P27450 · CST_ARATH
- ProteinProbable serine/threonine-protein kinase CST
- GeneCST
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids419 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | negative regulation of floral organ abscission |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable serine/threonine-protein kinase CST
- 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 accessionP27450
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Drastic reduction of plasma membrane localization and strong increase of nuclear localization. Partial redistribution from the plasma membrane to the cytoplasm. | ||||
Sequence: G → A | ||||||
Mutagenesis | 4 | Partial redistribution from the plasma membrane to the cytoplasm. | ||||
Sequence: C → S | ||||||
Mutagenesis | 124 | Abolishes kinase activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 157 | In cst-1; abolishes kinase activity. | ||||
Sequence: G → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 24 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000024321 | 2-419 | Probable serine/threonine-protein kinase CST | |||
Sequence: GACISFFSSSSPSKTGLHSHATTNNHSNGTEFSSTTGATTNSSVGQQSQFSDISTGIISDSGKLLESPNLKVYNFLDLKTATKNFKPDSMLGQGGFGKVYRGWVDATTLAPSRVGSGMIVAIKRLNSESVQGFAEWRSEVNFLGMLSHRNLVKLLGYCREDKELLLVYEFMPKGSLESHLFRRNDPFPWDLRIKIVIGAARGLAFLHSLQREVIYRDFKASNILLDSNYDAKLSDFGLAKLGPADEKSHVTTRIMGTYGYAAPEYMATGHLYVKSDVFAFGVVLLEIMTGLTAHNTKRPRGQESLVDWLRPELSNKHRVKQIMDKGIKGQYTTKVATEMARITLSCIEPDPKNRPHMKEVVEVLEHIQGLNVVPNRSSTKQAVANSSRSSPHHYRYKAGALGAERKRATPGRFGSVEK | ||||||
Lipidation | 4 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 117 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 169 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 222 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 253 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 258 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 266 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 8-48 | Disordered | ||||
Sequence: FSSSSPSKTGLHSHATTNNHSNGTEFSSTTGATTNSSVGQQ | ||||||
Domain | 86-368 | Protein kinase | ||||
Sequence: FKPDSMLGQGGFGKVYRGWVDATTLAPSRVGSGMIVAIKRLNSESVQGFAEWRSEVNFLGMLSHRNLVKLLGYCREDKELLLVYEFMPKGSLESHLFRRNDPFPWDLRIKIVIGAARGLAFLHSLQREVIYRDFKASNILLDSNYDAKLSDFGLAKLGPADEKSHVTTRIMGTYGYAAPEYMATGHLYVKSDVFAFGVVLLEIMTGLTAHNTKRPRGQESLVDWLRPELSNKHRVKQIMDKGIKGQYTTKVATEMARITLSCIEPDPKNRPHMKEVVEVLEHI | ||||||
Compositional bias | 378-393 | Polar residues | ||||
Sequence: SSTKQAVANSSRSSPH | ||||||
Region | 378-419 | Disordered | ||||
Sequence: SSTKQAVANSSRSSPHHYRYKAGALGAERKRATPGRFGSVEK |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
P27450-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length419
- Mass (Da)46,340
- Last updated2004-06-21 v2
- Checksum7C85AB6C38925145
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4JN38 | F4JN38_ARATH | CST | 420 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 378-393 | Polar residues | ||||
Sequence: SSTKQAVANSSRSSPH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M63234 EMBL· GenBank· DDBJ | AAA32850.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AL031135 EMBL· GenBank· DDBJ | CAA20030.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL161587 EMBL· GenBank· DDBJ | CAB80276.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002687 EMBL· GenBank· DDBJ | AEE86538.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY065403 EMBL· GenBank· DDBJ | AAL38844.1 EMBL· GenBank· DDBJ | mRNA | ||
AY096501 EMBL· GenBank· DDBJ | AAM20151.1 EMBL· GenBank· DDBJ | mRNA |