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O00154

- BACH_HUMAN

UniProt

O00154 - BACH_HUMAN

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
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (12 Feb 2003)
      Previous versions | rss
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    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. fatty-acyl-CoA binding Source: BHF-UCL
    2. long-chain fatty acyl-CoA binding Source: BHF-UCL
    3. palmitoyl-CoA hydrolase activity Source: BHF-UCL
    4. protein binding 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

    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-SubCell
    6. neuron projection Source: Ensembl
    7. nucleus Source: HPA

    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

    ArrayExpressiO00154.
    BgeeiO00154.
    GenevestigatoriO00154.

    Organism-specific databases

    HPAiHPA025735.
    HPA025762.

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Protein-protein interaction databases

    BioGridi116460. 17 interactions.
    IntActiO00154. 2 interactions.
    MINTiMINT-2869715.

    Structurei

    Secondary structure

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

    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.
    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

    MKLLARALRL CEFGRQASSR RLVAGQGCVG PRRGCCAPVQ VVGPRADLPP    50
    CGACITGRIM RPDDANVAGN VHGGTILKMI EEAGAIISTR HCNSQNGERC 100
    VAALARVERT DFLSPMCIGE VAHVSAEITY TSKHSVEVQV NVMSENILTG 150
    AKKLTNKATL WYVPLSLKNV DKVLEVPPVV YSRQEQEEEG RKRYEAQKLE 200
    RMETKWRNGD IVQPVLNPEP NTVSYSQSSL IHLVGPSDCT LHGFVHGGVT 250
    MKLMDEVAGI VAARHCKTNI VTASVDAINF HDKIRKGCVI TISGRMTFTS 300
    NKSMEIEVLV DADPVVDSSQ KRYRAASAFF TYVSLSQEGR SLPVPQLVPE 350
    TEDEKKRFEE GKGRYLQMKA KRQGHAEPQP 380
    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]
    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. 17 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 ]
    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.
    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

    ArrayExpressi O00154.
    Bgeei O00154.
    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

    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 1, 2014
    This is version 136 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