Q8RY65 · NIK2_ARATH
- ProteinProtein NSP-INTERACTING KINASE 2
- GeneNIK2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids635 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in defense response to geminivirus infection (By similarity).
Phosphorylates RPL10A in vitro
Phosphorylates RPL10A in vitro
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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 | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 318-326 | ATP (UniProtKB | ChEBI) | |||
Binding site | 340 | ATP (UniProtKB | ChEBI) | |||
Active site | 435 | Proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | histone H2AS1 kinase activity | |
Molecular Function | protein serine kinase activity | |
Biological Process | defense response | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein NSP-INTERACTING KINASE 2
- 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 accessionQ8RY65
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Topological domain | 33-248 | Extracellular | |||
Transmembrane | 249-269 | Helical | |||
Topological domain | 270-635 | Cytoplasmic | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-32 | ||||
Chain | PRO_0000409726 | 33-635 | Protein NSP-INTERACTING KINASE 2 | ||
Glycosylation | 92 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 103 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 140 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 162 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 175 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 188 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 219 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 231 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 235 | N-linked (GlcNAc...) asparagine | |||
Modified residue | 309 | Phosphothreonine | |||
Modified residue | 393 | Phosphoserine | |||
Modified residue | 396 | Phosphoserine | |||
Modified residue | 408 | Phosphothreonine | |||
Modified residue | 468 | Phosphothreonine | |||
Modified residue | 469 | Phosphothreonine | |||
Modified residue | 474 | Phosphothreonine | |||
Modified residue | 482 | Phosphotyrosine | |||
Modified residue | 484 | Phosphoserine | |||
Modified residue | 485 | Phosphothreonine | |||
Modified residue | 489 | Phosphoserine | |||
Modified residue | 564 | Phosphothreonine | |||
Post-translational modification
Autophosphorylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Oligomer. Interacts with geminivirus nuclear shuttle protein (NSP).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | Q8RY65 | BAK1 Q94F62 | 2 | EBI-20664696, EBI-617138 | |
BINARY | Q8RY65 | ERL2 Q6XAT2 | 4 | EBI-20664696, EBI-16895926 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, region, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Repeat | 104-128 | LRR 1 | |||
Repeat | 129-153 | LRR 2 | |||
Repeat | 155-176 | LRR 3 | |||
Repeat | 177-200 | LRR 4 | |||
Region | 214-242 | Disordered | |||
Domain | 312-591 | Protein kinase | |||
Region | 422-502 | Interaction with geminivirus NSP protein | |||
Region | 593-621 | Disordered | |||
Compositional bias | 596-621 | Polar residues | |||
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe 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.
- Name1
- Length635
- Mass (Da)70,606
- Last updated2002-06-01 v1
- Checksum848032CABD9DFA45
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 596-621 | Polar residues | |||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |