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Q9Y305

- ACOT9_HUMAN

UniProt

Q9Y305 - ACOT9_HUMAN

Protein

Acyl-coenzyme A thioesterase 9, mitochondrial

Gene

ACOT9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (03 Mar 2009)
      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. Active on long chain acyl-CoAs.

    GO - Molecular functioni

    1. acetyl-CoA hydrolase activity Source: HGNC

    GO - Biological processi

    1. acyl-CoA metabolic process Source: HGNC

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acyl-coenzyme A thioesterase 9, mitochondrial (EC:3.1.2.-)
    Short name:
    Acyl-CoA thioesterase 9
    Alternative name(s):
    Acyl-CoA thioester hydrolase 9
    Gene namesi
    Name:ACOT9
    ORF Names:CGI-16
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:17152. ACOT9.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: HGNC

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142672656.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2121MitochondrionBy similarityAdd
    BLAST
    Chaini22 – 439418Acyl-coenzyme A thioesterase 9, mitochondrialPRO_0000053812Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei103 – 1031N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9Y305.
    PaxDbiQ9Y305.
    PRIDEiQ9Y305.

    PTM databases

    PhosphoSiteiQ9Y305.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y305.
    BgeeiQ9Y305.
    CleanExiHS_ACOT9.
    GenevestigatoriQ9Y305.

    Organism-specific databases

    HPAiHPA035533.

    Interactioni

    Subunit structurei

    Interacts with NYAP1, NYAP2 and MYO16.By similarity

    Protein-protein interaction databases

    BioGridi117132. 8 interactions.
    IntActiQ9Y305. 7 interactions.
    MINTiMINT-3085225.
    STRINGi9606.ENSP00000368605.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y305.
    SMRiQ9Y305. Positions 279-400.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the acyl coenzyme A hydrolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG269414.
    HOGENOMiHOG000188398.
    HOVERGENiHBG004168.
    InParanoidiQ9Y305.
    KOiK17361.
    OMAiYTKVQVR.
    OrthoDBiEOG7GQXVJ.
    PhylomeDBiQ9Y305.
    TreeFamiTF313352.

    Family and domain databases

    Gene3Di3.10.129.10. 2 hits.
    InterProiIPR029069. HotDog_dom.
    IPR006683. Thioestr_supf.
    [Graphical view]
    PfamiPF03061. 4HBT. 1 hit.
    [Graphical view]
    SUPFAMiSSF54637. SSF54637. 2 hits.

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y305-1) [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

    MRRAALRLCA LGKGQLTPGR GLTQGPQNPK KQGIFHIHEV RDKLREIVGA    50
    STNWRDHVKA MEERKLLHSF LAKSQDGLPP RRMKDSYIEV LLPLGSEPEL 100
    REKYLTVQNT VRFGRILEDL DSLGVLICYM HNKIHSAKMS PLSIVTALVD 150
    KIDMCKKSLS PEQDIKFSGH VSWVGKTSME VKMQMFQLHG DEFCPVLDAT 200
    FVMVARDSEN KGPAFVNPLI PESPEEEELF RQGELNKGRR IAFSSTSLLK 250
    MAPSAEERTT IHEMFLSTLD PKTISFRSRV LPSNAVWMEN SKLKSLEICH 300
    PQERNIFNRI FGGFLMRKAY ELAWATACSF GGSRPFVVAV DDIMFQKPVE 350
    VGSLLFLSSQ VCFTQNNYIQ VRVHSEVASL QEKQHTTTNV FHFTFMSEKE 400
    VPLVFPKTYG ESMLYLDGQR HFNSMSGPAT LRKDYLVEP 439

    Note: No experimental confirmation available.

    Length:439
    Mass (Da):49,902
    Last modified:March 3, 2009 - v2
    Checksum:i1CE2158D4F83D4D6
    GO
    Isoform 2 (identifier: Q9Y305-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         5-39: ALRLCALGKGQLTPGRGLTQGPQNPKKQGIFHIHE → PC

    Note: No experimental confirmation available.

    Show »
    Length:406
    Mass (Da):46,355
    Checksum:i99ADE404D472CEEB
    GO
    Isoform 3 (identifier: Q9Y305-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:379
    Mass (Da):43,207
    Checksum:iAC76325AB9264911
    GO
    Isoform 4 (identifier: Q9Y305-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         39-39: E → EACSSIHVNH

    Show »
    Length:448
    Mass (Da):50,851
    Checksum:iAA20C18EF239983D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881L → S in BAG51291. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti305 – 3051N → H in a pancreatic ductal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_062668

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060Missing in isoform 3. 1 PublicationVSP_036420Add
    BLAST
    Alternative sequencei5 – 3935ALRLC…FHIHE → PC in isoform 2. 1 PublicationVSP_036419Add
    BLAST
    Alternative sequencei39 – 391E → EACSSIHVNH in isoform 4. 1 PublicationVSP_041093

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132950 mRNA. Translation: AAD27725.1.
    AK024337 mRNA. Translation: BAG51291.1.
    BX648512 mRNA. No translation available.
    AC093011 Genomic DNA. No translation available.
    AC131011 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98998.1.
    BC136671 mRNA. Translation: AAI36672.1.
    BC144360 mRNA. Translation: AAI44361.1.
    CCDSiCCDS35216.1. [Q9Y305-1]
    CCDS43924.1. [Q9Y305-4]
    RefSeqiNP_001028755.2. NM_001033583.2. [Q9Y305-1]
    NP_001032248.1. NM_001037171.1. [Q9Y305-4]
    XP_005274528.1. XM_005274471.1. [Q9Y305-3]
    XP_005274529.1. XM_005274472.1. [Q9Y305-3]
    UniGeneiHs.298885.

    Genome annotation databases

    EnsembliENST00000336430; ENSP00000336580; ENSG00000123130. [Q9Y305-1]
    ENST00000379295; ENSP00000368597; ENSG00000123130. [Q9Y305-3]
    ENST00000379303; ENSP00000368605; ENSG00000123130. [Q9Y305-4]
    GeneIDi23597.
    KEGGihsa:23597.
    UCSCiuc004dao.3. human. [Q9Y305-4]
    uc004dap.3. human. [Q9Y305-1]

    Polymorphism databases

    DMDMi224471815.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132950 mRNA. Translation: AAD27725.1 .
    AK024337 mRNA. Translation: BAG51291.1 .
    BX648512 mRNA. No translation available.
    AC093011 Genomic DNA. No translation available.
    AC131011 Genomic DNA. No translation available.
    CH471074 Genomic DNA. Translation: EAW98998.1 .
    BC136671 mRNA. Translation: AAI36672.1 .
    BC144360 mRNA. Translation: AAI44361.1 .
    CCDSi CCDS35216.1. [Q9Y305-1 ]
    CCDS43924.1. [Q9Y305-4 ]
    RefSeqi NP_001028755.2. NM_001033583.2. [Q9Y305-1 ]
    NP_001032248.1. NM_001037171.1. [Q9Y305-4 ]
    XP_005274528.1. XM_005274471.1. [Q9Y305-3 ]
    XP_005274529.1. XM_005274472.1. [Q9Y305-3 ]
    UniGenei Hs.298885.

    3D structure databases

    ProteinModelPortali Q9Y305.
    SMRi Q9Y305. Positions 279-400.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117132. 8 interactions.
    IntActi Q9Y305. 7 interactions.
    MINTi MINT-3085225.
    STRINGi 9606.ENSP00000368605.

    PTM databases

    PhosphoSitei Q9Y305.

    Polymorphism databases

    DMDMi 224471815.

    Proteomic databases

    MaxQBi Q9Y305.
    PaxDbi Q9Y305.
    PRIDEi Q9Y305.

    Protocols and materials databases

    DNASUi 23597.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336430 ; ENSP00000336580 ; ENSG00000123130 . [Q9Y305-1 ]
    ENST00000379295 ; ENSP00000368597 ; ENSG00000123130 . [Q9Y305-3 ]
    ENST00000379303 ; ENSP00000368605 ; ENSG00000123130 . [Q9Y305-4 ]
    GeneIDi 23597.
    KEGGi hsa:23597.
    UCSCi uc004dao.3. human. [Q9Y305-4 ]
    uc004dap.3. human. [Q9Y305-1 ]

    Organism-specific databases

    CTDi 23597.
    GeneCardsi GC0XM023629.
    HGNCi HGNC:17152. ACOT9.
    HPAi HPA035533.
    MIMi 300862. gene.
    neXtProti NX_Q9Y305.
    PharmGKBi PA142672656.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269414.
    HOGENOMi HOG000188398.
    HOVERGENi HBG004168.
    InParanoidi Q9Y305.
    KOi K17361.
    OMAi YTKVQVR.
    OrthoDBi EOG7GQXVJ.
    PhylomeDBi Q9Y305.
    TreeFami TF313352.

    Miscellaneous databases

    GenomeRNAii 23597.
    NextBioi 46262.
    PROi Q9Y305.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y305.
    Bgeei Q9Y305.
    CleanExi HS_ACOT9.
    Genevestigatori Q9Y305.

    Family and domain databases

    Gene3Di 3.10.129.10. 2 hits.
    InterProi IPR029069. HotDog_dom.
    IPR006683. Thioestr_supf.
    [Graphical view ]
    Pfami PF03061. 4HBT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54637. SSF54637. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    2. "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] (ISOFORM 3).
      Tissue: Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain and Testis.
    7. "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-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-305.

    Entry informationi

    Entry nameiACOT9_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y305
    Secondary accession number(s): B3KNC9, B7ZM94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3