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Protein

SNF1-related protein kinase catalytic subunit alpha KIN10

Gene

KIN10

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by phosphorylation at Thr-198.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711ATPPROSITE-ProRule annotation
Active sitei165 – 1651Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 569ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  • abscisic acid-activated signaling pathway Source: TAIR
  • carbohydrate metabolic process Source: UniProtKB-KW
  • detection of nutrient Source: TAIR
  • developmental process involved in reproduction Source: TAIR
  • fatty acid biosynthetic process Source: UniProtKB-KW
  • intracellular signal transduction Source: GO_Central
  • nitrate assimilation Source: UniProtKB-KW
  • organ senescence Source: TAIR
  • primary root development Source: TAIR
  • protein phosphorylation Source: GO_Central
  • sugar mediated signaling pathway Source: TAIR
  • vegetative phase change Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Nitrate assimilation, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G01090-MONOMER.
ARA:GQT-1037-MONOMER.
ARA:GQT-194-MONOMER.
BRENDAi2.7.11.1. 399.
ReactomeiREACT_275432. Translocation of GLUT4 to the plasma membrane.
REACT_301354. AMPK inhibits chREBP transcriptional activation activity.
REACT_351255. Regulation of AMPK activity via LKB1.
REACT_351268. Import of palmitoyl-CoA into the mitochondrial matrix.

Names & Taxonomyi

Protein namesi
Recommended name:
SNF1-related protein kinase catalytic subunit alpha KIN10 (EC:2.7.11.1)
Short name:
AKIN10
Alternative name(s):
AKIN alpha-2
Short name:
AKINalpha2
Gene namesi
Name:KIN10
Synonyms:AK21, SKIN10, SNR2, SNRK1.1
Ordered Locus Names:At3g01090
ORF Names:T4P13.22
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G01090.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi198 – 1981T → A: Abolishes phosphorylation by GRIK1 or GRIK2 leading to inactivation of the protein. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 535535SNF1-related protein kinase catalytic subunit alpha KIN10PRO_0000086128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki43 – 43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei187 – 1871PhosphoserineBy similarity
Modified residuei198 – 1981Phosphothreonine; by GRIK1 or GRIK21 Publication

Post-translational modificationi

Autophosphorylated. Phosphorylated at Thr-198 by GRIK1/SNAK2 and GRIK2/SNAK1.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ38997.
PRIDEiQ38997.

Expressioni

Inductioni

Induced by sucrose.1 Publication

Gene expression databases

ExpressionAtlasiQ38997. baseline and differential.

Interactioni

Subunit structurei

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 DSP4.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GRIK1Q93V582EBI-2107143,EBI-6399184
GRIK2Q5HZ382EBI-2107143,EBI-6399237
KINB2Q9SCY53EBI-2107143,EBI-2042436
PRL1Q423843EBI-2107143,EBI-1382964
SNF4Q944A62EBI-2107143,EBI-2360649

Protein-protein interaction databases

BioGridi6592. 29 interactions.
IntActiQ38997. 9 interactions.
STRINGi3702.AT3G01090.2.

Structurei

3D structure databases

ProteinModelPortaliQ38997.
SMRiQ38997. Positions 16-532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 294253Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini315 – 35541UBAPROSITE-ProRule annotationAdd
BLAST
Domaini486 – 53449KA1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 KA1 (kinase-associated) domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233016.
InParanoidiQ38997.
KOiK07198.
OMAiYLPNYKL.
PhylomeDBiQ38997.

Family and domain databases

InterProiIPR028375. 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.
IPR008271. Ser/Thr_kinase_AS.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF46934. SSF46934. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50032. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q38997-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MFKRVDEFNL VSSTIDHRIF KSRMDGSGTG SRSGVESILP NYKLGRTLGI
60 70 80 90 100
GSFGRVKIAE HALTGHKVAI KILNRRKIKN MEMEEKVRRE IKILRLFMHP
110 120 130 140 150
HIIRLYEVIE TPTDIYLVME YVNSGELFDY IVEKGRLQED EARNFFQQII
160 170 180 190 200
SGVEYCHRNM VVHRDLKPEN LLLDSKCNVK IADFGLSNIM RDGHFLKTSC
210 220 230 240 250
GSPNYAAPEV ISGKLYAGPE VDVWSCGVIL YALLCGTLPF DDENIPNLFK
260 270 280 290 300
KIKGGIYTLP SHLSPGARDL IPRMLVVDPM KRVTIPEIRQ HPWFQAHLPR
310 320 330 340 350
YLAVPPPDTV QQAKKIDEEI LQEVINMGFD RNHLIESLRN RTQNDGTVTY
360 370 380 390 400
YLILDNRFRA SSGYLGAEFQ ETMEGTPRMH PAESVASPVS HRLPGLMEYQ
410 420 430 440 450
GVGLRSQYPV ERKWALGLQS RAHPREIMTE VLKALQDLNV CWKKIGHYNM
460 470 480 490 500
KCRWVPNSSA DGMLSNSMHD NNYFGDESSI IENEAAVKSP NVVKFEIQLY
510 520 530
KTRDDKYLLD LQRVQGPQFL FLDLCAAFLA QLRVL
Note: No experimental confirmation available.
Length:535
Mass (Da):61,182
Last modified:November 21, 2003 - v2
Checksum:iFFFC383223FD8317
GO
Isoform 2 (identifier: Q38997-2) [UniParc]FASTAAdd to basket

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

Show »
Length:512
Mass (Da):58,373
Checksum:i5A18655A0AA506DF
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323Missing in isoform 2. 2 PublicationsVSP_009001Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJC1446.
RefSeqiNP_001118546.1. NM_001125074.1. [Q38997-2]
NP_566130.1. NM_110974.4. [Q38997-2]
NP_850488.1. NM_180157.1. [Q38997-1]
UniGeneiAt.22965.

Genome annotation databases

EnsemblPlantsiAT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
GeneIDi821259.
KEGGiath:AT3G01090.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJC1446.
RefSeqiNP_001118546.1. NM_001125074.1. [Q38997-2]
NP_566130.1. NM_110974.4. [Q38997-2]
NP_850488.1. NM_180157.1. [Q38997-1]
UniGeneiAt.22965.

3D structure databases

ProteinModelPortaliQ38997.
SMRiQ38997. Positions 16-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi6592. 29 interactions.
IntActiQ38997. 9 interactions.
STRINGi3702.AT3G01090.2.

Proteomic databases

PaxDbiQ38997.
PRIDEiQ38997.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
GeneIDi821259.
KEGGiath:AT3G01090.

Organism-specific databases

TAIRiAT3G01090.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233016.
InParanoidiQ38997.
KOiK07198.
OMAiYLPNYKL.
PhylomeDBiQ38997.

Enzyme and pathway databases

BioCyciARA:AT3G01090-MONOMER.
ARA:GQT-1037-MONOMER.
ARA:GQT-194-MONOMER.
BRENDAi2.7.11.1. 399.
ReactomeiREACT_275432. Translocation of GLUT4 to the plasma membrane.
REACT_301354. AMPK inhibits chREBP transcriptional activation activity.
REACT_351255. Regulation of AMPK activity via LKB1.
REACT_351268. Import of palmitoyl-CoA into the mitochondrial matrix.

Miscellaneous databases

PROiQ38997.

Gene expression databases

ExpressionAtlasiQ38997. baseline and differential.

Family and domain databases

InterProiIPR028375. 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.
IPR008271. Ser/Thr_kinase_AS.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
[Graphical view]
PfamiPF02149. KA1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF46934. SSF46934. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50032. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiKIN10_ARATH
AccessioniPrimary (citable) accession number: Q38997
Secondary accession number(s): A6XGR0
, O04728, Q38987, Q39076, Q8RWD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 21, 2003
Last modified: July 22, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.