| UniProt ID | FHY3_ARATH | |
|---|---|---|
| UniProt AC | Q9LIE5 | |
| Protein Name | Protein FAR-RED ELONGATED HYPOCOTYL 3 | |
| Gene Name | FHY3 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 839 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Transcription activator that recognizes and binds to the DNA consensus sequence 5'-CACGCGC-3'. Activates the expression of FHY1 and FHL involved in light responses. When associated with PHYA, protects it from being recognized and degraded by the COP1/SPA complex. Positive regulator of chlorophyll biosynthesis via the activation of HEMB1 gene expression.. | |
| Protein Sequence | MDIDLRLHSGDLCKGDDEDRGLDNVLHNEEDMDIGKIEDVSVEVNTDDSVGMGVPTGELVEYTEGMNLEPLNGMEFESHGEAYSFYQEYSRAMGFNTAIQNSRRSKTTREFIDAKFACSRYGTKREYDKSFNRPRARQSKQDPENMAGRRTCAKTDCKASMHVKRRPDGKWVIHSFVREHNHELLPAQAVSEQTRKIYAAMAKQFAEYKTVISLKSDSKSSFEKGRTLSVETGDFKILLDFLSRMQSLNSNFFYAVDLGDDQRVKNVFWVDAKSRHNYGSFCDVVSLDTTYVRNKYKMPLAIFVGVNQHYQYMVLGCALISDESAATYSWLMETWLRAIGGQAPKVLITELDVVMNSIVPEIFPNTRHCLFLWHVLMKVSENLGQVVKQHDNFMPKFEKCIYKSGKDEDFARKWYKNLARFGLKDDQWMISLYEDRKKWAPTYMTDVLLAGMSTSQRADSINAFFDKYMHKKTSVQEFVKVYDTVLQDRCEEEAKADSEMWNKQPAMKSPSPFEKSVSEVYTPAVFKKFQIEVLGAIACSPREENRDATCSTFRVQDFENNQDFMVTWNQTKAEVSCICRLFEYKGYLCRHTLNVLQCCHLSSIPSQYILKRWTKDAKSRHFSGEPQQLQTRLLRYNDLCERALKLNEEASLSQESYNIAFLAIEGAIGNCAGINTSGRSLPDVVTSPTQGLISVEEDNHSRSAGKTSKKKNPTKKRKVNPEQDVMPVAAPESLQQMDKLSPRTVGIESYYGTQQSVQGMVQLNLMGPTRDNFYGNQQTMQGLRQLNSIAPSYDSYYGPQQGIHGQGVDFFRPANFSYDIRDDPNVRTTQLHEDASRHS | |
| 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 |
|---|---|---|---|---|---|
| 9 | Phosphorylation | DIDLRLHSGDLCKGD CCEEEEECCCCCCCC | 38.30 | 25561503 | |
| 680 | Phosphorylation | GINTSGRSLPDVVTS CCCCCCCCCCCCCCC | 48.02 | 23776212 | |
| 686 | Phosphorylation | RSLPDVVTSPTQGLI CCCCCCCCCCCCCCE | 28.92 | 23776212 | |
| 687 | Phosphorylation | SLPDVVTSPTQGLIS CCCCCCCCCCCCCEE | 17.84 | 23776212 | |
| 689 | Phosphorylation | PDVVTSPTQGLISVE CCCCCCCCCCCEEEE | 34.73 | 23776212 | |
| 694 | Phosphorylation | SPTQGLISVEEDNHS CCCCCCEEEECCCCC | 28.63 | 23776212 | |
| 701 | Phosphorylation | SVEEDNHSRSAGKTS EEECCCCCCCCCCCC | 33.90 | 23776212 | |
| 741 | Phosphorylation | LQQMDKLSPRTVGIE HHHHHHCCCCEECCE | 20.34 | 30291188 | |
| 836 | Phosphorylation | TQLHEDASRHS---- HHCCCCHHCCC---- | 42.73 | 25561503 | |
| 839 | Phosphorylation | HEDASRHS------- CCCHHCCC------- | 40.58 | 30407730 |
| 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 FHY3_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FHY3_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 FHY3_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| FHY3_ARATH | FHY3 | physical | 11889039 | |
| FAR1_ARATH | FAR1 | physical | 11889039 | |
| PHYA_ARATH | PHYA | physical | 18722184 | |
| FHY3_ARATH | FHY3 | physical | 18715961 | |
| FAR1_ARATH | FAR1 | physical | 18715961 | |
| HY5_ARATH | HY5 | physical | 21097709 | |
| FAR1_ARATH | FAR1 | physical | 21097709 | |
| LHY_ARATH | LHY | physical | 21499259 | |
| CCA1_ARATH | CCA1 | physical | 21499259 | |
| HY5_ARATH | HY5 | physical | 21499259 | |
| PIF1_ARATH | PIL5 | physical | 22634759 | |
| HY5_ARATH | HY5 | physical | 23150635 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...