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O00154 (BACH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytosolic acyl coenzyme A thioester hydrolase

EC=3.1.2.2
Alternative name(s):
Acyl-CoA thioesterase 7
Brain acyl-CoA hydrolase
Short name=BACH
CTE-IIa
Short name=CTE-II
Long chain acyl-CoA thioester hydrolase
Gene names
Name:ACOT7
Synonyms:BACH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.

Catalytic activity

Palmitoyl-CoA + H2O = CoA + palmitate.

Subunit structure

Homohexamer By similarity.

Subcellular location

Isoform 4: Cytoplasm Ref.2.

Isoform 6: Cytoplasm Ref.2.

Isoform 1: Mitochondrion Ref.2.

Isoform 5: Mitochondrion Ref.2.

Tissue specificity

Isoform 4 is expressed exclusively in brain. Ref.2

Domain

Both hydrolase domains are required for efficient activity By similarity.

Sequence similarities

Contains 2 acyl coenzyme A hydrolase domains.

Sequence caution

The sequence AAB61211.1 differs from that shown. Reason: Frameshift at position 371.

The sequence AAH17365.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAI19435.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI19774.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionHydrolase
Serine esterase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcoenzyme A biosynthetic process

Inferred from direct assay Ref.1. Source: BHF-UCL

fatty acid catabolic process

Inferred from electronic annotation. Source: Ensembl

long-chain fatty-acyl-CoA catabolic process

Inferred from direct assay Ref.1. Source: BHF-UCL

medium-chain fatty acid biosynthetic process

Inferred from direct assay Ref.1. Source: BHF-UCL

medium-chain fatty-acyl-CoA catabolic process

Inferred from direct assay Ref.1. Source: BHF-UCL

palmitic acid biosynthetic process

Inferred from direct assay Ref.1. Source: BHF-UCL

   Cellular_componentcell body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.1. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionfatty-acyl-CoA binding

Inferred from direct assay Ref.1. Source: BHF-UCL

long-chain fatty acyl-CoA binding

Inferred from direct assay Ref.1. Source: BHF-UCL

palmitoyl-CoA hydrolase activity

Inferred from direct assay Ref.1. Source: BHF-UCL

protein homodimerization activity

Inferred from physical interaction Ref.1. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00154-1)

Also known as: B; HBACHb;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O00154-2)

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.
Isoform 3 (identifier: O00154-3)

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
Isoform 4 (identifier: O00154-4)

Also known as: A; hBACHa;

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITG → MSGPDVETPSAIQIC
Note: Major isoform.
Isoform 5 (identifier: O00154-5)

Also known as: C; hBACHc;

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: MKLLARALRL...PPCGACITGR → MLLLRRSLSLNVLRKEVDRACFGEKAKQ
Isoform 6 (identifier: O00154-6)

Also known as: D; hBACHd;

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITG → MAFQLS
Isoform 7 (identifier: O00154-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380Cytosolic acyl coenzyme A thioester hydrolase
PRO_0000053806

Regions

Domain56 – 15196Acyl coenzyme A hydrolase 1
Domain242 – 31978Acyl coenzyme A hydrolase 2

Sites

Active site661 By similarity
Active site2551 By similarity

Amino acid modifications

Modified residue1681N6-acetyllysine Ref.10
Modified residue1981N6-acetyllysine Ref.10
Modified residue2831N6-acetyllysine Ref.10

Natural variations

Alternative sequence1 – 5858MKLLA…CITGR → MLLLRRSLSLNVLRKEVDRA CFGEKAKQ in isoform 5.
VSP_000151
Alternative sequence1 – 5757MKLLA…ACITG → MSGPDVETPSAIQIC in isoform 2, isoform 3 and isoform 4.
VSP_000152
Alternative sequence1 – 5757MKLLA…ACITG → MAFQLS in isoform 6.
VSP_000153
Alternative sequence1 – 5757MKLLA…ACITG → MARPGLIHSAPGLPDTCALL QPPAASAAAAPSMSGPDVET PSAIQIC in isoform 7.
VSP_047094
Alternative sequence287 – 38094GCVIT…AEPQP → AHVMPAGADHTAPSSSPSTG TKCSLLRHHHLGTHDLHEQ in isoform 3.
VSP_000154
Alternative sequence287 – 2882GC → AP in isoform 2.
VSP_000155
Alternative sequence289 – 38092Missing in isoform 2.
VSP_000156

Experimental info

Sequence conflict821E → G in BAG51874. Ref.5
Sequence conflict371 – 3722KR → DD in AAB61211. Ref.3
Sequence conflict377 – 3782EP → DA in AAB61211. Ref.3

Secondary structure

.................... 380
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (B) (HBACHb) [UniParc].

Last modified February 12, 2003. Version 3.
Checksum: BDD75D62A60095BC

FASTA38041,796
        10         20         30         40         50         60 
MKLLARALRL CEFGRQASSR RLVAGQGCVG PRRGCCAPVQ VVGPRADLPP CGACITGRIM 

        70         80         90        100        110        120 
RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC VAALARVERT DFLSPMCIGE 

       130        140        150        160        170        180 
VAHVSAEITY TSKHSVEVQV NVMSENILTG AKKLTNKATL WYVPLSLKNV DKVLEVPPVV 

       190        200        210        220        230        240 
YSRQEQEEEG RKRYEAQKLE RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT 

       250        260        270        280        290        300 
LHGFVHGGVT MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS 

       310        320        330        340        350        360 
NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE 

       370        380 
GKGRYLQMKA KRQGHAEPQP 

« Hide

Isoform 2 (A-X) (hBACHa-X) [UniParc].

Checksum: 4CDCAD44CE427904
Show »

FASTA24627,041
Isoform 3 (A-Xi) (hBACHa-Xi) [UniParc].

Checksum: C21B4544638BA031
Show »

FASTA28330,977
Isoform 4 (A) (hBACHa) [UniParc].

Checksum: 95E4CB4B0A7AF34C
Show »

FASTA33837,420
Isoform 5 (C) (hBACHc) [UniParc].

Checksum: D8FA42B2583051BA
Show »

FASTA35038,991
Isoform 6 (D) (hBACHd) [UniParc].

Checksum: ECEB0F657ADF6E25
Show »

FASTA32936,568
Isoform 7 [UniParc].

Checksum: 28F0088FFF813417
Show »

FASTA37040,455

References

« Hide 'large scale' references
[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), CHARACTERIZATION.
Tissue: Brain.
[2]"Human brain acyl-CoA hydrolase isoforms encoded by a single gene."
Yamada J., Kuramochi Y., Takagi M., Watanabe T., Suga T.
Biochem. Biophys. Res. Commun. 299:49-56(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5 AND 6), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain.
[3]Hajra A.K., Uhler M.D., Larkins L.K.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Hippocampus.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4; 5; 6 AND 7).
Tissue: Cerebellum, Colon, Placenta, Stomach and Subthalamic nucleus.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[9]Lubec G., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 79-90, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168; LYS-198 AND LYS-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Human acyl-CoA thioesterase 7."
Structural genomics consortium (SGC)
Submitted (AUG-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 209-378.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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, AL031848 Genomic DNA. Translation: CAI19440.1.
AL031847, AL031848 Genomic DNA. Translation: CAI19435.1. Different initiation.
AL031847, AL031848 Genomic DNA. Translation: CAI19442.1.
AL031847, AL031848 Genomic DNA. Translation: CAI19443.1.
AL031848, AL031847 Genomic DNA. Translation: CAI19774.1. Different initiation.
AL031848, AL031847 Genomic DNA. Translation: CAI19777.1.
AL031848, AL031847 Genomic DNA. Translation: CAI19778.1.
AL031848, AL031847 Genomic DNA. Translation: CAI19779.1.
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.
PIRJC7161.
RefSeqNP_009205.3. NM_007274.3.
NP_863654.1. NM_181864.2.
NP_863655.1. NM_181865.2.
NP_863656.1. NM_181866.2.
UniGeneHs.126137.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QQ2X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L209-378[»]
ProteinModelPortalO00154.
SMRO00154. Positions 52-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116460. 17 interactions.
IntActO00154. 2 interactions.
MINTMINT-2869715.

PTM databases

PhosphoSiteO00154.

2D gel databases

UCD-2DPAGEO00154.

Proteomic databases

PaxDbO00154.
PRIDEO00154.

Protocols and materials databases

DNASU11332.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361521; 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]
ENST00000608083; ENSP00000476610; ENSG00000097021. [O00154-4]
GeneID11332.
KEGGhsa:11332.
UCSCuc001amq.3. human. [O00154-6]
uc001amr.3. human. [O00154-5]
uc001ams.3. human. [O00154-1]

Organism-specific databases

CTD11332.
GeneCardsGC01M006324.
HGNCHGNC:24157. ACOT7.
HPAHPA025735.
HPA025762.
MIM602587. gene.
neXtProtNX_O00154.
PharmGKBPA142672655.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1607.
HOVERGENHBG036928.
InParanoidO00154.
KOK17360.
OMAANKAALW.
OrthoDBEOG7QZGB2.
PhylomeDBO00154.
TreeFamTF329579.

Enzyme and pathway databases

BRENDA3.1.2.2. 2681.
SABIO-RKO00154.

Gene expression databases

ArrayExpressO00154.
BgeeO00154.
GenevestigatorO00154.

Family and domain databases

InterProIPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACOT7. human.
EvolutionaryTraceO00154.
GeneWikiACOT7.
GenomeRNAi11332.
NextBio35469290.
PROO00154.
SOURCESearch...

Entry information

Entry nameBACH_HUMAN
AccessionPrimary (citable) accession number: O00154
Secondary accession number(s): A8K0K7 expand/collapse secondary AC list , A8K232, A8K6B8, A8K837, B3KQ12, O43703, Q53Y78, Q5JYL2, Q5JYL3, Q5JYL4, Q5JYL5, Q5JYL6, Q5TGR4, Q9UJM9, Q9Y539, Q9Y540
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 12, 2003
Last modified: April 16, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM