JAR1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: JAR1_ARATH
• UniProt AC: Q9SKE2
• Protein Name: Jasmonic acid-amido synthetase JAR1
• Gene Name: JAR1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 575
• Subcellular Localization: Cytoplasm .
• Protein Description: Catalyzes the synthesis of jasmonates-amino acid conjugates by adenylation; can use Ile and, in vitro at least, Val, Leu and Phe as conjugating amino acids on jasmonic acid (JA) and 9,10-dihydro-JA substrates, and to a lower extent, on 3-oxo-2-(2Z-pentenyl)-cyclopentane-1-butyric acid (OPC-4) and 12-hydroxy-JA (12-OH-JA). Can synthesize adenosine 5-tetraphosphate in vitro. Required for the JA-mediated signaling pathway that regulates many developmental and defense mechanisms, including growth root inhibition, vegetative storage proteins (VSPs) accumulation, induced systemic resistance (ISR), response to wounding and herbivores, tolerance to ozone O(3) (probably having a role in lesion containment). Plays an important role in the accumulation of JA-Ile in response to wounding, both locally and systemically; promotes JA responding genes especially in distal part of wounded plants, via the JA-Ile-stimulated degradation of JAZ repressor proteins by the SCF(COI)E3 ubiquitin-protein ligase pathway. Involved in the apoptosis-like programmed cell death (PCD) induced by fungal toxin fumonisin B1-mediated (FB1). Required for volatile compounds (C6-aldehydes and allo-ocimene)-mediated defense activation. Involved in the non-pathogenic rhizobacterium-mediated ISR (defense priming) by P.fluorescens (strains CHAOr and WCS417r) and P.putida LSW17S against infection leaf pathogens such as P.syringae pv. tomato and H.parasitica. Required for the JA-dependent resistance to fungi such as P.irregulare, U.vignae and U.appendiculatus. Necessary to induce systemic resistance against R.solanaceraum and P.syringae pv. tomato with P.oligandrum (a non-pathogenic biocontrol agent) cell wall protein fraction (CWP). Mediates PGIP2 accumulation in response to B.cinerea infection and thus contributes to resistance against this pathogen. Modulates the UV-B alteration of leaves attractiveness to diamondback moths P.xylostella leading to insect oviposition. Involved in the regulation of far-red light influence on development. Seems necessary for the salicylic acid (SA)-mediated, NPR1-independent resistance pathway. May contribute to the chitin-elicited pathway. Contributes to the sensitivity toward F.graminearum..
• Protein Sequence: MLEKVETFDMNRVIDEFDEMTRNAHQVQKQTLKEILLKNQSAIYLQNCGLNGNATDPEEAFKSMVPLVTDVELEPYIKRMVDGDTSPILTGHPVPAISLSSGTSQGRPKFIPFTDELMENTLQLFRTAFAFRNRDFPIDDNGKALQFIFSSKQYISTGGVPVGTATTNVYRNPNFKAGMKSITSPSCSPDEVIFSPDVHQALYCHLLSGILFRDQVQYVFAVFAHGLVHAFRTFEQVWEEIVTDIKDGVLSNRITVPSVRTAMSKLLTPNPELAETIRTKCMSLSNWYGLIPALFPNAKYVYGIMTGSMEPYVPKLRHYAGDLPLVSHDYGSSEGWIAANVTPRLSPEEATFAVIPNLGYFEFLPVSETGEGEEKPVGLTQVKIGEEYEVVITNYAGLYRYRLGDVVKVIGFYNNTPQLKFICRRNLILSINIDKNTERDLQLSVESAAKRLSEEKIEVIDFSSYIDVSTDPGHYAIFWEISGETNEDVLQDCCNCLDRAFIDAGYVSSRKCKTIGALELRVVAKGTFRKIQEHFLGLGSSAGQFKMPRCVKPSNAKVLQILCENVVSSYFSTAF

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
261	Phosphorylation	ITVPSVRTAMSKLLT CCCHHHHHHHHHHCC	25.26	19880383

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

Oops, there are no upstream regulatory protein records of JAR1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of JAR1_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of JAR1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GEML1_ARATH	FIP1	physical	17220357
JAR1_ARATH	JAR1	physical	21525334
COP1_ARATH	COP1	physical	21525334

Drug and Disease Associations

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