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Q8WYK0

- ACO12_HUMAN

UniProt

Q8WYK0 - ACO12_HUMAN

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Protein

Acyl-coenzyme A thioesterase 12

Gene
ACOT12, CACH, CACH1, STARD15
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes acetyl-CoA to acetate and CoA.1 Publication

Catalytic activityi

Acetyl-CoA + H2O = CoA + acetate.

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441Coenzyme A

GO - Molecular functioni

  1. acetyl-CoA hydrolase activity Source: HGNC
  2. ATP binding Source: Ensembl
  3. lipid binding Source: InterPro

GO - Biological processi

  1. acetyl-CoA metabolic process Source: Ensembl
  2. acyl-CoA metabolic process Source: HGNC
  3. fatty acid metabolic process Source: UniProtKB-KW
  4. pyruvate metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.2.1. 2681.
SABIO-RKQ8WYK0.
UniPathwayiUPA00231.

Protein family/group databases

TCDBi4.C.3.1.2. the acyl-coa thioesterase (acot) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-coenzyme A thioesterase 12 (EC:3.1.2.1)
Short name:
Acyl-CoA thioesterase 12
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 namesi
Name:ACOT12
Synonyms:CACH, CACH1, STARD15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:24436. ACOT12.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672657.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 555555Acyl-coenzyme A thioesterase 12PRO_0000053809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331N6-succinyllysine By similarity
Modified residuei159 – 1591N6-succinyllysine By similarity
Modified residuei228 – 2281N6-succinyllysine By similarity

Proteomic databases

PaxDbiQ8WYK0.
PeptideAtlasiQ8WYK0.
PRIDEiQ8WYK0.

PTM databases

PhosphoSiteiQ8WYK0.

Expressioni

Gene expression databases

ArrayExpressiQ8WYK0.
BgeeiQ8WYK0.
CleanExiHS_ACOT12.
GenevestigatoriQ8WYK0.

Organism-specific databases

HPAiHPA037723.
HPA037724.

Interactioni

Subunit structurei

Homodimer or homotetramer By similarity.

Protein-protein interaction databases

STRINGi9606.ENSP00000303246.

Structurei

Secondary structure

1
555
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148
Helixi17 – 193
Beta strandi24 – 263
Helixi28 – 4720
Beta strandi51 – 566
Beta strandi69 – 8012
Beta strandi82 – 9514
Turni96 – 983
Beta strandi101 – 11313
Helixi131 – 14919
Beta strandi183 – 1886
Helixi191 – 1933
Helixi202 – 21817
Beta strandi220 – 2234
Beta strandi226 – 2305
Beta strandi244 – 25512
Beta strandi258 – 26811
Helixi270 – 2756
Beta strandi279 – 28911
Helixi294 – 2963

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B7KX-ray2.70A/B/C7-316[»]
ProteinModelPortaliQ8WYK0.
SMRiQ8WYK0. Positions 7-543.

Miscellaneous databases

EvolutionaryTraceiQ8WYK0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 127127Acyl coenzyme A hydrolase 1Add
BLAST
Domaini165 – 301137Acyl coenzyme A hydrolase 2Add
BLAST
Domaini340 – 549210STARTAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 553Coenzyme A binding
Regioni82 – 843Coenzyme A binding
Regioni234 – 2363Coenzyme A binding

Sequence similaritiesi

Contains 1 START domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1607.
HOGENOMiHOG000232032.
HOVERGENiHBG023847.
InParanoidiQ8WYK0.
KOiK01067.
OMAiPLWDPHY.
OrthoDBiEOG70CR6C.
PhylomeDBiQ8WYK0.
TreeFamiTF328368.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.530.20. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
IPR006683. Thioestr_supf.
[Graphical view]
PfamiPF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 2 hits.
PROSITEiPS50848. START. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8WYK0-1) [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

MERPAPGEVV MSQAIQPAHA TARGELSAGQ LLKWIDTTAC LAAEKHAGVS    50
CVTASVDDIQ FEETARVGQV ITIKAKVTRA FSTSMEISIK VMVQDMLTGI 100
EKLVSVAFST FVAKPVGKEK IHLKPVTLLT EQDHVEHNLA AERRKVRLQH 150
EDTFNNLMKE SSKFDDLIFD EEEGAVSTRG TSVQSIELVL PPHANHHGNT 200
FGGQIMAWME TVATISASRL CWAHPFLKSV DMFKFRGPST VGDRLVFTAI 250
VNNTFQTCVE VGVRVEAFDC QEWAEGRGRH INSAFLIYNA ADDKENLITF 300
PRIQPISKDD FRRYRGAIAR KRIRLGRKYV ISHKEEVPLC IHWDISKQAS 350
LSDSNVEALK KLAAKRGWEV TSTVEKIKIY TLEEHDVLSV WVEKHVGSPA 400
HLAYRLLSDF TKRPLWDPHF VSCEVIDWVS EDDQLYHITC PILNDDKPKD 450
LVVLVSRRKP LKDGNTYTVA VKSVILPSVP PSPQYIRSEI ICAGFLIHAI 500
DSNSCIVSYF NHMSASILPY FAGNLGGWSK SIEETAASCI QFLENPPDDG 550
FVSTF 555
Length:555
Mass (Da):62,034
Last modified:March 1, 2002 - v1
Checksum:i707560D55504732C
GO
Isoform 2 (identifier: Q8WYK0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     166-167: DL → GQ
     168-555: Missing.

Note: No experimental confirmation available.

Show »
Length:167
Mass (Da):18,327
Checksum:i58CB03F09579E5A4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti190 – 1901L → H Found in a clear cell renal carcinoma case; somatic mutation. 1 Publication
VAR_064691
Natural varianti230 – 2301V → I.
Corresponds to variant rs34607174 [ dbSNP | Ensembl ].
VAR_048192
Natural varianti403 – 4031A → T.
Corresponds to variant rs10371 [ dbSNP | Ensembl ].
VAR_048193

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei166 – 1672DL → GQ in isoform 2. VSP_055785
Alternative sequencei168 – 555388Missing in isoform 2. VSP_055786Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB078619 mRNA. Translation: BAB84022.1.
AK122960 mRNA. Translation: BAG53821.1.
AC008411 Genomic DNA. No translation available.
AC010623 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95875.1.
BC089437 mRNA. Translation: AAH89437.1.
BC075010 mRNA. Translation: AAH75010.1.
BC075011 mRNA. Translation: AAH75011.1.
CCDSiCCDS4055.1.
RefSeqiNP_570123.1. NM_130767.2.
UniGeneiHs.591756.

Genome annotation databases

EnsembliENST00000307624; ENSP00000303246; ENSG00000172497.
ENST00000513751; ENSP00000421628; ENSG00000172497.
GeneIDi134526.
KEGGihsa:134526.
UCSCiuc003khl.4. human.

Polymorphism databases

DMDMi25008183.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB078619 mRNA. Translation: BAB84022.1 .
AK122960 mRNA. Translation: BAG53821.1 .
AC008411 Genomic DNA. No translation available.
AC010623 Genomic DNA. No translation available.
CH471084 Genomic DNA. Translation: EAW95875.1 .
BC089437 mRNA. Translation: AAH89437.1 .
BC075010 mRNA. Translation: AAH75010.1 .
BC075011 mRNA. Translation: AAH75011.1 .
CCDSi CCDS4055.1.
RefSeqi NP_570123.1. NM_130767.2.
UniGenei Hs.591756.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3B7K X-ray 2.70 A/B/C 7-316 [» ]
ProteinModelPortali Q8WYK0.
SMRi Q8WYK0. Positions 7-543.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000303246.

Protein family/group databases

TCDBi 4.C.3.1.2. the acyl-coa thioesterase (acot) family.

PTM databases

PhosphoSitei Q8WYK0.

Polymorphism databases

DMDMi 25008183.

Proteomic databases

PaxDbi Q8WYK0.
PeptideAtlasi Q8WYK0.
PRIDEi Q8WYK0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307624 ; ENSP00000303246 ; ENSG00000172497 .
ENST00000513751 ; ENSP00000421628 ; ENSG00000172497 .
GeneIDi 134526.
KEGGi hsa:134526.
UCSCi uc003khl.4. human.

Organism-specific databases

CTDi 134526.
GeneCardsi GC05M080662.
HGNCi HGNC:24436. ACOT12.
HPAi HPA037723.
HPA037724.
MIMi 614315. gene.
neXtProti NX_Q8WYK0.
PharmGKBi PA142672657.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1607.
HOGENOMi HOG000232032.
HOVERGENi HBG023847.
InParanoidi Q8WYK0.
KOi K01067.
OMAi PLWDPHY.
OrthoDBi EOG70CR6C.
PhylomeDBi Q8WYK0.
TreeFami TF328368.

Enzyme and pathway databases

UniPathwayi UPA00231 .
BRENDAi 3.1.2.1. 2681.
SABIO-RK Q8WYK0.

Miscellaneous databases

EvolutionaryTracei Q8WYK0.
GeneWikii ACOT12.
GenomeRNAii 134526.
NextBioi 83397.
PROi Q8WYK0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8WYK0.
Bgeei Q8WYK0.
CleanExi HS_ACOT12.
Genevestigatori Q8WYK0.

Family and domain databases

Gene3Di 3.10.129.10. 2 hits.
3.30.530.20. 1 hit.
InterProi IPR029069. HotDog_dom.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
IPR006683. Thioestr_supf.
[Graphical view ]
Pfami PF03061. 4HBT. 2 hits.
PF01852. START. 1 hit.
[Graphical view ]
SUPFAMi SSF54637. SSF54637. 2 hits.
PROSITEi PS50848. START. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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.
    , 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 1).
    Tissue: Liver.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORMS 1 AND 2).
    Tissue: Chondrosarcoma.
  6. "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.
  7. Cited for: VARIANT HIS-190.

Entry informationi

Entry nameiACO12_HUMAN
AccessioniPrimary (citable) accession number: Q8WYK0
Secondary accession number(s): B3KVK9, Q5FWE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: March 1, 2002
Last modified: September 3, 2014
This is version 109 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 5
    Human chromosome 5: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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