RGL2_ARATH - dbPTM
RGL2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGL2_ARATH
UniProt AC Q8GXW1
Protein Name DELLA protein RGL2
Gene Name RGL2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 547
Subcellular Localization Nucleus .
Protein Description Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. No effect of the BOI proteins on its stability. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway. Acts as a major GA-response repressor of seed germination, including seed thermoinhibition. Promotes the biosynthesis of abscisic acid (ABA), especially in seed coats to maintain seed dormancy. Delays flowering and adult leaf production. Also regulates the floral development, petal, stamen and anther development, by repressing the continued growth of floral organs. Its activity is probably regulated by other phytohormones such as auxin and ethylene. Involved in the regulation of seed dormancy and germination, including glucose-induced delay of seed germination. Promotes salt tolerance. Acts as a repressor of positive regulators of trichome initiation. Required during the flagellin-derived peptide flg22-mediated growth inhibition. Contributes to the susceptibility to the biotrophic pathogen P.syringae pv. tomato and to the resistance to the necrotrophic pathogens B.cinerea A.brassicicola, probably by repressing the SA-defense pathway and preventing cell death. Prevents stress-induced reactive oxygen species (ROS) accumulation (e.g. salt stress) by acting on the ROS scavenging system, and delays ROS-induced cell death, thus promoting stress tolerance..
Protein Sequence MKRGYGETWDPPPKPLPASRSGEGPSMADKKKADDDNNNSNMDDELLAVLGYKVRSSEMAEVAQKLEQLEMVLSNDDVGSTVLNDSVHYNPSDLSNWVESMLSELNNPASSDLDTTRSCVDRSEYDLRAIPGLSAFPKEEEVFDEEASSKRIRLGSWCESSDESTRSVVLVDSQETGVRLVHALVACAEAIHQENLNLADALVKRVGTLAGSQAGAMGKVATYFAQALARRIYRDYTAETDVCAAVNPSFEEVLEMHFYESCPYLKFAHFTANQAILEAVTTARRVHVIDLGLNQGMQWPALMQALALRPGGPPSFRLTGIGPPQTENSDSLQQLGWKLAQFAQNMGVEFEFKGLAAESLSDLEPEMFETRPESETLVVNSVFELHRLLARSGSIEKLLNTVKAIKPSIVTVVEQEANHNGIVFLDRFNEALHYYSSLFDSLEDSYSLPSQDRVMSEVYLGRQILNVVAAEGSDRVERHETAAQWRIRMKSAGFDPIHLGSSAFKQASMLLSLYATGDGYRVEENDGCLMIGWQTRPLITTSAWKLA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster

Oops, there are no PTM records of RGL2_ARATH !!

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseGID2Q9STX3
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGL2_ARATH !!

Disease-associated PTM Sites based on SAP

* 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 RGL2_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIF4_ARATHPIF4physical
20093430
PIF1_ARATHPIL5physical
20093430
SPT_ARATHSPTphysical
20093430
PIF6_ARATHPIL2physical
20093430
SWI3C_ARATHSWI3Cphysical
23893173
TI10A_ARATHJAZ1physical
21145503
ATML1_ARATHATML1physical
24989044
PDF2_ARATHPDF2physical
24989044

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGL2_ARATH

loading...

Related Literatures of Post-Translational Modification

TOP