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Q8WYK0 (ACO12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acyl-coenzyme A thioesterase 12

Short name=Acyl-CoA thioesterase 12
EC=3.1.2.1
Alternative name(s):
Acyl-CoA thioester hydrolase 12
Cytoplasmic acetyl-CoA hydrolase 1
Short name=CACH-1
Short name=hCACH-1
START domain-containing protein 15
Short name=StARD15
Gene names
Name:ACOT12
Synonyms:CACH, CACH1, STARD15
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes acetyl-CoA to acetate and CoA. Ref.1

Catalytic activity

Acetyl-CoA + H2O = CoA + acetate.

Enzyme regulation

Inhibited by ADP. Active in the presence of ATP. Ref.1

Pathway

Carbohydrate metabolism; pyruvate metabolism.

Subunit structure

Homodimer or homotetramer By similarity.

Subcellular location

Cytoplasm Ref.1.

Sequence similarities

Contains 2 acyl coenzyme A hydrolase domains.

Contains 1 START domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 555555Acyl-coenzyme A thioesterase 12
PRO_0000053809

Regions

Domain1 – 127127Acyl coenzyme A hydrolase 1
Domain165 – 301137Acyl coenzyme A hydrolase 2
Domain340 – 549210START
Region53 – 553Coenzyme A binding
Region82 – 843Coenzyme A binding
Region234 – 2363Coenzyme A binding

Sites

Binding site1441Coenzyme A

Amino acid modifications

Modified residue331N6-succinyllysine By similarity
Modified residue1591N6-succinyllysine By similarity
Modified residue2281N6-succinyllysine By similarity

Natural variations

Natural variant1901L → H Found in a clear cell renal carcinoma case; somatic mutation. Ref.6
VAR_064691
Natural variant2301V → I.
Corresponds to variant rs34607174 [ dbSNP | Ensembl ].
VAR_048192
Natural variant4031A → T.
Corresponds to variant rs10371 [ dbSNP | Ensembl ].
VAR_048193

Secondary structure

........................................ 555
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8WYK0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 707560D55504732C

FASTA55562,034
        10         20         30         40         50         60 
MERPAPGEVV MSQAIQPAHA TARGELSAGQ LLKWIDTTAC LAAEKHAGVS CVTASVDDIQ 

        70         80         90        100        110        120 
FEETARVGQV ITIKAKVTRA FSTSMEISIK VMVQDMLTGI EKLVSVAFST FVAKPVGKEK 

       130        140        150        160        170        180 
IHLKPVTLLT EQDHVEHNLA AERRKVRLQH EDTFNNLMKE SSKFDDLIFD EEEGAVSTRG 

       190        200        210        220        230        240 
TSVQSIELVL PPHANHHGNT FGGQIMAWME TVATISASRL CWAHPFLKSV DMFKFRGPST 

       250        260        270        280        290        300 
VGDRLVFTAI VNNTFQTCVE VGVRVEAFDC QEWAEGRGRH INSAFLIYNA ADDKENLITF 

       310        320        330        340        350        360 
PRIQPISKDD FRRYRGAIAR KRIRLGRKYV ISHKEEVPLC IHWDISKQAS LSDSNVEALK 

       370        380        390        400        410        420 
KLAAKRGWEV TSTVEKIKIY TLEEHDVLSV WVEKHVGSPA HLAYRLLSDF TKRPLWDPHF 

       430        440        450        460        470        480 
VSCEVIDWVS EDDQLYHITC PILNDDKPKD LVVLVSRRKP LKDGNTYTVA VKSVILPSVP 

       490        500        510        520        530        540 
PSPQYIRSEI ICAGFLIHAI DSNSCIVSYF NHMSASILPY FAGNLGGWSK SIEETAASCI 

       550 
QFLENPPDDG FVSTF 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase."
Suematsu N., Isohashi F.
Acta Biochim. Pol. 53:553-561(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, ENZYME REGULATION, FUNCTION.
Tissue: Liver.
[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. expand/collapse author list , 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].
Tissue: Liver.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
[5]"Human acyl-coenzyme A thioesterase 12."
Structural genomics consortium (SGC)
Submitted (NOV-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-316 IN COMPLEX WITH COENZYME A.
[6]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-190.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB078619 mRNA. Translation: BAB84022.1.
AK122960 mRNA. Translation: BAG53821.1.
CH471084 Genomic DNA. Translation: EAW95875.1.
BC075010 mRNA. Translation: AAH75010.1.
BC075011 mRNA. Translation: AAH75011.1.
CCDSCCDS4055.1.
RefSeqNP_570123.1. NM_130767.2.
UniGeneHs.591756.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3B7KX-ray2.70A/B/C7-316[»]
ProteinModelPortalQ8WYK0.
SMRQ8WYK0. Positions 7-543.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000303246.

Protein family/group databases

TCDB4.C.3.1.2. the acyl-coa thioesterase (acot) family.

PTM databases

PhosphoSiteQ8WYK0.

Polymorphism databases

DMDM25008183.

Proteomic databases

PaxDbQ8WYK0.
PeptideAtlasQ8WYK0.
PRIDEQ8WYK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307624; ENSP00000303246; ENSG00000172497.
GeneID134526.
KEGGhsa:134526.
UCSCuc003khl.4. human.

Organism-specific databases

CTD134526.
GeneCardsGC05M080662.
HGNCHGNC:24436. ACOT12.
HPAHPA037723.
HPA037724.
MIM614315. gene.
neXtProtNX_Q8WYK0.
PharmGKBPA142672657.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1607.
HOGENOMHOG000232032.
HOVERGENHBG023847.
InParanoidQ8WYK0.
KOK01067.
OMAPLWDPHY.
OrthoDBEOG70CR6C.
PhylomeDBQ8WYK0.
TreeFamTF328368.

Enzyme and pathway databases

BRENDA3.1.2.1. 2681.
SABIO-RKQ8WYK0.
UniPathwayUPA00231.

Gene expression databases

ArrayExpressQ8WYK0.
BgeeQ8WYK0.
CleanExHS_ACOT12.
GenevestigatorQ8WYK0.

Family and domain databases

Gene3D3.10.129.10. 2 hits.
3.30.530.20. 1 hit.
InterProIPR029069. HotDog_dom.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
IPR006683. Thioestr_supf.
[Graphical view]
PfamPF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view]
SUPFAMSSF54637. SSF54637. 2 hits.
PROSITEPS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8WYK0.
GeneWikiACOT12.
GenomeRNAi134526.
NextBio83397.
PROQ8WYK0.
SOURCESearch...

Entry information

Entry nameACO12_HUMAN
AccessionPrimary (citable) accession number: Q8WYK0
Secondary accession number(s): B3KVK9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM