UniProt ID | ACOT5_MOUSE | |
---|---|---|
UniProt AC | Q6Q2Z6 | |
Protein Name | Acyl-coenzyme A thioesterase 5 | |
Gene Name | Acot5 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 421 | |
Subcellular Localization | Peroxisome. | |
Protein Description | 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. Seems to be involved in intraperoxisomal regulation of acyl-CoA levels, but not CoASH levels. Mainly active on medium-chain acyl-CoAs. May have a function in termination of beta-oxidation of fatty acids.. | |
Protein Sequence | MVPTVSLEPTGHSCWDEPLSIAVRGLAPEQPVTLRTALRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLIKRDVQTPFVVELEVLDGHEPDGGRLLARAVHERHFMAPGVRRVPVREGRVRATLFLPPGTGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYKYDDLPKVIDILHLEYFEEAVTYLLSHPQVKGPGVGLLGISKGAELSLSMASFLKGITAAVVINGATVNVISTLYYKEESLPGLGMHLERIKVTKDGFKDIIDILNVPLEAPDQKSLIPLERSDTAFLFLVGQDDHNWKSEFYAREASKRLQAHGKEKPQIVCYPKTGHHIEPPYIPWSIAAPHSYFDKPILLGGEPRAHAMAQVDAWQRLQTFFHKHLSGDKRPSPAKL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
13 | Phosphorylation | SLEPTGHSCWDEPLS CEECCCCCCCCCCCE | 20.46 | 26525534 | |
42 | Acetylation | RTALRDEKGALFRAH HHHHCCCCCCEEEEE | 54.49 | 23576753 | |
42 | Ubiquitination | RTALRDEKGALFRAH HHHHCCCCCCEEEEE | 54.49 | - | |
52 | Phosphorylation | LFRAHARYRADSHGE EEEEEEECCCCCCCC | 15.78 | 26239621 | |
56 | Phosphorylation | HARYRADSHGELDLA EEECCCCCCCCCCEE | 32.19 | 25521595 | |
249 | Phosphorylation | ASFLKGITAAVVING HHHHCCCCEEEEECC | 19.75 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ACOT5_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACOT5_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ACOT5_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ACOT5_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASSSPECTROMETRY. |