| UniProt ID | ALFP2_ARATH | |
|---|---|---|
| UniProt AC | Q944G9 | |
| Protein Name | Fructose-bisphosphate aldolase 2, chloroplastic {ECO:0000305} | |
| Gene Name | FBA2 {ECO:0000303|PubMed:22561114} | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 398 | |
| Subcellular Localization | Plastid, chloroplast, plastoglobule . Plastid, chloroplast stroma . | |
| Protein Description | Plays a key role in glycolysis and gluconeogenesis.. | |
| Protein Sequence | MASTSLLKASPVLDKSEWVKGQSVLFRQPSSASVVLRNRATSLTVRAASSYADELVKTAKTIASPGRGILAMDESNATCGKRLDSIGLENTEANRQAFRTLLVSAPGLGQYVSGAILFEETLYQSTTEGKKMVDVLVEQNIVPGIKVDKGLVPLVGSNNESWCQGLDGLSSRTAAYYQQGARFAKWRTVVSIPNGPSALAVKEAAWGLARYAAISQDSGLVPIVEPEILLDGEHDIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAESKDRATPEQVAAYTLKLLRNRVPPAVPGIMFLSGGQSEVEATLNLNAMNQAPNPWHVSFSYARALQNTCLKTWGGRPENVNAAQTTLLARAKANSLAQLGKYTGEGESEEAKEGMFVKGYTY | |
| 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 |
|---|---|---|---|---|---|
| 30 | Phosphorylation | SVLFRQPSSASVVLR EEEEECCCCCEEEEE | 29654922 | ||
| 31 | Phosphorylation | VLFRQPSSASVVLRN EEEECCCCCEEEEEC | 25561503 | ||
| 49 | Phosphorylation | SLTVRAASSYADELV CHHHHHHHHCHHHHH | 30291188 | ||
| 50 | Phosphorylation | LTVRAASSYADELVK HHHHHHHHCHHHHHH | 29797451 | ||
| 58 | Phosphorylation | YADELVKTAKTIASP CHHHHHHHHHHHCCC | 25561503 | ||
| 61 | Phosphorylation | ELVKTAKTIASPGRG HHHHHHHHHCCCCCC | 19880383 | ||
| 64 | Phosphorylation | KTAKTIASPGRGILA HHHHHHCCCCCCEEE | 19880383 | ||
| 75 | Phosphorylation | GILAMDESNATCGKR CEEEEECCCCCCCCC | 30291188 | ||
| 78 | Phosphorylation | AMDESNATCGKRLDS EEECCCCCCCCCHHH | 23111157 | ||
| 85 | Phosphorylation | TCGKRLDSIGLENTE CCCCCHHHHCCCCHH | 30291188 | ||
| 91 | Phosphorylation | DSIGLENTEANRQAF HHHCCCCHHHHHHHH | 22092075 | ||
| 157 | Phosphorylation | GLVPLVGSNNESWCQ CCEECCCCCCCCHHH | 30291188 | ||
| 161 | Phosphorylation | LVGSNNESWCQGLDG CCCCCCCCHHHCCCC | 30291188 | ||
| 170 | Phosphorylation | CQGLDGLSSRTAAYY HHCCCCCCHHHHHHH | 30291188 | ||
| 176 | Phosphorylation | LSSRTAAYYQQGARF CCHHHHHHHHHCCCC | 24894044 | ||
| 188 | Phosphorylation | ARFAKWRTVVSIPNG CCCCEEEEEEECCCC | 22092075 | ||
| 211 | Phosphorylation | AAWGLARYAAISQDS HHHHHHHHHHHHCCC | 25368622 | ||
| 215 | Phosphorylation | LARYAAISQDSGLVP HHHHHHHHCCCCCEE | 25368622 | ||
| 218 | Phosphorylation | YAAISQDSGLVPIVE HHHHHCCCCCEEECC | 25368622 | ||
| 282 | Phosphorylation | AESKDRATPEQVAAY CCCCCCCCHHHHHHH | 28295753 | ||
| 289 | Phosphorylation | TPEQVAAYTLKLLRN CHHHHHHHHHHHHHC | 28295753 | ||
| 290 | Phosphorylation | PEQVAAYTLKLLRNR HHHHHHHHHHHHHCC | 22092075 | ||
| 371 | Phosphorylation | LARAKANSLAQLGKY HHHHHHHHHHHHHCC | 25561503 | ||
| 384 | Phosphorylation | KYTGEGESEEAKEGM CCCCCCCCHHHHCCC | 25561503 | ||
| 394 | "N6,N6,N6-trimethyllysine" | AKEGMFVKGYTY--- HHCCCEECCCCC--- | - | ||
| 394 | Methylation | AKEGMFVKGYTY--- HHCCCEECCCCC--- | 22547063 | ||
| 394 | Acetylation | AKEGMFVKGYTY--- HHCCCEECCCCC--- | 21311031 |
| 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 ALFP2_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 394 | K | Methylation |
| 22547063 |
* 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 ALFP2_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ALFP2_ARATH !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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