Q38997 · KIN10_ARATH

Function

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).

Miscellaneous

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).

Catalytic activity

Activity regulation

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 H2O2 treatment. The redox-state of Cys-177 seems to directly influence its kinase activity (PubMed:28940407).
Down-regulated by FLZ6 and FLZ10 (PubMed:29406622).

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site25-33ATP (UniProtKB | ChEBI)
Binding site48ATP (UniProtKB | ChEBI)
Active site142Proton acceptor

GO annotations

AspectTerm
Cellular Componentchloroplast
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum
Cellular ComponentGolgi apparatus
Cellular Componentnuclear ubiquitin ligase complex
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionkinase activity
Molecular Functionkinase binding
Molecular Functionphosphatase binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processabscisic acid-activated signaling pathway
Biological Processdetection of nutrient
Biological Processdevelopmental process involved in reproduction
Biological Processfatty acid biosynthetic process
Biological Processleaf senescence
Biological Processnitrate assimilation
Biological Processplant organ development
Biological Processpositive regulation of abscisic acid-activated signaling pathway
Biological Processpositive regulation of autophagy
Biological Processprimary root development
Biological Processregulation of leaf senescence
Biological Processresponse to glucose
Biological Processresponse to herbicide
Biological Processresponse to hypoxia
Biological Processresponse to oxidative stress
Biological Processresponse to salt
Biological Processstarch metabolic process
Biological Processsugar mediated signaling pathway
Biological Processvegetative phase change
Biological Processvegetative to reproductive phase transition of meristem

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    SNF1-related protein kinase catalytic subunit alpha KIN10
  • EC number
  • Short names
    AKIN10
  • Alternative names
    • AKIN alpha-2 (AKINalpha2)
    • SNF1-related kinase 1.1
      (SnRK1.1
      )

Gene names

    • Name
      KIN10
    • Synonyms
      AK21
      , AKIN10
      , SKIN10
      , SNR2
      , SNRK1.1
    • ORF names
      T4P13.22
    • Ordered locus names
      At3g01090

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Columbia
    • cv. Eil-0
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q38997
  • Secondary accessions
    • A6XGR0
    • O04728
    • Q38987
    • Q39076
    • Q8RWD2

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Isoform 1

Plastid, chloroplast
Cytoplasm
Nucleus
Golgi apparatus
Note: Shuttles from the cytoplasm to the nucleus when associated with a FLZ protein.

Isoform 2

Cytoplasm
Nucleus
Endoplasmic reticulum
Note: Co-localized with ER marker when associated with FLZ6 or FLZ10.

Keywords

Phenotypes & Variants

Disruption phenotype

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).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis34Abolishes sumoylation. When associated with R-63 and R-390.
Mutagenesis48Abolishes kinase activity. Enhances sensitivity to submergence.
Mutagenesis63Abolishes sumoylation. When associated with R-34 and R-390.
Mutagenesis133Reduced kinase activity and retained redox sensitivity.
Mutagenesis175Abolishes phosphorylation by GRIK1 or GRIK2 leading to inactivation of the protein. Enhances sensitivity to submergence.
Mutagenesis175Enhances tolerance to submergence.
Mutagenesis177Retained kinase activity and abolished redox sensitivity.
Mutagenesis390Abolishes sumoylation. When associated with R-34 and R-63.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 13 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, cross-link, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000861281-512
Cross-link20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-link63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residue164Phosphoserine
Modified residue175Phosphothreonine; by GRIK1 or GRIK2
Modified residue364Phosphoserine
Cross-link390Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modification

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).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

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).

Induction

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).

Developmental stage

Expressed throughout embryo development from the heart to mature embryo stages.

Gene expression databases

Interaction

Subunit

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).

Binary interactions

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain19-271Protein kinase
Region290-389Auto-inhibitory domain (AID)
Domain292-332UBA
Region294-512Regulatory domain (RD)
Region390-512PPI
Domain463-511KA1

Domain

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.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q38997-2

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    512
  • Mass (Da)
    58,373
  • Last updated
    2018-10-10 v3
  • Checksum
    5A18655A0AA506DF
MDGSGTGSRSGVESILPNYKLGRTLGIGSFGRVKIAEHALTGHKVAIKILNRRKIKNMEMEEKVRREIKILRLFMHPHIIRLYEVIETPTDIYLVMEYVNSGELFDYIVEKGRLQEDEARNFFQQIISGVEYCHRNMVVHRDLKPENLLLDSKCNVKIADFGLSNIMRDGHFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGTLPFDDENIPNLFKKIKGGIYTLPSHLSPGARDLIPRMLVVDPMKRVTIPEIRQHPWFQAHLPRYLAVPPPDTVQQAKKIDEEILQEVINMGFDRNHLIESLRNRTQNDGTVTYYLILDNRFRASSGYLGAEFQETMEGTPRMHPAESVASPVSHRLPGLMEYQGVGLRSQYPVERKWALGLQSRAHPREIMTEVLKALQDLNVCWKKIGHYNMKCRWVPNSSADGMLSNSMHDNNYFGDESSIIENEAAVKSPNVVKFEIQLYKTRDDKYLLDLQRVQGPQFLFLDLCAAFLAQLRVL

Q38997-1

  • Name
    1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1: M → MFKRVDEFNLVSSTIDHRIFKSRM

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0598901in isoform 1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M93023
EMBL· GenBank· DDBJ
AAA32736.1
EMBL· GenBank· DDBJ
Genomic DNA
X94757
EMBL· GenBank· DDBJ
CAA64384.1
EMBL· GenBank· DDBJ
mRNA
DQ778957
EMBL· GenBank· DDBJ
ABH11527.1
EMBL· GenBank· DDBJ
mRNA
AC008261
EMBL· GenBank· DDBJ
AAF26165.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE73607.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE73608.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002686
EMBL· GenBank· DDBJ
AEE73609.1
EMBL· GenBank· DDBJ
Genomic DNA
AY093170
EMBL· GenBank· DDBJ
AAM13169.1
EMBL· GenBank· DDBJ
mRNA
BT010386
EMBL· GenBank· DDBJ
AAQ56829.1
EMBL· GenBank· DDBJ
mRNA
X79707
EMBL· GenBank· DDBJ
CAA56146.1
EMBL· GenBank· DDBJ
Genomic DNA
X86966
EMBL· GenBank· DDBJ
CAA60529.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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