GO_REF:0000002
Gene Ontology annotation through association of InterPro records with GO terms
GO_REF:0000003
Gene Ontology annotation based on Enzyme Commission mapping
GO_REF:0000033
Annotation inferences using phylogenetic trees
GO_REF:0000044
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
GO_REF:0000116
Automatic Gene Ontology annotation based on Rhea mapping
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
GO_REF:0000122
AtSubP analysis
PMID:13678909
Growth signalling pathways in Arabidopsis and the AGC protein kinases.
PMID:14749726
A protein kinase target of a PDK1 signalling pathway is involved in root hair growth in Arabidopsis.
PMID:16973627
Structural and functional insights into the regulation of Arabidopsis AGC VIIIa kinases.
PMID:19168677
The polarly localized D6 PROTEIN KINASE is required for efficient auxin transport in Arabidopsis thaliana.
PMID:27251533
Arabidopsis D6PK is a lipid domain-dependent mediator of root epidermal planar polarity.
PMID:29490064
Roles of AGCVIII Kinases in the Hypocotyl Phototropism of Arabidopsis Seedlings.
PMID:32612234
Extensive signal integration by the phytohormone protein network.
PMID:33705718
AGC kinases and MAB4/MEL proteins maintain PIN polarity by limiting lateral diffusion in plant cells.
PMID:24948515
Auxin efflux by PIN-FORMED proteins is activated by two different protein kinases, D6 PROTEIN KINASE and PINOID.
PMID:27836964
Phospholipid composition and a polybasic motif determine D6 PROTEIN KINASE polar association with the plasma membrane and tropic responses.
PMID:23709629
D6PK AGCVIII kinases are required for auxin transport and phototropic hypocotyl bending in Arabidopsis.
file:publications/url_https___www.nature.com_articles_nplants2015162_figures_5.md
Figure 5: Direct D6PK interaction with phosphatidylinositol phosphates in vitro. | Nature Plants | Nature Plants
PMID:38278951
D6PK plasma membrane polarity requires a repeated CXX(X)P motif and PDK1-dependent phosphorylation.