Q84JK2 · FD_ARATH
- ProteinProtein FD
- GeneFD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids285 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcription factor required for the transition to flowering promoted by FT.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | DNA-binding transcription factor activity | |
Biological Process | photoperiodism | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | positive regulation of flower development | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | regulation of flower development | |
Biological Process | regulation of photoperiodism, flowering |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameProtein FD
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ84JK2
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 13 | in strain: cv. No-0 | ||||
Sequence: L → V | ||||||
Natural variant | 112 | in strain: cv. Cvi-1 and cv. No-0 | ||||
Sequence: K → N | ||||||
Natural variant | 141 | in strain: cv. Cvi-1, cv. Landsberg erecta, cv. No-0 and cv. Wassilewskija | ||||
Sequence: Y → C | ||||||
Natural variant | 161 | in strain: cv. Cvi-1 and cv. No-0 | ||||
Sequence: E → D | ||||||
Mutagenesis | 276 | No effect on phosphorylation. Loss of phosphorylation; when associated with A-282. | ||||
Sequence: T → A | ||||||
Mutagenesis | 277 | Loss of phosphorylation and loss of interaction with FD, GRF3 and GRF4. No effect on interaction with FD, GRF3 and GRF4; when associated with E-282. | ||||
Sequence: L → Q | ||||||
Mutagenesis | 279-285 | Loss of interaction with FT. | ||||
Sequence: Missing | ||||||
Mutagenesis | 282 | Loss of phosphorylation and loss of interaction with FT. Loss of phosphorylation; when associated with A-276. | ||||
Sequence: T → A | ||||||
Mutagenesis | 282 | Normal interaction with FT. No effect on interaction with FD, GRF3 and GRF4; when associated with Q-277. | ||||
Sequence: T → E | ||||||
Mutagenesis | 282 | Normal interaction with FT. | ||||
Sequence: T → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000245359 | 1-285 | Protein FD | |||
Sequence: MLSSAKHQRNHRLSATNKNQTLTKVSSISSSSPSSSSSSSSTSSSSPLPSQDSQAQKRSLVTMEEVWNDINLASIHHLNRHSPHPQHNHEPRFRGQNHHNQNPNSIFQDFLKGSLNQEPAPTSQTTGSAPNGDSTTVTVLYSSPFPPPATVLSLNSGAGFEFLDNQDPLVTSNSNLHTHHHLSNAHAFNTSFEALVPSSSFGKKRGQDSNEGSGNRRHKRMIKNRESAARSRARKQAYTNELELEVAHLQAENARLKRQQDQLKMAAAIQQPKKNTLQRSSTAPF | ||||||
Modified residue | 282 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated at Thr-282 in a calcium-dependent manner by CPK6 and CPK33.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Self-interacts (PubMed:16099979).
Interacts with FT and FDP/BZIP27 (PubMed:16099979, PubMed:16099980, PubMed:25661797).
Interacts with GRF3 and GRF4, and in a calcium-independent manner, with CPK6 and CPK33 (PubMed:25661797).
Interacts with FT and FDP/BZIP27 (PubMed:16099979, PubMed:16099980, PubMed:25661797).
Interacts with GRF3 and GRF4, and in a calcium-independent manner, with CPK6 and CPK33 (PubMed:25661797).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q84JK2 | FT Q9SXZ2 | 4 | EBI-636507, EBI-636490 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-59 | Disordered | ||||
Sequence: MLSSAKHQRNHRLSATNKNQTLTKVSSISSSSPSSSSSSSSTSSSSPLPSQDSQAQKRS | ||||||
Region | 79-107 | Disordered | ||||
Sequence: NRHSPHPQHNHEPRFRGQNHHNQNPNSIF | ||||||
Region | 115-134 | Disordered | ||||
Sequence: LNQEPAPTSQTTGSAPNGDS | ||||||
Region | 198-236 | Disordered | ||||
Sequence: SSSFGKKRGQDSNEGSGNRRHKRMIKNRESAARSRARKQ | ||||||
Domain | 214-277 | bZIP | ||||
Sequence: GNRRHKRMIKNRESAARSRARKQAYTNELELEVAHLQAENARLKRQQDQLKMAAAIQQPKKNTL | ||||||
Region | 216-235 | Basic motif | ||||
Sequence: RRHKRMIKNRESAARSRARK | ||||||
Region | 242-263 | Leucine-zipper | ||||
Sequence: LELEVAHLQAENARLKRQQDQL | ||||||
Region | 257-285 | Disordered | ||||
Sequence: KRQQDQLKMAAAIQQPKKNTLQRSSTAPF | ||||||
Compositional bias | 264-285 | Polar residues | ||||
Sequence: KMAAAIQQPKKNTLQRSSTAPF |
Sequence similarities
Belongs to the bZIP family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length285
- Mass (Da)31,377
- Last updated2003-06-01 v1
- Checksum9F50BE3364C89D54
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8B8Q9 | A0A1P8B8Q9_ARATH | FD | 244 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 264-285 | Polar residues | ||||
Sequence: KMAAAIQQPKKNTLQRSSTAPF |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB105818 EMBL· GenBank· DDBJ | BAC65864.1 EMBL· GenBank· DDBJ | mRNA | ||
AB105819 EMBL· GenBank· DDBJ | BAC65865.1 EMBL· GenBank· DDBJ | mRNA | ||
AB105820 EMBL· GenBank· DDBJ | BAC65866.1 EMBL· GenBank· DDBJ | mRNA | ||
AB105821 EMBL· GenBank· DDBJ | BAC65867.1 EMBL· GenBank· DDBJ | mRNA | ||
AB105822 EMBL· GenBank· DDBJ | BAC65868.1 EMBL· GenBank· DDBJ | mRNA | ||
AB105823 EMBL· GenBank· DDBJ | BAC65869.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB105824 EMBL· GenBank· DDBJ | BAC65870.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB105825 EMBL· GenBank· DDBJ | BAC65871.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB105826 EMBL· GenBank· DDBJ | BAC65872.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB105827 EMBL· GenBank· DDBJ | BAC65873.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL022373 EMBL· GenBank· DDBJ | CAA18484.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL031986 EMBL· GenBank· DDBJ | CAA21476.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161588 EMBL· GenBank· DDBJ | CAB81499.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE86586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BN000021 EMBL· GenBank· DDBJ | CAD29860.1 EMBL· GenBank· DDBJ | Genomic DNA |