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). ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein] ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein] Activated by phosphorylation at Thr-175 by GRIK1/SNAK2 and GRIK2/SNAK1 (PubMed:19339507). Inactivated by dephosphorylation at Thr-175 (PubMed:24179127). Inhibited by trehalose-6-phosphate (PubMed:19193861). Down-regulated by SR45 by affecting its stability (PubMed:27436712). Reduced kinase activity in response to H(2)O(2) treatment. The redox-state of Cys-177 seems to directly influence its kinase activity (PubMed:28940407). Down-regulated by FLZ6 and FLZ10 (PubMed:29406622). Subunit of a probable heterotrimeric complex consisting of an alpha catalytic (KIN10 or KIN11) subunit, and a beta (KINB) and a gamma (KING or SNF4) non-catalytic regulatory subunits (PubMed:17028154, PubMed:25736509). Interacts with KINB2, KINB3, SNF4 and probably with KINB1 and KING1 (PubMed:10929106, PubMed:11522840, PubMed:15803412, PubMed:17028154, PubMed:21235649). Interacts with SKP1/ASK1, PAD1, the N-terminus of PRL1 and the WD40 domain of 5PTase13 (PubMed:10220464, PubMed:11387208, PubMed:18931139). Potential subunit of a SCF ubiquitin ligase complex consisting of a SNF1-related protein kinase, SKP1 and CUL1. The association of the SCF complex with the proteasome may be mediated by PAD1 and seems to be inhibited by the interaction with PRL1 (PubMed:11387208). Interacts with ATAF1 (Ref.26). Interacts with ESD4 (PubMed:20855607). Interacts with SCE1 (PubMed:20855607, PubMed:26662259). Interacts with FUS3 (PubMed:22026387). Interacts with PP2C74 (PubMed:22449965). Interacts with CDKE1 (PubMed:23229550). Interacts with ABI1 and PP2CA (PubMed:24179127). Interacts with KRP6 (PubMed:23617622). Interacts with CIPK14 (PubMed:25058458). Interacts with FLZ proteins through their FLZ-type zinc finger domains (PubMed:24600465, PubMed:29945970). Interacts with GEBP/STKR1 (PubMed:24600465, PubMed:29192025). Interacts with MYC2 (PubMed:24890857). Interacts with IDD8 (PubMed:25929516). Interacts with BZIP63 (PubMed:26263501). Interacts with PTL (PubMed:25697797). Interacts with FLZ3, FLZ9, TCP3, TCP13, HB21/ZHD3 and HB23/ZHD10 (Ref.50). Interacts with PTP1 (PubMed:27029354). Interacts with RAPTOR1B (PubMed:27545962). Forms oligomers in vitro under strongly reducing conditions (PubMed:28940407). Interacts with WRI1 (PubMed:28314829). Interacts with EIN3 (PubMed:28600557). Component of a ternary complex composed of BZIP2-BZIP63 heterodimer and KIN10 (PubMed:29348240). Interacts with IPK2b (PubMed:29216370). Interacts with FLZ6 and FLZ10 (PubMed:29406622). Shuttles from the cytoplasm to the nucleus when associated with a FLZ protein. Co-localized with ER marker when associated with FLZ6 or FLZ10. Isoform 2 is widely expressed, especially in newly developing tissues (PubMed:25697797). Isoform 2 is expressed throughout the seedling, with highest expression in leaf primordia and vascular tissue, and the seedling root tip. Isoform 2 is later expressed in developing lateral root primordia and developing embryos within siliques (PubMed:25071807). Isoform 1 is widely expressed but at very low levels (PubMed:25071807). Expressed throughout embryo development from the heart to mature embryo stages. Induced by sucrose (PubMed:10220464). Induced by DCMU herbicide (PubMed:17671505). Induced by glucose (PubMed:19302419). Up-regulated by beta-aminobutyric acid (BABA) (PubMed:20484986). Induced by hypoxia following submergence (PubMed:22232383). Induced by salt and oxidative stresses (at the protein level) (PubMed:26471895). The regulatory domain (RD) contains the auto-inhibitory domain (AID) that inhibits kinase activity of the protein kinase domain (KD). The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases. Phosphorylated at Thr-175 in response to glucose (PubMed:19302419). Phosphorylated at Thr-175 under submergence (PubMed:27029354). Autophosphorylated (PubMed:10220464, PubMed:24179127, PubMed:25929516). Dephosphorylated at Thr-175 by ABI1 and PP2CA (PubMed:24179127). Ubiquitinated (PubMed:26662259). Degradation is mediated by a CUL4-based E3 ligase that uses PRL1 as a substrate receptor (PubMed:18223036). Sumoylated by SIZ1 (PubMed:20855607, PubMed:26662259). Sumoylated SnRK1 is ubiquitinated and degraded by the proteasome (PubMed:26662259). Anthocyanin accumulation and accelerated senescence (PubMed:17671505). Starch accumulation during phosphate deficiency (PubMed:19211700). Reduced sensitivity to glucose during early development (PubMed:27436712). Increased seed abortion (PubMed:28922765). Blocked autophagy during abiotic stresses but not under control conditions (PubMed:28783755). Enhanced sucrose-induced hypocotyl elongation (PubMed:29584583). Overexpressing plants show delayed leaf senescence, enhanced tolerance to nutrient starvation dependent on a functional autophagy pathway, enhanced formation of autophagosomes, and tolerance to drought and submergence (PubMed:28740502). Overexpression of KIN10 leads to increased autophagy (PubMed:28783755). Overexpression inhibits sucrose-induced hypocotyl elongation (PubMed:29114081). Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.