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Q38997 (KIN10_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SNF1-related protein kinase catalytic subunit alpha KIN10

Short name=AKIN10
EC=2.7.11.1
Alternative name(s):
AKIN alpha-2
Short name=AKINalpha2
Gene names
Name:KIN10
Synonyms:AK21, SKIN10, SNR2, SNRK1.1
Ordered Locus Names:At3g01090
ORF Names:T4P13.22
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which 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. In vitro, KIN10 exhibits kinase activity on sucrose phosphate synthase and the kinase activity is inhibited by PRL1. May be a subunit of a SCF ubiquitin ligase complex and thus be involved in proteasomal ubiquitination. Phosphorylates GRIK1/SNAK2 and GRIK2/SNAK1 in vitro. Ref.9 Ref.11 Ref.18

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by phosphorylation at Thr-198. Ref.17

Subunit structure

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. Interacts with KINB2, KINB3, SNF4 and probably with KINB1 and KING1. Interacts with SKP1/ASK1, PAD1, the N-terminus of PRL1 and the WD40 domain of 5PTase13. 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. Interacts with DSP4. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Induction

Induced by sucrose. Ref.9 Ref.17

Post-translational modification

Autophosphorylated. Phosphorylated at Thr-198 by GRIK1/SNAK2 and GRIK2/SNAK1. Ref.9 Ref.17

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 KA1 (kinase-associated) domain.

Contains 1 protein kinase domain.

Contains 1 UBA domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Fatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Nitrate assimilation
Ubl conjugation pathway
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processabscisic acid-activated signaling pathway

Inferred from mutant phenotype PubMed 19302419. Source: TAIR

carbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

detection of nutrient

Inferred from direct assay Ref.15. Source: TAIR

developmental process involved in reproduction

Inferred from mutant phenotype PubMed 17671505. Source: TAIR

fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

nitrate assimilation

Inferred from electronic annotation. Source: UniProtKB-KW

organ senescence

Inferred from mutant phenotype PubMed 17671505. Source: TAIR

primary root development

Inferred from mutant phenotype PubMed 17671505. Source: TAIR

sugar mediated signaling pathway

Inferred from mutant phenotype PubMed 19302419. Source: TAIR

vegetative phase change

Inferred from mutant phenotype PubMed 17671505. Source: TAIR

   Cellular_componentnuclear ubiquitin ligase complex

Inferred from physical interaction Ref.11. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.10Ref.11Ref.13PubMed 17028154. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay PubMed 19302419. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q38997-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q38997-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 535535SNF1-related protein kinase catalytic subunit alpha KIN10
PRO_0000086128

Regions

Domain42 – 294253Protein kinase
Domain315 – 35541UBA
Domain486 – 53449KA1
Nucleotide binding48 – 569ATP By similarity

Sites

Active site1651Proton acceptor By similarity
Binding site711ATP By similarity

Amino acid modifications

Modified residue1871Phosphoserine By similarity
Modified residue1981Phosphothreonine; by GRIK1 or GRIK2 Ref.17
Cross-link43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.14

Natural variations

Alternative sequence1 – 2323Missing in isoform 2.
VSP_009001

Experimental info

Mutagenesis1981T → A: Abolishes phosphorylation by GRIK1 or GRIK2 leading to inactivation of the protein. Ref.17 Ref.18

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 21, 2003. Version 2.
Checksum: FFFC383223FD8317

FASTA53561,182
        10         20         30         40         50         60 
MFKRVDEFNL VSSTIDHRIF KSRMDGSGTG SRSGVESILP NYKLGRTLGI GSFGRVKIAE 

        70         80         90        100        110        120 
HALTGHKVAI KILNRRKIKN MEMEEKVRRE IKILRLFMHP HIIRLYEVIE TPTDIYLVME 

       130        140        150        160        170        180 
YVNSGELFDY IVEKGRLQED EARNFFQQII SGVEYCHRNM VVHRDLKPEN LLLDSKCNVK 

       190        200        210        220        230        240 
IADFGLSNIM RDGHFLKTSC GSPNYAAPEV ISGKLYAGPE VDVWSCGVIL YALLCGTLPF 

       250        260        270        280        290        300 
DDENIPNLFK KIKGGIYTLP SHLSPGARDL IPRMLVVDPM KRVTIPEIRQ HPWFQAHLPR 

       310        320        330        340        350        360 
YLAVPPPDTV QQAKKIDEEI LQEVINMGFD RNHLIESLRN RTQNDGTVTY YLILDNRFRA 

       370        380        390        400        410        420 
SSGYLGAEFQ ETMEGTPRMH PAESVASPVS HRLPGLMEYQ GVGLRSQYPV ERKWALGLQS 

       430        440        450        460        470        480 
RAHPREIMTE VLKALQDLNV CWKKIGHYNM KCRWVPNSSA DGMLSNSMHD NNYFGDESSI 

       490        500        510        520        530 
IENEAAVKSP NVVKFEIQLY KTRDDKYLLD LQRVQGPQFL FLDLCAAFLA QLRVL 

« Hide

Isoform 2 [UniParc].

Checksum: 5A18655A0AA506DF
Show »

FASTA51258,373

References

« Hide 'large scale' references
[1]"Structure and expression of a gene from Arabidopsis thaliana encoding a protein related to SNF1 protein kinase."
le Guen L., Thomas M., Bianchi M., Halford N.G., Kreis M.
Gene 120:249-254(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]Lessard P., Kreis M., Thomas M.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: cv. Columbia.
Tissue: Seedling.
[3]"Functional differentiation of ubiquitin-interacting factors from Arabidopsis."
Fu H.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[4]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[7]"Gene density and organization in a small region of the Arabidopsis thaliana genome."
le Guen L., Thomas M., Kreis M.
Mol. Gen. Genet. 245:390-396(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-42 (ISOFORM 2).
Strain: cv. Columbia.
[8]"Differential accumulation of the transcripts of 22 novel protein kinase genes in Arabidopsis thaliana."
Thuemmler F., Kirchner M., Teuber R., Dittrich P.
Plant Mol. Biol. 29:551-565(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-221.
Strain: cv. Eil-0.
Tissue: Leaf.
[9]"Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like protein kinases."
Bhalerao R.P., Salchert K., Bako L., Oekresz L., Szabados L., Muranaka T., Machida Y., Schell J., Koncz C.
Proc. Natl. Acad. Sci. U.S.A. 96:5322-5327(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INDUCTION, INTERACTION WITH PRL1.
[10]"Functional identification of an Arabidopsis Snf4 ortholog by screening for heterologous multicopy suppressors of snf4 deficiency in yeast."
Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.
Plant J. 23:115-122(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNF4.
[11]"SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase."
Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A., Salchert K., del Pozo C., Schell J., Koncz C.
EMBO J. 20:2742-2756(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SKP1 AND PAD1.
[12]"Detection of in vivo protein interactions between Snf1-related kinase subunits with intron-tagged epitope-labelling in plants cells."
Ferrando A., Koncz-Kalman Z., Farras R., Tiburcio A., Schell J., Koncz C.
Nucleic Acids Res. 29:3685-3693(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KINB2.
[13]"AKINbeta3, a plant specific SnRK1 protein, is lacking domains present in yeast and mammals non-catalytic beta-subunits."
Gissot L., Polge C., Bouly J.P., Lemaitre T., Kreis M., Thomas M.
Plant Mol. Biol. 56:747-759(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KINB3.
[14]"Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants."
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.
Mol. Cell. Proteomics 6:601-610(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-43.
Strain: cv. Landsberg erecta.
[15]"Interaction of the WD40 domain of a myoinositol polyphosphate 5-phosphatase with SnRK1 links inositol, sugar, and stress signaling."
Ananieva E.A., Gillaspy G.E., Ely A., Burnette R.N., Erickson F.L.
Plant Physiol. 148:1868-1882(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH 5PTASE13, SUBCELLULAR LOCATION.
[16]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate SnRK1 by phosphorylating its activation loop."
Shen W., Reyes M.I., Hanley-Bowdoin L.
Plant Physiol. 150:996-1005(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-198, MUTAGENESIS OF THR-198, ENZYME REGULATION.
[18]"Cross-phosphorylation between Arabidopsis thaliana sucrose nonfermenting 1-related protein kinase 1 (AtSnRK1) and its activating kinase (AtSnAK) determines their catalytic activities."
Crozet P., Jammes F., Valot B., Ambard-Bretteville F., Nessler S., Hodges M., Vidal J., Thomas M.
J. Biol. Chem. 285:12071-12077(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-198.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93023 Genomic DNA. Translation: AAA32736.1.
X94757 mRNA. Translation: CAA64384.1.
DQ778957 mRNA. Translation: ABH11527.1.
AC008261 Genomic DNA. Translation: AAF26165.1.
CP002686 Genomic DNA. Translation: AEE73607.1.
CP002686 Genomic DNA. Translation: AEE73608.1.
CP002686 Genomic DNA. Translation: AEE73609.1.
AY093170 mRNA. Translation: AAM13169.1.
BT010386 mRNA. Translation: AAQ56829.1.
X79707 Genomic DNA. Translation: CAA56146.1.
X86966 Genomic DNA. Translation: CAA60529.1.
PIRJC1446.
RefSeqNP_001118546.1. NM_001125074.1. [Q38997-2]
NP_566130.1. NM_110974.4. [Q38997-2]
NP_850488.1. NM_180157.1. [Q38997-1]
UniGeneAt.22965.

3D structure databases

ProteinModelPortalQ38997.
SMRQ38997. Positions 41-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid6592. 27 interactions.
IntActQ38997. 9 interactions.

Proteomic databases

PaxDbQ38997.
PRIDEQ38997.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
GeneID821259.
KEGGath:AT3G01090.

Organism-specific databases

TAIRAT3G01090.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233016.
InParanoidQ38997.
KOK07198.
OMALPGLMEY.
PhylomeDBQ38997.

Enzyme and pathway databases

BioCycARA:AT3G01090-MONOMER.
ARA:GQT-1037-MONOMER.
ARA:GQT-194-MONOMER.
BRENDA2.7.11.1. 399.

Gene expression databases

ArrayExpressQ38997.
GenevestigatorQ38997.

Family and domain databases

InterProIPR028375. KA1/Ssp2_C.
IPR001772. KA1_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
[Graphical view]
PfamPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF103243. SSF103243. 1 hit.
SSF46934. SSF46934. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50032. KA1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ38997.

Entry information

Entry nameKIN10_ARATH
AccessionPrimary (citable) accession number: Q38997
Secondary accession number(s): A6XGR0 expand/collapse secondary AC list , O04728, Q38987, Q39076, Q8RWD2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 21, 2003
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names