NCBI Accession #
NP_176610.1
NCBI GenBank Nucleotide #
NM_105102.3
NCBI Official Full Name
regulatory protein (NPR1)
NCBI Official Symbol
NPR1
NCBI Official Synonym Symbols
ARABIDOPSIS NONEXPRESSER OF PR GENES 1; ATNPR1; F15H21.6; F15H21_6; NIM1; NON-INDUCIBLE IMMUNITY 1; NONEXPRESSER OF PR GENES 1; REGULATORY PROTEIN NPR1; SAI1; SALICYLIC ACID INSENSITIVE 1
NCBI Protein Information
regulatory protein (NPR1)
NCBI Summary
This gene is a key regulator of the salicylic acid (SA)-mediated systemic acquired resistance (SAR) pathway. It is similar to the transcription factor inhibitor I kappa B, and contains ankyrin repeats. It confers resistance to the pathogens Pseudomonas syringae and Peronospora parasitica in a dosage-dependent fashion. Although transgenic Arabidopsis plants overexpressing NPR1 acquire enhanced sensitivity to SA and (benzothiadiazole) BTH, they display no obvious detrimental morphological changes and do not have elevated pathogenesis-related gene expression until activated by inducers or pathogens.
UniProt Synonym Gene Names
NIM1; SAI1; Nim1; Sai1
UniProt Protein Name
Regulatory protein NPR1
UniProt Synonym Protein Names
BTB/POZ domain-containing protein NPR1; Non-inducible immunity protein 1; Nim1; Nonexpresser of PR genes 1; Salicylic acid insensitive 1; Sai1
UniProt Primary Accession #
P93002
UniProt Secondary Accession #
O04742
UniProt Related Accession #
P93002
UniProt Comments
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins . Key positive regulator of the SA-dependent signaling pathway that negatively regulates JA-dependent signaling pathway. Mediates the binding of TGA factors to the as-1 motif found in the pathogenesis-related PR-1 gene, leading to the transcriptional regulation of the gene defense. Controls the onset of systemic acquired resistance (SAR). Upon SAR induction, a biphasic change in cellular reduction potential occurs, resulting in reduction of the cytoplasmic oligomeric form to a monomeric form that accumulates in the nucleus and activates gene expression. Phosphorylated form is target of proteasome degradation.