GDIR_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GDIR_ARATH
• UniProt AC: Q9SFC6
• Protein Name: Rho GDP-dissociation inhibitor 1
• Gene Name: GDI1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 240
• Subcellular Localization: Cytoplasm.
• Protein Description: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them..
• Protein Sequence: MSLVSGARDMGFDDNNNNKNNKDGDDENSSSRTRADDDALSRQMSESSLCATEEEEDDDSKLQLGPQYTIKEHLEKDKDDESLRKWKEQLLGSVDVTNIGETLDPEVRIDSLAIISPGRPDIVLLVPENGNPKGMWFTLKEGSKYNLKFTFHVNNNIVSGLRYTNTVWKTGVKVDRAKEMLGTFSPQLEPYNHVMPEETTPSGMFARGSYSARTKFLDDDNKCYLEINYSFDIRKEWPAL

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
41	Phosphorylation	RADDDALSRQMSESS HHCHHHHHHHHHHHH	23.37	25561503
45	Phosphorylation	DALSRQMSESSLCAT HHHHHHHHHHHCCCC	26.45	23776212
47	Phosphorylation	LSRQMSESSLCATEE HHHHHHHHHCCCCCC	22.70	23776212
48	Phosphorylation	SRQMSESSLCATEEE HHHHHHHHCCCCCCC	24.34	23776212
52	Phosphorylation	SESSLCATEEEEDDD HHHHCCCCCCCCCCC	42.82	23776212
60	Phosphorylation	EEEEDDDSKLQLGPQ CCCCCCCCCCCCCCC	42.11	23776212
68	Phosphorylation	KLQLGPQYTIKEHLE CCCCCCCCCHHHHHH	17.36	23776212
69	Phosphorylation	LQLGPQYTIKEHLEK CCCCCCCCHHHHHHH	21.96	23776212

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GDIR_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 GDIR_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAC5_ARATH	ARAC5	physical	10798620
SUMO3_ARATH	SUMO3	physical	20855607
SUMO1_ARATH	SUMO1	physical	20855607

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52, AND MASSSPECTROMETRY.
PubMed: 19376835