UniProt ID | ACBG1_HUMAN | |
---|---|---|
UniProt AC | Q96GR2 | |
Protein Name | Long-chain-fatty-acid--CoA ligase ACSBG1 | |
Gene Name | ACSBG1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 724 | |
Subcellular Localization | Cytoplasm . Cytoplasmic vesicle. Microsome. Endoplasmic reticulum. | |
Protein Description | Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Also able to activate very long-chain fatty acids; however, the relevance of such activity is unclear in vivo. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids.. | |
Protein Sequence | MPRNSGAGYGCPHGDPSMLDSRETPQESRQDMIVRTTQEKLKTSSLTDRQPLSKESLNHALELSVPEKVNNAQWDAPEEALWTTRADGRVRLRIDPSCPQLPYTVHRMFYEALDKYGDLIALGFKRQDKWEHISYSQYYLLARRAAKGFLKLGLKQAHSVAILGFNSPEWFFSAVGTVFAGGIVTGIYTTSSPEACQYIAYDCCANVIMVDTQKQLEKILKIWKQLPHLKAVVIYKEPPPNKMANVYTMEEFMELGNEVPEEALDAIIDTQQPNQCCVLVYTSGTTGNPKGVMLSQDNITWTARYGSQAGDIRPAEVQQEVVVSYLPLSHIAAQIYDLWTGIQWGAQVCFAEPDALKGSLVNTLREVEPTSHMGVPRVWEKIMERIQEVAAQSGFIRRKMLLWAMSVTLEQNLTCPGSDLKPFTTRLADYLVLAKVRQALGFAKCQKNFYGAAPMMAETQHFFLGLNIRLYAGYGLSETSGPHFMSSPYNYRLYSSGKLVPGCRVKLVNQDAEGIGEICLWGRTIFMGYLNMEDKTCEAIDEEGWLHTGDAGRLDADGFLYITGRLKELIITAGGENVPPVPIEEAVKMELPIISNAMLIGDQRKFLSMLLTLKCTLDPDTSDQTDNLTEQAMEFCQRVGSRATTVSEIIEKKDEAVYQAIEEGIRRVNMNAAARPYHIQKWAILERDFSISGGELGPTMKLKRLTVLEKYKGIIDSFYQEQKM | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MPRNSGAGYGCP ---CCCCCCCCCCCC | 31.16 | 22210691 | |
17 | Phosphorylation | GCPHGDPSMLDSRET CCCCCCHHHCCCCCC | 36.40 | 22210691 | |
24 | Phosphorylation | SMLDSRETPQESRQD HHCCCCCCCHHHHHC | 29.21 | 25690035 | |
53 | Phosphorylation | LTDRQPLSKESLNHA CCCCCCCCHHHHHHH | 40.85 | - | |
56 | Phosphorylation | RQPLSKESLNHALEL CCCCCHHHHHHHHHH | 37.90 | 27732954 | |
64 | Phosphorylation | LNHALELSVPEKVNN HHHHHHHCCCHHHCC | 26.67 | 27732954 | |
134 | Phosphorylation | QDKWEHISYSQYYLL CCCCCCCCHHHHHHH | 22.19 | 19690332 | |
135 | Phosphorylation | DKWEHISYSQYYLLA CCCCCCCHHHHHHHH | 10.13 | 2074991 | |
136 | Phosphorylation | KWEHISYSQYYLLAR CCCCCCHHHHHHHHH | 12.62 | 19690332 | |
138 | Phosphorylation | EHISYSQYYLLARRA CCCCHHHHHHHHHHH | 7.08 | 22817900 | |
139 | Phosphorylation | HISYSQYYLLARRAA CCCHHHHHHHHHHHH | 6.39 | 2075207 | |
236 | Acetylation | LKAVVIYKEPPPNKM CEEEEEECCCCCCCC | 53.25 | 30586703 | |
295 | Phosphorylation | NPKGVMLSQDNITWT CCCCEEEECCCEEEE | 19.86 | 22496350 | |
300 | Phosphorylation | MLSQDNITWTARYGS EEECCCEEEEEECCC | 24.02 | 67054361 | |
359 | Phosphorylation | EPDALKGSLVNTLRE CCHHHCCCHHHHHCC | 27.79 | 46158013 | |
370 | Phosphorylation | TLREVEPTSHMGVPR HHCCCCCCCCCCCHH | 20.12 | 30206219 | |
371 | Phosphorylation | LREVEPTSHMGVPRV HCCCCCCCCCCCHHH | 23.38 | 30206219 | |
595 | Phosphorylation | KMELPIISNAMLIGD HCCCCEECCCEECCC | 21.18 | 46158019 | |
641 | Phosphorylation | EFCQRVGSRATTVSE HHHHHHHCCCCCHHH | 18.84 | 28258704 | |
644 | Phosphorylation | QRVGSRATTVSEIIE HHHHCCCCCHHHHHH | 26.98 | 28258704 | |
647 | Phosphorylation | GSRATTVSEIIEKKD HCCCCCHHHHHHHHC | 22.45 | 28258704 | |
658 | Phosphorylation | EKKDEAVYQAIEEGI HHHCHHHHHHHHHHH | 10.16 | - | |
690 | Phosphorylation | AILERDFSISGGELG HEEEEECCCCCCCCC | 21.82 | 26074081 | |
692 | Phosphorylation | LERDFSISGGELGPT EEEECCCCCCCCCCC | 39.28 | 26074081 | |
699 | Phosphorylation | SGGELGPTMKLKRLT CCCCCCCCEEEEEHH | 25.74 | 26074081 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ACBG1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACBG1_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 ACBG1_HUMAN !! |
Kegg Disease | ||||||
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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. |
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Phosphorylation | |
Reference | PubMed |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135; TYR-138 ANDTYR-139, AND MASS SPECTROMETRY. |