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Protein

Acyl-coenzyme A thioesterase 13

Gene

ACOT13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis (By similarity).By similarity

Kineticsi

  1. KM=4.9 µM for n-decanoyl-CoA1 Publication
  2. KM=26 µM for n-octanoyl-CoA1 Publication
  3. KM=5 µM for myristoyl-CoA1 Publication
  4. KM=9 µM for palmitoyl-CoA1 Publication
  5. KM=9 µM for oleoyl-CoA1 Publication
  6. KM=10 µM for 3,4-dihydroxyphenylacetyl-CoA1 Publication
  7. KM=40 µM for 3-hydroxyphenylacetyl-CoA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei50 – 501Substrate

    GO - Molecular functioni

    • acyl-CoA hydrolase activity Source: UniProtKB

    GO - Biological processi

    • metabolic process Source: GOC
    • protein homotetramerization Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BRENDAi3.1.2.20. 2681.
    SABIO-RKQ9NPJ3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 13 (EC:3.1.2.-)
    Short name:
    Acyl-CoA thioesterase 13
    Alternative name(s):
    Thioesterase superfamily member 2
    Cleaved into the following chain:
    Gene namesi
    Name:ACOT13
    Synonyms:THEM2
    ORF Names:HT012, PNAS-27
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20999. ACOT13.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB-SubCell
    • extracellular exosome Source: UniProtKB
    • mitochondrion Source: UniProtKB-SubCell
    • nucleus Source: UniProtKB
    • spindle Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi50 – 501N → A: Reduced activity. 1 Publication
    Mutagenesisi56 – 561H → A: Decreases affinity for substrate. 1 Publication
    Mutagenesisi65 – 651D → A: Loss of activity. 2 Publications
    Mutagenesisi65 – 651D → E or N: Reduced activity. 2 Publications
    Mutagenesisi83 – 831S → A: Reduced activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA165617655.

    Polymorphism and mutation databases

    BioMutaiACOT13.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 140140Acyl-coenzyme A thioesterase 13PRO_0000424501Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate3 Publications
    Chaini2 – 140139Acyl-coenzyme A thioesterase 13, N-terminally processedPRO_0000156697Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei2 – 21N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processed3 Publications
    Modified residuei27 – 271N6-acetyllysineBy similarity
    Modified residuei37 – 371N6-acetyllysineBy similarity
    Modified residuei43 – 431N6-acetyllysineBy similarity
    Modified residuei108 – 1081N6-acetyllysineBy similarity
    Modified residuei127 – 1271N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NPJ3.
    PaxDbiQ9NPJ3.
    PeptideAtlasiQ9NPJ3.
    PRIDEiQ9NPJ3.

    PTM databases

    PhosphoSiteiQ9NPJ3.

    Expressioni

    Gene expression databases

    BgeeiQ9NPJ3.
    CleanExiHS_THEM2.
    GenevisibleiQ9NPJ3. HS.

    Organism-specific databases

    HPAiHPA019881.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi120958. 12 interactions.
    IntActiQ9NPJ3. 3 interactions.
    STRINGi9606.ENSP00000230048.

    Structurei

    Secondary structure

    1
    140
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1513Combined sources
    Beta strandi18 – 203Combined sources
    Helixi21 – 255Combined sources
    Beta strandi29 – 346Combined sources
    Beta strandi37 – 437Combined sources
    Helixi46 – 483Combined sources
    Beta strandi53 – 553Combined sources
    Helixi57 – 7317Combined sources
    Beta strandi75 – 773Combined sources
    Beta strandi82 – 909Combined sources
    Beta strandi99 – 10911Combined sources
    Beta strandi111 – 12212Combined sources
    Turni123 – 1253Combined sources
    Beta strandi128 – 13710Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F0XX-ray2.30A/B/C/D/E/F/G/H1-140[»]
    2H4UX-ray2.20A/B/C/D19-140[»]
    3F5OX-ray1.70A/B/C/D/E/F/G/H1-140[»]
    ProteinModelPortaliQ9NPJ3.
    SMRiQ9NPJ3. Positions 2-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NPJ3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thioesterase PaaI family.Curated

    Phylogenomic databases

    eggNOGiCOG2050.
    GeneTreeiENSGT00390000013934.
    HOGENOMiHOG000170540.
    InParanoidiQ9NPJ3.
    KOiK17362.
    OMAiICEMKVE.
    OrthoDBiEOG7Q8CQ4.
    PhylomeDBiQ9NPJ3.
    TreeFamiTF315062.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_supf.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9NPJ3-1) [UniParc]FASTAAdd to basket

    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
    MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN
    60 70 80 90 100
    AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI
    110 120 130 140
    VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN
    Length:140
    Mass (Da):14,960
    Last modified:October 1, 2000 - v1
    Checksum:i084E36EFEE715A18
    GO
    Isoform 2 (identifier: Q9NPJ3-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: MTSMTQSLREVIKAMTKARNFERVLG → MVR

    Note: No experimental confirmation available.
    Show »
    Length:117
    Mass (Da):12,366
    Checksum:iA6F50AA63A00583A
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626MTSMT…ERVLG → MVR in isoform 2. 1 PublicationVSP_046101Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF155649 mRNA. Translation: AAF67006.1.
    AF220186 mRNA. Translation: AAF67651.1.
    AF274952 mRNA. Translation: AAK07529.1.
    AK000508 mRNA. Translation: BAA91215.1.
    AK309738 mRNA. No translation available.
    AL031775 Genomic DNA. Translation: CAD92509.1.
    BC000894 mRNA. Translation: AAH00894.1.
    CCDSiCCDS4558.1. [Q9NPJ3-1]
    CCDS54972.1. [Q9NPJ3-2]
    RefSeqiNP_001153566.1. NM_001160094.1. [Q9NPJ3-2]
    NP_060943.1. NM_018473.3. [Q9NPJ3-1]
    UniGeneiHs.731605.

    Genome annotation databases

    EnsembliENST00000230048; ENSP00000230048; ENSG00000112304.
    ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2]
    GeneIDi55856.
    KEGGihsa:55856.
    UCSCiuc003nek.3. human. [Q9NPJ3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF155649 mRNA. Translation: AAF67006.1.
    AF220186 mRNA. Translation: AAF67651.1.
    AF274952 mRNA. Translation: AAK07529.1.
    AK000508 mRNA. Translation: BAA91215.1.
    AK309738 mRNA. No translation available.
    AL031775 Genomic DNA. Translation: CAD92509.1.
    BC000894 mRNA. Translation: AAH00894.1.
    CCDSiCCDS4558.1. [Q9NPJ3-1]
    CCDS54972.1. [Q9NPJ3-2]
    RefSeqiNP_001153566.1. NM_001160094.1. [Q9NPJ3-2]
    NP_060943.1. NM_018473.3. [Q9NPJ3-1]
    UniGeneiHs.731605.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F0XX-ray2.30A/B/C/D/E/F/G/H1-140[»]
    2H4UX-ray2.20A/B/C/D19-140[»]
    3F5OX-ray1.70A/B/C/D/E/F/G/H1-140[»]
    ProteinModelPortaliQ9NPJ3.
    SMRiQ9NPJ3. Positions 2-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi120958. 12 interactions.
    IntActiQ9NPJ3. 3 interactions.
    STRINGi9606.ENSP00000230048.

    PTM databases

    PhosphoSiteiQ9NPJ3.

    Polymorphism and mutation databases

    BioMutaiACOT13.

    Proteomic databases

    MaxQBiQ9NPJ3.
    PaxDbiQ9NPJ3.
    PeptideAtlasiQ9NPJ3.
    PRIDEiQ9NPJ3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000230048; ENSP00000230048; ENSG00000112304.
    ENST00000537591; ENSP00000445552; ENSG00000112304. [Q9NPJ3-2]
    GeneIDi55856.
    KEGGihsa:55856.
    UCSCiuc003nek.3. human. [Q9NPJ3-1]

    Organism-specific databases

    CTDi55856.
    GeneCardsiGC06P024667.
    H-InvDBHIX0005627.
    HGNCiHGNC:20999. ACOT13.
    HPAiHPA019881.
    MIMi615652. gene.
    neXtProtiNX_Q9NPJ3.
    PharmGKBiPA165617655.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG2050.
    GeneTreeiENSGT00390000013934.
    HOGENOMiHOG000170540.
    InParanoidiQ9NPJ3.
    KOiK17362.
    OMAiICEMKVE.
    OrthoDBiEOG7Q8CQ4.
    PhylomeDBiQ9NPJ3.
    TreeFamiTF315062.

    Enzyme and pathway databases

    BRENDAi3.1.2.20. 2681.
    SABIO-RKQ9NPJ3.

    Miscellaneous databases

    ChiTaRSiACOT13. human.
    EvolutionaryTraceiQ9NPJ3.
    GenomeRNAii55856.
    NextBioi61135.
    PROiQ9NPJ3.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NPJ3.
    CleanExiHS_THEM2.
    GenevisibleiQ9NPJ3. HS.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    InterProiIPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_supf.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 1 hit.
    TIGRFAMsiTIGR00369. unchar_dom_1. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adrenal gland and Hypothalamus.
    2. "Human acute promyelocytic leukemia cell line NB4's apoptosis related genes."
      Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Promyelocytic leukemia.
    3. "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 AND 2).
      Tissue: Teratocarcinoma.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1).
      Tissue: Cervix.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF ASP-65, SUBUNIT.
    12. "The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis."
      Cao J., Xu H., Zhao H., Gong W., Dunaway-Mariano D.
      Biochemistry 48:1293-1304(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-50; HIS-56; ASP-65 AND SER-83, SUBUNIT.
    13. "The crystal structure of human thioesterase superfamily member 2."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiACO13_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPJ3
    Secondary accession number(s): F5H2L4, O95549
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: October 1, 2000
    Last modified: July 22, 2015
    This is version 123 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.