P27450 · CST_ARATH

Function

function

Acts as a spatial inhibitor of signaling that modulates abscission zone cell adhesion and expansion. Acts both directly and indirectly by physically interacting with RLK5/HAE and SOBIR1/EVR at the cell surface.

Caution

Was originally (PubMed:1851993) reported to be a connexin and to contain transmembrane domains. PubMed:8400879 authors have assigned that this is not a connexin, but rather a protein kinase.

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site92-100ATP (UniProtKB | ChEBI)
Binding site124ATP (UniProtKB | ChEBI)
Active site218Proton acceptor

GO annotations

AspectTerm
Cellular Componentnucleus
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processnegative regulation of floral organ abscission

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable serine/threonine-protein kinase CST
  • EC number
  • Alternative names
    • Protein CAST AWAY

Gene names

    • Name
      CST
    • Synonyms
      CX32
      , KIN4
    • ORF names
      F8D20.110
    • Ordered locus names
      At4g35600

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    P27450
  • Secondary accessions
    • O81792
    • Q8VZ07
    • Q9M068

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Cell membrane
; Lipid-anchor
Nucleus
Note: Predominantly localized at the plasma membrane.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis2Drastic reduction of plasma membrane localization and strong increase of nuclear localization. Partial redistribution from the plasma membrane to the cytoplasm.
Mutagenesis4Partial redistribution from the plasma membrane to the cytoplasm.
Mutagenesis124Abolishes kinase activity.
Mutagenesis157In cst-1; abolishes kinase activity.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for initiator methionine, lipidation, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
Lipidation2N-myristoyl glycine
ChainPRO_00000243212-419Probable serine/threonine-protein kinase CST
Lipidation4S-palmitoyl cysteine
Modified residue117Phosphoserine
Modified residue169Phosphotyrosine
Modified residue222Phosphoserine
Modified residue253Phosphothreonine
Modified residue258Phosphothreonine
Modified residue266Phosphotyrosine

Post-translational modification

Autophosphorylated on serine, threonine and tyrosine residues.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with SOBIR1/EVR and RLK5/HAE.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region8-48Disordered
Domain86-368Protein kinase
Compositional bias378-393Polar residues
Region378-419Disordered

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete

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.

  • Length
    419
  • Mass (Da)
    46,340
  • Last updated
    2004-06-21 v2
  • Checksum
    7C85AB6C38925145
MGACISFFSSSSPSKTGLHSHATTNNHSNGTEFSSTTGATTNSSVGQQSQFSDISTGIISDSGKLLESPNLKVYNFLDLKTATKNFKPDSMLGQGGFGKVYRGWVDATTLAPSRVGSGMIVAIKRLNSESVQGFAEWRSEVNFLGMLSHRNLVKLLGYCREDKELLLVYEFMPKGSLESHLFRRNDPFPWDLRIKIVIGAARGLAFLHSLQREVIYRDFKASNILLDSNYDAKLSDFGLAKLGPADEKSHVTTRIMGTYGYAAPEYMATGHLYVKSDVFAFGVVLLEIMTGLTAHNTKRPRGQESLVDWLRPELSNKHRVKQIMDKGIKGQYTTKVATEMARITLSCIEPDPKNRPHMKEVVEVLEHIQGLNVVPNRSSTKQAVANSSRSSPHHYRYKAGALGAERKRATPGRFGSVEK

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F4JN38F4JN38_ARATHCST420

Sequence caution

The sequence AAA32850.1 differs from that shown. Reason: Frameshift
The sequence AAA32850.1 differs from that shown. Reason: Miscellaneous discrepancy Sequencing errors.
The sequence CAA20030.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAB80276.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias378-393Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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