Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NPJ3

- ACO13_HUMAN

UniProt

Q9NPJ3 - ACO13_HUMAN

Protein

Acyl-coenzyme A thioesterase 13

Gene

ACOT13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    1. acyl-CoA hydrolase activity Source: UniProtKB

    GO - Biological processi

    1. metabolic process Source: GOC
    2. protein homotetramerization Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20999. ACOT13.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Mitochondrion By similarity. Nucleus By similarity. Cytoplasmcytoskeletonspindle By similarity
    Note: During interphase, found both in the nucleus and in the cytoplasm. At mitosis, localizes to the spindle. Colocalizes with tubulin By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrion Source: UniProtKB-SubCell
    4. nucleus Source: UniProt
    5. spindle Source: UniProtKB-SubCell

    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.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 140140Acyl-coenzyme A thioesterase 13PRO_0000156697Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 140139Acyl-coenzyme A thioesterase 13, N-terminally processedPRO_0000424501Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; in Acyl-coenzyme A thioesterase 13; alternate2 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.
    GenevestigatoriQ9NPJ3.

    Organism-specific databases

    HPAiHPA019881.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi120958. 14 interactions.
    IntActiQ9NPJ3. 3 interactions.
    STRINGi9606.ENSP00000230048.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000170540.
    InParanoidiQ9NPJ3.
    KOiK17362.
    OMAiMNITYMS.
    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. Align

    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

    MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN    50
    AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI 100
    VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN 140
    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:
    EMBL
    GenBank
    DDBJ
    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. [Q9NPJ3-1]
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS4558.1. [Q9NPJ3-1 ]
    CCDS54972.1. [Q9NPJ3-2 ]
    RefSeqi NP_001153566.1. NM_001160094.1. [Q9NPJ3-2 ]
    NP_060943.1. NM_018473.3. [Q9NPJ3-1 ]
    UniGenei Hs.731605.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F0X X-ray 2.30 A/B/C/D/E/F/G/H 1-140 [» ]
    2H4U X-ray 2.20 A/B/C/D 19-140 [» ]
    3F5O X-ray 1.70 A/B/C/D/E/F/G/H 1-140 [» ]
    ProteinModelPortali Q9NPJ3.
    SMRi Q9NPJ3. Positions 2-139.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120958. 14 interactions.
    IntActi Q9NPJ3. 3 interactions.
    STRINGi 9606.ENSP00000230048.

    PTM databases

    PhosphoSitei Q9NPJ3.

    Proteomic databases

    MaxQBi Q9NPJ3.
    PaxDbi Q9NPJ3.
    PeptideAtlasi Q9NPJ3.
    PRIDEi Q9NPJ3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230048 ; ENSP00000230048 ; ENSG00000112304 . [Q9NPJ3-1 ]
    ENST00000537591 ; ENSP00000445552 ; ENSG00000112304 . [Q9NPJ3-2 ]
    GeneIDi 55856.
    KEGGi hsa:55856.
    UCSCi uc003nek.3. human. [Q9NPJ3-1 ]

    Organism-specific databases

    CTDi 55856.
    GeneCardsi GC06P024667.
    H-InvDB HIX0005627.
    HGNCi HGNC:20999. ACOT13.
    HPAi HPA019881.
    MIMi 615652. gene.
    neXtProti NX_Q9NPJ3.
    PharmGKBi PA165617655.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2050.
    HOGENOMi HOG000170540.
    InParanoidi Q9NPJ3.
    KOi K17362.
    OMAi MNITYMS.
    OrthoDBi EOG7Q8CQ4.
    PhylomeDBi Q9NPJ3.
    TreeFami TF315062.

    Enzyme and pathway databases

    SABIO-RK Q9NPJ3.

    Miscellaneous databases

    ChiTaRSi ACOT13. human.
    EvolutionaryTracei Q9NPJ3.
    GenomeRNAii 55856.
    NextBioi 61135.
    PROi Q9NPJ3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NPJ3.
    CleanExi HS_THEM2.
    Genevestigatori Q9NPJ3.

    Family and domain databases

    Gene3Di 3.10.129.10. 1 hit.
    InterProi IPR029069. HotDog_dom.
    IPR003736. PAAI_dom.
    IPR006683. Thioestr_supf.
    [Graphical view ]
    Pfami PF03061. 4HBT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54637. SSF54637. 1 hit.
    TIGRFAMsi TIGR00369. unchar_dom_1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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].
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF ASP-65, SUBUNIT.
    11. "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.
    12. "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: October 1, 2014
    This is version 114 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