RAC3_ARATH - dbPTM
RAC3_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAC3_ARATH
UniProt AC Q38912
Protein Name Rac-like GTP-binding protein ARAC3
Gene Name ARAC3
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 198
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Associated with the membrane when activated.
Protein Description Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation. May be involved in cell polarity control during the actin-dependent tip growth of root hairs. [PubMed: 11387211 SPK1-dependent activation is required for auxin-mediated inhibition of PIN2 internalization during gravitropic responses]
Protein Sequence MSASRFIKCVTVGDGAVGKTCLLISYTSNTFPTDYVPTVFDNFSANVIVDGNTINLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLVSKASYENVSKKWVPELRHYAPGVPIILVGTKLDLRDDKQFFAEHPGAVPISTAQGEELKKLIGAPAYIECSAKTQQNVKAVFDAAIKVVLQPPKNKKKKKRKSQKGCSIL
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 Orthologous
Protein Cluster
21S-palmitoylationDGAVGKTCLLISYTS
CCCCCCEEEEEEEEC
3.1120451389
158S-palmitoylationGAPAYIECSAKTQQN
CCCEEEECCHHCHHH
3.30-
158S-palmitoylationGAPAYIECSAKTQQN
CCCEEEECCHHCHHH
3.3020451389
195GeranylgeranylationKRKSQKGCSIL----
CCCCCCCCCCC----
2.7017242203
195MethylationKRKSQKGCSIL----
CCCCCCCCCCC----
2.70-
195S-palmitoylationKRKSQKGCSIL----
CCCCCCCCCCC----
2.7028894027
195GeranylgeranylationKRKSQKGCSIL----
CCCCCCCCCCC----
2.7017242203

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 RAC3_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAC3_ARATH !!

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 RAC3_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GDIR_ARATHSCN1physical
10798620
RIC1_ARATHRIC1physical
19818614
ROGF8_ARATHROPGEF8physical
19070620

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAC3_ARATH

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Activation status-coupled transient S acylation determines membranepartitioning of a plant Rho-related GTPase.";
Sorek N., Poraty L., Sternberg H., Bar E., Lewinsohn E., Yalovsky S.;
Mol. Cell. Biol. 27:2144-2154(2007).
Cited for: SUBCELLULAR LOCATION,PALMITOYLATION AT CYS-158, ISOPRENYLATION ATCYS-195, MUTAGENESIS OF CYS-158, AND MASS SPECTROMETRY.
Prenylation
ReferencePubMed
"Activation status-coupled transient S acylation determines membranepartitioning of a plant Rho-related GTPase.";
Sorek N., Poraty L., Sternberg H., Bar E., Lewinsohn E., Yalovsky S.;
Mol. Cell. Biol. 27:2144-2154(2007).
Cited for: SUBCELLULAR LOCATION,PALMITOYLATION AT CYS-158, ISOPRENYLATION ATCYS-195, MUTAGENESIS OF CYS-158, AND MASS SPECTROMETRY.

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