| UniProt ID | SGAT_ARATH | |
|---|---|---|
| UniProt AC | Q56YA5 | |
| Protein Name | Serine--glyoxylate aminotransferase | |
| Gene Name | AGT1 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 401 | |
| Subcellular Localization | Peroxisome . | |
| Protein Description | Photorespiratory enzyme that catalyzes transamination reactions with multiple substrates, including asparagine. Function exclusively as a catabolic enzyme in Asn metabolism.. | |
| Protein Sequence | MDYMYGPGRHHLFVPGPVNIPEPVIRAMNRNNEDYRSPAIPALTKTLLEDVKKIFKTTSGTPFLFPTTGTGAWESALTNTLSPGDRIVSFLIGQFSLLWIDQQKRLNFNVDVVESDWGQGANLQVLASKLSQDENHTIKAICIVHNETATGVTNDISAVRTLLDHYKHPALLLVDGVSSICALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEATKTSKSLKVFFDWNDYLKFYKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENIIARHARLGKATRLAVEAWGLKNCTQKEEWISNTVTAVMVPPHIDGSEIVRRAWQRYNLSLGLGLNKVAGKVFRIGHLGNVNELQLLGCLAGVEMILKDVGYPVVMGSGVAAASTYLQHHIPLIPSRI | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDYMYGPG -------CCCCCCCC | 8.21 | 22223895 | |
| 37 | Phosphorylation | RNNEDYRSPAIPALT CCCCCCCCCHHHHHH | 16.68 | 24043427 | |
| 46 | Phosphorylation | AIPALTKTLLEDVKK HHHHHHHHHHHHHHH | 31.19 | 24299221 | |
| 131 | Phosphorylation | QVLASKLSQDENHTI HHHHHHCCCCCCCCE | 39.04 | 24299221 | |
| 148 | Phosphorylation | ICIVHNETATGVTND EEEEECCCCCCCCCC | 34.53 | 24299221 | |
| 201 | N6-(pyridoxal phosphate)lysine | VALTGSQKALSLPTG EEECCCCCCCCCCCC | 53.65 | - | |
| 201 | Other | VALTGSQKALSLPTG EEECCCCCCCCCCCC | 53.65 | - | |
| 204 | Phosphorylation | TGSQKALSLPTGLGI CCCCCCCCCCCCCEE | 36.84 | 30291188 | |
| 215 | Phosphorylation | GLGIVCASPKALEAT CCEEEEECHHHHHHH | 23.08 | 19880383 | |
| 330 | Phosphorylation | VRRAWQRYNLSLGLG HHHHHHHHCCCCCCC | 12.83 | 14506206 | |
| 387 | Phosphorylation | GSGVAAASTYLQHHI CCCHHHHHHHHHHCC | 16.92 | 29654922 | |
| 388 | Phosphorylation | SGVAAASTYLQHHIP CCHHHHHHHHHHCCC | 24.43 | 29654922 |
| 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 SGAT_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SGAT_ARATH !! | ||||||
* 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 SGAT_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SGAT_ARATH | AGT | physical | 21798944 | |
| GLO2_ARATH | AT3G14415 | physical | 21798944 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, AND MASSSPECTROMETRY. | |
