UniProt ID | RGA_ARATH | |
---|---|---|
UniProt AC | Q9SLH3 | |
Protein Name | DELLA protein RGA | |
Gene Name | RGA | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 587 | |
Subcellular Localization | Nucleus . | |
Protein Description | Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Positively regulates XERICO expression in seeds. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway. Compared to other DELLA proteins, it is the most sensitive to GA application. No effect of the BOI proteins on its stability. Its activity is probably regulated by other phytohormones such as auxin and ethylene, attenuation of auxin transport delaying its GA-induced degradation.. | |
Protein Sequence | MKRDHHQFQGRLSNHGTSSSSSSISKDKMMMVKKEEDGGGNMDDELLAVLGYKVRSSEMAEVALKLEQLETMMSNVQEDGLSHLATDTVHYNPSELYSWLDNMLSELNPPPLPASSNGLDPVLPSPEICGFPASDYDLKVIPGNAIYQFPAIDSSSSSNNQNKRLKSCSSPDSMVTSTSTGTQIGGVIGTTVTTTTTTTTAAGESTRSVILVDSQENGVRLVHALMACAEAIQQNNLTLAEALVKQIGCLAVSQAGAMRKVATYFAEALARRIYRLSPPQNQIDHCLSDTLQMHFYETCPYLKFAHFTANQAILEAFEGKKRVHVIDFSMNQGLQWPALMQALALREGGPPTFRLTGIGPPAPDNSDHLHEVGCKLAQLAEAIHVEFEYRGFVANSLADLDASMLELRPSDTEAVAVNSVFELHKLLGRPGGIEKVLGVVKQIKPVIFTVVEQESNHNGPVFLDRFTESLHYYSTLFDSLEGVPNSQDKVMSEVYLGKQICNLVACEGPDRVERHETLSQWGNRFGSSGLAPAHLGSNAFKQASMLLSVFNSGQGYRVEESNGCLMLGWHTRPLITTSAWKLSTAAY | |
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 | Phosphorylation | HQFQGRLSNHGTSSS CCCCCCCCCCCCCCC | 25.97 | 28295753 | |
17 | O-linked_Glycosylation | GRLSNHGTSSSSSSI CCCCCCCCCCCCCCC | 20.20 | 26773002 | |
18 | O-linked_Glycosylation | RLSNHGTSSSSSSIS CCCCCCCCCCCCCCC | 32.58 | 26773002 | |
18 | Phosphorylation | RLSNHGTSSSSSSIS CCCCCCCCCCCCCCC | 32.58 | 19880383 | |
19 | Phosphorylation | LSNHGTSSSSSSISK CCCCCCCCCCCCCCC | 33.79 | 28295753 | |
20 | O-linked_Glycosylation | SNHGTSSSSSSISKD CCCCCCCCCCCCCCC | 33.72 | 26773002 | |
21 | Phosphorylation | NHGTSSSSSSISKDK CCCCCCCCCCCCCCC | 30.01 | 23111157 | |
22 | Phosphorylation | HGTSSSSSSISKDKM CCCCCCCCCCCCCCE | 33.37 | 28295753 | |
23 | Phosphorylation | GTSSSSSSISKDKMM CCCCCCCCCCCCCEE | 32.59 | 28295753 | |
25 | Phosphorylation | SSSSSSISKDKMMMV CCCCCCCCCCCEEEE | 36.43 | 28295753 | |
56 | O-linked_Glycosylation | VLGYKVRSSEMAEVA HHCEEECCHHHHHHH | 33.37 | 26773002 | |
57 | O-linked_Glycosylation | LGYKVRSSEMAEVAL HCEEECCHHHHHHHH | 22.34 | 26773002 | |
82 | O-linked_Glycosylation | NVQEDGLSHLATDTV HCCCCHHHHHCCCCC | 23.22 | 26773002 | |
115 | O-linked_Glycosylation | NPPPLPASSNGLDPV CCCCCCCCCCCCCCC | 23.54 | 26773002 | |
116 | O-linked_Glycosylation | PPPLPASSNGLDPVL CCCCCCCCCCCCCCC | 36.70 | 26773002 | |
176 | O-linked_Glycosylation | SSPDSMVTSTSTGTQ CCCCCCCEECCCCCE | 20.04 | 26773002 | |
177 | O-linked_Glycosylation | SPDSMVTSTSTGTQI CCCCCCEECCCCCEE | 14.67 | 26773002 | |
178 | O-linked_Glycosylation | PDSMVTSTSTGTQIG CCCCCEECCCCCEEC | 22.42 | 26773002 | |
179 | O-linked_Glycosylation | DSMVTSTSTGTQIGG CCCCEECCCCCEECC | 25.30 | 26773002 | |
193 | O-linked_Glycosylation | GVIGTTVTTTTTTTT CEEEEEEEEEEEEEE | 19.14 | 26773002 | |
253 | O-linked_Glycosylation | QIGCLAVSQAGAMRK HHCHHHHHCCCHHHH | 14.54 | 26773002 | |
527 | O-linked_Glycosylation | QWGNRFGSSGLAPAH HHHHCCCCCCCCCCC | 20.65 | 26773002 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RGA_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 RGA_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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