ARR1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ARR1_ARATH
• UniProt AC: Q940D0
• Protein Name: Two-component response regulator ARR1
• Gene Name: ARR1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 690
• Subcellular Localization: Nucleus .
• Protein Description: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]GATT-3'. Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Could directly activate some type-A response regulators in response to cytokinins. Regulates SHY2 by binding to its promoter. [PubMed: 19039136 Involved in the root-meristem size determination through the regulation of cell differentiation]
• Protein Sequence: MMNPSHGRGLGSAGGSSSGRNQGGGGETVVEMFPSGLRVLVVDDDPTCLMILERMLRTCLYEVTKCNRAEMALSLLRKNKHGFDIVISDVHMPDMDGFKLLEHVGLEMDLPVIMMSADDSKSVVLKGVTHGAVDYLIKPVRMEALKNIWQHVVRKRRSEWSVPEHSGSIEETGERQQQQHRGGGGGAAVSGGEDAVDDNSSSVNEGNNWRSSSRKRKDEEGEEQGDDKDEDASNLKKPRVVWSVELHQQFVAAVNQLGVEKAVPKKILELMNVPGLTRENVASHLQKYRIYLRRLGGVSQHQGNLNNSFMTGQDASFGPLSTLNGFDLQALAVTGQLPAQSLAQLQAAGLGRPAMVSKSGLPVSSIVDERSIFSFDNTKTRFGEGLGHHGQQPQQQPQMNLLHGVPTGLQQQLPMGNRMSIQQQIAAVRAGNSVQNNGMLMPLAGQQSLPRGPPPMLTSSQSSIRQPMLSNRISERSGFSGRNNIPESSRVLPTSYTNLTTQHSSSSMPYNNFQPELPVNSFPLASAPGISVPVRKATSYQEEVNSSEAGFTTPSYDMFTTRQNDWDLRNIGIAFDSHQDSESAAFSASEAYSSSSMSRHNTTVAATEHGRNHQQPPSGMVQHHQVYADGNGGSVRVKSERVATDTATMAFHEQYSNQEDLMSALLKQEGIAPVDGEFDFDAYSIDNIPV

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
17	Phosphorylation	LGSAGGSSSGRNQGG CCCCCCCCCCCCCCC	39.83	25561503
89	Phosphorylation	GFDIVISDVHMPDMD CCCEEEECCCCCCCC	24.18	-
166	Phosphorylation	EWSVPEHSGSIEETG CCCCCCCCCCCCCCC	32.35	23111157
168	Phosphorylation	SVPEHSGSIEETGER CCCCCCCCCCCCCHH	29.82	23111157
172	Phosphorylation	HSGSIEETGERQQQQ CCCCCCCCCHHHHHH	31.39	25561503
190	Phosphorylation	GGGGAAVSGGEDAVD CCCCCCCCCCCCCCC	36.03	30291188
200	Phosphorylation	EDAVDDNSSSVNEGN CCCCCCCCCCCCCCC	30.87	23776212
201	Phosphorylation	DAVDDNSSSVNEGNN CCCCCCCCCCCCCCC	44.55	23776212
202	Phosphorylation	AVDDNSSSVNEGNNW CCCCCCCCCCCCCCC	28.87	23776212
474	Phosphorylation	PMLSNRISERSGFSG CHHHCHHHHCCCCCC	24.58	24894044
477	Phosphorylation	SNRISERSGFSGRNN HCHHHHCCCCCCCCC	39.89	24894044
538	Phosphorylation	SVPVRKATSYQEEVN CCEEEECCCCHHHHC	30.88	24924143
539	Phosphorylation	VPVRKATSYQEEVNS CEEEECCCCHHHHCC	29.67	19880383
546	Phosphorylation	SYQEEVNSSEAGFTT CCHHHHCCCCCCCCC	34.43	19880383
547	Phosphorylation	YQEEVNSSEAGFTTP CHHHHCCCCCCCCCC	26.68	19880383
552	Phosphorylation	NSSEAGFTTPSYDMF CCCCCCCCCCCCCCC	36.56	19880383
553	Phosphorylation	SSEAGFTTPSYDMFT CCCCCCCCCCCCCCC	14.15	24924143
556	Phosphorylation	AGFTTPSYDMFTTRQ CCCCCCCCCCCCCCC	16.78	19880383
560	Phosphorylation	TPSYDMFTTRQNDWD CCCCCCCCCCCCCCC	17.90	19880383

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

Oops, there are no upstream regulatory protein records of ARR1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ARR1_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 ARR1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AHP3_ARATH	AHP3	physical	18642946
ERF79_ARATH	ERF8	physical	18642946
AHP2_ARATH	AHP2	physical	18642946
AHP1_ARATH	AHP1	physical	18642946
TBB9_ARATH	TUB9	physical	18642946
AHP2_ARATH	AHP2	physical	11158442
AHP1_ARATH	AHP1	physical	16965536
AHP2_ARATH	AHP2	physical	16965536
AHP3_ARATH	AHP3	physical	16965536
AHP4_ARATH	AHP4	physical	16965536
AHP5_ARATH	AHP5	physical	16965536

Drug and Disease Associations

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