UniProt ID | 14339_ARATH | |
---|---|---|
UniProt AC | Q96299 | |
Protein Name | 14-3-3-like protein GF14 mu | |
Gene Name | GRF9 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 263 | |
Subcellular Localization | Nucleus . Cytoplasm . Translocates from the cytosol to the nucleus when phosphorylated. | |
Protein Description | Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes.. | |
Protein Sequence | MGSGKERDTFVYLAKLSEQAERYEEMVESMKSVAKLNVDLTVEERNLLSVGYKNVIGSRRASWRIFSSIEQKEAVKGNDVNVKRIKEYMEKVELELSNICIDIMSVLDEHLIPSASEGESTVFFNKMKGDYYRYLAEFKSGNERKEAADQSLKAYEIATTAAEAKLPPTHPIRLGLALNFSVFYYEIMNAPERACHLAKQAFDEAISELDTLNEESYKDSTLIMQLLRDNLTLWTSDISEEGGDDAHKTNGSAKPGAGGDDAE | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MGSGKERDTF -----CCCCCCCHHH | 45.45 | 26091701 | |
67 | Phosphorylation | RASWRIFSSIEQKEA HHHHHHHHCHHHHHH | 28.21 | - | |
207 | Phosphorylation | QAFDEAISELDTLNE HHHHHHHHHHHCCCH | 38.87 | 30291188 | |
211 | Phosphorylation | EAISELDTLNEESYK HHHHHHHCCCHHHHC | 44.07 | - | |
232 | Phosphorylation | QLLRDNLTLWTSDIS HHHHCCCEEEECCCH | 26.89 | 23776212 | |
235 | Phosphorylation | RDNLTLWTSDISEEG HCCCEEEECCCHHHC | 21.45 | 23776212 | |
236 | Phosphorylation | DNLTLWTSDISEEGG CCCEEEECCCHHHCC | 22.74 | 23776212 | |
239 | Phosphorylation | TLWTSDISEEGGDDA EEEECCCHHHCCCCH | 34.29 | 30291188 | |
249 | Phosphorylation | GGDDAHKTNGSAKPG CCCCHHHCCCCCCCC | 34.64 | 23776212 | |
252 | Phosphorylation | DAHKTNGSAKPGAGG CHHHCCCCCCCCCCC | 34.88 | 23776212 |
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 14339_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 14339_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 14339_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CNG13_ARATH | CNGC13 | physical | 22737156 | |
PUP21_ARATH | AT4G18220 | physical | 22737156 | |
FB316_ARATH | AT1G61340 | physical | 22920997 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASSSPECTROMETRY. | |
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASSSPECTROMETRY. |