| UniProt ID | ACDSB_HUMAN | |
|---|---|---|
| UniProt AC | P45954 | |
| Protein Name | Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial | |
| Gene Name | ACADSB | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 432 | |
| Subcellular Localization | Mitochondrion matrix. | |
| Protein Description | Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent.. | |
| Protein Sequence | MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 35 | Phosphorylation | IPPHVSKSSQSEALL CCCCCCCCCCCHHHH | 26.55 | 27251275 | |
| 36 | Phosphorylation | PPHVSKSSQSEALLN CCCCCCCCCCHHHHH | 41.27 | 27251275 | |
| 70 | Ubiquitination | MIKSSVKKFAQEQIA HHHHHHHHHHHHHHH | 43.72 | 21890473 | |
| 70 | Ubiquitination | MIKSSVKKFAQEQIA HHHHHHHHHHHHHHH | 43.72 | 21890473 | |
| 70 | Ubiquitination | MIKSSVKKFAQEQIA HHHHHHHHHHHHHHH | 43.72 | 21890473 | |
| 70 | Acetylation | MIKSSVKKFAQEQIA HHHHHHHHHHHHHHH | 43.72 | 25953088 | |
| 70 | Succinylation | MIKSSVKKFAQEQIA HHHHHHHHHHHHHHH | 43.72 | 21890473 | |
| 70 | Succinylation | MIKSSVKKFAQEQIA HHHHHHHHHHHHHHH | 43.72 | - | |
| 81 | Phosphorylation | EQIAPLVSTMDENSK HHHHHHHHCCCCCCH | 26.20 | 46157407 | |
| 82 | Phosphorylation | QIAPLVSTMDENSKM HHHHHHHCCCCCCHH | 22.59 | 46157413 | |
| 182 | Ubiquitination | CLSEAGAGSDSFALK ECCCCCCCCCCEEEE | 30.94 | - | |
| 182 | Acetylation | CLSEAGAGSDSFALK ECCCCCCCCCCEEEE | 30.94 | - | |
| 183 | Phosphorylation | LSEAGAGSDSFALKT CCCCCCCCCCEEEEE | 29.55 | 27251275 | |
| 185 | Phosphorylation | EAGAGSDSFALKTRA CCCCCCCCEEEEECC | 17.70 | 69000345 | |
| 198 | Phosphorylation | RADKEGDYYVLNGSK CCCCCCCEEEECCCE | 13.31 | 75089 | |
| 199 | Phosphorylation | ADKEGDYYVLNGSKM CCCCCCEEEECCCEE | 11.82 | 22817900 | |
| 226 | Phosphorylation | VMANVDPTIGYKGIT EEECCCCCCCCCCHH | 23.67 | 28258704 | |
| 229 | Phosphorylation | NVDPTIGYKGITSFL CCCCCCCCCCHHEEE | 11.37 | 28258704 | |
| 259 | Phosphorylation | KLGLRASSTCPLTFE CCCCCCCCCCCCEEC | 32.80 | 26503514 | |
| 284 | Ubiquitination | GQIGHGYKYAIGSLN EEECCHHHHEEECCC | 32.57 | 21890473 | |
| 284 | Ubiquitination | GQIGHGYKYAIGSLN EEECCHHHHEEECCC | 32.57 | 21890473 | |
| 284 | Ubiquitination | GQIGHGYKYAIGSLN EEECCHHHHEEECCC | 32.57 | 21890473 | |
| 284 | Succinylation | GQIGHGYKYAIGSLN EEECCHHHHEEECCC | 32.57 | 21890473 | |
| 284 | Acetylation | GQIGHGYKYAIGSLN EEECCHHHHEEECCC | 32.57 | 19608861 | |
| 284 | Succinylation | GQIGHGYKYAIGSLN EEECCHHHHEEECCC | 32.57 | - | |
| 285 | Phosphorylation | QIGHGYKYAIGSLNE EECCHHHHEEECCCC | 8.58 | 28258704 | |
| 289 | Phosphorylation | GYKYAIGSLNEGRIG HHHHEEECCCCCCHH | 23.16 | 69008769 | |
| 365 | Acetylation | EAGKPFIKEASMAKY HCCCCCHHHHHHHHH | 47.83 | 7462021 | |
| 371 | Acetylation | IKEASMAKYYASEIA HHHHHHHHHHHHHHC | 30.10 | 25038526 | |
| 372 | Phosphorylation | KEASMAKYYASEIAG HHHHHHHHHHHHHCC | 8.50 | 28152594 | |
| 373 | Phosphorylation | EASMAKYYASEIAGQ HHHHHHHHHHHHCCC | 11.71 | 28152594 | |
| 413 | Phosphorylation | DAKIGTIYEGASNIQ CCCCCCEEECCCCCC | 14.24 | 7105053 | |
| 426 | Acetylation | IQLNTIAKHIDAEY- CCHHHHHHHHCCCC- | 36.92 | - |
| 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 ACDSB_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACDSB_HUMAN !! | ||||||
* 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 ACDSB_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| YTHD1_HUMAN | YTHDF1 | physical | 26186194 | |
| ACTZ_HUMAN | ACTR1A | physical | 26344197 | |
| KDSR_HUMAN | KDSR | physical | 26344197 | |
| PXDN_HUMAN | PXDN | physical | 28514442 |
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| Acetylation | |
| Reference | PubMed |
| "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-284, AND MASS SPECTROMETRY. | |