dbPTM

RAC8_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAC8_ARATH
UniProt AC	Q9SU67
Protein Name	Rac-like GTP-binding protein ARAC8
Gene Name	ARAC8
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	208
Subcellular Localization	Membrane Lipid-anchor .
Protein Description	Acts as a negative regulator of abscisic acid (ABA) responses..
Protein Sequence	MASSASKFIKCVTVGDGAVGKTCMLICYTSNKFPTDYIPTVFDNFSVNVVVEGITVNLGLWDTAGQEDYNRLRPLSYRGADVFVLAFSLISRASYENVFKKWIPELQHFAPGVPIVLVGTKMDLREDRHYLSDHPGLSPVTTSQGEELRKHIGATYYIECSSKTQQNVKAVFDAAIKVVIKPAVKQKEKKKKQKPRSGCLSNILCGKN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
199	S-palmitoylation	KQKPRSGCLSNILCG CCCCCCCCCHHHHCC	3.87	-
199	S-palmitoylation	KQKPRSGCLSNILCG CCCCCCCCCHHHHCC	3.87	12368496
205	S-palmitoylation	GCLSNILCGKN---- CCCHHHHCCCC----	6.89	-
205	S-palmitoylation	GCLSNILCGKN---- CCCHHHHCCCC----	6.89	12368496

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of RAC8_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
205	C	Palmitoylation		12368496
Although this sequence has a C-terminal -CXXX, it is palmitoylated at Cys-205, rather than prenylated.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RAC8_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CBSX1_ARATH	LEJ2	physical	21798944
ROGF1_ARATH	ROPGEF1	physical	21798944

Drug and Disease Associations

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

Regulatory Network of RAC8_ARATH

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"A cell-specific, prenylation-independent mechanism regulatestargeting of type II RACs."; Lavy M., Bracha-Drori K., Sternberg H., Yalovsky S.; Plant Cell 14:2431-2450(2002). Cited for: PALMITOYLATION AT CYS-199 AND CYS-205, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF CYS-199 AND CYS-205.	12368496 [Abstract]