Protein: KIN10_ARATH
Sequence: MDGSGTGSRSGVESILPNYKLGRTLGIGSFGRVKIAEHALTGHKVAIKILNRRKIKNMEMEEKVRREIKILRLFMHPHIIRLYEVIETPTDIYLVMEYVNSGELFDYIVEKGRLQEDEARNFFQQIISGVEYCHRNMVVHRDLKPENLLLDSKCNVKIADFGLSNIMRDGHFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGTLPFDDENIPNLFKKIKGGIYTLPSHLSPGARDLIPRMLVVDPMKRVTIPEIRQHPWFQAHLPRYLAVPPPDTVQQAKKIDEEILQEVINMGFDRNHLIESLRNRTQNDGTVTYYLILDNRFRASSGYLGAEFQETMEGTPRMHPAESVASPVSHRLPGLMEYQGVGLRSQYPVERKWALGLQSRAHPREIMTEVLKALQDLNVCWKKIGHYNMKCRWVPNSSADGMLSNSMHDNNYFGDESSIIENEAAVKSPNVVKFEIQLYKTRDDKYLLDLQRVQGPQFLFLDLCAAFLAQLRVL
What is the function of this protein?
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).
What are the official names of this protein?
SNF1-related protein kinase catalytic subunit alpha KIN10, AKIN10, AKIN alpha-2, AKINalpha2, SNF1-related kinase 1.1, SnRK1.1.
What is the protein family that this protein belongs to?
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
What are the subcellular locations of this protein?
[Isoform 1]: Plastid, chloroplast. Cytoplasm. Nucleus. Golgi apparatus. Note=Shuttles from the cytoplasm to the nucleus when associated with a FLZ protein. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Endoplasmic reticulum. Note=Co-localized with ER marker when associated with FLZ6 or FLZ10.