THIM_MOUSE - dbPTM
THIM_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THIM_MOUSE
UniProt AC Q8BWT1
Protein Name 3-ketoacyl-CoA thiolase, mitochondrial
Gene Name Acaa2
Organism Mus musculus (Mouse).
Sequence Length 397
Subcellular Localization Mitochondrion. Colocalizes with BNIP3 in the mitochondria..
Protein Description Abolishes BNIP3-mediated apoptosis and mitochondrial damage..
Protein Sequence MALLRGVFIVAAKRTPFGAYGGLLKDFSATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYCVRNVRFGTKFGLDLKLEDTLWAGLTDQHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPSVFKKDGTVTAGNASGVSDGAGAVIIASEDAVKKHNFTPLARVVGYFVSGCDPTIMGIGPVPAINGALKKAGLSLKDMDLIDVNEAFAPQFLSVQKALDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIALIIQNTA
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
13AcetylationGVFIVAAKRTPFGAY
CEEEEEEECCCCCCC
47.2523864654
13GlutarylationGVFIVAAKRTPFGAY
CEEEEEEECCCCCCC
47.2524703693
13SuccinylationGVFIVAAKRTPFGAY
CEEEEEEECCCCCCC
47.2523806337
25AcetylationGAYGGLLKDFSATDL
CCCCCCCCCCCCCCH
62.8723576753
25SuccinylationGAYGGLLKDFSATDL
CCCCCCCCCCCCCCH
62.87-
25SuccinylationGAYGGLLKDFSATDL
CCCCCCCCCCCCCCH
62.8723806337
28PhosphorylationGGLLKDFSATDLTEF
CCCCCCCCCCCHHHH
40.1521082442
30PhosphorylationLLKDFSATDLTEFAA
CCCCCCCCCHHHHHH
30.2823984901
33PhosphorylationDFSATDLTEFAARAA
CCCCCCHHHHHHHHH
31.6923984901
45AcetylationRAALSAGKVPPETID
HHHHHCCCCCHHHCC
51.8123806337
45SuccinylationRAALSAGKVPPETID
HHHHHCCCCCHHHCC
51.81-
45SuccinylationRAALSAGKVPPETID
HHHHHCCCCCHHHCC
51.8123806337
45UbiquitinationRAALSAGKVPPETID
HHHHHCCCCCHHHCC
51.81-
62PhosphorylationIVGNVMQSSSDAAYL
EECCCCCCCHHHHHH
17.4523140645
63PhosphorylationVGNVMQSSSDAAYLA
ECCCCCCCHHHHHHH
18.4923140645
64PhosphorylationGNVMQSSSDAAYLAR
CCCCCCCHHHHHHHH
36.1923140645
81PhosphorylationGLRVGVPTETGALTL
CCCCCCCCCCCCEEH
43.7129472430
83PhosphorylationRVGVPTETGALTLNR
CCCCCCCCCCEEHHH
30.1722324799
92S-palmitoylationALTLNRLCGSGFQSI
CEEHHHHHCCCHHHH
3.5328526873
103S-palmitoylationFQSIVSGCQEICSKD
HHHHHHCHHHHHCCC
2.2728526873
107S-palmitoylationVSGCQEICSKDAEVV
HHCHHHHHCCCCCEE
3.9928526873
109SuccinylationGCQEICSKDAEVVLC
CHHHHHCCCCCEEEE
57.4526388266
116S-palmitoylationKDAEVVLCGGTESMS
CCCCEEEECCCCCCC
2.9728526873
119PhosphorylationEVVLCGGTESMSQSP
CEEEECCCCCCCCCC
15.3523984901
121PhosphorylationVLCGGTESMSQSPYC
EEECCCCCCCCCCCE
24.4623984901
123PhosphorylationCGGTESMSQSPYCVR
ECCCCCCCCCCCEEE
36.4623984901
125PhosphorylationGTESMSQSPYCVRNV
CCCCCCCCCCEEEEE
15.5523984901
127PhosphorylationESMSQSPYCVRNVRF
CCCCCCCCEEEEECC
14.60-
128S-palmitoylationSMSQSPYCVRNVRFG
CCCCCCCEEEEECCC
2.3528526873
136PhosphorylationVRNVRFGTKFGLDLK
EEEECCCCCCCCCEE
22.0822817900
137AcetylationRNVRFGTKFGLDLKL
EEECCCCCCCCCEEE
37.5023576753
137GlutarylationRNVRFGTKFGLDLKL
EEECCCCCCCCCEEE
37.5024703693
137MalonylationRNVRFGTKFGLDLKL
EEECCCCCCCCCEEE
37.5026073543
137SuccinylationRNVRFGTKFGLDLKL
EEECCCCCCCCCEEE
37.50-
137SuccinylationRNVRFGTKFGLDLKL
EEECCCCCCCCCEEE
37.5023806337
137UbiquitinationRNVRFGTKFGLDLKL
EEECCCCCCCCCEEE
37.5027667366
143AcetylationTKFGLDLKLEDTLWA
CCCCCCEEEECCEEC
49.8823576753
143SuccinylationTKFGLDLKLEDTLWA
CCCCCCEEEECCEEC
49.88-
143SuccinylationTKFGLDLKLEDTLWA
CCCCCCEEEECCEEC
49.8823806337
158AcetylationGLTDQHVKLPMGMTA
CCCCCCEECCCCCCH
44.7623576753
158SuccinylationGLTDQHVKLPMGMTA
CCCCCCEECCCCCCH
44.76-
158SuccinylationGLTDQHVKLPMGMTA
CCCCCCEECCCCCCH
44.7623806337
171AcetylationTAENLAAKYNISRED
CHHHHHHHHCCCHHH
32.9723576753
171GlutarylationTAENLAAKYNISRED
CHHHHHHHHCCCHHH
32.9724703693
171MalonylationTAENLAAKYNISRED
CHHHHHHHHCCCHHH
32.9726320211
171SuccinylationTAENLAAKYNISRED
CHHHHHHHHCCCHHH
32.97-
171SuccinylationTAENLAAKYNISRED
CHHHHHHHHCCCHHH
32.9723806337
171UbiquitinationTAENLAAKYNISRED
CHHHHHHHHCCCHHH
32.9727667366
175PhosphorylationLAAKYNISREDCDRY
HHHHHCCCHHHHHHH
26.4473245785
179S-nitrosocysteineYNISREDCDRYALQS
HCCCHHHHHHHHHHH
2.48-
179S-nitrosylationYNISREDCDRYALQS
HCCCHHHHHHHHHHH
2.4822178444
179S-palmitoylationYNISREDCDRYALQS
HCCCHHHHHHHHHHH
2.4826165157
191AcetylationLQSQQRWKAANEAGY
HHHHHHHHHHHHHCC
39.5523806337
191GlutarylationLQSQQRWKAANEAGY
HHHHHHHHHHHHHCC
39.5524703693
191SuccinylationLQSQQRWKAANEAGY
HHHHHHHHHHHHHCC
39.55-
191SuccinylationLQSQQRWKAANEAGY
HHHHHHHHHHHHHCC
39.5523806337
191UbiquitinationLQSQQRWKAANEAGY
HHHHHHHHHHHHHCC
39.55-
198PhosphorylationKAANEAGYFNEEMAP
HHHHHHCCCCCCCCC
15.4120561251
209AcetylationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE
41.6623576753
209GlutarylationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE
41.6624703693
209MalonylationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE
41.6626073543
209SuccinylationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE
41.66-
209SuccinylationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE
41.6623806337
209UbiquitinationEMAPIEVKTKKGKQT
CCCCEEEEECCCCCE
41.66-
211AcetylationAPIEVKTKKGKQTMQ
CCEEEEECCCCCEEC
54.5323201123
211MalonylationAPIEVKTKKGKQTMQ
CCEEEEECCCCCEEC
54.5325418362
211SuccinylationAPIEVKTKKGKQTMQ
CCEEEEECCCCCEEC
54.53-
211SuccinylationAPIEVKTKKGKQTMQ
CCEEEEECCCCCEEC
54.5323806337
212AcetylationPIEVKTKKGKQTMQV
CEEEEECCCCCEECC
76.2723806337
212GlutarylationPIEVKTKKGKQTMQV
CEEEEECCCCCEECC
76.2724703693
212MalonylationPIEVKTKKGKQTMQV
CEEEEECCCCCEECC
76.2725418362
212SuccinylationPIEVKTKKGKQTMQV
CEEEEECCCCCEECC
76.27-
212SuccinylationPIEVKTKKGKQTMQV
CEEEEECCCCCEECC
76.2723806337
214AcetylationEVKTKKGKQTMQVDE
EEEECCCCCEECCCC
52.0223864654
214GlutarylationEVKTKKGKQTMQVDE
EEEECCCCCEECCCC
52.0224703693
214MalonylationEVKTKKGKQTMQVDE
EEEECCCCCEECCCC
52.0226320211
214SuccinylationEVKTKKGKQTMQVDE
EEEECCCCCEECCCC
52.02-
214SuccinylationEVKTKKGKQTMQVDE
EEEECCCCCEECCCC
52.0223806337
234AcetylationTTLEQLQKLPSVFKK
CHHHHHHCCCHHHCC
71.5923576753
234GlutarylationTTLEQLQKLPSVFKK
CHHHHHHCCCHHHCC
71.5924703693
234MalonylationTTLEQLQKLPSVFKK
CHHHHHHCCCHHHCC
71.5926073543
234SuccinylationTTLEQLQKLPSVFKK
CHHHHHHCCCHHHCC
71.59-
234SuccinylationTTLEQLQKLPSVFKK
CHHHHHHCCCHHHCC
71.5923806337
234UbiquitinationTTLEQLQKLPSVFKK
CHHHHHHCCCHHHCC
71.59-
237PhosphorylationEQLQKLPSVFKKDGT
HHHHCCCHHHCCCCC
51.0922817900
240AcetylationQKLPSVFKKDGTVTA
HCCCHHHCCCCCEEC
48.0424062335
240GlutarylationQKLPSVFKKDGTVTA
HCCCHHHCCCCCEEC
48.0424703693
240SuccinylationQKLPSVFKKDGTVTA
HCCCHHHCCCCCEEC
48.04-
240SuccinylationQKLPSVFKKDGTVTA
HCCCHHHCCCCCEEC
48.0423806337
241AcetylationKLPSVFKKDGTVTAG
CCCHHHCCCCCEECC
50.3423576753
241GlutarylationKLPSVFKKDGTVTAG
CCCHHHCCCCCEECC
50.3424703693
241MalonylationKLPSVFKKDGTVTAG
CCCHHHCCCCCEECC
50.3426073543
241UbiquitinationKLPSVFKKDGTVTAG
CCCHHHCCCCCEECC
50.34-
244PhosphorylationSVFKKDGTVTAGNAS
HHHCCCCCEECCCCC
25.4723984901
246PhosphorylationFKKDGTVTAGNASGV
HCCCCCEECCCCCCC
28.7823984901
251PhosphorylationTVTAGNASGVSDGAG
CEECCCCCCCCCCCC
43.6723984901
254PhosphorylationAGNASGVSDGAGAVI
CCCCCCCCCCCCEEE
33.5823984901
269AcetylationIASEDAVKKHNFTPL
EECHHHHHHCCCCHH
50.4623576753
269MalonylationIASEDAVKKHNFTPL
EECHHHHHHCCCCHH
50.4626320211
269SuccinylationIASEDAVKKHNFTPL
EECHHHHHHCCCCHH
50.4626388266
270AcetylationASEDAVKKHNFTPLA
ECHHHHHHCCCCHHH
36.8623576753
270GlutarylationASEDAVKKHNFTPLA
ECHHHHHHCCCCHHH
36.8624703693
270MalonylationASEDAVKKHNFTPLA
ECHHHHHHCCCCHHH
36.8626320211
270UbiquitinationASEDAVKKHNFTPLA
ECHHHHHHCCCCHHH
36.8627667366
274PhosphorylationAVKKHNFTPLARVVG
HHHHCCCCHHHHHHH
23.789509249
287S-nitrosocysteineVGYFVSGCDPTIMGI
HHHHHHCCCCCCCCC
4.39-
287S-nitrosylationVGYFVSGCDPTIMGI
HHHHHHCCCCCCCCC
4.3922178444
287S-palmitoylationVGYFVSGCDPTIMGI
HHHHHHCCCCCCCCC
4.3928526873
305AcetylationPAINGALKKAGLSLK
HHHCHHHHHCCCCCC
39.7923576753
305SuccinylationPAINGALKKAGLSLK
HHHCHHHHHCCCCCC
39.79-
305SuccinylationPAINGALKKAGLSLK
HHHCHHHHHCCCCCC
39.7923806337
305UbiquitinationPAINGALKKAGLSLK
HHHCHHHHHCCCCCC
39.79-
306AcetylationAINGALKKAGLSLKD
HHCHHHHHCCCCCCC
48.8424062335
306SuccinylationAINGALKKAGLSLKD
HHCHHHHHCCCCCCC
48.8424315375
310PhosphorylationALKKAGLSLKDMDLI
HHHHCCCCCCCCCEE
32.2425266776
312AcetylationKKAGLSLKDMDLIDV
HHCCCCCCCCCEECC
47.8623576753
312SuccinylationKKAGLSLKDMDLIDV
HHCCCCCCCCCEECC
47.86-
312SuccinylationKKAGLSLKDMDLIDV
HHCCCCCCCCCEECC
47.8623806337
312UbiquitinationKKAGLSLKDMDLIDV
HHCCCCCCCCCEECC
47.86-
329PhosphorylationAFAPQFLSVQKALDL
HHHHHHHCHHHHHCC
24.6423984901
332AcetylationPQFLSVQKALDLDPS
HHHHCHHHHHCCCCC
49.0822733758
332SuccinylationPQFLSVQKALDLDPS
HHHHCHHHHHCCCCC
49.0826388266
339PhosphorylationKALDLDPSKTNVSGG
HHHCCCCCCCCCCCC
52.3523737553
340AcetylationALDLDPSKTNVSGGA
HHCCCCCCCCCCCCE
49.8923576753
340SuccinylationALDLDPSKTNVSGGA
HHCCCCCCCCCCCCE
49.8924315375
340UbiquitinationALDLDPSKTNVSGGA
HHCCCCCCCCCCCCE
49.89-
341PhosphorylationLDLDPSKTNVSGGAI
HCCCCCCCCCCCCEE
45.2321082442
344PhosphorylationDPSKTNVSGGAIALG
CCCCCCCCCCEEEEC
33.3117208939
357PhosphorylationLGHPLGGSGSRITAH
ECCCCCCCCCHHHHH
31.6273244741
375AcetylationELRRRGGKYAVGSAC
HHHHCCCCEEEECEE
32.6223576753
382S-palmitoylationKYAVGSACIGGGQGI
CEEEECEEECCCCEE
2.9626165157

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 THIM_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 THIM_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of THIM_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THIM_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-270, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASSSPECTROMETRY.

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