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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
13 | Acetylation | GVFIVAAKRTPFGAY CEEEEEEECCCCCCC | 47.25 | 23864654 | |
13 | Glutarylation | GVFIVAAKRTPFGAY CEEEEEEECCCCCCC | 47.25 | 24703693 | |
13 | Succinylation | GVFIVAAKRTPFGAY CEEEEEEECCCCCCC | 47.25 | 23806337 | |
25 | Acetylation | GAYGGLLKDFSATDL CCCCCCCCCCCCCCH | 62.87 | 23576753 | |
25 | Succinylation | GAYGGLLKDFSATDL CCCCCCCCCCCCCCH | 62.87 | - | |
25 | Succinylation | GAYGGLLKDFSATDL CCCCCCCCCCCCCCH | 62.87 | 23806337 | |
28 | Phosphorylation | GGLLKDFSATDLTEF CCCCCCCCCCCHHHH | 40.15 | 21082442 | |
30 | Phosphorylation | LLKDFSATDLTEFAA CCCCCCCCCHHHHHH | 30.28 | 23984901 | |
33 | Phosphorylation | DFSATDLTEFAARAA CCCCCCHHHHHHHHH | 31.69 | 23984901 | |
45 | Acetylation | RAALSAGKVPPETID HHHHHCCCCCHHHCC | 51.81 | 23806337 | |
45 | Succinylation | RAALSAGKVPPETID HHHHHCCCCCHHHCC | 51.81 | - | |
45 | Succinylation | RAALSAGKVPPETID HHHHHCCCCCHHHCC | 51.81 | 23806337 | |
45 | Ubiquitination | RAALSAGKVPPETID HHHHHCCCCCHHHCC | 51.81 | - | |
62 | Phosphorylation | IVGNVMQSSSDAAYL EECCCCCCCHHHHHH | 17.45 | 23140645 | |
63 | Phosphorylation | VGNVMQSSSDAAYLA ECCCCCCCHHHHHHH | 18.49 | 23140645 | |
64 | Phosphorylation | GNVMQSSSDAAYLAR CCCCCCCHHHHHHHH | 36.19 | 23140645 | |
81 | Phosphorylation | GLRVGVPTETGALTL CCCCCCCCCCCCEEH | 43.71 | 29472430 | |
83 | Phosphorylation | RVGVPTETGALTLNR CCCCCCCCCCEEHHH | 30.17 | 22324799 | |
92 | S-palmitoylation | ALTLNRLCGSGFQSI CEEHHHHHCCCHHHH | 3.53 | 28526873 | |
103 | S-palmitoylation | FQSIVSGCQEICSKD HHHHHHCHHHHHCCC | 2.27 | 28526873 | |
107 | S-palmitoylation | VSGCQEICSKDAEVV HHCHHHHHCCCCCEE | 3.99 | 28526873 | |
109 | Succinylation | GCQEICSKDAEVVLC CHHHHHCCCCCEEEE | 57.45 | 26388266 | |
116 | S-palmitoylation | KDAEVVLCGGTESMS CCCCEEEECCCCCCC | 2.97 | 28526873 | |
119 | Phosphorylation | EVVLCGGTESMSQSP CEEEECCCCCCCCCC | 15.35 | 23984901 | |
121 | Phosphorylation | VLCGGTESMSQSPYC EEECCCCCCCCCCCE | 24.46 | 23984901 | |
123 | Phosphorylation | CGGTESMSQSPYCVR ECCCCCCCCCCCEEE | 36.46 | 23984901 | |
125 | Phosphorylation | GTESMSQSPYCVRNV CCCCCCCCCCEEEEE | 15.55 | 23984901 | |
127 | Phosphorylation | ESMSQSPYCVRNVRF CCCCCCCCEEEEECC | 14.60 | - | |
128 | S-palmitoylation | SMSQSPYCVRNVRFG CCCCCCCEEEEECCC | 2.35 | 28526873 | |
136 | Phosphorylation | VRNVRFGTKFGLDLK EEEECCCCCCCCCEE | 22.08 | 22817900 | |
137 | Acetylation | RNVRFGTKFGLDLKL EEECCCCCCCCCEEE | 37.50 | 23576753 | |
137 | Glutarylation | RNVRFGTKFGLDLKL EEECCCCCCCCCEEE | 37.50 | 24703693 | |
137 | Malonylation | RNVRFGTKFGLDLKL EEECCCCCCCCCEEE | 37.50 | 26073543 | |
137 | Succinylation | RNVRFGTKFGLDLKL EEECCCCCCCCCEEE | 37.50 | - | |
137 | Succinylation | RNVRFGTKFGLDLKL EEECCCCCCCCCEEE | 37.50 | 23806337 | |
137 | Ubiquitination | RNVRFGTKFGLDLKL EEECCCCCCCCCEEE | 37.50 | 27667366 | |
143 | Acetylation | TKFGLDLKLEDTLWA CCCCCCEEEECCEEC | 49.88 | 23576753 | |
143 | Succinylation | TKFGLDLKLEDTLWA CCCCCCEEEECCEEC | 49.88 | - | |
143 | Succinylation | TKFGLDLKLEDTLWA CCCCCCEEEECCEEC | 49.88 | 23806337 | |
158 | Acetylation | GLTDQHVKLPMGMTA CCCCCCEECCCCCCH | 44.76 | 23576753 | |
158 | Succinylation | GLTDQHVKLPMGMTA CCCCCCEECCCCCCH | 44.76 | - | |
158 | Succinylation | GLTDQHVKLPMGMTA CCCCCCEECCCCCCH | 44.76 | 23806337 | |
171 | Acetylation | TAENLAAKYNISRED CHHHHHHHHCCCHHH | 32.97 | 23576753 | |
171 | Glutarylation | TAENLAAKYNISRED CHHHHHHHHCCCHHH | 32.97 | 24703693 | |
171 | Malonylation | TAENLAAKYNISRED CHHHHHHHHCCCHHH | 32.97 | 26320211 | |
171 | Succinylation | TAENLAAKYNISRED CHHHHHHHHCCCHHH | 32.97 | - | |
171 | Succinylation | TAENLAAKYNISRED CHHHHHHHHCCCHHH | 32.97 | 23806337 | |
171 | Ubiquitination | TAENLAAKYNISRED CHHHHHHHHCCCHHH | 32.97 | 27667366 | |
175 | Phosphorylation | LAAKYNISREDCDRY HHHHHCCCHHHHHHH | 26.44 | 73245785 | |
179 | S-nitrosocysteine | YNISREDCDRYALQS HCCCHHHHHHHHHHH | 2.48 | - | |
179 | S-nitrosylation | YNISREDCDRYALQS HCCCHHHHHHHHHHH | 2.48 | 22178444 | |
179 | S-palmitoylation | YNISREDCDRYALQS HCCCHHHHHHHHHHH | 2.48 | 26165157 | |
191 | Acetylation | LQSQQRWKAANEAGY HHHHHHHHHHHHHCC | 39.55 | 23806337 | |
191 | Glutarylation | LQSQQRWKAANEAGY HHHHHHHHHHHHHCC | 39.55 | 24703693 | |
191 | Succinylation | LQSQQRWKAANEAGY HHHHHHHHHHHHHCC | 39.55 | - | |
191 | Succinylation | LQSQQRWKAANEAGY HHHHHHHHHHHHHCC | 39.55 | 23806337 | |
191 | Ubiquitination | LQSQQRWKAANEAGY HHHHHHHHHHHHHCC | 39.55 | - | |
198 | Phosphorylation | KAANEAGYFNEEMAP HHHHHHCCCCCCCCC | 15.41 | 20561251 | |
209 | Acetylation | EMAPIEVKTKKGKQT CCCCEEEEECCCCCE | 41.66 | 23576753 | |
209 | Glutarylation | EMAPIEVKTKKGKQT CCCCEEEEECCCCCE | 41.66 | 24703693 | |
209 | Malonylation | EMAPIEVKTKKGKQT CCCCEEEEECCCCCE | 41.66 | 26073543 | |
209 | Succinylation | EMAPIEVKTKKGKQT CCCCEEEEECCCCCE | 41.66 | - | |
209 | Succinylation | EMAPIEVKTKKGKQT CCCCEEEEECCCCCE | 41.66 | 23806337 | |
209 | Ubiquitination | EMAPIEVKTKKGKQT CCCCEEEEECCCCCE | 41.66 | - | |
211 | Acetylation | APIEVKTKKGKQTMQ CCEEEEECCCCCEEC | 54.53 | 23201123 | |
211 | Malonylation | APIEVKTKKGKQTMQ CCEEEEECCCCCEEC | 54.53 | 25418362 | |
211 | Succinylation | APIEVKTKKGKQTMQ CCEEEEECCCCCEEC | 54.53 | - | |
211 | Succinylation | APIEVKTKKGKQTMQ CCEEEEECCCCCEEC | 54.53 | 23806337 | |
212 | Acetylation | PIEVKTKKGKQTMQV CEEEEECCCCCEECC | 76.27 | 23806337 | |
212 | Glutarylation | PIEVKTKKGKQTMQV CEEEEECCCCCEECC | 76.27 | 24703693 | |
212 | Malonylation | PIEVKTKKGKQTMQV CEEEEECCCCCEECC | 76.27 | 25418362 | |
212 | Succinylation | PIEVKTKKGKQTMQV CEEEEECCCCCEECC | 76.27 | - | |
212 | Succinylation | PIEVKTKKGKQTMQV CEEEEECCCCCEECC | 76.27 | 23806337 | |
214 | Acetylation | EVKTKKGKQTMQVDE EEEECCCCCEECCCC | 52.02 | 23864654 | |
214 | Glutarylation | EVKTKKGKQTMQVDE EEEECCCCCEECCCC | 52.02 | 24703693 | |
214 | Malonylation | EVKTKKGKQTMQVDE EEEECCCCCEECCCC | 52.02 | 26320211 | |
214 | Succinylation | EVKTKKGKQTMQVDE EEEECCCCCEECCCC | 52.02 | - | |
214 | Succinylation | EVKTKKGKQTMQVDE EEEECCCCCEECCCC | 52.02 | 23806337 | |
234 | Acetylation | TTLEQLQKLPSVFKK CHHHHHHCCCHHHCC | 71.59 | 23576753 | |
234 | Glutarylation | TTLEQLQKLPSVFKK CHHHHHHCCCHHHCC | 71.59 | 24703693 | |
234 | Malonylation | TTLEQLQKLPSVFKK CHHHHHHCCCHHHCC | 71.59 | 26073543 | |
234 | Succinylation | TTLEQLQKLPSVFKK CHHHHHHCCCHHHCC | 71.59 | - | |
234 | Succinylation | TTLEQLQKLPSVFKK CHHHHHHCCCHHHCC | 71.59 | 23806337 | |
234 | Ubiquitination | TTLEQLQKLPSVFKK CHHHHHHCCCHHHCC | 71.59 | - | |
237 | Phosphorylation | EQLQKLPSVFKKDGT HHHHCCCHHHCCCCC | 51.09 | 22817900 | |
240 | Acetylation | QKLPSVFKKDGTVTA HCCCHHHCCCCCEEC | 48.04 | 24062335 | |
240 | Glutarylation | QKLPSVFKKDGTVTA HCCCHHHCCCCCEEC | 48.04 | 24703693 | |
240 | Succinylation | QKLPSVFKKDGTVTA HCCCHHHCCCCCEEC | 48.04 | - | |
240 | Succinylation | QKLPSVFKKDGTVTA HCCCHHHCCCCCEEC | 48.04 | 23806337 | |
241 | Acetylation | KLPSVFKKDGTVTAG CCCHHHCCCCCEECC | 50.34 | 23576753 | |
241 | Glutarylation | KLPSVFKKDGTVTAG CCCHHHCCCCCEECC | 50.34 | 24703693 | |
241 | Malonylation | KLPSVFKKDGTVTAG CCCHHHCCCCCEECC | 50.34 | 26073543 | |
241 | Ubiquitination | KLPSVFKKDGTVTAG CCCHHHCCCCCEECC | 50.34 | - | |
244 | Phosphorylation | SVFKKDGTVTAGNAS HHHCCCCCEECCCCC | 25.47 | 23984901 | |
246 | Phosphorylation | FKKDGTVTAGNASGV HCCCCCEECCCCCCC | 28.78 | 23984901 | |
251 | Phosphorylation | TVTAGNASGVSDGAG CEECCCCCCCCCCCC | 43.67 | 23984901 | |
254 | Phosphorylation | AGNASGVSDGAGAVI CCCCCCCCCCCCEEE | 33.58 | 23984901 | |
269 | Acetylation | IASEDAVKKHNFTPL EECHHHHHHCCCCHH | 50.46 | 23576753 | |
269 | Malonylation | IASEDAVKKHNFTPL EECHHHHHHCCCCHH | 50.46 | 26320211 | |
269 | Succinylation | IASEDAVKKHNFTPL EECHHHHHHCCCCHH | 50.46 | 26388266 | |
270 | Acetylation | ASEDAVKKHNFTPLA ECHHHHHHCCCCHHH | 36.86 | 23576753 | |
270 | Glutarylation | ASEDAVKKHNFTPLA ECHHHHHHCCCCHHH | 36.86 | 24703693 | |
270 | Malonylation | ASEDAVKKHNFTPLA ECHHHHHHCCCCHHH | 36.86 | 26320211 | |
270 | Ubiquitination | ASEDAVKKHNFTPLA ECHHHHHHCCCCHHH | 36.86 | 27667366 | |
274 | Phosphorylation | AVKKHNFTPLARVVG HHHHCCCCHHHHHHH | 23.78 | 9509249 | |
287 | S-nitrosocysteine | VGYFVSGCDPTIMGI HHHHHHCCCCCCCCC | 4.39 | - | |
287 | S-nitrosylation | VGYFVSGCDPTIMGI HHHHHHCCCCCCCCC | 4.39 | 22178444 | |
287 | S-palmitoylation | VGYFVSGCDPTIMGI HHHHHHCCCCCCCCC | 4.39 | 28526873 | |
305 | Acetylation | PAINGALKKAGLSLK HHHCHHHHHCCCCCC | 39.79 | 23576753 | |
305 | Succinylation | PAINGALKKAGLSLK HHHCHHHHHCCCCCC | 39.79 | - | |
305 | Succinylation | PAINGALKKAGLSLK HHHCHHHHHCCCCCC | 39.79 | 23806337 | |
305 | Ubiquitination | PAINGALKKAGLSLK HHHCHHHHHCCCCCC | 39.79 | - | |
306 | Acetylation | AINGALKKAGLSLKD HHCHHHHHCCCCCCC | 48.84 | 24062335 | |
306 | Succinylation | AINGALKKAGLSLKD HHCHHHHHCCCCCCC | 48.84 | 24315375 | |
310 | Phosphorylation | ALKKAGLSLKDMDLI HHHHCCCCCCCCCEE | 32.24 | 25266776 | |
312 | Acetylation | KKAGLSLKDMDLIDV HHCCCCCCCCCEECC | 47.86 | 23576753 | |
312 | Succinylation | KKAGLSLKDMDLIDV HHCCCCCCCCCEECC | 47.86 | - | |
312 | Succinylation | KKAGLSLKDMDLIDV HHCCCCCCCCCEECC | 47.86 | 23806337 | |
312 | Ubiquitination | KKAGLSLKDMDLIDV HHCCCCCCCCCEECC | 47.86 | - | |
329 | Phosphorylation | AFAPQFLSVQKALDL HHHHHHHCHHHHHCC | 24.64 | 23984901 | |
332 | Acetylation | PQFLSVQKALDLDPS HHHHCHHHHHCCCCC | 49.08 | 22733758 | |
332 | Succinylation | PQFLSVQKALDLDPS HHHHCHHHHHCCCCC | 49.08 | 26388266 | |
339 | Phosphorylation | KALDLDPSKTNVSGG HHHCCCCCCCCCCCC | 52.35 | 23737553 | |
340 | Acetylation | ALDLDPSKTNVSGGA HHCCCCCCCCCCCCE | 49.89 | 23576753 | |
340 | Succinylation | ALDLDPSKTNVSGGA HHCCCCCCCCCCCCE | 49.89 | 24315375 | |
340 | Ubiquitination | ALDLDPSKTNVSGGA HHCCCCCCCCCCCCE | 49.89 | - | |
341 | Phosphorylation | LDLDPSKTNVSGGAI HCCCCCCCCCCCCEE | 45.23 | 21082442 | |
344 | Phosphorylation | DPSKTNVSGGAIALG CCCCCCCCCCEEEEC | 33.31 | 17208939 | |
357 | Phosphorylation | LGHPLGGSGSRITAH ECCCCCCCCCHHHHH | 31.62 | 73244741 | |
375 | Acetylation | ELRRRGGKYAVGSAC HHHHCCCCEEEECEE | 32.62 | 23576753 | |
382 | S-palmitoylation | KYAVGSACIGGGQGI CEEEECEEECCCCEE | 2.96 | 26165157 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of THIM_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of THIM_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |