ACOT1_HUMAN - dbPTM
ACOT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACOT1_HUMAN
UniProt AC Q86TX2
Protein Name Acyl-coenzyme A thioesterase 1
Gene Name ACOT1
Organism Homo sapiens (Human).
Sequence Length 421
Subcellular Localization Cytoplasm .
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. Active towards fatty acyl-CoA with chain-lengths of C12-C16 (By similarity)..
Protein Sequence MAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLLCRVRHERYFLPPGVRREPVRAGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAVNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLRYKGETLPPVGVNRNRIKVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPETGHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIPSKV
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
24MethylationEPVRIAVRGLAPEQP
CCCEEEEECCCCCCC
25.94-
37PhosphorylationQPVTLRASLRDEKGA
CCEEEEEEECCCCCC
19.9423532336
42AcetylationRASLRDEKGALFQAH
EEEECCCCCCHHHHH
54.492403393
52PhosphorylationLFQAHARYRADTLGE
HHHHHHHHCCCCCCC
15.7827251275
56PhosphorylationHARYRADTLGELDLE
HHHHCCCCCCCCCHH
35.3630266825
100PhosphorylationLVKRDVRTPLAVELE
HHHCCCCCCEEEEEE
23.6272593193
166PhosphorylationGIVDMFGTGGGLLEY
CCEECCCCCCCHHHH
22.7622210691
232PhosphorylationGVGLLGISKGGELCL
CEEEEEECCHHHHHH
24.3724275569
240PhosphorylationKGGELCLSMASFLKG
CHHHHHHHHHHHHCC
16.0022210691
243PhosphorylationELCLSMASFLKGITA
HHHHHHHHHHCCCCE
23.5924719451
257PhosphorylationAAVVINGSVANVGGT
EEEEECCEEECCCCE
17.3669214229
264PhosphorylationSVANVGGTLRYKGET
EEECCCCEEEECCCC
11.3522210691
267PhosphorylationNVGGTLRYKGETLPP
CCCCEEEECCCCCCC
26.8522210691
286UbiquitinationRNRIKVTKDGYADIV
CCCEEECCCCCCHHH
52.7421890473
289PhosphorylationIKVTKDGYADIVDVL
EEECCCCCCHHHHHH
15.96-
306UbiquitinationPLEGPDQKSFIPVER
CCCCCCCCCCCCHHH
55.50-
340AcetylationFYANEACKRLQAHGR
HHHHHHHHHHHHCCC
64.2930585289
400AcetylationMAQVDAWKQLQTFFH
HHHHHHHHHHHHHHH
42.7430585295
416O-linked_GlycosylationHLGGHEGTIPSKV--
HHCCCCCCCCCCC--
27.08OGP
419PhosphorylationGHEGTIPSKV-----
CCCCCCCCCC-----
42.0524719451
420UbiquitinationHEGTIPSKV------
CCCCCCCCC------
46.76-
4202-HydroxyisobutyrylationHEGTIPSKV------
CCCCCCCCC------
46.76-

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 ACOT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACOT1_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 ACOT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CXAR_HUMANCXADRphysical
22939629
HIBCH_HUMANHIBCHphysical
22939629

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 ACOT1_HUMAN

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Related Literatures of Post-Translational Modification

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