UniProt ID | 14335_ARATH | |
---|---|---|
UniProt AC | P42645 | |
Protein Name | 14-3-3-like protein GF14 upsilon | |
Gene Name | GRF5 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 268 | |
Subcellular Localization | Cytoplasm . Nucleus . Not associated with microtubules (PubMed:21558460). Translocates from the cytosol to the nucleus when phosphorylated (By similarity). | |
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. May be involved in cell cycle regulation by binding to soluble EDE1 and sequestering it in an inactive form during the early stages of mitosis.. | |
Protein Sequence | MSSDSSREENVYLAKLAEQAERYEEMVEFMEKVAKTVETEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEDSRGNSDHVSIIKDYRGKIETELSKICDGILNLLEAHLIPAASLAESKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLVAYKSAQDIALADLAPTHPIRLGLALNFSVFYYEILNSSDRACSLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDLNDEAGDDIKEAPKEVQKVDEQAQPPPSQ | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSSDSSREE ------CCCCCCHHH | 42.74 | 27531888 | |
3 | Phosphorylation | -----MSSDSSREEN -----CCCCCCHHHH | 39.97 | 19880383 | |
5 | Phosphorylation | ---MSSDSSREENVY ---CCCCCCHHHHHH | 32.99 | 27531888 | |
6 | Phosphorylation | --MSSDSSREENVYL --CCCCCCHHHHHHH | 49.02 | 27643528 | |
12 | Phosphorylation | SSREENVYLAKLAEQ CCHHHHHHHHHHHHH | 16.72 | 27643528 | |
51 | Phosphorylation | VEERNLLSVAYKNVI HHHHHHHHHHHHHHH | 14.10 | 25561503 | |
69 | Phosphorylation | RASWRIISSIEQKED HHHHHHHHHHHHCCC | 23.92 | - | |
192 | Phosphorylation | FYYEILNSSDRACSL HHHHHHCCCHHHHHH | 30.12 | - | |
209 | Phosphorylation | QAFDEAISELDTLGE HHHHHHHHHHHHCCC | 38.87 | 30291188 | |
213 | Phosphorylation | EAISELDTLGEESYK HHHHHHHHCCCCHHC | 49.65 | 25368622 | |
218 | Phosphorylation | LDTLGEESYKDSTLI HHHCCCCHHCCHHHH | 32.93 | 25368622 | |
219 | Phosphorylation | DTLGEESYKDSTLIM HHCCCCHHCCHHHHH | 23.30 | 25368622 | |
222 | Phosphorylation | GEESYKDSTLIMQLL CCCHHCCHHHHHHHH | 22.44 | 25368622 | |
223 | Phosphorylation | EESYKDSTLIMQLLR CCHHCCHHHHHHHHH | 30.36 | 25368622 | |
234 | Phosphorylation | QLLRDNLTLWTSDLN HHHHCCCEEEECCCC | 26.89 | 23776212 | |
237 | Phosphorylation | RDNLTLWTSDLNDEA HCCCEEEECCCCCCC | 18.57 | 23776212 | |
238 | Phosphorylation | DNLTLWTSDLNDEAG CCCEEEECCCCCCCC | 28.63 | 30291188 | |
267 | Phosphorylation | EQAQPPPSQ------ HHCCCCCCC------ | 55.05 | 30291188 |
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 14335_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 14335_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 14335_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
GCL1_ARATH | GCL1 | physical | 22737156 | |
CDPK1_ARATH | CPK1 | physical | 22737156 | |
EDE1_ARATH | EDE1 | physical | 21558460 |
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-267, AND MASSSPECTROMETRY. |