NPR1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NPR1_ARATH
• UniProt AC: P93002
• Protein Name: Regulatory protein NPR1
• Gene Name: NPR1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 593
• Subcellular Localization: Cytoplasm. Nucleus. Accumulation in nucleus after induction by salicylic acid (SA) treatment or after pathogen infection.
• Protein Description: 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 (By similarity). 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..
• Protein Sequence: MDTTIDGFADSYEISSTSFVATDNTDSSIVYLAAEQVLTGPDVSALQLLSNSFESVFDSPDDFYSDAKLVLSDGREVSFHRCVLSARSSFFKSALAAAKKEKDSNNTAAVKLELKEIAKDYEVGFDSVVTVLAYVYSSRVRPPPKGVSECADENCCHVACRPAVDFMLEVLYLAFIFKIPELITLYQRHLLDVVDKVVIEDTLVILKLANICGKACMKLLDRCKEIIVKSNVDMVSLEKSLPEELVKEIIDRRKELGLEVPKVKKHVSNVHKALDSDDIELVKLLLKEDHTNLDDACALHFAVAYCNVKTATDLLKLDLADVNHRNPRGYTVLHVAAMRKEPQLILSLLEKGASASEATLEGRTALMIAKQATMAVECNNIPEQCKHSLKGRLCVEILEQEDKREQIPRDVPPSFAVAADELKMTLLDLENRVALAQRLFPTEAQAAMEIAEMKGTCEFIVTSLEPDRLTGTKRTSPGVKIAPFRILEEHQSRLKALSKTVELGKRFFPRCSAVLDQIMNCEDLTQLACGEDDTAEKRLQKKQRYMEIQETLKKAFSEDNLELGNSSLTDSTSSTSKSTGGKRSNRKLSHRRR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	TIDGFADSYEISSTS CCCCCCCEEEEECEE	22.64	19490895
15	Phosphorylation	FADSYEISSTSFVAT CCCEEEEECEEEEEE	18.67	19490895
104	Phosphorylation	AAKKEKDSNNTAAVK HHHHHHCCCCCHHHH	42.94	24894044
156	S-nitrosylation	ECADENCCHVACRPA HCCCCCCCCCCCHHH	4.33	18635760
347	Phosphorylation	KEPQLILSLLEKGAS CCCHHHHHHHHCCCC	24.74	19880383

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NPR1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
11	S	Phosphorylation	Phosphorylated at Ser-11 and Ser-15 in the nucleus; facilitates its recruitment to a cullin3-based ubiquitin ligase leading to polyubiquitination and subsequent CUL3/CSN-mediated degradation.	19490895
11	S	ubiquitylation	Phosphorylated at Ser-11 and Ser-15 in the nucleus; facilitates its recruitment to a cullin3-based ubiquitin ligase leading to polyubiquitination and subsequent CUL3/CSN-mediated degradation.	19490895
15	S	Phosphorylation	Phosphorylated at Ser-11 and Ser-15 in the nucleus; facilitates its recruitment to a cullin3-based ubiquitin ligase leading to polyubiquitination and subsequent CUL3/CSN-mediated degradation.	19490895
15	S	ubiquitylation	Phosphorylated at Ser-11 and Ser-15 in the nucleus; facilitates its recruitment to a cullin3-based ubiquitin ligase leading to polyubiquitination and subsequent CUL3/CSN-mediated degradation.	19490895
156	C	S-nitrosylation	S-nitrosylation at Cys-156 facilitates its oligomerization.	18635760

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NPR1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TGA5_ARATH	OBF5	physical	10659709
TGA1_ARATH	TGA1	physical	10659709
TGA2_ARATH	AHBP-1B	physical	10659709
TGA3_ARATH	TGA3	physical	10659709
TGA6_ARATH	TGA6	physical	10659709
TGA2_ARATH	AHBP-1B	physical	12383081
TGA5_ARATH	OBF5	physical	12383081
TGA1_ARATH	TGA1	physical	12953119
TGA2_ARATH	AHBP-1B	physical	12953119
TGA6_ARATH	TGA6	physical	10339621
TGA5_ARATH	OBF5	physical	10339621
TGA2_ARATH	AHBP-1B	physical	10339621
TGA2_ARATH	AHBP-1B	physical	10662863
TGA3_ARATH	TGA3	physical	10662863
TGA2_ARATH	AHBP-1B	physical	15634206
TGA3_ARATH	TGA3	physical	15634206
TGA5_ARATH	OBF5	physical	15634206
TGA6_ARATH	TGA6	physical	15634206
NIMI3_ARATH	NIMIN-3	physical	15634206
SKL1_ARATH	SKL1	physical	21798944
NIMI2_ARATH	NIMIN-2	physical	21798944
TGA2_ARATH	AHBP-1B	physical	22986789
NPR3_ARATH	NPR3	physical	22986789
CIPKB_ARATH	SIP4	physical	20621018
NPR1_ARATH	NPR1	physical	25201412

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Proteasome-mediated turnover of the transcription coactivator NPR1plays dual roles in regulating plant immunity.";
Spoel S.H., Mou Z., Tada Y., Spivey N.W., Genschik P., Dong X.;
Cell 137:860-872(2009).
Cited for: PHOSPHORYLATION AT SER-11 AND SER-15, MUTAGENESIS OF SER-11 ANDSER-15, UBIQUITINATION, AND PROTEASOMAL DEGRADATION.
PubMed: 19490895

S-nitrosylation

"Plant immunity requires conformational changes of NPR1 via S-nitrosylation and thioredoxins.";
Tada Y., Spoel S.H., Pajerowska-Mukhtar K., Mou Z., Song J., Wang C.,Zuo J., Dong X.;
Science 321:952-956(2008).
Cited for: S-NITROSYLATION AT CYS-156.
PubMed: 18635760