ACOT8_HUMAN - dbPTM
ACOT8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSSPQAPED
------CCCCCCCCC
51.2130108239
3Phosphorylation-----MSSPQAPEDG
-----CCCCCCCCCC
21.5225159151
52AcetylationRHYWVPAKRLFGGQI
CCCEEECHHHCCCHH
43.4919608861
52UbiquitinationRHYWVPAKRLFGGQI
CCCEEECHHHCCCHH
43.4919608861
91AcetylationFVRAGDPKLPVLYQV
EEECCCCCCCEEEEE
70.8923749302
96PhosphorylationDPKLPVLYQVERTRT
CCCCCEEEEEEECCC
15.678281689
101PhosphorylationVLYQVERTRTGSSFS
EEEEEEECCCCCCEE
21.0528102081
103PhosphorylationYQVERTRTGSSFSVR
EEEEECCCCCCEEEE
40.5828102081
105PhosphorylationVERTRTGSSFSVRSV
EEECCCCCCEEEEEE
27.8323312004
106PhosphorylationERTRTGSSFSVRSVK
EECCCCCCEEEEEEE
23.9228102081
111PhosphorylationGSSFSVRSVKAVQHG
CCCEEEEEEEEEECC
26.3022985185
169UbiquitinationLRDPNLQKRYPLALN
HHCCCHHHHHCCHHH
58.00-
188AcetylationQEVPIEIKPVNPSPL
CCCCCEEECCCCCCH
30.0726051181
188UbiquitinationQEVPIEIKPVNPSPL
CCCCCEEECCCCCCH
30.07-
311AcetylationQEGVIRVKPQVSESK
CCCEEEEECCCCCCC
21.6318525915
311MalonylationQEGVIRVKPQVSESK
CCCEEEEECCCCCCC
21.6326320211
315PhosphorylationIRVKPQVSESKL---
EEEECCCCCCCC---
30.7930108239
317PhosphorylationVKPQVSESKL-----
EECCCCCCCC-----
31.5830108239
318AcetylationKPQVSESKL------
ECCCCCCCC------
54.9119608861

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACOT8_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEF_HV1H2nefphysical
9153233
PML_HUMANPMLphysical
26186194
KLH23_HUMANKLHL23physical
26186194
PML_HUMANPMLphysical
28514442
KLH23_HUMANKLHL23physical
28514442

Drug and Disease Associations
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.
Regulatory Network of ACOT8_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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
ReferencePubMed
"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.

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