UniProt ID | ACOT8_HUMAN | |
---|---|---|
UniProt AC | O14734 | |
Protein Name | Acyl-coenzyme A thioesterase 8 | |
Gene Name | ACOT8 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 319 | |
Subcellular Localization | Cytoplasm . Peroxisome matrix . Predominantly localized in the peroxisome (PubMed:10092594, PubMed:15194431). | |
Protein Description | Acyl-coenzyme A (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. [PubMed: 9299485] | |
Protein Sequence | MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAAQEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTALLPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVKPQVSESKL | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSSPQAPED ------CCCCCCCCC | 51.21 | 30108239 | |
3 | Phosphorylation | -----MSSPQAPEDG -----CCCCCCCCCC | 21.52 | 25159151 | |
52 | Acetylation | RHYWVPAKRLFGGQI CCCEEECHHHCCCHH | 43.49 | 19608861 | |
52 | Ubiquitination | RHYWVPAKRLFGGQI CCCEEECHHHCCCHH | 43.49 | 19608861 | |
91 | Acetylation | FVRAGDPKLPVLYQV EEECCCCCCCEEEEE | 70.89 | 23749302 | |
96 | Phosphorylation | DPKLPVLYQVERTRT CCCCCEEEEEEECCC | 15.67 | 8281689 | |
101 | Phosphorylation | VLYQVERTRTGSSFS EEEEEEECCCCCCEE | 21.05 | 28102081 | |
103 | Phosphorylation | YQVERTRTGSSFSVR EEEEECCCCCCEEEE | 40.58 | 28102081 | |
105 | Phosphorylation | VERTRTGSSFSVRSV EEECCCCCCEEEEEE | 27.83 | 23312004 | |
106 | Phosphorylation | ERTRTGSSFSVRSVK EECCCCCCEEEEEEE | 23.92 | 28102081 | |
111 | Phosphorylation | GSSFSVRSVKAVQHG CCCEEEEEEEEEECC | 26.30 | 22985185 | |
169 | Ubiquitination | LRDPNLQKRYPLALN HHCCCHHHHHCCHHH | 58.00 | - | |
188 | Acetylation | QEVPIEIKPVNPSPL CCCCCEEECCCCCCH | 30.07 | 26051181 | |
188 | Ubiquitination | QEVPIEIKPVNPSPL CCCCCEEECCCCCCH | 30.07 | - | |
311 | Acetylation | QEGVIRVKPQVSESK CCCEEEEECCCCCCC | 21.63 | 18525915 | |
311 | Malonylation | QEGVIRVKPQVSESK CCCEEEEECCCCCCC | 21.63 | 26320211 | |
315 | Phosphorylation | IRVKPQVSESKL--- EEEECCCCCCCC--- | 30.79 | 30108239 | |
317 | Phosphorylation | VKPQVSESKL----- EECCCCCCCC----- | 31.58 | 30108239 | |
318 | Acetylation | KPQVSESKL------ ECCCCCCCC------ | 54.91 | 19608861 |
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 ACOT8_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACOT8_HUMAN !! |
* 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 ACOT8_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NEF_HV1H2 | nef | physical | 9153233 | |
PML_HUMAN | PML | physical | 26186194 | |
KLH23_HUMAN | KLHL23 | physical | 26186194 | |
PML_HUMAN | PML | physical | 28514442 | |
KLH23_HUMAN | KLHL23 | physical | 28514442 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-318, AND MASSSPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY. |