Q8RY65 · NIK2_ARATH

Function

function

Involved in defense response to geminivirus infection (By similarity).
Phosphorylates RPL10A in vitro

Catalytic activity

Activity regulation

Inhibited by the viral nuclear shuttle protein (NSP) that binds to the region required for oligomerization.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site318-326ATP (UniProtKB | ChEBI)
Binding site340ATP (UniProtKB | ChEBI)
Active site435Proton acceptor

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionhistone H2AS1 kinase activity
Molecular Functionprotein serine kinase activity
Biological Processdefense response
Biological Processprotein phosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein NSP-INTERACTING KINASE 2
  • EC number
  • Alternative names
    • LRR receptor-like serine/threonine-protein kinase NIK2

Gene names

    • Name
      NIK2
    • ORF names
      MWL2.18
    • Ordered locus names
      At3g25560

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
    Q8RY65
  • Secondary accessions
    • Q9LSU7

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Cell membrane
; Single-pass type I membrane protein

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain33-248Extracellular
Transmembrane249-269Helical
Topological domain270-635Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, modified residue.

Type
IDPosition(s)Description
Signal1-32
ChainPRO_000040972633-635Protein NSP-INTERACTING KINASE 2
Glycosylation92N-linked (GlcNAc...) asparagine
Glycosylation103N-linked (GlcNAc...) asparagine
Glycosylation140N-linked (GlcNAc...) asparagine
Glycosylation162N-linked (GlcNAc...) asparagine
Glycosylation175N-linked (GlcNAc...) asparagine
Glycosylation188N-linked (GlcNAc...) asparagine
Glycosylation219N-linked (GlcNAc...) asparagine
Glycosylation231N-linked (GlcNAc...) asparagine
Glycosylation235N-linked (GlcNAc...) asparagine
Modified residue309Phosphothreonine
Modified residue393Phosphoserine
Modified residue396Phosphoserine
Modified residue408Phosphothreonine
Modified residue468Phosphothreonine
Modified residue469Phosphothreonine
Modified residue474Phosphothreonine
Modified residue482Phosphotyrosine
Modified residue484Phosphoserine
Modified residue485Phosphothreonine
Modified residue489Phosphoserine
Modified residue564Phosphothreonine

Post-translational modification

Autophosphorylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in flowers and roots.

Gene expression databases

Interaction

Subunit

Oligomer. Interacts with geminivirus nuclear shuttle protein (NSP).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q8RY65BAK1 Q94F622EBI-20664696, EBI-617138
BINARY Q8RY65ERL2 Q6XAT24EBI-20664696, EBI-16895926

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for repeat, region, domain, compositional bias.

Type
IDPosition(s)Description
Repeat104-128LRR 1
Repeat129-153LRR 2
Repeat155-176LRR 3
Repeat177-200LRR 4
Region214-242Disordered
Domain312-591Protein kinase
Region422-502Interaction with geminivirus NSP protein
Region593-621Disordered
Compositional bias596-621Polar residues

Sequence similarities

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.

Q8RY65-1

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
    635
  • Mass (Da)
    70,606
  • Last updated
    2002-06-01 v1
  • Checksum
    848032CABD9DFA45
MLQGRREAKKSYALFSSTFFFFFICFLSSSSAELTDKGVNFEVVALIGIKSSLTDPHGVLMNWDDTAVDPCSWNMITCSDGFVIRLEAPSQNLSGTLSSSIGNLTNLQTVLLQNNYITGNIPHEIGKLMKLKTLDLSTNNFTGQIPFTLSYSKNLQYLRVNNNSLTGTIPSSLANMTQLTFLDLSYNNLSGPVPRSLAKTFNVMGNSQICPTGTEKDCNGTQPKPMSITLNSSQNKSSDGGTKNRKIAVVFGVSLTCVCLLIIGFGFLLWWRRRHNKQVLFFDINEQNKEEMCLGNLRRFNFKELQSATSNFSSKNLVGKGGFGNVYKGCLHDGSIIAVKRLKDINNGGGEVQFQTELEMISLAVHRNLLRLYGFCTTSSERLLVYPYMSNGSVASRLKAKPVLDWGTRKRIALGAGRGLLYLHEQCDPKIIHRDVKAANILLDDYFEAVVGDFGLAKLLDHEESHVTTAVRGTVGHIAPEYLSTGQSSEKTDVFGFGILLLELITGLRALEFGKAANQRGAILDWVKKLQQEKKLEQIVDKDLKSNYDRIEVEEMVQVALLCTQYLPIHRPKMSEVVRMLEGDGLVEKWEASSQRAETNRSYSKPNEFSSSERYSDLTDDSSVLVQAMELSGPR

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F4JA15F4JA15_ARATHNIK2647
F4JA17F4JA17_ARATHNIK2636

Sequence caution

The sequence BAB01326.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias596-621Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB025639
EMBL· GenBank· DDBJ
BAB01326.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002686
EMBL· GenBank· DDBJ
AEE77026.1
EMBL· GenBank· DDBJ
Genomic DNA
AY075617
EMBL· GenBank· DDBJ
AAL91629.1
EMBL· GenBank· DDBJ
mRNA
BT002619
EMBL· GenBank· DDBJ
AAO11535.1
EMBL· GenBank· DDBJ
mRNA
FJ708728
EMBL· GenBank· DDBJ
ACN59323.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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