ACOT9_HUMAN - dbPTM
ACOT9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACOT9_HUMAN
UniProt AC Q9Y305
Protein Name Acyl-coenzyme A thioesterase 9, mitochondrial
Gene Name ACOT9
Organism Homo sapiens (Human).
Sequence Length 439
Subcellular Localization Mitochondrion.
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 on long chain acyl-CoAs..
Protein Sequence MRRAALRLCALGKGQLTPGRGLTQGPQNPKKQGIFHIHEVRDKLREIVGASTNWRDHVKAMEERKLLHSFLAKSQDGLPPRRMKDSYIEVLLPLGSEPELREKYLTVQNTVRFGRILEDLDSLGVLICYMHNKIHSAKMSPLSIVTALVDKIDMCKKSLSPEQDIKFSGHVSWVGKTSMEVKMQMFQLHGDEFCPVLDATFVMVARDSENKGPAFVNPLIPESPEEEELFRQGELNKGRRIAFSSTSLLKMAPSAEERTTIHEMFLSTLDPKTISFRSRVLPSNAVWMENSKLKSLEICHPQERNIFNRIFGGFLMRKAYELAWATACSFGGSRPFVVAVDDIMFQKPVEVGSLLFLSSQVCFTQNNYIQVRVHSEVASLQEKQHTTTNVFHFTFMSEKEVPLVFPKTYGESMLYLDGQRHFNSMSGPATLRKDYLVEP
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
5Ubiquitination---MRRAALRLCALG
---CCHHHHHHHHCC		7.4521890473
13UbiquitinationLRLCALGKGQLTPGR
HHHHHCCCCCCCCCC		44.3121890473
13 (in isoform 3)Ubiquitination-44.3121890473
23PhosphorylationLTPGRGLTQGPQNPK
CCCCCCCCCCCCCCC		34.0146157931
26 (in isoform 2)Ubiquitination-22.4321890473
32 (in isoform 2)Ubiquitination-57.2321890473
40 (in isoform 2)Ubiquitination-6.2421890473
59UbiquitinationTNWRDHVKAMEERKL
CCHHHHHHHHHHHHH		38.3022817900
59 (in isoform 1)Ubiquitination-38.3021890473
65UbiquitinationVKAMEERKLLHSFLA
HHHHHHHHHHHHHHH		59.6922817900
65 (in isoform 1)Ubiquitination-59.6921890473
68UbiquitinationMEERKLLHSFLAKSQ
HHHHHHHHHHHHHCC		27.2621890473
68 (in isoform 4)Ubiquitination-27.26-
69PhosphorylationEERKLLHSFLAKSQD
HHHHHHHHHHHHCCC		23.1724719451
73UbiquitinationLLHSFLAKSQDGLPP
HHHHHHHHCCCCCCC		51.2873
73 (in isoform 1)Ubiquitination-51.2821890473
74UbiquitinationLHSFLAKSQDGLPPR
HHHHHHHCCCCCCCC		28.0921890473
74 (in isoform 4)Ubiquitination-28.09-
78UbiquitinationLAKSQDGLPPRRMKD
HHHCCCCCCCCCCCC		7.6921890473
78 (in isoform 3)Ubiquitination-7.6921890473
82UbiquitinationQDGLPPRRMKDSYIE
CCCCCCCCCCCCEEE		42.1321890473
82 (in isoform 4)Ubiquitination-42.13-
87PhosphorylationPRRMKDSYIEVLLPL
CCCCCCCEEEEEEEC		15.9683553
96PhosphorylationEVLLPLGSEPELREK
EEEEECCCCHHHHHH		58.63108430773
97UbiquitinationVLLPLGSEPELREKY
EEEECCCCHHHHHHH		40.7829967540
103AcetylationSEPELREKYLTVQNT
CCHHHHHHHEECCCH		38.8419608861
103MalonylationSEPELREKYLTVQNT
CCHHHHHHHEECCCH		38.8426320211
103SuccinylationSEPELREKYLTVQNT
CCHHHHHHHEECCCH		38.8427452117
104PhosphorylationEPELREKYLTVQNTV
CHHHHHHHEECCCHH		11.6755817215
105 (in isoform 2)Ubiquitination-5.8321890473
106PhosphorylationELREKYLTVQNTVRF
HHHHHHEECCCHHHH		19.5620639409
110PhosphorylationKYLTVQNTVRFGRIL
HHEECCCHHHHHHHH		8.9320639409
112AcetylationLTVQNTVRFGRILED
EECCCHHHHHHHHHH		26.6819608861
122PhosphorylationRILEDLDSLGVLICY
HHHHHHHHHCHHHHH		34.0329083192
129PhosphorylationSLGVLICYMHNKIHS
HHCHHHHHHHCCHHC		8.4029083192
133UbiquitinationLICYMHNKIHSAKMS
HHHHHHCCHHCCCCC		27.4122817900
138UbiquitinationHNKIHSAKMSPLSIV
HCCHHCCCCCHHHHH		42.8121890473
138 (in isoform 1)Ubiquitination-42.8121890473
142UbiquitinationHSAKMSPLSIVTALV
HCCCCCHHHHHHHHH		4.2422817900
147UbiquitinationSPLSIVTALVDKIDM
CHHHHHHHHHHHHHH		8.4921890473
147 (in isoform 4)Ubiquitination-8.49-
151UbiquitinationIVTALVDKIDMCKKS
HHHHHHHHHHHHCCC		32.8821963094
151 (in isoform 3)Ubiquitination-32.8821890473
156AcetylationVDKIDMCKKSLSPEQ
HHHHHHHCCCCCHHH		38.477406693
157AcetylationDKIDMCKKSLSPEQD
HHHHHHCCCCCHHHC		52.2619608861
157MalonylationDKIDMCKKSLSPEQD
HHHHHHCCCCCHHHC		52.2626320211
157SuccinylationDKIDMCKKSLSPEQD
HHHHHHCCCCCHHHC		52.2627452117
157UbiquitinationDKIDMCKKSLSPEQD
HHHHHHCCCCCHHHC		52.2619608861
158PhosphorylationKIDMCKKSLSPEQDI
HHHHHCCCCCHHHCC		21.4123312004
160PhosphorylationDMCKKSLSPEQDIKF
HHHCCCCCHHHCCEE		33.2221815630
166AcetylationLSPEQDIKFSGHVSW
CCHHHCCEECEEEEE		41.5930585521
166UbiquitinationLSPEQDIKFSGHVSW
CCHHHCCEECEEEEE		41.5929967540
177UbiquitinationHVSWVGKTSMEVKMQ
EEEECCCCCHHHHHH		27.6427667366
178 (in isoform 2)Ubiquitination-19.2121890473
190UbiquitinationMQMFQLHGDEFCPVL
HHHHHHHCCCCCCCC		44.7421890473
190 (in isoform 3)Ubiquitination-44.7421890473
211UbiquitinationVARDSENKGPAFVNP
EEECCCCCCCCCCCC		63.3221906983
211 (in isoform 1)Ubiquitination-63.3221890473
212UbiquitinationARDSENKGPAFVNPL
EECCCCCCCCCCCCC		30.2821890473
212 (in isoform 3)Ubiquitination-30.2821890473
217 (in isoform 2)Ubiquitination-21.1421890473
220UbiquitinationPAFVNPLIPESPEEE
CCCCCCCCCCCHHHH		3.6221963094
223PhosphorylationVNPLIPESPEEEELF
CCCCCCCCHHHHHHH		32.0526657352
232 (in isoform 4)Phosphorylation-42.2427251275
237UbiquitinationFRQGELNKGRRIAFS
HHCCCCCCCCEEEEE		67.4327667366
239 (in isoform 2)Ubiquitination-28.5721890473
244PhosphorylationKGRRIAFSSTSLLKM
CCCEEEEECHHHHHC		24.5521406692
245PhosphorylationGRRIAFSSTSLLKMA
CCEEEEECHHHHHCC		18.6321406692
246PhosphorylationRRIAFSSTSLLKMAP
CEEEEECHHHHHCCC		23.3821406692
246UbiquitinationRRIAFSSTSLLKMAP
CEEEEECHHHHHCCC		23.3827667366
247PhosphorylationRIAFSSTSLLKMAPS
EEEEECHHHHHCCCC		33.3830576142
250AcetylationFSSTSLLKMAPSAEE
EECHHHHHCCCCHHH		38.0119608861
250UbiquitinationFSSTSLLKMAPSAEE
EECHHHHHCCCCHHH		38.0122817900
250 (in isoform 1)Ubiquitination-38.0121890473
259AcetylationAPSAEERTTIHEMFL
CCCHHHCCCHHHHHH		33.1219608861
259UbiquitinationAPSAEERTTIHEMFL
CCCHHHCCCHHHHHH		33.1221890473
259 (in isoform 4)Ubiquitination-33.12-
272AcetylationFLSTLDPKTISFRSR
HHHCCCCCCCEECCC		59.1523236377
272UbiquitinationFLSTLDPKTISFRSR
HHHCCCCCCCEECCC		59.1522817900
272 (in isoform 1)Ubiquitination-59.1521890473
273PhosphorylationLSTLDPKTISFRSRV
HHCCCCCCCEECCCC		27.5223927012
275PhosphorylationTLDPKTISFRSRVLP
CCCCCCCEECCCCCC		21.6029496963
278PhosphorylationPKTISFRSRVLPSNA
CCCCEECCCCCCCCC		25.4029978859
281UbiquitinationISFRSRVLPSNAVWM
CEECCCCCCCCCEEE		3.6021890473
281 (in isoform 4)Ubiquitination-3.60-
283PhosphorylationFRSRVLPSNAVWMEN
ECCCCCCCCCEEECC		33.0129978859
284 (in isoform 4)Phosphorylation-36.2524719451
292AcetylationAVWMENSKLKSLEIC
CEEECCCCCCCCEEC		72.0825825284
294MalonylationWMENSKLKSLEICHP
EECCCCCCCCEECCH		57.6526320211
294SuccinylationWMENSKLKSLEICHP
EECCCCCCCCEECCH		57.6527452117
347UbiquitinationVDDIMFQKPVEVGSL
EEHHEECCCCCCCCE		39.5023503661
374 (in isoform 2)Ubiquitination-14.00-
375PhosphorylationYIQVRVHSEVASLQE
EEEEEEEHHHHHHHH		30.8037817017
379PhosphorylationRVHSEVASLQEKQHT
EEEHHHHHHHHCEEC		35.4421406692
386PhosphorylationSLQEKQHTTTNVFHF
HHHHCEECCCCEEEE		32.59110760849
407AcetylationEVPLVFPKTYGESML
CCCEEECCCCCCCEE		42.8023954790
407MalonylationEVPLVFPKTYGESML
CCCEEECCCCCCCEE		42.8026320211
407SuccinylationEVPLVFPKTYGESML
CCCEEECCCCCCCEE		42.8027452117
407UbiquitinationEVPLVFPKTYGESML
CCCEEECCCCCCCEE		42.8023503661
416AcetylationYGESMLYLDGQRHFN
CCCCEEEECCCCCCC		5.4119608861
416UbiquitinationYGESMLYLDGQRHFN
CCCCEEEECCCCCCC		5.4123503661
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 ACOT9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACOT9_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 ACOT9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACOT9_HUMAN !!
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 ACOT9_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-103; LYS-157; LYS-250 ANDLYS-407, AND MASS SPECTROMETRY.

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