ACOT7

Functionⁱ

Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:10578051).

Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 (PubMed:10578051).

May play an important physiological function in brain (PubMed:10578051).

1 Publication

Catalytic activityⁱ

H₂O
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+
hexadecanoyl-CoA
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=
CoA
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+
H⁺
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+
hexadecanoate
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1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
EC:
3.1.2.2
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
This reaction proceeds in the
forward
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See the description of this reaction in Rhea.
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
direction.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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H₂O
+
hexadecanoyl-CoA
zoom
=
CoA
+
H⁺
+
hexadecanoate
zoom
H₂O
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+
octanoyl-CoA
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=
CoA
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+
H⁺
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+
octanoate
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1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
This reaction proceeds in the
forward
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See the description of this reaction in Rhea.
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
direction.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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H₂O
+
octanoyl-CoA
zoom
=
CoA
+
H⁺
+
octanoate
zoom
dodecanoyl-CoA
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See the description of this molecule in ChEBI.
+
H₂O
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=
CoA
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+
dodecanoate
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+
H⁺
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See the description of this molecule in ChEBI.
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
This reaction proceeds in the
forward
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See the description of this reaction in Rhea.
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
direction.
Source:
Rhea
Search for this reaction in UniProtKB.
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dodecanoyl-CoA
zoom
+
H₂O
=
CoA
+
dodecanoate
zoom
+
H⁺
(9Z)-octadecenoyl-CoA
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+
H₂O
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=
(9Z)-octadecenoate
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+
CoA
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+
H⁺
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1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
This reaction proceeds in the
forward
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.
direction.
Source:
Rhea
Search for this reaction in UniProtKB.
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(9Z)-octadecenoyl-CoA
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+
H₂O
=
(9Z)-octadecenoate
zoom
+
CoA
+
H⁺
H₂O
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+
tetradecanoyl-CoA
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=
CoA
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+
H⁺
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+
tetradecanoate
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By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:Q64559 (BACH_RAT)
This reaction proceeds in the
forward
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See the description of this reaction in Rhea.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:Q64559 (BACH_RAT)
direction.
Source:
Rhea
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H₂O
+
tetradecanoyl-CoA
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=
CoA
+
H⁺
+
tetradecanoate
zoom
decanoyl-CoA
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+
H₂O
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=
CoA
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+
decanoate
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+
H⁺
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By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:Q64559 (BACH_RAT)
This reaction proceeds in the
forward
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:Q64559 (BACH_RAT)
direction.
Source:
Rhea
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See the description of this reaction in Rhea.
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decanoyl-CoA
zoom
+
H₂O
=
CoA
+
decanoate
zoom
+
H⁺
H₂O
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+
octadecanoyl-CoA
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=
CoA
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+
H⁺
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+
octadecanoate
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By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:Q64559 (BACH_RAT)
This reaction proceeds in the
forward
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:Q64559 (BACH_RAT)
direction.
Source:
Rhea
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H₂O
+
octadecanoyl-CoA
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=
CoA
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H⁺
+
octadecanoate
zoom

Pathwayⁱ: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	66	By similarity		1
Active siteⁱ	255	By similarity		1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Serine esterase
Biological process	Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS01875-MONOMER
BRENDAⁱ	3.1.2.2, 2681 3.1.2.20, 2681
PathwayCommonsⁱ	O00154
Reactomeⁱ	R-HSA-77289, Mitochondrial Fatty Acid Beta-Oxidation
SABIO-RKⁱ	O00154
UniPathwayⁱ	UPA00199

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cytosolic acyl coenzyme A thioester hydrolase (EC:3.1.2.21 Publication) Alternative name(s): Acyl-CoA thioesterase 7 Brain acyl-CoA hydrolase Short name: BACH Short name: hBACH1 Publication CTE-IIa Short name: CTE-II Long chain acyl-CoA thioester hydrolase
Gene namesⁱ	Name:ACOT7 Synonyms:BACH
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:24157, ACOT7
MIMⁱ	602587, gene
neXtProtⁱ	NX_O00154
VEuPathDBⁱ	HostDB:ENSG00000097021

Keywords - Cellular componentⁱ

Cytoplasm, Mitochondrion

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	11332
Open Targets More...OpenTargetsⁱ	ENSG00000097021
PharmGKBⁱ	PA142672655

Miscellaneous databases

Pharosⁱ	O00154, Tbio

Pharosⁱ

O00154, Tbio

Genetic variation databases

BioMutaⁱ	ACOT7

BioMutaⁱ

ACOT7

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000053806	1 – 380	Cytosolic acyl coenzyme A thioester hydrolaseAdd BLAST		380

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	168	N6-acetyllysineCombined sources	1
Modified residueⁱ	198	N6-acetyllysineCombined sources	1
Modified residueⁱ	283	N6-acetyllysineCombined sources	1

Keywords - PTMⁱ

Acetylation

Proteomic databases

The CPTAC Assay portal More...CPTACⁱ	CPTAC-303 CPTAC-304
EPDⁱ	O00154
jPOSTⁱ	O00154
MassIVEⁱ	O00154
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O00154
PaxDbⁱ	O00154
PeptideAtlas More...PeptideAtlasⁱ	O00154
PRIDEⁱ	O00154
ProteomicsDBⁱ	47737 [O00154-1] 47738 [O00154-2] 47739 [O00154-3] 47740 [O00154-4] 47741 [O00154-5] 47742 [O00154-6]
TopDownProteomicsⁱ	O00154-1 [O00154-1]

2D gel databases

UCD-2DPAGEⁱ	O00154

UCD-2DPAGEⁱ

O00154

PTM databases

GlyGenⁱ	O00154, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	O00154
MetOSiteⁱ	O00154
PhosphoSitePlusⁱ	O00154
SwissPalmⁱ	O00154

Expressionⁱ

Tissue specificityⁱ

Isoform 4 is expressed exclusively in brain.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000097021, Expressed in prefrontal cortex and 218 other tissues
ExpressionAtlasⁱ	O00154, baseline and differential
Genevisibleⁱ	O00154, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000097021, Tissue enhanced (brain)

HPAⁱ

ENSG00000097021, Tissue enhanced (brain)

Interactionⁱ

Subunit structureⁱ

Homohexamer.

By similarity

Binary interactionsⁱ

Hide details

O00154

With	#Exp.	IntAct
ANK2 [Q01484]	2	EBI-948905,EBI-941975
CAMK2B [Q13554]	3	EBI-948905,EBI-1058722
CHD8 [Q9HCK8]	2	EBI-948905,EBI-1169146
CUL3 [Q13618]	2	EBI-948905,EBI-456129
FMR1 [Q06787]	2	EBI-948905,EBI-366305
HEL-S-101 [V9HW27]	3	EBI-948905,EBI-10178933
MAGEA6 [P43360]	3	EBI-948905,EBI-1045155
THAP1 [Q9NVV9]	3	EBI-948905,EBI-741515
UBQLN1 [Q9UMX0]	3	EBI-948905,EBI-741480
UBQLN1 - isoform 2 [Q9UMX0-2]	3	EBI-948905,EBI-10173939

Isoform 4 [O00154-4]

With	#Exp.	IntAct
ACOT12 [Q8WYK0]	3	EBI-12007918,EBI-11954993
BAG4 [O95429]	3	EBI-12007918,EBI-2949658
CAMK2B - isoform 2 [Q13554-3]	3	EBI-12007918,EBI-11523526
DAZAP2 [Q15038]	3	EBI-12007918,EBI-724310
DCTD [P32321]	3	EBI-12007918,EBI-739870
ENKD1 [Q9H0I2]	3	EBI-12007918,EBI-744099
MAGEA3 [P43357]	3	EBI-12007918,EBI-5651459
MAGEA6 [P43360]	3	EBI-12007918,EBI-1045155
POU6F1 [Q14863]	3	EBI-12007918,EBI-18138148
SPATC1L - isoform 2 [Q9H0A9-2]	3	EBI-12007918,EBI-11995806
THAP1 [Q9NVV9]	3	EBI-12007918,EBI-741515
UBQLN1 [Q9UMX0]	3	EBI-12007918,EBI-741480
UBQLN2 [Q9UHD9]	3	EBI-12007918,EBI-947187
UBXN1 - isoform 2 [Q04323-2]	3	EBI-12007918,EBI-11530712
ZNF438 [Q7Z4V0]	3	EBI-12007918,EBI-11962468

GO - Molecular functionⁱ

protein homodimerization activity
Source: BHF-UCL
Inferred from physical interactionⁱ
- Ref.1
  "Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase."
  Yamada J., Kurata A., Hirata M., Taniguchi T., Takama H., Furihata T., Shiratori K., Iida N., Takagi-Sakuma M., Watanabe T., Kurosaki K., Endo T., Suga T.
  J. Biochem. 126:1013-1019(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY.

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	116460, 81 interactors
IntActⁱ	O00154, 52 interactors
Molecular INTeraction database More...MINTⁱ	O00154
STRINGⁱ	9606.ENSP00000367086

Miscellaneous databases

RNActⁱ	O00154, protein

RNActⁱ

O00154, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	223 – 226	Combined sources	4
Beta strandⁱ	228 – 233	Combined sources	6
Helixⁱ	236 – 238	Combined sources	3
Beta strandⁱ	241 – 245	Combined sources	5
Helixⁱ	247 – 266	Combined sources	20
Beta strandⁱ	267 – 280	Combined sources	14
Beta strandⁱ	288 – 299	Combined sources	12
Beta strandⁱ	301 – 314	Combined sources	14
Beta strandⁱ	323 – 335	Combined sources	13
Helixⁱ	352 – 371	Combined sources	20

Show more details

3D structure databases

SMRⁱ	O00154
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	O00154

EvolutionaryTraceⁱ

O00154

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	50 – 168	HotDog ACOT-type 1PROSITE-ProRule annotationAdd BLAST		119
Domainⁱ	224 – 338	HotDog ACOT-type 2PROSITE-ProRule annotationAdd BLAST		115

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	350 – 380	DisorderedSequence analysisAdd BLAST		31

Domainⁱ

Both HotDog ACOT-type hydrolase domains are required for efficient activity.By similarity

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG2763, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155229
HOGENOMⁱ	CLU_050164_0_0_1
InParanoidⁱ	O00154
OMAⁱ	PTDVNWG
Database of Orthologous Groups More...OrthoDBⁱ	1069806at2759
PhylomeDBⁱ	O00154
TreeFamⁱ	TF329579

Family and domain databases

InterProⁱ	View protein in InterPro IPR040170, Cytosol_ACT IPR033120, HOTDOG_ACOT IPR029069, HotDog_dom_sf IPR006683, Thioestr_dom
PANTHERⁱ	PTHR11049, PTHR11049, 2 hits
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03061, 4HBT, 2 hits
SUPFAMⁱ	SSF54637, SSF54637, 2 hits
PROSITEⁱ	View protein in PROSITE PS51770, HOTDOG_ACOT, 2 hits

Sequences (7+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 7 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 7 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

Isoform 1 (identifier: O00154-1) [UniParc]FASTA Add to basket

Also known as: B, HBACHb

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

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MKLLARALRL CEFGRQASSR RLVAGQGCVG PRRGCCAPVQ VVGPRADLPP 
        60         70         80         90        100
CGACITGRIM RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC 
       110        120        130        140        150
VAALARVERT DFLSPMCIGE VAHVSAEITY TSKHSVEVQV NVMSENILTG 
       160        170        180        190        200
AKKLTNKATL WYVPLSLKNV DKVLEVPPVV YSRQEQEEEG RKRYEAQKLE 
       210        220        230        240        250
RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT LHGFVHGGVT 
       260        270        280        290        300
MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS 
       310        320        330        340        350
NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE 
       360        370        380
TEDEKKRFEE GKGRYLQMKA KRQGHAEPQP

Length:380

Mass (Da):41,796

Last modified:February 12, 2003 - v3

Checksum:ⁱBDD75D62A60095BC

GO

Isoform 2 (identifier: O00154-2) [UniParc]FASTA Add to basket

Also known as: A-X, hBACHa-X

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITG → MSGPDVETPSAIQIC
     287-288: GC → AP
     289-380: Missing.

« Hide

        10         20         30         40         50
MSGPDVETPS AIQICRIMRP DDANVAGNVH GGTILKMIEE AGAIISTRHC 
        60         70         80         90        100
NSQNGERCVA ALARVERTDF LSPMCIGEVA HVSAEITYTS KHSVEVQVNV 
       110        120        130        140        150
MSENILTGAK KLTNKATLWY VPLSLKNVDK VLEVPPVVYS RQEQEEEGRK 
       160        170        180        190        200
RYEAQKLERM ETKWRNGDIV QPVLNPEPNT VSYSQSSLIH LVGPSDCTLH 
       210        220        230        240 
GFVHGGVTMK LMDEVAGIVA ARHCKTNIVT ASVDAINFHD KIRKAP

Show »

Length:246

Mass (Da):27,041

Checksum:ⁱ4CDCAD44CE427904

GO

Isoform 3 (identifier: O00154-3) [UniParc]FASTA Add to basket

Also known as: A-Xi, hBACHa-Xi

The sequence of this isoform differs from the canonical sequence as follows:
1-57: MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITG → MSGPDVETPSAIQIC
287-380: GCVITISGRM...KRQGHAEPQP → AHVMPAGADH...HLGTHDLHEQ

« Hide

        10         20         30         40         50
MSGPDVETPS AIQICRIMRP DDANVAGNVH GGTILKMIEE AGAIISTRHC 
        60         70         80         90        100
NSQNGERCVA ALARVERTDF LSPMCIGEVA HVSAEITYTS KHSVEVQVNV 
       110        120        130        140        150
MSENILTGAK KLTNKATLWY VPLSLKNVDK VLEVPPVVYS RQEQEEEGRK 
       160        170        180        190        200
RYEAQKLERM ETKWRNGDIV QPVLNPEPNT VSYSQSSLIH LVGPSDCTLH 
       210        220        230        240        250
GFVHGGVTMK LMDEVAGIVA ARHCKTNIVT ASVDAINFHD KIRKAHVMPA 
       260        270        280 
GADHTAPSSS PSTGTKCSLL RHHHLGTHDL HEQ

Show »

Length:283

Mass (Da):30,977

Checksum:ⁱC21B4544638BA031

GO

Isoform 4 (identifier: O00154-4) [UniParc]FASTA Add to basket

Also known as: A, hBACHa

The sequence of this isoform differs from the canonical sequence as follows:
1-57: MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITG → MSGPDVETPSAIQIC

« Hide

        10         20         30         40         50
MSGPDVETPS AIQICRIMRP DDANVAGNVH GGTILKMIEE AGAIISTRHC 
        60         70         80         90        100
NSQNGERCVA ALARVERTDF LSPMCIGEVA HVSAEITYTS KHSVEVQVNV 
       110        120        130        140        150
MSENILTGAK KLTNKATLWY VPLSLKNVDK VLEVPPVVYS RQEQEEEGRK 
       160        170        180        190        200
RYEAQKLERM ETKWRNGDIV QPVLNPEPNT VSYSQSSLIH LVGPSDCTLH 
       210        220        230        240        250
GFVHGGVTMK LMDEVAGIVA ARHCKTNIVT ASVDAINFHD KIRKGCVITI 
       260        270        280        290        300
SGRMTFTSNK SMEIEVLVDA DPVVDSSQKR YRAASAFFTY VSLSQEGRSL 
       310        320        330 
PVPQLVPETE DEKKRFEEGK GRYLQMKAKR QGHAEPQP

Note: Major isoform.Curated

Show »

Length:338

Mass (Da):37,420

Checksum:ⁱ95E4CB4B0A7AF34C

GO

Isoform 5 (identifier: O00154-5) [UniParc]FASTA Add to basket

Also known as: C, hBACHc

The sequence of this isoform differs from the canonical sequence as follows:
1-58: MKLLARALRL...PPCGACITGR → MLLLRRSLSLNVLRKEVDRACFGEKAKQ

« Hide

        10         20         30         40         50
MLLLRRSLSL NVLRKEVDRA CFGEKAKQIM RPDDANVAGN VHGGTILKMI 
        60         70         80         90        100
EEAGAIISTR HCNSQNGERC VAALARVERT DFLSPMCIGE VAHVSAEITY 
       110        120        130        140        150
TSKHSVEVQV NVMSENILTG AKKLTNKATL WYVPLSLKNV DKVLEVPPVV 
       160        170        180        190        200
YSRQEQEEEG RKRYEAQKLE RMETKWRNGD IVQPVLNPEP NTVSYSQSSL 
       210        220        230        240        250
IHLVGPSDCT LHGFVHGGVT MKLMDEVAGI VAARHCKTNI VTASVDAINF 
       260        270        280        290        300
HDKIRKGCVI TISGRMTFTS NKSMEIEVLV DADPVVDSSQ KRYRAASAFF 
       310        320        330        340        350
TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE GKGRYLQMKA KRQGHAEPQP

Show »

Length:350

Mass (Da):38,991

Checksum:ⁱD8FA42B2583051BA

GO

Isoform 6 (identifier: O00154-6) [UniParc]FASTA Add to basket

Also known as: D, hBACHd

The sequence of this isoform differs from the canonical sequence as follows:
1-57: MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITG → MAFQLS

« Hide

        10         20         30         40         50
MAFQLSRIMR PDDANVAGNV HGGTILKMIE EAGAIISTRH CNSQNGERCV 
        60         70         80         90        100
AALARVERTD FLSPMCIGEV AHVSAEITYT SKHSVEVQVN VMSENILTGA 
       110        120        130        140        150
KKLTNKATLW YVPLSLKNVD KVLEVPPVVY SRQEQEEEGR KRYEAQKLER 
       160        170        180        190        200
METKWRNGDI VQPVLNPEPN TVSYSQSSLI HLVGPSDCTL HGFVHGGVTM 
       210        220        230        240        250
KLMDEVAGIV AARHCKTNIV TASVDAINFH DKIRKGCVIT ISGRMTFTSN 
       260        270        280        290        300
KSMEIEVLVD ADPVVDSSQK RYRAASAFFT YVSLSQEGRS LPVPQLVPET 
       310        320 
EDEKKRFEEG KGRYLQMKAK RQGHAEPQP

Show »

Length:329

Mass (Da):36,568

Checksum:ⁱECEB0F657ADF6E25

GO

Isoform 7 (identifier: O00154-7) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-57: MKLLARALRL...LPPCGACITG → MARPGLIHSA...VETPSAIQIC

« Hide

        10         20         30         40         50
MARPGLIHSA PGLPDTCALL QPPAASAAAA PSMSGPDVET PSAIQICRIM 
        60         70         80         90        100
RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC VAALARVERT 
       110        120        130        140        150
DFLSPMCIGE VAHVSAEITY TSKHSVEVQV NVMSENILTG AKKLTNKATL 
       160        170        180        190        200
WYVPLSLKNV DKVLEVPPVV YSRQEQEEEG RKRYEAQKLE RMETKWRNGD 
       210        220        230        240        250
IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT LHGFVHGGVT MKLMDEVAGI 
       260        270        280        290        300
VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS NKSMEIEVLV 
       310        320        330        340        350
DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE 
       360        370
GKGRYLQMKA KRQGHAEPQP

Show »

Length:370

Mass (Da):40,455

Checksum:ⁱ28F0088FFF813417

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	K7EKP8	K7EKP8_HUMAN		Cytosolic acyl coenzyme A thioester... Cytosolic acyl coenzyme A thioester hydrolase	ACOT7	279	Annotation score:

Sequence cautionⁱ

The sequence AAB61211 differs from that shown. Reason: Frameshift.Curated

The sequence AAH17365 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	82	E → G in BAG51874 (PubMed:14702039).Curated	1
Sequence conflictⁱ	371 – 372	KR → DD in AAB61211 (Ref. 3) Curated	2
Sequence conflictⁱ	377 – 378	EP → DA in AAB61211 (Ref. 3) Curated	2

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_000151	1 – 58	MKLLA…CITGR → MLLLRRSLSLNVLRKEVDRA CFGEKAKQ in isoform 5. 2 PublicationsAdd BLAST	58
Alternative sequenceⁱVSP_000152	1 – 57	MKLLA…ACITG → MSGPDVETPSAIQIC in isoform 2, isoform 3 and isoform 4. 6 PublicationsAdd BLAST	57
Alternative sequenceⁱVSP_000153	1 – 57	MKLLA…ACITG → MAFQLS in isoform 6. 2 PublicationsAdd BLAST	57
Alternative sequenceⁱVSP_047094	1 – 57	MKLLA…ACITG → MARPGLIHSAPGLPDTCALL QPPAASAAAAPSMSGPDVET PSAIQIC in isoform 7. 1 PublicationAdd BLAST	57
Alternative sequenceⁱVSP_000154	287 – 380	GCVIT…AEPQP → AHVMPAGADHTAPSSSPSTG TKCSLLRHHHLGTHDLHEQ in isoform 3. 1 PublicationAdd BLAST	94
Alternative sequenceⁱVSP_000155	287 – 288	GC → AP in isoform 2. 1 Publication	2
Alternative sequenceⁱVSP_000156	289 – 380	Missing in isoform 2. 1 PublicationAdd BLAST	92

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D88894 mRNA Translation: BAA24350.1 AB074415 mRNA Translation: BAC20174.1 AB074416 mRNA Translation: BAC20175.1 AB074417 mRNA Translation: BAC20176.1 AB074418 mRNA Translation: BAC20177.1 AB074419 mRNA Translation: BAC20178.1 U91316 mRNA Translation: AAB61211.1 Frameshift. BT006888 mRNA Translation: AAP35534.1 AK289572 mRNA Translation: BAF82261.1 AK290097 mRNA Translation: BAF82786.1 AK291583 mRNA Translation: BAF84272.1 AK292202 mRNA Translation: BAF84891.1 AK057168 mRNA Translation: BAG51874.1 AL031847 Genomic DNA No translation available. AL031848 Genomic DNA No translation available. CH471130 Genomic DNA Translation: EAW71528.1 CH471130 Genomic DNA Translation: EAW71529.1 CH471130 Genomic DNA Translation: EAW71530.1 BC017365 mRNA Translation: AAH17365.2 Different initiation.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS30573.1 [O00154-7] CCDS65.1 [O00154-1] CCDS66.1 [O00154-5] CCDS67.1 [O00154-6]
PIRⁱ	JC7161
NCBI Reference Sequences More...RefSeqⁱ	NP_009205.3, NM_007274.3 [O00154-7] NP_863654.1, NM_181864.2 [O00154-1] NP_863655.1, NM_181865.2 [O00154-5] NP_863656.1, NM_181866.2 [O00154-6]

Genome annotation databases

Ensemblⁱ	ENST00000361521; ENSP00000354615; ENSG00000097021 [O00154-7] ENST00000377842; ENSP00000367073; ENSG00000097021 [O00154-6] ENST00000377845; ENSP00000367076; ENSG00000097021 [O00154-5] ENST00000377855; ENSP00000367086; ENSG00000097021 [O00154-1] ENST00000377860; ENSP00000367091; ENSG00000097021 [O00154-3] ENST00000418124; ENSP00000402532; ENSG00000097021 [O00154-2] ENST00000545482; ENSP00000439218; ENSG00000097021 [O00154-7] ENST00000608083; ENSP00000476610; ENSG00000097021 [O00154-4]
GeneIDⁱ	11332
KEGGⁱ	hsa:11332
UCSC genome browser More...UCSCⁱ	uc001amq.4, human [O00154-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O00154	cDNA FLJ60167, highly similar to Cytosolic acyl coenzyme A thioester hydrolase		HUMAN		265	UniRef100_O00154
O00154-2	ACOT7 isoform 6		PONAB		246	UniRef100_A0A2J8URW8
ACOT7 isoform 3		PANTR		246
O00154-4	ACOT7 isoform 2		PONAB		370	UniRef100_A0A2J8URX5
ACOT7 isoform 4		PANTR		338
ACOT7 isoform 1		PONAB		338
O00154-5	ACOT7 isoform 7		PONAB		350	UniRef100_A0A2J8URV1
Acyl-CoA thioesterase 7		PANTR		350
Acyl-CoA thioesterase 7		PANPA		350
Uncharacterized protein		NOMLE		350
ACOT7 isoform 7		PANTR		350
O00154-6	ACOT7 isoform 5		PONAB		329	UniRef100_A0A2J8URW9
Acyl-CoA thioesterase 7		PANTR		329
Acyl-CoA thioesterase 7		PANPA		329
Uncharacterized protein		NOMLE		329
ACOT7 isoform 8		PANTR		329
O00154-7	Acyl-CoA thioesterase 7		PANTR		370	UniRef100_K7DQW5
ACOT7 isoform 1		PANTR		370

Protein	Similar proteins		Species	Score	Length	Source
O00154	cDNA FLJ60167, highly similar to Cytosolic acyl coenzyme A thioester hydrolase		HUMAN		265	UniRef90_O00154
Uncharacterized protein		MACMU		380
Acyl-CoA thioesterase 7		SURSU		360
Uncharacterized protein		SAIBB		313
+1
O00154-2	ACOT7 isoform 6		PONAB		246	UniRef90_A0A2J8URW8
ACOT7 isoform 3		PANTR		246
Acyl-CoA thioesterase 7		MOLMO		254
O00154-3	Acyl-CoA thioesterase 7		RHIFE		284	UniRef90_O00154-3
ACOT7 isoform 5		PANTR		283
ACOT7 isoform 8		PONAB		283
O00154-4	Acyl-CoA thioesterase 7		PAPAN		383	UniRef90_A0A2I3M4B4
Testis cDNA, clone: QtsA-15551, similar to human brain acyl-CoA hydrolase (BACH), transcript varianthBACHa		MACFA		397
Acyl-CoA thioesterase 7		PANTR		389
Acyl-CoA thioesterase 7		CERAT		387
Acyl-CoA thioesterase 7		PANPA		386
+20
O00154-5	Acyl-CoA thioesterase 7		PANTR		332	UniRef90_A0A2I3SPW0
Acyl-CoA thioesterase 7		PANPA		332
ACOT7 isoform 7		PONAB		350
Uncharacterized protein		NOMLE		350
Acyl-CoA thioesterase 7		PANTR		350
+2
O00154-6	Acyl-CoA thioesterase 7		PIG		406	UniRef90_A0A5G2QIZ9
cytosolic acyl coenzyme A thioester hydrolase isoform X2		DELLE		360
Cytosolic acyl coenzyme A thioester hydrolase (Fragment)		NEOVI		338
Uncharacterized protein		SAIBB		330
Cytosolic acyl coenzyme A thioester hydrolase isoform hBACHd		CALJA		329
+25

Protein	Similar proteins		Species	Score	Length	Source
O00154	cDNA FLJ60167, highly similar to Cytosolic acyl coenzyme A thioester hydrolase		HUMAN		265	UniRef50_O00154
Uncharacterized protein		MACMU		380
Acyl-CoA thioesterase 7		SURSU		360
Uncharacterized protein		SAIBB		313
Acyl-CoA thioesterase 7		VOMUR		347
+78
O00154-2	Putative cytosolic acyl coenzyme A thioester hydrolase-like		HUMAN		252	UniRef50_Q6ZUV0
HotDog ACOT-type domain-containing protein		MONMO		262
cytosolic acyl coenzyme A thioester hydrolase-like isoform X7		CARAU		265
Uncharacterized protein		Sinocyclocheilus rhinocerous		241
ACOT7 isoform 6		PONAB		246
+24
O00154-3	Acyl-CoA thioesterase 7		RHIFE		284	UniRef50_O00154-3
ACOT7 isoform 5		PANTR		283
ACOT7 isoform 8		PONAB		283
Acyl-CoA thioesterase 7		XENTR		306
Acyl-CoA thioesterase 7		AOTNA		334
+32
O00154-4	Cytosolic acyl coenzyme A thioester hydrolase	)	MOUSE		381	UniRef50_Q91V12
Cytosolic acyl coenzyme A thioester hydrolase		RAT		381
cytosolic acyl coenzyme A thioester hydrolase isoform X1		MUSCR		388
(mimic poison frog) hypothetical protein		mimic poison frog		381
Acyl-coA thioesterase 7 (Fragment)		MUSMC		27
+926
O00154-6	Acyl-CoA thioesterase 7		BOVIN		398	UniRef50_A0A3Q1MI69
Acyl-CoA thioesterase 7		BOBOX		398
Uncharacterized protein		wild yak		338
cytosolic acyl coenzyme A thioester hydrolase isoform X2		Odocoileus virginianus texanus		374
cytosolic acyl coenzyme A thioester hydrolase isoform X1		BOSIN		374
+196

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D88894 mRNA Translation: BAA24350.1 AB074415 mRNA Translation: BAC20174.1 AB074416 mRNA Translation: BAC20175.1 AB074417 mRNA Translation: BAC20176.1 AB074418 mRNA Translation: BAC20177.1 AB074419 mRNA Translation: BAC20178.1 U91316 mRNA Translation: AAB61211.1 Frameshift. BT006888 mRNA Translation: AAP35534.1 AK289572 mRNA Translation: BAF82261.1 AK290097 mRNA Translation: BAF82786.1 AK291583 mRNA Translation: BAF84272.1 AK292202 mRNA Translation: BAF84891.1 AK057168 mRNA Translation: BAG51874.1 AL031847 Genomic DNA No translation available. AL031848 Genomic DNA No translation available. CH471130 Genomic DNA Translation: EAW71528.1 CH471130 Genomic DNA Translation: EAW71529.1 CH471130 Genomic DNA Translation: EAW71530.1 BC017365 mRNA Translation: AAH17365.2 Different initiation.
CCDSⁱ	CCDS30573.1 [O00154-7] CCDS65.1 [O00154-1] CCDS66.1 [O00154-5] CCDS67.1 [O00154-6]
PIRⁱ	JC7161
RefSeqⁱ	NP_009205.3, NM_007274.3 [O00154-7] NP_863654.1, NM_181864.2 [O00154-1] NP_863655.1, NM_181865.2 [O00154-5] NP_863656.1, NM_181866.2 [O00154-6]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2QQ2	X-ray	2.80	A/B/C/D/E/F/G/H/I/J/K/L	209-378	[»]
SMRⁱ	O00154
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	116460, 81 interactors
IntActⁱ	O00154, 52 interactors
MINTⁱ	O00154
STRINGⁱ	9606.ENSP00000367086

PTM databases

GlyGenⁱ	O00154, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	O00154
MetOSiteⁱ	O00154
PhosphoSitePlusⁱ	O00154
SwissPalmⁱ	O00154

Genetic variation databases

BioMutaⁱ	ACOT7

BioMutaⁱ

ACOT7

2D gel databases

UCD-2DPAGEⁱ	O00154

UCD-2DPAGEⁱ

O00154

Proteomic databases

CPTACⁱ	CPTAC-303 CPTAC-304
EPDⁱ	O00154
jPOSTⁱ	O00154
MassIVEⁱ	O00154
MaxQBⁱ	O00154
PaxDbⁱ	O00154
PeptideAtlasⁱ	O00154
PRIDEⁱ	O00154
ProteomicsDBⁱ	47737 [O00154-1] 47738 [O00154-2] 47739 [O00154-3] 47740 [O00154-4] 47741 [O00154-5] 47742 [O00154-6]
TopDownProteomicsⁱ	O00154-1 [O00154-1]

Protocols and materials databases

Antibodypediaⁱ	12967, 159 antibodies
The DNASU plasmid repository More...DNASUⁱ	11332

Genome annotation databases

Ensemblⁱ	ENST00000361521; ENSP00000354615; ENSG00000097021 [O00154-7] ENST00000377842; ENSP00000367073; ENSG00000097021 [O00154-6] ENST00000377845; ENSP00000367076; ENSG00000097021 [O00154-5] ENST00000377855; ENSP00000367086; ENSG00000097021 [O00154-1] ENST00000377860; ENSP00000367091; ENSG00000097021 [O00154-3] ENST00000418124; ENSP00000402532; ENSG00000097021 [O00154-2] ENST00000545482; ENSP00000439218; ENSG00000097021 [O00154-7] ENST00000608083; ENSP00000476610; ENSG00000097021 [O00154-4]
GeneIDⁱ	11332
KEGGⁱ	hsa:11332
UCSCⁱ	uc001amq.4, human [O00154-1]

Organism-specific databases

CTDⁱ	11332
DisGeNETⁱ	11332
GeneCardsⁱ	ACOT7
HGNCⁱ	HGNC:24157, ACOT7
HPAⁱ	ENSG00000097021, Tissue enhanced (brain)
MIMⁱ	602587, gene
neXtProtⁱ	NX_O00154
OpenTargetsⁱ	ENSG00000097021
PharmGKBⁱ	PA142672655
VEuPathDBⁱ	HostDB:ENSG00000097021
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2763, Eukaryota
GeneTreeⁱ	ENSGT00940000155229
HOGENOMⁱ	CLU_050164_0_0_1
InParanoidⁱ	O00154
OMAⁱ	PTDVNWG
OrthoDBⁱ	1069806at2759
PhylomeDBⁱ	O00154
TreeFamⁱ	TF329579

Enzyme and pathway databases

UniPathwayⁱ	UPA00199
BioCycⁱ	MetaCyc:HS01875-MONOMER
BRENDAⁱ	3.1.2.2, 2681 3.1.2.20, 2681
PathwayCommonsⁱ	O00154
Reactomeⁱ	R-HSA-77289, Mitochondrial Fatty Acid Beta-Oxidation
SABIO-RKⁱ	O00154

Miscellaneous databases

BioGRID-ORCSⁱ	11332, 4 hits in 1017 CRISPR screens
ChiTaRSⁱ	ACOT7, human
EvolutionaryTraceⁱ	O00154
GeneWikiⁱ	ACOT7
GenomeRNAiⁱ	11332
Pharosⁱ	O00154, Tbio
Protein Ontology More...PROⁱ	PR:O00154
RNActⁱ	O00154, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000097021, Expressed in prefrontal cortex and 218 other tissues
ExpressionAtlasⁱ	O00154, baseline and differential
Genevisibleⁱ	O00154, HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR040170, Cytosol_ACT IPR033120, HOTDOG_ACOT IPR029069, HotDog_dom_sf IPR006683, Thioestr_dom
PANTHERⁱ	PTHR11049, PTHR11049, 2 hits
Pfamⁱ	View protein in Pfam PF03061, 4HBT, 2 hits
SUPFAMⁱ	SSF54637, SSF54637, 2 hits
PROSITEⁱ	View protein in PROSITE PS51770, HOTDOG_ACOT, 2 hits
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	BACH_HUMAN
Accessionⁱ	O00154Primary (citable) accession number: O00154 Secondary accession number(s): A8K0K7 Q9Y540
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	February 12, 2003
	Last modified:	September 29, 2021
	This is version 193 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - O00154 (BACH_HUMAN)

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Cytosolic acyl coenzyme A thioester hydrolase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid metabolism

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoplasm and Cytosol

Cytoplasm and Cytosol

Mitochondrion

Mitochondrion

Cytosol

Extracellular region or secreted

Mitochondrion

Nucleus

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Miscellaneous databases

Genetic variation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

O00154

Isoform 4 [O00154-4]

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genetic variation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: fatty acid metabolism

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ