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Protein

Shaggy-related protein kinase eta

Gene

ASK7

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

Functioni

Negative regulator in brassinosteroid signal transduction pathway important for plant growth. May be also involved in auxin signaling pathway. Phosphorylates and increases the degradation of BZR1 and BZR2/BES1 by the proteasome. Phosphorylates BHLH150, beet curly top virus C4 and tomato golden mosaic virus AC4 on threonine and serine residues. Upon brassinosteroid signaling, inhibits stomatal development by phosphorylating and inhibiting the MAPKK kinase YDA and the MAPK kinases MKK4 and MKK5.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Inactivated by an unknown mechanism after binding of brassinosteroids to the brassinosteroid receptor complex. Inhibited by lithium. Inhibited by dephosphorylation at Tyr-200 by BSU1 (PubMed:21855796).Curated1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691ATPPROSITE-ProRule annotation
Active sitei165 – 1651Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 549ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • brassinosteroid mediated signaling pathway Source: TAIR
  • detection of brassinosteroid stimulus Source: TAIR
  • leaf morphogenesis Source: TAIR
  • multidimensional cell growth Source: TAIR
  • positive regulation of protein export from nucleus Source: TAIR
  • protein autophosphorylation Source: TAIR
  • protein phosphorylation Source: TAIR
  • response to auxin Source: TAIR
  • root hair cell differentiation Source: TAIR
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G18710-MONOMER.
ARA:GQT-2728-MONOMER.
BRENDAi2.7.11.26. 399.
ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
Shaggy-related protein kinase eta (EC:2.7.11.1)
Alternative name(s):
ASK-eta
Protein BRASSINOSTEROID INSENSITIVE 2
Protein ULTRACURVATA 1
Gene namesi
Name:ASK7
Synonyms:BIN2, DWF12, UCU1
Ordered Locus Names:At4g18710
ORF Names:F28A21.120
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G18710.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691K → R: No kinase activity.
Mutagenesisi80 – 801R → A: No effect. 1 Publication
Mutagenesisi261 – 2611T → I in bin2-2; brassinosteroid-insensitive dwarf mutant; increased kinase activity.
Mutagenesisi263 – 2631E → K in dwf12-2D/bin2-1; brassinosteroid-insensitive dwarf mutant; increased kinase activity.
Mutagenesisi264 – 2641E → K in dwf12-1D/ucu1-1/ucu1-2; brassinosteroid-insensitive dwarf mutant.
Mutagenesisi284 – 2841P → S in ucu1-3; leaves rolled spirally downward.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Shaggy-related protein kinase etaPRO_0000086222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041PhosphothreonineSequence analysis
Modified residuei105 – 1051PhosphoserineSequence analysis
Modified residuei187 – 1871PhosphoserineSequence analysis
Modified residuei200 – 2001Phosphotyrosine1 Publication
Modified residuei220 – 2201PhosphothreonineSequence analysis
Modified residuei261 – 2611PhosphothreonineSequence analysis
Modified residuei310 – 3101PhosphoserineSequence analysis
Modified residuei314 – 3141PhosphothreonineSequence analysis
Modified residuei353 – 3531PhosphoserineSequence analysis

Post-translational modificationi

Autophosphorylated mainly on threonine and serine residues.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ39011.
PRIDEiQ39011.

PTM databases

iPTMnetiQ39011.

Expressioni

Tissue specificityi

In the two outer cell layers of the developing seed coat and restricted to the suspensor cells in developing embryos.1 Publication

Gene expression databases

ExpressionAtlasiQ39011. baseline and differential.
GenevisibleiQ39011. AT.

Interactioni

Subunit structurei

Interacts in vitro with the C-terminal fragment of BZR1 and with BES1/BZR2, but not through the kinase domain. Interacts with BHLH150, beet curly top virus AL4/C4 and tomato golden mosaic virus AL4/AC4. Interacts with YDA. Interacts with MKK4.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARF2Q94JM33EBI-1798250,EBI-1799262
BZR2Q9LN632EBI-1798250,EBI-617078

Protein-protein interaction databases

BioGridi12898. 29 interactions.
DIPiDIP-46010N.
IntActiQ39011. 4 interactions.
MINTiMINT-8146086.
STRINGi3702.AT4G18710.1.

Structurei

3D structure databases

ProteinModelPortaliQ39011.
SMRiQ39011. Positions 29-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 324285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0658. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233017.
InParanoidiQ39011.
OMAiKHGASLM.
PhylomeDBiQ39011.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q39011-1) [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
MADDKEMPAA VVDGHDQVTG HIISTTIGGK NGEPKQTISY MAERVVGTGS
60 70 80 90 100
FGIVFQAKCL ETGETVAIKK VLQDRRYKNR ELQLMRVMDH PNVVCLKHCF
110 120 130 140 150
FSTTSKDELF LNLVMEYVPE SLYRVLKHYS SANQRMPLVY VKLYMYQIFR
160 170 180 190 200
GLAYIHNVAG VCHRDLKPQN LLVDPLTHQV KICDFGSAKQ LVKGEANISY
210 220 230 240 250
ICSRFYRAPE LIFGATEYTT SIDIWSAGCV LAELLLGQPL FPGENAVDQL
260 270 280 290 300
VEIIKVLGTP TREEIRCMNP HYTDFRFPQI KAHPWHKIFH KRMPPEAIDF
310 320 330 340 350
ASRLLQYSPS LRCTALEACA HPFFDELREP NARLPNGRPF PPLFNFKQEV
360 370 380
AGSSPELVNK LIPDHIKRQL GLSFLNQSGT
Length:380
Mass (Da):43,099
Last modified:May 10, 2004 - v2
Checksum:i86C2FD5F77201168
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051S → E in CAA64409 (Ref. 1) Curated
Sequence conflicti105 – 1051S → E in CAA70144 (PubMed:9611268).Curated
Sequence conflicti121 – 1211S → T in CAA64409 (Ref. 1) Curated
Sequence conflicti121 – 1211S → T in CAA70144 (PubMed:9611268).Curated
Sequence conflicti145 – 1451M → S in CAA64409 (Ref. 1) Curated
Sequence conflicti145 – 1451M → S in CAA70144 (PubMed:9611268).Curated
Sequence conflicti157 – 1593NVA → SCP in CAA64409 (Ref. 1) Curated
Sequence conflicti157 – 1593NVA → SCP in CAA70144 (PubMed:9611268).Curated
Sequence conflicti196 – 1961A → P in CAA64409 (Ref. 1) Curated
Sequence conflicti196 – 1961A → P in CAA70144 (PubMed:9611268).Curated
Sequence conflicti271 – 2711H → N in CAA64409 (Ref. 1) Curated
Sequence conflicti271 – 2711H → N in CAA70144 (PubMed:9611268).Curated
Sequence conflicti276 – 2761R → K in CAA64409 (Ref. 1) Curated
Sequence conflicti276 – 2761R → K in CAA70144 (PubMed:9611268).Curated
Sequence conflicti298 – 3003IDF → VDL in CAA64409 (Ref. 1) Curated
Sequence conflicti298 – 3003IDF → VDL in CAA70144 (PubMed:9611268).Curated
Sequence conflicti327 – 3271L → H in AAL77705 (PubMed:14593172).Curated
Sequence conflicti340 – 3401F → L in CAA64409 (Ref. 1) Curated
Sequence conflicti340 – 3401F → L in CAA70144 (PubMed:9611268).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94939 mRNA. Translation: CAA64409.1.
Y08947 Genomic DNA. Translation: CAA70144.1.
AY157149 Genomic DNA. Translation: AAN71719.1.
AL035526 Genomic DNA. Translation: CAB37456.1.
AL161549 Genomic DNA. Translation: CAB78873.1.
CP002687 Genomic DNA. Translation: AEE84079.1.
AY075699 mRNA. Translation: AAL77705.1.
BT026031 mRNA. Translation: ABG48387.1.
AY086529 mRNA. Translation: AAM63594.1.
PIRiT04863.
RefSeqiNP_193606.1. NM_117987.3. [Q39011-1]
UniGeneiAt.22875.

Genome annotation databases

EnsemblPlantsiAT4G18710.1; AT4G18710.1; AT4G18710. [Q39011-1]
GeneIDi827605.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94939 mRNA. Translation: CAA64409.1.
Y08947 Genomic DNA. Translation: CAA70144.1.
AY157149 Genomic DNA. Translation: AAN71719.1.
AL035526 Genomic DNA. Translation: CAB37456.1.
AL161549 Genomic DNA. Translation: CAB78873.1.
CP002687 Genomic DNA. Translation: AEE84079.1.
AY075699 mRNA. Translation: AAL77705.1.
BT026031 mRNA. Translation: ABG48387.1.
AY086529 mRNA. Translation: AAM63594.1.
PIRiT04863.
RefSeqiNP_193606.1. NM_117987.3. [Q39011-1]
UniGeneiAt.22875.

3D structure databases

ProteinModelPortaliQ39011.
SMRiQ39011. Positions 29-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12898. 29 interactions.
DIPiDIP-46010N.
IntActiQ39011. 4 interactions.
MINTiMINT-8146086.
STRINGi3702.AT4G18710.1.

PTM databases

iPTMnetiQ39011.

Proteomic databases

PaxDbiQ39011.
PRIDEiQ39011.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G18710.1; AT4G18710.1; AT4G18710. [Q39011-1]
GeneIDi827605.

Organism-specific databases

TAIRiAT4G18710.

Phylogenomic databases

eggNOGiKOG0658. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233017.
InParanoidiQ39011.
OMAiKHGASLM.
PhylomeDBiQ39011.

Enzyme and pathway databases

BioCyciARA:AT4G18710-MONOMER.
ARA:GQT-2728-MONOMER.
BRENDAi2.7.11.26. 399.
ReactomeiR-ATH-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

PROiQ39011.

Gene expression databases

ExpressionAtlasiQ39011. baseline and differential.
GenevisibleiQ39011. AT.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Three new cDNAs related to SGG/GSK-3 (SHAGGY/glycogen synthase kinase-3) from Arabidopsis thaliana."
    Dornelas M.C., Schwebel-Dugue N., Thomas M., Lecharny A., Kreis M.
    Plant Gene Register PGR97-008
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "The Arabidopsis SHAGGY-related protein kinase (ASK) gene family: structure, organization and evolution."
    Dornelas M.C., Lejeune B., Dron M., Kreis M.
    Gene 212:249-257(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Arabidopsis brassinosteroid-insensitive dwarf12 mutants are semidominant and defective in a glycogen synthase kinase 3beta-like kinase."
    Choe S., Schmitz R.J., Fujioka S., Takatsuto S., Lee M.-O., Yoshida S., Feldmann K.A., Tax F.E.
    Plant Physiol. 130:1506-1515(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS DWF12.
  4. "The UCU1 Arabidopsis gene encodes a SHAGGY/GSK3-like kinase required for cell expansion along the proximodistal axis."
    Perez-Perez J.M., Ponce M.R., Micol J.L.
    Dev. Biol. 242:161-173(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS UCU1.
  5. "Regulation of brassinosteroid signaling by a GSK3/SHAGGY-like kinase."
    Li J., Nam K.H.
    Science 295:1299-1301(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTANTS LYS-69 AND BIN2.
  6. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  7. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  8. "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].
    Strain: cv. Columbia.
  9. "Arabidopsis ORF clone."
    Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  10. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  11. "Characterization of three novel members of the Arabidopsis SHAGGY-related protein kinase (ASK) multigene family."
    Dornelas M.C., Wittich P., von Recklinghausen I., van Lammeren A., Kreis M.
    Plant Mol. Biol. 39:137-147(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "Two putative BIN2 substrates are nuclear components of brassinosteroid signaling."
    Zhao J., Peng P., Schmitz R.J., Decker A.D., Tax F.E., Li J.
    Plant Physiol. 130:1221-1229(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-80, INTERACTION WITH BZR1 AND BZR2/BES1.
  13. "The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in Arabidopsis."
    He J.-X., Gendron J.M., Yang Y., Li J., Wang Z.-Y.
    Proc. Natl. Acad. Sci. U.S.A. 99:10185-10190(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BZR1.
  14. "Geminivirus pathogenicity protein C4 interacts with Arabidopsis thaliana shaggy-related protein kinase AtSKeta, a component of the brassinosteroid signalling pathway."
    Piroux N., Saunders K., Page A., Stanley J.
    Virology 362:428-440(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BEET CURLY TOP VIRUS AL4 AND TOMATO GOLDEN MOSAIC VIRUS AL4, AUTOPHOSPHORYLATION.
  15. "Regulation of Arabidopsis brassinosteroid signaling by atypical basic helix-loop-helix proteins."
    Wang H., Zhu Y., Fujioka S., Asami T., Li J., Li J.
    Plant Cell 21:3781-3791(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BHLH150.
  16. "The CDG1 kinase mediates brassinosteroid signal transduction from BRI1 receptor kinase to BSU1 phosphatase and GSK3-like kinase BIN2."
    Kim T.W., Guan S., Burlingame A.L., Wang Z.Y.
    Mol. Cell 43:561-571(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH BSU1, DEPHOSPHORYLATION AT TYR-200 BY BSU1.
  17. "Brassinosteroid regulates stomatal development by GSK3-mediated inhibition of a MAPK pathway."
    Kim T.W., Michniewicz M., Bergmann D.C., Wang Z.Y.
    Nature 482:419-422(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YDA.
  18. "Brassinosteroid-regulated GSK3/Shaggy-like kinases phosphorylate mitogen-activated protein (MAP) kinase kinases, which control stomata development in Arabidopsis thaliana."
    Khan M., Rozhon W., Bigeard J., Pflieger D., Husar S., Pitzschke A., Teige M., Jonak C., Hirt H., Poppenberger B.
    J. Biol. Chem. 288:7519-7527(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MKK4.

Entry informationi

Entry nameiKSG7_ARATH
AccessioniPrimary (citable) accession number: Q39011
Secondary accession number(s): Q147R2, Q8S9H8, Q9SN42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2004
Last modified: May 11, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Unlike other GSK3 kinases, does not require a priming phosphorylation event or the presence of a scaffold protein to phosphorylate its substrates.

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

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 one 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.