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KIN10

Gene
KIN10
Protein
SNF1-related protein kinase catalytic subunit alpha KIN10
Organism
Arabidopsis thaliana
Length
512 amino acids
Function
Catalytic subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, a central regulator of cellular energy homeostasis, which, in response to seemingly unrelated darkness, sugar and stress conditions, activates energy-producing pathways and inhibits energy-consuming processes. May play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase and in assimilation of nitrogen by phosphorylating nitrate reductase (PubMed:17671505). In vitro, KIN10 exhibits kinase activity on sucrose phosphate synthase and the kinase activity is inhibited by PRL1 (PubMed:10220464). May be a subunit of a SCF ubiquitin ligase complex and thus be involved in proteasomal ubiquitination (PubMed:11387208). Phosphorylates GRIK1/SNAK2 and GRIK2/SNAK1 in vitro (PubMed:20164192). Cooperates with FUS3 to regulate developmental phase transitions and lateral organ development and act both as positive regulators of abscisic acid (ABA) signaling during germination (PubMed:22026387, PubMed:22902692). Phosphorylates FUS3 in embryo (PubMed:28922765). Negatively modulates MYC2 accumulation through its protein phosphorylation (PubMed:24890857). Phosphorylates geminivirus (CaLCuV, TGMV, ToMoV) AL2 protein resulting in a delay in the viral DNA accumulation and symptom appearance during infection (PubMed:24990996). Regulates bZIP63 activity to alter metabolism in response to starvation through its protein phosphorylation (PubMed:26263501). Under sugar deprivation conditions, antagonizes the IDD8 function in flowering time control by its protein phosphorylation (PubMed:25929516). Plays a cardinal role in the control of cell proliferation through inhibition of KRP6 activity by its protein phosphorylation (PubMed:23617622). Under submergence, phosphorylates PTP1, leading to the release of the MPK6 signaling pathway inhibition (PubMed:27029354). Triggers its own SUMO-mediated proteasomal degradation, establishing a negative feedback loop that attenuates SnRK1 signaling and prevents detrimental hyperactivation of stress responses (PubMed:26662259). Phosphorylates RAPTOR1B in vitro (PubMed:27545962). Phosphorylates and down-regulates HMGR1S in vitro (PubMed:28263378). Kinase activity is redox-sensitive (PubMed:28940407). Acts upstream of TOR in the regulation of autophagy. Required for the activation of autophagy by many abiotic stresses (PubMed:28783755). Involved in positive regulation of autophagy, possibly by affecting the phosphorylation of ATG1 proteins (PubMed:28740502). Negatively modulates WRI1 accumulation through its protein phosphorylation (PubMed:28314829). Modulates leaf senescence progression by the negative regulation of EIN3 accumulation through its protein phosphorylation (PubMed:28600557). Under extended darkness, C/S1-bZIP-SnRK1 complex interacts with the histone acetylation machinery to remodel chromatin and facilitate transcription. BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to up-regulate its transcription (PubMed:29348240). Phosphorylates and down-regulates IPK2b in vitro (PubMed:29216370). Involved in the regulation of sucrose-induced hypocotyl elongation under light/dark cycles (PubMed:29114081, PubMed:29584583).
Similarity
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
Mass
58.373 kDa
Sequence
MDGSGTGSRSGVESILPNYKLGRTLGIGSFGRVKIAEHALTGHKVAIKILNRRKIKNMEMEEKVRREIKILRLFMHPHIIRLYEVIETPTDIYLVMEYVNSGELFDYIVEKGRLQEDEARNFFQQIISGVEYCHRNMVVHRDLKPENLLLDSKCNVKIADFGLSNIMRDGHFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGTLPFDDENIPNLFKKIKGGIYTLPSHLSPGARDLIPRMLVVDPMKRVTIPEIRQHPWFQAHLPRYLAVPPPDTVQQAKKIDEEILQEVINMGFDRNHLIESLRNRTQNDGTVTYYLILDNRFRASSGYLGAEFQETMEGTPRMHPAESVASPVSHRLPGLMEYQGVGLRSQYPVERKWALGLQSRAHPREIMTEVLKALQDLNVCWKKIGHYNMKCRWVPNSSADGMLSNSMHDNNYFGDESSIIENEAAVKSPNVVKFEIQLYKTRDDKYLLDLQRVQGPQFLFLDLCAAFLAQLRVL