O00154 (BACH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Hydrolase Serine esterase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid catabolic process Inferred from electronic annotation. Source: Compara lipid metabolic process Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cell body Inferred from electronic annotation. Source: Compara cytoplasm Traceable author statement Ref.1. Source: ProtInc cytosol Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell neuron projection Inferred from electronic annotation. Source: Compara
Molecular_function	carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW catalytic activity Traceable author statement Ref.1. Source: ProtInc fatty-acyl-CoA binding Traceable author statement Ref.1. Source: ProtInc palmitoyl-CoA hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 6 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 380

380

Cytosolic acyl coenzyme A thioester hydrolase

PRO_0000053806

Regions

Domain

56 – 151

96

Acyl coenzyme A hydrolase 1

Domain

242 – 319

78

Acyl coenzyme A hydrolase 2

Sites

Active site

66

1

By similarity

Active site

255

1

By similarity

Amino acid modifications

Modified residue

168

1

N6-acetyllysine Ref.10

Modified residue

198

1

N6-acetyllysine Ref.10

Modified residue

283

1

N6-acetyllysine Ref.10

Natural variations

Alternative sequence

1 – 58

58

MKLLA…CITGR → MLLLRRSLSLNVLRKEVDRA CFGEKAKQ in isoform 5.

VSP_000151

Alternative sequence

1 – 57

57

MKLLA…ACITG → MSGPDVETPSAIQIC in isoform 2, isoform 3 and isoform 4.

VSP_000152

Alternative sequence

1 – 57

57

MKLLA…ACITG → MAFQLS in isoform 6.

VSP_000153

Alternative sequence

287 – 380

94

GCVIT…AEPQP → AHVMPAGADHTAPSSSPSTG TKCSLLRHHHLGTHDLHEQ in isoform 3.

VSP_000154

Alternative sequence

287 – 288

2

GC → AP in isoform 2.

VSP_000155

Alternative sequence

289 – 380

92

Missing in isoform 2.

VSP_000156

Experimental info

Sequence conflict

371 – 372

2

KR → DD in AAB61211. Ref.3

Sequence conflict

377 – 378

2

EP → DA in AAB61211. Ref.3

Secondary structure

1

.

.

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.

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380

Helix Strand Turn

Details...

Helix

223 – 226

4

Beta strand

228 – 233

6

Helix

236 – 238

3

Beta strand

241 – 245

5

Helix

247 – 266

20

Beta strand

267 – 280

14

Beta strand

288 – 299

12

Beta strand

301 – 314

14

Beta strand

323 – 335

13

Helix

352 – 371

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (B) (HBACHb) [UniParc]. Last modified February 12, 2003. Version 3. Checksum: BDD75D62A60095BC	FASTA	380	41,796
	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
	Isoform 2 (A-X) (hBACHa-X) [UniParc]. Checksum: 4CDCAD44CE427904	FASTA	246	27,041
	10 20 30 40 50 60 MSGPDVETPS AIQICRIMRP DDANVAGNVH GGTILKMIEE AGAIISTRHC NSQNGERCVA 70 80 90 100 110 120 ALARVERTDF LSPMCIGEVA HVSAEITYTS KHSVEVQVNV MSENILTGAK KLTNKATLWY 130 140 150 160 170 180 VPLSLKNVDK VLEVPPVVYS RQEQEEEGRK RYEAQKLERM ETKWRNGDIV QPVLNPEPNT 190 200 210 220 230 240 VSYSQSSLIH LVGPSDCTLH GFVHGGVTMK LMDEVAGIVA ARHCKTNIVT ASVDAINFHD KIRKAP
	Isoform 3 (A-Xi) (hBACHa-Xi) [UniParc]. Checksum: C21B4544638BA031	FASTA	283	30,977
	10 20 30 40 50 60 MSGPDVETPS AIQICRIMRP DDANVAGNVH GGTILKMIEE AGAIISTRHC NSQNGERCVA 70 80 90 100 110 120 ALARVERTDF LSPMCIGEVA HVSAEITYTS KHSVEVQVNV MSENILTGAK KLTNKATLWY 130 140 150 160 170 180 VPLSLKNVDK VLEVPPVVYS RQEQEEEGRK RYEAQKLERM ETKWRNGDIV QPVLNPEPNT 190 200 210 220 230 240 VSYSQSSLIH LVGPSDCTLH GFVHGGVTMK LMDEVAGIVA ARHCKTNIVT ASVDAINFHD 250 260 270 280 KIRKAHVMPA GADHTAPSSS PSTGTKCSLL RHHHLGTHDL HEQ
	Isoform 4 (A) (hBACHa) [UniParc]. Checksum: 95E4CB4B0A7AF34C	FASTA	338	37,420
	10 20 30 40 50 60 MSGPDVETPS AIQICRIMRP DDANVAGNVH GGTILKMIEE AGAIISTRHC NSQNGERCVA 70 80 90 100 110 120 ALARVERTDF LSPMCIGEVA HVSAEITYTS KHSVEVQVNV MSENILTGAK KLTNKATLWY 130 140 150 160 170 180 VPLSLKNVDK VLEVPPVVYS RQEQEEEGRK RYEAQKLERM ETKWRNGDIV QPVLNPEPNT 190 200 210 220 230 240 VSYSQSSLIH LVGPSDCTLH GFVHGGVTMK LMDEVAGIVA ARHCKTNIVT ASVDAINFHD 250 260 270 280 290 300 KIRKGCVITI SGRMTFTSNK SMEIEVLVDA DPVVDSSQKR YRAASAFFTY VSLSQEGRSL 310 320 330 PVPQLVPETE DEKKRFEEGK GRYLQMKAKR QGHAEPQP
	Isoform 5 (C) (hBACHc) [UniParc]. Checksum: D8FA42B2583051BA	FASTA	350	38,991
	10 20 30 40 50 60 MLLLRRSLSL NVLRKEVDRA CFGEKAKQIM RPDDANVAGN VHGGTILKMI EEAGAIISTR 70 80 90 100 110 120 HCNSQNGERC VAALARVERT DFLSPMCIGE VAHVSAEITY TSKHSVEVQV NVMSENILTG 130 140 150 160 170 180 AKKLTNKATL WYVPLSLKNV DKVLEVPPVV YSRQEQEEEG RKRYEAQKLE RMETKWRNGD 190 200 210 220 230 240 IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT LHGFVHGGVT MKLMDEVAGI VAARHCKTNI 250 260 270 280 290 300 VTASVDAINF HDKIRKGCVI TISGRMTFTS NKSMEIEVLV DADPVVDSSQ KRYRAASAFF 310 320 330 340 350 TYVSLSQEGR SLPVPQLVPE TEDEKKRFEE GKGRYLQMKA KRQGHAEPQP
	Isoform 6 (D) (hBACHd) [UniParc]. Checksum: ECEB0F657ADF6E25	FASTA	329	36,568
	10 20 30 40 50 60 MAFQLSRIMR PDDANVAGNV HGGTILKMIE EAGAIISTRH CNSQNGERCV AALARVERTD 70 80 90 100 110 120 FLSPMCIGEV AHVSAEITYT SKHSVEVQVN VMSENILTGA KKLTNKATLW YVPLSLKNVD 130 140 150 160 170 180 KVLEVPPVVY SRQEQEEEGR KRYEAQKLER METKWRNGDI VQPVLNPEPN TVSYSQSSLI 190 200 210 220 230 240 HLVGPSDCTL HGFVHGGVTM KLMDEVAGIV AARHCKTNIV TASVDAINFH DKIRKGCVIT 250 260 270 280 290 300 ISGRMTFTSN KSMEIEVLVD ADPVVDSSQK RYRAASAFFT YVSLSQEGRS LPVPQLVPET 310 320 EDEKKRFEEG KGRYLQMKAK RQGHAEPQP

References

	« Hide 'large scale' referencesShow '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. , 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 AND 6). Tissue: Cerebellum, Colon, Placenta 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. , 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. , 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, 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, MASS SPECTROMETRY.
[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.
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.

IPI

IPI00010415.
IPI00219451.
IPI00219452.
IPI00395748.
IPI00746126.
IPI00883762.

PIR

JC7161.

RefSeq

NP_009205.3. NM_007274.3.
NP_863654.1. NM_181864.2.
NP_863655.1. NM_181865.2.
NP_863656.1. NM_181866.2.

UniGene

Hs.126137.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O00154.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00154. 2 interactions.

MINT

MINT-2869715.

PTM databases

PhosphoSite

O00154.

2D gel databases

UCD-2DPAGE

O00154.

Proteomic databases

PaxDb

O00154.

PRIDE

O00154.

Protocols and materials databases

DNASU

11332.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361521; ENSP00000354615; ENSG00000097021.
ENST00000377842; ENSP00000367073; ENSG00000097021.
ENST00000377845; ENSP00000367076; ENSG00000097021.
ENST00000377855; ENSP00000367086; ENSG00000097021.
ENST00000377860; ENSP00000367091; ENSG00000097021.
ENST00000418124; ENSP00000402532; ENSG00000097021.

GeneID

11332.

KEGG

hsa:11332.

UCSC

uc001amq.3. human.
uc001amr.3. human.
uc001ams.3. human.

Organism-specific databases

CTD

11332.

GeneCards

GC01M006324.

HGNC

HGNC:24157. ACOT7.

HPA

HPA025735.
HPA025762.

MIM

602587. gene.

neXtProt

NX_O00154.

PharmGKB

PA142672655.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1607.

HOVERGEN

HBG036928.

InParanoid

O00154.

KO

K01068.

OrthoDB

EOG4JWVF5.

PhylomeDB

O00154.

Enzyme and pathway databases

BRENDA

3.1.2.2. 2681.

Gene expression databases

ArrayExpress

O00154.

Bgee

O00154.

Genevestigator

O00154.

GermOnline

ENSG00000097021. Homo sapiens.

Family and domain databases

InterPro

IPR006683. Thioestr_supf.
[Graphical view]

Pfam

PF03061. 4HBT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ACOT7. human.

EvolutionaryTrace

O00154.

GenomeRNAi

11332.

NextBio

43047.

SOURCE

Search...

Entry information

Entry name

BACH_HUMAN

Accession

Primary (citable) accession number: O00154
Secondary accession number(s): A8K0K7 , A8K232, A8K6B8, A8K837, 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:	May 1, 2013
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

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.