ACOT2_HUMAN - dbPTM
ACOT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACOT2_HUMAN
UniProt AC P49753
Protein Name Acyl-coenzyme A thioesterase 2, mitochondrial
Gene Name ACOT2
Organism Homo sapiens (Human).
Sequence Length 483
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. Displays high levels of activity on medium- and long chain acyl CoAs..
Protein Sequence MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVPARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRIKVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPETGHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIPSKV
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
7Phosphorylation-MSNKLLSPHPHSVV
-CCCCCCCCCCCCEE		31.4425159151
23PhosphorylationRSEFKMASSPAVLRA
CHHCHHCCCHHHHHH		33.1024972180
24PhosphorylationSEFKMASSPAVLRAS
HHCHHCCCHHHHHHH		13.8246157907
47PhosphorylationSSAQFLGSPQLRQVG
HHHHHHCCHHHHHHC		16.1863755645
66PhosphorylationVPARMAATLILEPAG
HCHHHHHHHEEECCC		12.5646157913
86MethylationEPVRIAVRGLAPEQP
CCCEEEEECCCCCCC		25.94-
99PhosphorylationQPVTLRASLRDEKGA
CCEEEEEEECCCCCC		19.9423532336
104AcetylationRASLRDEKGALFQAH
EEEECCCCCCHHHHH		54.4923236377
104SuccinylationRASLRDEKGALFQAH
EEEECCCCCCHHHHH		54.4923954790
104MalonylationRASLRDEKGALFQAH
EEEECCCCCCHHHHH		54.4926320211
114PhosphorylationLFQAHARYRADTLGE
HHHHHHHHCCCCCCC		15.7827251275
118PhosphorylationHARYRADTLGELDLE
HHHHCCCCCCCCCHH		35.3630266825
148UbiquitinationGLLWALEPEKPLVRL
CCHHHCCCCCCCCHH		56.6222817900
151UbiquitinationWALEPEKPLVRLVKR
HHCCCCCCCCHHHHC		34.1321890473
162PhosphorylationLVKRDVRTPLAVELE
HHHCCCCCCEEEEEE		23.6272593193
166 (in isoform 2)Ubiquitination-13.0521890473
171UbiquitinationLAVELEVLDGHDPDP
EEEEEEEECCCCCCC		4.8221963094
228PhosphorylationGIVDMFGTGGGLLEY
CCEECCCCCCCHHHH		22.7622210691
265UbiquitinationLPKTMETLHLEYFEE
CCCHHHHHCHHHHHH		2.5021963094
294PhosphorylationGVGLLGISKGGELCL
CEEEEEECCHHHHHH		24.3769006205
305PhosphorylationELCLSMASFLKGITA
HHHHHHHHHHCCCCE		23.5924719451
319PhosphorylationAAVVINGSVANVGGT
EEEEECCEEECCCCE		17.36-
345UbiquitinationGVNRNRIKVTKDGYA
CCCCCCEEECCCCCC		40.3822817900
348UbiquitinationRNRIKVTKDGYADIV
CCCEEECCCCCCHHH		52.7421890473
348 (in isoform 1)Ubiquitination-52.7421890473
351PhosphorylationIKVTKDGYADIVDVL
EEECCCCCCHHHHHH		15.96-
368UbiquitinationPLEGPDQKSFIPVER
CCCCCCCCCCCCHHH		55.5021963094
402AcetylationFYANEACKRLQAHGR
HHHHHHHHHHHHCCC		64.2930584489
462UbiquitinationMAQVDAWKQLQTFFH
HHHHHHHHHHHHHHH		42.7421963094
462AcetylationMAQVDAWKQLQTFFH
HHHHHHHHHHHHHHH		42.7430584495
470SuccinylationQLQTFFHKHLGGHEG
HHHHHHHHHHCCCCC		35.05-
470SuccinylationQLQTFFHKHLGGHEG
HHHHHHHHHHCCCCC		35.05-
481PhosphorylationGHEGTIPSKV-----
CCCCCCCCCC-----		42.0524719451
482UbiquitinationHEGTIPSKV------
CCCCCCCCC------		46.7629967540
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 ACOT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACOT2_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 ACOT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACOT1_HUMANACOT1physical
28514442
SPT33_HUMANSPATA33physical
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 ACOT2_HUMAN

loading...

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-104, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory