Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
SCABP8/CBL10, a putative calcium sensor, interacts with the protein kinase SOS2 to protect Arabidopsis shoots from salt stress.
The calcium sensor CBL10 mediates salt tolerance by regulating ion homeostasis in Arabidopsis.
Calcineurin B-like protein CBL10 directly interacts with AKT1 and modulates K+ homeostasis in Arabidopsis.
Phosphorylation of SOS3-LIKE CALCIUM BINDING PROTEIN8 by SOS2 protein kinase stabilizes their protein complex and regulates salt tolerance in Arabidopsis.
S-acylation of CBL10/SCaBP8 by PAT10 is crucial for its tonoplast association and function in salt tolerance.
CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores.
Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins.
Arabidopsis CALCINEURIN B-LIKE10 Functions Independently of the SOS Pathway during Reproductive Development in Saline Conditions.
The protein kinase complex CBL10-CIPK8-SOS1 functions in Arabidopsis to regulate salt tolerance.
UniProtKB/Swiss-Prot entry Q7FRS8 (CNBLA_ARATH)
OpenScientist hypothesis adjudication: CBL10 direct inhibition of AKT1
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A screen of the papers citing Ren et al. 2013 found no independent re-measurement of CBL10 effects on AKT1 currents or root K+ in cbl10 loss-of-function plants; the in-planta evidence is from overexpression lines. Verdict partially supported, single-source. Claims about the Ren 2013 abstract and about CBL10 activating HAK5 with CIPK23 (PMID:26474642) were checked against the abstracts; the citation counts were not re-checked.
"The in-planta support that does exist is overexpression-based, not derived from *cbl10*-null plants, so it cannot distinguish a physiological inhibitory role from an overexpression artifact."
The CBL-Interacting Protein Kinase CIPK23 Regulates HAK5-Mediated High-Affinity K+ Uptake in Arabidopsis Roots.
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CBL10, like CBL1, CBL8 and CBL9, together with CIPK23 activates the high-affinity K+ transporter HAK5 in a heterologous system. The OpenScientist report cites this against a K+ channel inhibitor term for CBL10; it concerns a different target reached through a kinase, so it does not bear on direct AKT1 inhibition.
"together with CBL-interacting protein kinase23 (CIPK23), activated HAK5 in vivo"