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O00154

- BACH_HUMAN

UniProt

O00154 - BACH_HUMAN

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Protein

Cytosolic acyl coenzyme A thioester hydrolase

Gene

ACOT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

Palmitoyl-CoA + H2O = CoA + palmitate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661By similarity
Active sitei255 – 2551By similarity

GO - Molecular functioni

  1. carboxylic ester hydrolase activity Source: UniProtKB-KW
  2. fatty-acyl-CoA binding Source: BHF-UCL
  3. long-chain fatty acyl-CoA binding Source: BHF-UCL
  4. palmitoyl-CoA hydrolase activity Source: BHF-UCL
  5. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. coenzyme A biosynthetic process Source: BHF-UCL
  2. fatty acid catabolic process Source: Ensembl
  3. long-chain fatty-acyl-CoA catabolic process Source: BHF-UCL
  4. medium-chain fatty acid biosynthetic process Source: BHF-UCL
  5. medium-chain fatty-acyl-CoA catabolic process Source: BHF-UCL
  6. palmitic acid biosynthetic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BRENDAi3.1.2.2. 2681.
SABIO-RKO00154.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ACOT7
Synonyms:BACH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:24157. ACOT7.

Subcellular locationi

GO - Cellular componenti

  1. cell body Source: Ensembl
  2. cytoplasm Source: HPA
  3. cytosol Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProt
  5. mitochondrion Source: UniProtKB-KW
  6. neuron projection Source: Ensembl
  7. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672655.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Cytosolic acyl coenzyme A thioester hydrolasePRO_0000053806Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei168 – 1681N6-acetyllysine1 Publication
Modified residuei198 – 1981N6-acetyllysine1 Publication
Modified residuei283 – 2831N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO00154.
PaxDbiO00154.
PRIDEiO00154.

2D gel databases

UCD-2DPAGEO00154.

PTM databases

PhosphoSiteiO00154.

Expressioni

Tissue specificityi

Isoform 4 is expressed exclusively in brain.1 Publication

Gene expression databases

BgeeiO00154.
ExpressionAtlasiO00154. baseline and differential.
GenevestigatoriO00154.

Organism-specific databases

HPAiHPA025735.
HPA025762.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

BioGridi116460. 21 interactions.
IntActiO00154. 2 interactions.
MINTiMINT-2869715.

Structurei

Secondary structure

1
380
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi223 – 2264Combined sources
Beta strandi228 – 2336Combined sources
Helixi236 – 2383Combined sources
Beta strandi241 – 2455Combined sources
Helixi247 – 26620Combined sources
Beta strandi267 – 28014Combined sources
Beta strandi288 – 29912Combined sources
Beta strandi301 – 31414Combined sources
Beta strandi323 – 33513Combined sources
Helixi352 – 37120Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QQ2X-ray2.80A/B/C/D/E/F/G/H/I/J/K/L209-378[»]
ProteinModelPortaliO00154.
SMRiO00154. Positions 52-373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00154.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 15196Acyl coenzyme A hydrolase 1Add
BLAST
Domaini242 – 31978Acyl coenzyme A hydrolase 2Add
BLAST

Domaini

Both hydrolase domains are required for efficient activity.By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1607.
GeneTreeiENSGT00760000119297.
HOVERGENiHBG036928.
InParanoidiO00154.
KOiK17360.
OMAiEPHTVGY.
OrthoDBiEOG7QZGB2.
PhylomeDBiO00154.
TreeFamiTF329579.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
InterProiIPR029069. HotDog_dom.
IPR006683. Thioestr_supf.
[Graphical view]
PfamiPF03061. 4HBT. 2 hits.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 2 hits.

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O00154-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
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]FASTAAdd 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.

Show »
Length:246
Mass (Da):27,041
Checksum:i4CDCAD44CE427904
GO
Isoform 3 (identifier: O00154-3) [UniParc]FASTAAdd 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

Show »
Length:283
Mass (Da):30,977
Checksum:iC21B4544638BA031
GO
Isoform 4 (identifier: O00154-4) [UniParc]FASTAAdd to Basket

Also known as: A, hBACHa

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

Note: Major isoform.

Show »
Length:338
Mass (Da):37,420
Checksum:i95E4CB4B0A7AF34C
GO
Isoform 5 (identifier: O00154-5) [UniParc]FASTAAdd to Basket

Also known as: C, hBACHc

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

Show »
Length:350
Mass (Da):38,991
Checksum:iD8FA42B2583051BA
GO
Isoform 6 (identifier: O00154-6) [UniParc]FASTAAdd to Basket

Also known as: D, hBACHd

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

Show »
Length:329
Mass (Da):36,568
Checksum:iECEB0F657ADF6E25
GO
Isoform 7 (identifier: O00154-7) [UniParc]FASTAAdd to Basket

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

Show »
Length:370
Mass (Da):40,455
Checksum:i28F0088FFF813417
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821E → G in BAG51874. (PubMed:14702039)Curated
Sequence conflicti371 – 3722KR → DD in AAB61211. 1 PublicationCurated
Sequence conflicti377 – 3782EP → DA in AAB61211. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858MKLLA…CITGR → MLLLRRSLSLNVLRKEVDRA CFGEKAKQ in isoform 5. 2 PublicationsVSP_000151Add
BLAST
Alternative sequencei1 – 5757MKLLA…ACITG → MSGPDVETPSAIQIC in isoform 2, isoform 3 and isoform 4. 6 PublicationsVSP_000152Add
BLAST
Alternative sequencei1 – 5757MKLLA…ACITG → MAFQLS in isoform 6. 2 PublicationsVSP_000153Add
BLAST
Alternative sequencei1 – 5757MKLLA…ACITG → MARPGLIHSAPGLPDTCALL QPPAASAAAAPSMSGPDVET PSAIQIC in isoform 7. 1 PublicationVSP_047094Add
BLAST
Alternative sequencei287 – 38094GCVIT…AEPQP → AHVMPAGADHTAPSSSPSTG TKCSLLRHHHLGTHDLHEQ in isoform 3. 1 PublicationVSP_000154Add
BLAST
Alternative sequencei287 – 2882GC → AP in isoform 2. 1 PublicationVSP_000155
Alternative sequencei289 – 38092Missing in isoform 2. 1 PublicationVSP_000156Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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, 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.
CCDSiCCDS30573.1. [O00154-7]
CCDS65.1. [O00154-1]
CCDS66.1. [O00154-5]
CCDS67.1. [O00154-6]
PIRiJC7161.
RefSeqiNP_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]
UniGeneiHs.126137.

Genome annotation databases

EnsembliENST00000361521; 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]
GeneIDi11332.
KEGGihsa:11332.
UCSCiuc001amq.3. human. [O00154-6]
uc001amr.3. human. [O00154-5]
uc001ams.3. human. [O00154-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 , 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.
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 ]
UniGenei Hs.126137.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali O00154.
SMRi O00154. Positions 52-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116460. 21 interactions.
IntActi O00154. 2 interactions.
MINTi MINT-2869715.

PTM databases

PhosphoSitei O00154.

2D gel databases

UCD-2DPAGE O00154.

Proteomic databases

MaxQBi O00154.
PaxDbi O00154.
PRIDEi O00154.

Protocols and materials databases

DNASUi 11332.
Structural Biology Knowledgebase Search...

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.3. human. [O00154-6 ]
uc001amr.3. human. [O00154-5 ]
uc001ams.3. human. [O00154-1 ]

Organism-specific databases

CTDi 11332.
GeneCardsi GC01M006324.
HGNCi HGNC:24157. ACOT7.
HPAi HPA025735.
HPA025762.
MIMi 602587. gene.
neXtProti NX_O00154.
PharmGKBi PA142672655.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1607.
GeneTreei ENSGT00760000119297.
HOVERGENi HBG036928.
InParanoidi O00154.
KOi K17360.
OMAi EPHTVGY.
OrthoDBi EOG7QZGB2.
PhylomeDBi O00154.
TreeFami TF329579.

Enzyme and pathway databases

BRENDAi 3.1.2.2. 2681.
SABIO-RK O00154.

Miscellaneous databases

ChiTaRSi ACOT7. human.
EvolutionaryTracei O00154.
GeneWikii ACOT7.
GenomeRNAii 11332.
NextBioi 35469290.
PROi O00154.
SOURCEi Search...

Gene expression databases

Bgeei O00154.
ExpressionAtlasi O00154. baseline and differential.
Genevestigatori O00154.

Family and domain databases

Gene3Di 3.10.129.10. 2 hits.
InterProi IPR029069. HotDog_dom.
IPR006683. Thioestr_supf.
[Graphical view ]
Pfami PF03061. 4HBT. 2 hits.
[Graphical view ]
SUPFAMi SSF54637. SSF54637. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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; 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.
    , 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. 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. 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.

Entry informationi

Entry nameiBACH_HUMAN
AccessioniPrimary (citable) accession number: O00154
Secondary accession number(s): A8K0K7
, A8K232, A8K6B8, A8K837, B3KQ12, O43703, Q53Y78, Q5JYL2, Q5JYL3, Q5JYL4, Q5JYL5, Q5JYL6, Q5TGR4, Q9UJM9, Q9Y539, Q9Y540
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 12, 2003
Last modified: October 29, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3