Q8RWL6 · STY17_ARATH
- ProteinSerine/threonine-protein kinase STY17
- GeneSTY17
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids570 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine/threonine protein kinase that specifically phosphorylates chloroplast precursor proteins in the cytosol within the cleavable presequences (transit peptides). May be part of a cytosolic regulatory network involved in chloroplast protein import. Does not phosphorylate mitochondrion precursor proteins. Specific for ATP and does not utilize other NTPs (PubMed:16429265, PubMed:17090544).
Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins (PubMed:21799034).
Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins (PubMed:21799034).
Miscellaneous
Plants silencing STY17 does not show visible phenotype under normal growth conditions, but plants silencing STY17 in the double mutant sty8 and sty46 background show more severe retarded growth compared to the double mutant itself.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by autophosphorylation at Thr-445.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
14 μM | ATP |
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | protein serine/threonine/tyrosine kinase activity | |
Biological Process | chloroplast organization |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase STY17
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8RWL6
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 445 | Loss of autophosphorylation and enzyme activation. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 21 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_0000433999 | 1-570 | Serine/threonine-protein kinase STY17 | |||
Sequence: MAIKEETEESCGSRAVVASITKESPRQHRMKLEVYGEVLQRIQESNYEEANFPGFDDLLWLHFNRLPARYALDVNVERAEDVLTHQRLLKLAEDPATRPVFEVRCVQVSPTLNGNSGDVDPSDPAVNEDAQSSYNSRSLAPPTFGSSPNFEALTQAYKDHAQDDDSAVNAQLPNSRPMHEITFSTIDRPKLLSQLTSMLGELGLNIQEAHAFSTADGFSLDVFVVDGWSQEETEGLKDALKKEIRKFKDQPCSKQKSITFFEHDKSTNELLPACVEIPTDGTDEWEIDMKQLKIEKKVACGSYGELFRGTYCSQEVAIKILKPERVNAEMLREFSQEVYIMRKVRHKNVVQFIGACTRSPNLCIVTEFMTRGSIYDFLHKHKGVFKIQSLLKVALDVSKGMNYLHQNNIIHRDLKTANLLMDEHEVVKVADFGVARVQTESGVMTAETGTYRWMAPEVIEHKPYDHRADVFSYAIVLWELLTGELPYSYLTPLQAAVGVVQKGLRPKIPKETHPKLTELLEKCWQQDPALRPNFAEIIEMLNQLIREVGDDERHKDKHGGYFSGLKKGHR | ||||||
Modified residue | 441 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 445 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Autophosphorylated on serine and threonine residues. Autophosphorylated at Thr-445.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 112-145 | Disordered | ||||
Sequence: LNGNSGDVDPSDPAVNEDAQSSYNSRSLAPPTFG | ||||||
Domain | 180-260 | ACT | ||||
Sequence: EITFSTIDRPKLLSQLTSMLGELGLNIQEAHAFSTADGFSLDVFVVDGWSQEETEGLKDALKKEIRKFKDQPCSKQKSITF | ||||||
Domain | 292-545 | Protein kinase | ||||
Sequence: LKIEKKVACGSYGELFRGTYCSQEVAIKILKPERVNAEMLREFSQEVYIMRKVRHKNVVQFIGACTRSPNLCIVTEFMTRGSIYDFLHKHKGVFKIQSLLKVALDVSKGMNYLHQNNIIHRDLKTANLLMDEHEVVKVADFGVARVQTESGVMTAETGTYRWMAPEVIEHKPYDHRADVFSYAIVLWELLTGELPYSYLTPLQAAVGVVQKGLRPKIPKETHPKLTELLEKCWQQDPALRPNFAEIIEMLNQLI |
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length570
- Mass (Da)64,696
- Last updated2002-06-01 v1
- ChecksumD0961D218BE49344
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL031135 EMBL· GenBank· DDBJ | CAA20048.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161588 EMBL· GenBank· DDBJ | CAB81487.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE86563.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY093017 EMBL· GenBank· DDBJ | AAM13016.1 EMBL· GenBank· DDBJ | mRNA | ||
AY128938 EMBL· GenBank· DDBJ | AAM91338.1 EMBL· GenBank· DDBJ | mRNA |