J. Biol. Chem. 280 38125-32 PubMed GONUTS page
↑ Jones, JM et al. (2004) PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins. J. Cell Biol. 164 57-67 PubMed GONUTS page
↑ Ghosh, D & Berg, JM (2010) A proteome-wide perspective on peroxisome targeting signal 1(PTS1)-Pex5p affinities. J. Am. Chem. Soc. 132 3973-9 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 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:9153233-1] 1.0 ^1.1 ^1.2 ^1.3 Liu, LX et al. (1997) Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J. Biol. Chem. 272 13779-85 PubMed GONUTS page

[PMID:9299485-2] 2.0 ^2.1 ^2.2 Watanabe, H et al. (1997) A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem. Biophys. Res. Commun. 238 234-9 PubMed GONUTS page

[PMID:15194431-3] 3.0 ^3.1 Ishizuka, M et al. (2004) Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. Exp. Cell Res. 297 127-41 PubMed GONUTS page

[PMID:10092594-4] 4.0 ^4.1 Jones, JM et al. (1999) Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J. Biol. Chem. 274 9216-23 PubMed GONUTS page

[PMID:16141203-5] Westin, MA et al. (2005) The identification of a succinyl-CoA thioesterase suggests a novel pathway for succinate production in peroxisomes. J. Biol. Chem. 280 38125-32 PubMed GONUTS page

[PMID:14709540-6] Jones, JM et al. (2004) PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins. J. Cell Biol. 164 57-67 PubMed GONUTS page

[PMID:20178365-7] Ghosh, D & Berg, JM (2010) A proteome-wide perspective on peroxisome targeting signal 1(PTS1)-Pex5p affinities. J. Am. Chem. Soc. 132 3973-9 PubMed GONUTS page

[PMID:21873635-8] 8.0 ^8.1 ^8.2 ^8.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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HUMAN:ACOT8

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