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Q9Y305

- ACOT9_HUMAN

UniProt

Q9Y305 - ACOT9_HUMAN

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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

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
  2. carboxylic ester hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. acyl-CoA metabolic process Source: HGNC
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9Y305.
CleanExiHS_ACOT9.
ExpressionAtlasiQ9Y305. baseline and differential.
GenevestigatoriQ9Y305.

Organism-specific databases

HPAiHPA035533.

Interactioni

Subunit structurei

Interacts with NYAP1, NYAP2 and MYO16.By similarity

Protein-protein interaction databases

BioGridi117132. 14 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.
GeneTreeiENSGT00390000005330.
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

        10         20         30         40         50
MRRAALRLCA LGKGQLTPGR GLTQGPQNPK KQGIFHIHEV RDKLREIVGA
60 70 80 90 100
STNWRDHVKA MEERKLLHSF LAKSQDGLPP RRMKDSYIEV LLPLGSEPEL
110 120 130 140 150
REKYLTVQNT VRFGRILEDL DSLGVLICYM HNKIHSAKMS PLSIVTALVD
160 170 180 190 200
KIDMCKKSLS PEQDIKFSGH VSWVGKTSME VKMQMFQLHG DEFCPVLDAT
210 220 230 240 250
FVMVARDSEN KGPAFVNPLI PESPEEEELF RQGELNKGRR IAFSSTSLLK
260 270 280 290 300
MAPSAEERTT IHEMFLSTLD PKTISFRSRV LPSNAVWMEN SKLKSLEICH
310 320 330 340 350
PQERNIFNRI FGGFLMRKAY ELAWATACSF GGSRPFVVAV DDIMFQKPVE
360 370 380 390 400
VGSLLFLSSQ VCFTQNNYIQ VRVHSEVASL QEKQHTTTNV FHFTFMSEKE
410 420 430
VPLVFPKTYG ESMLYLDGQR HFNSMSGPAT LRKDYLVEP

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. 14 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.
GeneTreei ENSGT00390000005330.
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

Bgeei Q9Y305.
CleanExi HS_ACOT9.
ExpressionAtlasi Q9Y305. baseline and differential.
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 29, 2014
This is version 106 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