BSK1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000325 plant-type vacuole	HDA PMID:15539469 The vegetative vacuole proteome of Arabidopsis thaliana reve...	MARK AS OVER ANNOTATED	Summary: Detected in a vacuole proteome. Reason: High-throughput organelle proteomics hit; BSK1 is a plasma-membrane-anchored kinase, and vacuolar detection most likely reflects membrane contamination or turnover. Supporting Evidence: PMID:38315835 The PM abundance of BSK1 was reduced by functional loss of PAT19, PAT20, and PAT22 whereas abolished by its S-acylation-deficient point mutations, suggesting a key role of S-acylation in its PM targeting.
GO:0004672 protein kinase activity	IBA GO_REF:0000033	ACCEPT	Summary: Protein kinase activity of BSK1. Reason: BSK1 kinase activity is experimentally reported and required for its immune function, although structural work on the paralog BSK8 suggests BSKs may act largely as pseudokinase scaffolds; the activity annotation is retained with that caveat. Supporting Evidence: PMID:23532072 BSK1 belongs to a receptor-like cytoplasmic kinase family and displays kinase activity in vitro; this kinase activity is required for its function. PMID:23911552 suggest that BSKs represent constitutively inactive protein kinases that regulate brassinosteroid signal transfer through an allosteric mechanism
GO:0004672 protein kinase activity	IDA PMID:23532072 BR-SIGNALING KINASE1 physically associates with FLAGELLIN SE...	ACCEPT	Summary: Protein kinase activity of BSK1. Reason: BSK1 kinase activity is experimentally reported and required for its immune function, although structural work on the paralog BSK8 suggests BSKs may act largely as pseudokinase scaffolds; the activity annotation is retained with that caveat. Supporting Evidence: PMID:23532072 BSK1 belongs to a receptor-like cytoplasmic kinase family and displays kinase activity in vitro; this kinase activity is required for its function. PMID:23911552 suggest that BSKs represent constitutively inactive protein kinases that regulate brassinosteroid signal transfer through an allosteric mechanism
GO:0004672 protein kinase activity	IEA GO_REF:0000002	ACCEPT	Summary: Protein kinase activity of BSK1. Reason: BSK1 kinase activity is experimentally reported and required for its immune function, although structural work on the paralog BSK8 suggests BSKs may act largely as pseudokinase scaffolds; the activity annotation is retained with that caveat. Supporting Evidence: PMID:23532072 BSK1 belongs to a receptor-like cytoplasmic kinase family and displays kinase activity in vitro; this kinase activity is required for its function.
GO:0004674 protein serine/threonine kinase activity	IEA GO_REF:0000003	ACCEPT	Summary: EC 2.7.11.1-derived serine/threonine kinase activity. Reason: BSK1 kinase activity is experimentally reported and required for its immune function, although structural work on the paralog BSK8 suggests BSKs may act largely as pseudokinase scaffolds; the activity annotation is retained with that caveat. Supporting Evidence: PMID:23532072 BSK1 belongs to a receptor-like cytoplasmic kinase family and displays kinase activity in vitro; this kinase activity is required for its function.
GO:0005515 protein binding	IPI PMID:18653891 BSKs mediate signal transduction from the receptor kinase BR...	MODIFY	Summary: IPI with BRI1, a protein kinase that BSK1 binds as a substrate or signalling partner. Reason: Generic protein binding is uninformative; the partner is a protein kinase, so protein kinase binding is the more informative term supported by the same evidence. Proposed replacements: protein kinase binding Supporting Evidence: PMID:18653891 The BSKs are phosphorylated by BRI1 in vitro and interact with BRI1 in vivo.
GO:0005515 protein binding	IPI PMID:23496207 BSKs are partially redundant positive regulators of brassino...	REMOVE	Summary: IPI with BSK11. Reason: Generic protein binding is uninformative; removal does not imply the interaction is false (it is recorded in the description/notes). Supporting Evidence: PMID:23496207 multiple BSKs interacted in vivo with the BR receptor BRI1, and served as its phosphorylation substrates in vitro
GO:0005515 protein binding	IPI PMID:23496207 BSKs are partially redundant positive regulators of brassino...	MODIFY	Summary: IPI with BRI1, a protein kinase that BSK1 binds as a substrate or signalling partner. Reason: Generic protein binding is uninformative; the partner is a protein kinase, so protein kinase binding is the more informative term supported by the same evidence. Proposed replacements: protein kinase binding Supporting Evidence: PMID:23496207 multiple BSKs interacted in vivo with the BR receptor BRI1, and served as its phosphorylation substrates in vitro
GO:0005515 protein binding	IPI PMID:23496207 BSKs are partially redundant positive regulators of brassino...	MODIFY	Summary: IPI with BIN2, a protein kinase that BSK1 binds as a substrate or signalling partner. Reason: Generic protein binding is uninformative; the partner is a protein kinase, so protein kinase binding is the more informative term supported by the same evidence. Proposed replacements: protein kinase binding Supporting Evidence: PMID:23496207 The BIN2 and BIL2 GSK3-like kinases, which are negative regulators of BR signaling, interacted in vivo with BSKs and phosphorylated them in vitro, probably at different sites to BRI1.
GO:0005515 protein binding	IPI PMID:23496207 BSKs are partially redundant positive regulators of brassino...	REMOVE	Summary: IPI with BSK8. Reason: Generic protein binding is uninformative; removal does not imply the interaction is false (it is recorded in the description/notes). Supporting Evidence: PMID:23496207 multiple BSKs interacted in vivo with the BR receptor BRI1, and served as its phosphorylation substrates in vitro
GO:0005515 protein binding	IPI PMID:23496207 BSKs are partially redundant positive regulators of brassino...	REMOVE	Summary: IPI with BSK5. Reason: Generic protein binding is uninformative; removal does not imply the interaction is false (it is recorded in the description/notes). Supporting Evidence: PMID:23496207 multiple BSKs interacted in vivo with the BR receptor BRI1, and served as its phosphorylation substrates in vitro
GO:0005515 protein binding	IPI PMID:23496207 BSKs are partially redundant positive regulators of brassino...	REMOVE	Summary: IPI with BSK6. Reason: Generic protein binding is uninformative; removal does not imply the interaction is false (it is recorded in the description/notes). Supporting Evidence: PMID:23496207 multiple BSKs interacted in vivo with the BR receptor BRI1, and served as its phosphorylation substrates in vitro
GO:0005515 protein binding	IPI PMID:23532072 BR-SIGNALING KINASE1 physically associates with FLAGELLIN SE...	MODIFY	Summary: IPI with FLS2, a protein kinase that BSK1 binds as a substrate or signalling partner. Reason: Generic protein binding is uninformative; the partner is a protein kinase, so protein kinase binding is the more informative term supported by the same evidence. Proposed replacements: protein kinase binding Supporting Evidence: PMID:23532072 BSK1 physically associates with the PAMP receptor FLAGELLIN SENSING2 and is required for a subset of flg22-induced responses, including the reactive oxygen burst, but not for mitogen-activated protein kinase activation.
GO:0005515 protein binding	IPI PMID:38315835 Arabidopsis protein S-acyl transferases positively mediate B...	REMOVE	Summary: IPI with PAT19/PAT20/PAT22 S-acyltransferases. Reason: Generic protein binding is uninformative; removal does not imply the interaction is false (it is recorded in the description/notes). Supporting Evidence: PMID:38315835 PAT19, PAT20, and PAT22 interact with BSK1 and are critical for the S-acylation of BSK1, and for BR signaling.
GO:0005524 ATP binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: ATP binding inferred from the protein kinase domain. Reason: Nucleotide binding is consistent with the kinase fold (BSK8 co-crystallized with AMP-PNP) but is not an informative functional descriptor. Supporting Evidence: PMID:23911552 suggest that BSKs represent constitutively inactive protein kinases that regulate brassinosteroid signal transfer through an allosteric mechanism
GO:0005886 plasma membrane	EXP PMID:23532072 BR-SIGNALING KINASE1 physically associates with FLAGELLIN SE...	ACCEPT	Summary: Plasma membrane localization of BSK1. Reason: Direct evidence. Supporting Evidence: PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0005886 plasma membrane	HDA PMID:14506206 Large-scale analysis of in vivo phosphorylated membrane prot...	ACCEPT	Summary: Plasma membrane proteomics detection of BSK1. Reason: Consistent with targeted localization studies. Supporting Evidence: PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0005886 plasma membrane	HDA PMID:16618929 Mapping the Arabidopsis organelle proteome.	ACCEPT	Summary: Plasma membrane proteomics detection of BSK1. Reason: Consistent with targeted localization studies. Supporting Evidence: PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0005886 plasma membrane	HDA PMID:17644812 A high content in lipid-modified peripheral proteins and int...	ACCEPT	Summary: Plasma membrane proteomics detection of BSK1. Reason: Consistent with targeted localization studies. Supporting Evidence: PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0005886 plasma membrane	HDA PMID:22923678 Putative glycosyltransferases and other plant Golgi apparatu...	ACCEPT	Summary: Plasma membrane proteomics detection of BSK1. Reason: Consistent with targeted localization studies. Supporting Evidence: PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0005886 plasma membrane	HDA PMID:28887381 Global Analysis of Membrane-associated Protein Oligomerizati...	ACCEPT	Summary: Plasma membrane proteomics detection of BSK1. Reason: Consistent with targeted localization studies. Supporting Evidence: PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0005886 plasma membrane	IBA GO_REF:0000033	ACCEPT	Summary: BSKs are plasma membrane-anchored RLCKs. Reason: Consistent with direct evidence. Supporting Evidence: PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0005886 plasma membrane	IDA PMID:18653891 BSKs mediate signal transduction from the receptor kinase BR...	ACCEPT	Summary: Plasma membrane localization of BSK1. Reason: Direct evidence. Supporting Evidence: PMID:18653891 The BSKs are phosphorylated by BRI1 in vitro and interact with BRI1 in vivo. PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0005886 plasma membrane	IEA GO_REF:0000044	ACCEPT	Summary: UniProt subcellular location mapping. Reason: Consistent with direct evidence. Supporting Evidence: PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0009506 plasmodesma	HDA PMID:21533090 Arabidopsis plasmodesmal proteome.	MARK AS OVER ANNOTATED	Summary: Detected in a plasmodesmal proteome. Reason: Plasmodesmal fractions contain plasma membrane; there is no targeted evidence for plasmodesmal enrichment or function of BSK1. Supporting Evidence: PMID:21855796 BSK1 is localized at the plasma membrane and is phosphorylated at Ser230 by BRI1 upon BR treatment
GO:0009742 brassinosteroid mediated signaling pathway	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic inference of BR signalling for the BSK clade. Reason: BSK1 has its own direct experimental evidence; the IBA indicates the role is shared across the BSK family. Supporting Evidence: PMID:18653891 These results demonstrate that BSKs are the substrates of BRI1 kinase that activate downstream BR signal transduction. PMID:23496207 multiple BSKs interacted in vivo with the BR receptor BRI1, and served as its phosphorylation substrates in vitro
GO:0009742 brassinosteroid mediated signaling pathway	IDA PMID:18653891 BSKs mediate signal transduction from the receptor kinase BR...	ACCEPT	Summary: BSK1 is a direct BRI1 substrate that relays the BR signal downstream of the receptor. Reason: Core process; direct biochemical and genetic evidence. Supporting Evidence: PMID:18653891 The BSKs are phosphorylated by BRI1 in vitro and interact with BRI1 in vivo. PMID:18653891 These results demonstrate that BSKs are the substrates of BRI1 kinase that activate downstream BR signal transduction.
GO:0009742 brassinosteroid mediated signaling pathway	IEA GO_REF:0000120	ACCEPT	Summary: Automated BR signalling annotation. Reason: Consistent with experimental evidence. Supporting Evidence: PMID:18653891 These results demonstrate that BSKs are the substrates of BRI1 kinase that activate downstream BR signal transduction.
GO:0009898 cytoplasmic side of plasma membrane	IDA PMID:39077775 The cytoskeleton controls the dynamics of plasma membrane pr...	ACCEPT	Summary: BSK1 tracked as a membrane-anchored (cytoplasmic-face) plasma membrane protein by single-molecule imaging. Reason: BSK1 lacks a transmembrane domain and is lipid-anchored on the cytoplasmic face of the plasma membrane via N-myristoylation and S-acylation. Supporting Evidence: PMID:38315835 The PM abundance of BSK1 was reduced by functional loss of PAT19, PAT20, and PAT22 whereas abolished by its S-acylation-deficient point mutations, suggesting a key role of S-acylation in its PM targeting.
GO:0042742 defense response to bacterium	IMP PMID:23532072 BR-SIGNALING KINASE1 physically associates with FLAGELLIN SE...	KEEP AS NON CORE	Summary: bsk1 loss of function increases susceptibility to Pseudomonas syringae. Reason: Genuine but secondary role in pattern-triggered immunity, distinct from the core BR-relay function. Supporting Evidence: PMID:23532072 A loss-of-function bsk1 mutant displayed enhanced susceptibility to virulent and avirulent pathogens, including Golovinomyces cichoracearum, Pseudomonas syringae, and Hyaloperonospora arabidopsidis.
GO:0050832 defense response to fungus	IMP PMID:23532072 BR-SIGNALING KINASE1 physically associates with FLAGELLIN SE...	KEEP AS NON CORE	Summary: bsk1 loss of function increases susceptibility to powdery mildew and oomycete pathogens. Reason: Genuine secondary immune role. Supporting Evidence: PMID:23532072 A loss-of-function bsk1 mutant displayed enhanced susceptibility to virulent and avirulent pathogens, including Golovinomyces cichoracearum, Pseudomonas syringae, and Hyaloperonospora arabidopsidis.
GO:0106310 protein serine kinase activity	EXP PMID:23532072 BR-SIGNALING KINASE1 physically associates with FLAGELLIN SE...	ACCEPT	Summary: Serine kinase activity of BSK1 shown in vitro. Reason: BSK1 kinase activity is experimentally reported and required for its immune function, although structural work on the paralog BSK8 suggests BSKs may act largely as pseudokinase scaffolds; the activity annotation is retained with that caveat. Supporting Evidence: PMID:23532072 BSK1 belongs to a receptor-like cytoplasmic kinase family and displays kinase activity in vitro; this kinase activity is required for its function.
GO:0106310 protein serine kinase activity	IEA GO_REF:0000116	ACCEPT	Summary: Rhea-derived protein serine kinase activity. Reason: BSK1 kinase activity is experimentally reported and required for its immune function, although structural work on the paralog BSK8 suggests BSKs may act largely as pseudokinase scaffolds; the activity annotation is retained with that caveat. Supporting Evidence: PMID:23532072 BSK1 belongs to a receptor-like cytoplasmic kinase family and displays kinase activity in vitro; this kinase activity is required for its function.

Gene Description

Existing Annotations Review

Core Functions

References

Suggested Questions for Experts

Suggested Experiments

📚 Additional Documentation

Notes

📄 View Raw YAML