Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Shaggy-related protein kinase eta (EC 2.7.11.1) (ASK-eta) (Protein BRASSINOSTEROID INSENSITIVE 2) (Protein ULTRACURVATA 1) (Shaggy-related protein kinase 21) (AtSK21)

 KSG7_ARATH              Reviewed;         380 AA.
Q39011; Q147R2; Q8S9H8; Q9SN42;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
12-SEP-2018, entry version 169.
RecName: Full=Shaggy-related protein kinase eta {ECO:0000303|PubMed:9611268};
EC=2.7.11.1 {ECO:0000269|PubMed:11847343, ECO:0000269|PubMed:12428015};
AltName: Full=ASK-eta {ECO:0000303|PubMed:10080716};
AltName: Full=Protein BRASSINOSTEROID INSENSITIVE 2 {ECO:0000303|PubMed:11847343};
AltName: Full=Protein ULTRACURVATA 1 {ECO:0000303|PubMed:11820813};
AltName: Full=Shaggy-related protein kinase 21 {ECO:0000303|PubMed:28575660};
Short=AtSK21 {ECO:0000303|PubMed:28575660};
Name=ASK7 {ECO:0000303|PubMed:10080716};
Synonyms=BIN2 {ECO:0000303|PubMed:11847343},
DWF12 {ECO:0000303|PubMed:12428015},
SK21 {ECO:0000303|PubMed:28575660},
UCU1 {ECO:0000303|PubMed:11820813};
OrderedLocusNames=At4g18710 {ECO:0000312|Araport:AT4G18710};
ORFNames=F28A21.120 {ECO:0000312|EMBL:CAB37456.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Dornelas M.C., Schwebel-Dugue N., Thomas M., Lecharny A., Kreis M.;
"Three new cDNAs related to SGG/GSK-3 (SHAGGY/glycogen synthase
kinase-3) from Arabidopsis thaliana.";
(er) Plant Gene Register PGR97-008(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9611268; DOI=10.1016/S0378-1119(98)00147-4;
Dornelas M.C., Lejeune B., Dron M., Kreis M.;
"The Arabidopsis SHAGGY-related protein kinase (ASK) gene family:
structure, organization and evolution.";
Gene 212:249-257(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLU-263 AND GLU-264,
AND MUTANTS DWF12.
PubMed=12428015; DOI=10.1104/pp.010496;
Choe S., Schmitz R.J., Fujioka S., Takatsuto S., Lee M.-O.,
Yoshida S., Feldmann K.A., Tax F.E.;
"Arabidopsis brassinosteroid-insensitive dwarf12 mutants are
semidominant and defective in a glycogen synthase kinase 3beta-like
kinase.";
Plant Physiol. 130:1506-1515(2002).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLU-264 AND PRO-284,
AND MUTANTS UCU1.
PubMed=11820813; DOI=10.1006/dbio.2001.0543;
Perez-Perez J.M., Ponce M.R., Micol J.L.;
"The UCU1 Arabidopsis gene encodes a SHAGGY/GSK3-like kinase required
for cell expansion along the proximodistal axis.";
Dev. Biol. 242:161-173(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF LYS-69 AND
THR-261, AND MUTANTS BIN2.
PubMed=11847343; DOI=10.1126/science.1065769;
Li J., Nam K.H.;
"Regulation of brassinosteroid signaling by a GSK3/SHAGGY-like
kinase.";
Science 295:1299-1301(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[7]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clone.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[11]
TISSUE SPECIFICITY.
PubMed=10080716; DOI=10.1023/A:1006102812280;
Dornelas M.C., Wittich P., von Recklinghausen I., van Lammeren A.,
Kreis M.;
"Characterization of three novel members of the Arabidopsis SHAGGY-
related protein kinase (ASK) multigene family.";
Plant Mol. Biol. 39:137-147(1999).
[12]
FUNCTION, MUTAGENESIS OF ARG-80, AND INTERACTION WITH BZR1 AND
BZR2/BES1.
PubMed=12427989; DOI=10.1104/pp.102.010918;
Zhao J., Peng P., Schmitz R.J., Decker A.D., Tax F.E., Li J.;
"Two putative BIN2 substrates are nuclear components of
brassinosteroid signaling.";
Plant Physiol. 130:1221-1229(2002).
[13]
FUNCTION, AND INTERACTION WITH BZR1.
PubMed=12114546; DOI=10.1073/pnas.152342599;
He J.-X., Gendron J.M., Yang Y., Li J., Wang Z.-Y.;
"The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a
positive regulator of the brassinosteroid signaling pathway in
Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 99:10185-10190(2002).
[14]
FUNCTION, INTERACTION WITH BEET CURLY TOP VIRUS AL4 AND TOMATO GOLDEN
MOSAIC VIRUS AL4, AND AUTOPHOSPHORYLATION.
PubMed=17280695; DOI=10.1016/j.virol.2006.12.034;
Piroux N., Saunders K., Page A., Stanley J.;
"Geminivirus pathogenicity protein C4 interacts with Arabidopsis
thaliana shaggy-related protein kinase AtSKeta, a component of the
brassinosteroid signalling pathway.";
Virology 362:428-440(2007).
[15]
INTERACTION WITH BHLH150.
PubMed=20023194; DOI=10.1105/tpc.109.072504;
Wang H., Zhu Y., Fujioka S., Asami T., Li J., Li J.;
"Regulation of Arabidopsis brassinosteroid signaling by atypical basic
helix-loop-helix proteins.";
Plant Cell 21:3781-3791(2009).
[16]
ACTIVITY REGULATION, INTERACTION WITH BSU1, AND PHOSPHORYLATION AT
TYR-200.
PubMed=21855796; DOI=10.1016/j.molcel.2011.05.037;
Kim T.W., Guan S., Burlingame A.L., Wang Z.Y.;
"The CDG1 kinase mediates brassinosteroid signal transduction from
BRI1 receptor kinase to BSU1 phosphatase and GSK3-like kinase BIN2.";
Mol. Cell 43:561-571(2011).
[17]
FUNCTION, AND INTERACTION WITH YDA.
PubMed=22307275; DOI=10.1038/nature10794;
Kim T.W., Michniewicz M., Bergmann D.C., Wang Z.Y.;
"Brassinosteroid regulates stomatal development by GSK3-mediated
inhibition of a MAPK pathway.";
Nature 482:419-422(2012).
[18]
FUNCTION, AND INTERACTION WITH MKK4.
PubMed=23341468; DOI=10.1074/jbc.M112.384453;
Khan M., Rozhon W., Bigeard J., Pflieger D., Husar S., Pitzschke A.,
Teige M., Jonak C., Hirt H., Poppenberger B.;
"Brassinosteroid-regulated GSK3/Shaggy-like kinases phosphorylate
mitogen-activated protein (MAP) kinase kinases, which control stomata
development in Arabidopsis thaliana.";
J. Biol. Chem. 288:7519-7527(2013).
[19]
FUNCTION, INTERACTION WITH BSK1; BSK6; BSK8 AND BSK11, AND MUTAGENESIS
OF LYS-69.
PubMed=23496207; DOI=10.1111/tpj.12175;
Sreeramulu S., Mostizky Y., Sunitha S., Shani E., Nahum H.,
Salomon D., Hayun L.B., Gruetter C., Rauh D., Ori N., Sessa G.;
"BSKs are partially redundant positive regulators of brassinosteroid
signaling in Arabidopsis.";
Plant J. 74:905-919(2013).
[20]
UBIQUITINATION, ACTIVITY REGULATION, INTERACTION WITH KIB1 AND KIB2,
AND MUTAGENESIS OF TYR-200 AND GLU-263.
STRAIN=cv. Columbia, and cv. Wassilewskija;
PubMed=28575660; DOI=10.1016/j.molcel.2017.05.012;
Zhu J.-Y., Li Y., Cao D.-M., Yang H., Oh E., Bi Y., Zhu S.,
Wang Z.-Y.;
"The F-box protein KIB1 mediates brassinosteroid-induced inactivation
and degradation of GSK3-like kinases in Arabidopsis.";
Mol. Cell 66:648-657(2017).
-!- FUNCTION: 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 (PubMed:11847343, PubMed:12114546,
PubMed:12427989, PubMed:17280695, PubMed:22307275,
PubMed:23341468). Phosphorylates BSK1, BSK3, BSK5, BSK6, BSK8 AND
BSK11 in vitro (PubMed:23496207). {ECO:0000269|PubMed:11847343,
ECO:0000269|PubMed:12114546, ECO:0000269|PubMed:12427989,
ECO:0000269|PubMed:17280695, ECO:0000269|PubMed:22307275,
ECO:0000269|PubMed:23341468, ECO:0000269|PubMed:23496207}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11847343, ECO:0000269|PubMed:12428015}.
-!- ACTIVITY REGULATION: Inactivated by an unknown mechanism after
binding of brassinosteroids to the brassinosteroid receptor
complex (Probable). Inhibited by lithium. Inhibited by
dephosphorylation at Tyr-200 by BSU1 (PubMed:21855796).
Competitive inhibition by KIB1 that reduces substrate (e.g. BZR1)
access (PubMed:28575660). {ECO:0000269|PubMed:21855796,
ECO:0000269|PubMed:28575660, ECO:0000305}.
-!- SUBUNIT: 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. Interacts
with KIB1 and KIB2 in a brassinosteroid (BR)-dependent manner
(PubMed:28575660). Interacts with BSK1, BSK6, BSK8 and BSK11
(PubMed:23496207). {ECO:0000269|PubMed:12114546,
ECO:0000269|PubMed:12427989, ECO:0000269|PubMed:17280695,
ECO:0000269|PubMed:20023194, ECO:0000269|PubMed:22307275,
ECO:0000269|PubMed:23341468, ECO:0000269|PubMed:23496207,
ECO:0000269|PubMed:28575660}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-1798250, EBI-1798250;
Q9C9A5:ARABIDOPSIS MYB-LIKE 2; NbExp=2; IntAct=EBI-1798250, EBI-1546577;
Q94JM3:ARF2; NbExp=3; IntAct=EBI-1798250, EBI-1799262;
P93022:ARF7; NbExp=2; IntAct=EBI-1798250, EBI-632284;
Q8S307:BZR1; NbExp=2; IntAct=EBI-1798250, EBI-1803261;
Q9LN63:BZR2; NbExp=2; IntAct=EBI-1798250, EBI-617078;
Q9FII5:TDR; NbExp=2; IntAct=EBI-1798250, EBI-15730235;
Q9CAD5:YDA; NbExp=4; IntAct=EBI-1798250, EBI-15967064;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced. According to EST
sequences.;
Name=1;
IsoId=Q39011-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: In the two outer cell layers of the developing
seed coat and restricted to the suspensor cells in developing
embryos. {ECO:0000269|PubMed:10080716}.
-!- PTM: Autophosphorylated mainly on threonine and serine residues.
{ECO:0000269|PubMed:17280695}.
-!- PTM: Ubiquitination and subsequent proteasomal degradation
mediated by KIB1. {ECO:0000269|PubMed:28575660}.
-!- MISCELLANEOUS: Unlike other GSK3 kinases, does not require a
priming phosphorylation event or the presence of a scaffold
protein to phosphorylate its substrates.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. GSK-3 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X94939; CAA64409.1; -; mRNA.
EMBL; Y08947; CAA70144.1; -; Genomic_DNA.
EMBL; AY157149; AAN71719.1; -; Genomic_DNA.
EMBL; AL035526; CAB37456.1; -; Genomic_DNA.
EMBL; AL161549; CAB78873.1; -; Genomic_DNA.
EMBL; CP002687; AEE84079.1; -; Genomic_DNA.
EMBL; AY075699; AAL77705.1; -; mRNA.
EMBL; BT026031; ABG48387.1; -; mRNA.
EMBL; AY086529; AAM63594.1; -; mRNA.
PIR; T04863; T04863.
RefSeq; NP_193606.1; NM_117987.4. [Q39011-1]
UniGene; At.22875; -.
ProteinModelPortal; Q39011; -.
SMR; Q39011; -.
BioGrid; 12898; 30.
DIP; DIP-46010N; -.
IntAct; Q39011; 10.
MINT; Q39011; -.
STRING; 3702.AT4G18710.1; -.
iPTMnet; Q39011; -.
PaxDb; Q39011; -.
EnsemblPlants; AT4G18710.1; AT4G18710.1; AT4G18710. [Q39011-1]
GeneID; 827605; -.
Gramene; AT4G18710.1; AT4G18710.1; AT4G18710. [Q39011-1]
KEGG; ath:AT4G18710; -.
Araport; AT4G18710; -.
TAIR; locus:2124082; AT4G18710.
eggNOG; KOG0658; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233017; -.
InParanoid; Q39011; -.
KO; K14502; -.
OMA; HARRHCG; -.
OrthoDB; EOG09360BBG; -.
PhylomeDB; Q39011; -.
BRENDA; 2.7.11.26; 399.
Reactome; R-ATH-3371453; Regulation of HSF1-mediated heat shock response.
PRO; PR:Q39011; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q39011; baseline and differential.
Genevisible; Q39011; AT.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004672; F:protein kinase activity; TAS:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
GO; GO:0009729; P:detection of brassinosteroid stimulus; IMP:TAIR.
GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
GO; GO:1900458; P:negative regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:TAIR.
GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
GO; GO:0009733; P:response to auxin; IMP:TAIR.
GO; GO:0048765; P:root hair cell differentiation; IGI:TAIR.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd14137; STKc_GSK3; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR039192; STKc_GSK3.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Brassinosteroid signaling pathway;
Complete proteome; Host-virus interaction; Kinase; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase; Ubl conjugation.
CHAIN 1 380 Shaggy-related protein kinase eta.
/FTId=PRO_0000086222.
DOMAIN 40 324 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 46 54 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 165 165 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 69 69 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 104 104 Phosphothreonine. {ECO:0000255}.
MOD_RES 105 105 Phosphoserine. {ECO:0000255}.
MOD_RES 187 187 Phosphoserine. {ECO:0000255}.
MOD_RES 200 200 Phosphotyrosine.
{ECO:0000269|PubMed:21855796}.
MOD_RES 220 220 Phosphothreonine. {ECO:0000255}.
MOD_RES 261 261 Phosphothreonine. {ECO:0000255}.
MOD_RES 310 310 Phosphoserine. {ECO:0000255}.
MOD_RES 314 314 Phosphothreonine. {ECO:0000255}.
MOD_RES 353 353 Phosphoserine. {ECO:0000255}.
MUTAGEN 69 69 K->R: Abolishes kinase activity.
{ECO:0000269|PubMed:11847343,
ECO:0000269|PubMed:23496207}.
MUTAGEN 80 80 R->A: No effect.
{ECO:0000269|PubMed:12427989}.
MUTAGEN 200 200 Y->F: Normal interaction with KIB1.
{ECO:0000269|PubMed:28575660}.
MUTAGEN 261 261 T->I: In bin2-2; brassinosteroid-
insensitive dwarf mutant; increased
kinase activity.
{ECO:0000269|PubMed:11847343}.
MUTAGEN 263 263 E->K: In dwf12-2D/bin2-1;
brassinosteroid-insensitive dwarf mutant;
increased kinase activity. Reduced
interaction with KIB1.
{ECO:0000269|PubMed:11847343,
ECO:0000269|PubMed:12428015,
ECO:0000269|PubMed:28575660}.
MUTAGEN 264 264 E->K: In dwf12-1D/ucu1-1/ucu1-2;
brassinosteroid-insensitive dwarf mutant.
{ECO:0000269|PubMed:11820813,
ECO:0000269|PubMed:12428015}.
MUTAGEN 284 284 P->S: In ucu1-3; leaves rolled spirally
downward. {ECO:0000269|PubMed:11820813}.
CONFLICT 105 105 S -> E (in Ref. 1; CAA64409 and 2;
CAA70144). {ECO:0000305}.
CONFLICT 121 121 S -> T (in Ref. 1; CAA64409 and 2;
CAA70144). {ECO:0000305}.
CONFLICT 145 145 M -> S (in Ref. 1; CAA64409 and 2;
CAA70144). {ECO:0000305}.
CONFLICT 157 159 NVA -> SCP (in Ref. 1; CAA64409 and 2;
CAA70144). {ECO:0000305}.
CONFLICT 196 196 A -> P (in Ref. 1; CAA64409 and 2;
CAA70144). {ECO:0000305}.
CONFLICT 271 271 H -> N (in Ref. 1; CAA64409 and 2;
CAA70144). {ECO:0000305}.
CONFLICT 276 276 R -> K (in Ref. 1; CAA64409 and 2;
CAA70144). {ECO:0000305}.
CONFLICT 298 300 IDF -> VDL (in Ref. 1; CAA64409 and 2;
CAA70144). {ECO:0000305}.
CONFLICT 327 327 L -> H (in Ref. 8; AAL77705).
{ECO:0000305}.
CONFLICT 340 340 F -> L (in Ref. 1; CAA64409 and 2;
CAA70144). {ECO:0000305}.
SEQUENCE 380 AA; 43099 MW; 86C2FD5F77201168 CRC64;
MADDKEMPAA VVDGHDQVTG HIISTTIGGK NGEPKQTISY MAERVVGTGS FGIVFQAKCL
ETGETVAIKK VLQDRRYKNR ELQLMRVMDH PNVVCLKHCF FSTTSKDELF LNLVMEYVPE
SLYRVLKHYS SANQRMPLVY VKLYMYQIFR GLAYIHNVAG VCHRDLKPQN LLVDPLTHQV
KICDFGSAKQ LVKGEANISY ICSRFYRAPE LIFGATEYTT SIDIWSAGCV LAELLLGQPL
FPGENAVDQL VEIIKVLGTP TREEIRCMNP HYTDFRFPQI KAHPWHKIFH KRMPPEAIDF
ASRLLQYSPS LRCTALEACA HPFFDELREP NARLPNGRPF PPLFNFKQEV AGSSPELVNK
LIPDHIKRQL GLSFLNQSGT


Related products :

Catalog number Product name Quantity
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB31333 Homo sapiens,Human,PAK1,PAK-1,PKN,PKN1,PRK1,PRKCL1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threo
EIAAB31331 PAK-1,Pkn,Pkn1,Prk1,Prkcl1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Rat,Rattus norvegicus,Serine_threonine-protein kinase N1,Seri
EIAAB40326 Pancreatic serine_threonine-protein kinase,Pask,PS_TK,PSTK1,Rat,Rattus norvegicus,Serine_threonine-protein kinase 39,Spak,STE20_SPS1-related proline-alanine-rich protein kinase,Ste-20-related kinase,S
EIAAB26898 Homo sapiens,Human,NEK6,Never in mitosis A-related kinase 6,NimA-related protein kinase 6,Protein kinase SID6-1512,Serine_threonine-protein kinase Nek6
EIAAB26905 Homo sapiens,Human,JCK,NEK12A,NEK8,Never in mitosis A-related kinase 8,Nima-related protein kinase 12a,NimA-related protein kinase 8,Serine_threonine-protein kinase Nek8
EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
EIAAB06503 Cdc2-related kinase, arginine_serine-rich,CDC2-related protein kinase 7,CDK12,Cell division cycle 2-related protein kinase 7,Cell division protein kinase 12,CRK7,CrkRS,CRKRS,Cyclin-dependent kinase 12
EIAAB06502 Cdc2-related kinase, arginine_serine-rich,CDC2-related protein kinase 7,Cdk12,Cell division cycle 2-related protein kinase 7,Cell division protein kinase 12,Crk7,CrkRS,Crkrs,Cyclin-dependent kinase 12
EIAAB06501 Cdc2-related kinase, arginine_serine-rich,CDC2-related protein kinase 7,Cdk12,Cell division cycle 2-related protein kinase 7,Cell division protein kinase 12,Crk7,CrkRS,Crkrs,Cyclin-dependent kinase 12
EIAAB31335 PAK-2,Pkn2,Prk2,Prkcl2,Protease-activated kinase 2,Protein kinase C-like 2,Protein-kinase C-related kinase 2,Rat,Rattus norvegicus,Serine_threonine-protein kinase N2
EIAAB40324 DCHT,Homo sapiens,Human,Serine_threonine-protein kinase 39,SPAK,STE20_SPS1-related proline-alanine-rich protein kinase,Ste-20-related kinase,STK39
EIAAB26894 Homo sapiens,Human,NEK4,Never in mitosis A-related kinase 4,NimA-related protein kinase 4,Serine_threonine-protein kinase 2,Serine_threonine-protein kinase Nek4,Serine_threonine-protein kinase NRK2,ST
18-461-10255 Cell division cycle 2-related protein kinase 7 - EC 2.7.11.22; CDC2-related protein kinase 7; Cdc2-related kinase. arginine_serine-rich; CrkRS Polyclonal 0.05 ml
EIAAB40325 Mouse,Mus musculus,Serine_threonine-protein kinase 39,Spak,STE20_SPS1-related proline-alanine-rich protein kinase,Ste-20-related kinase,Stk39
EIAAB26907 Homo sapiens,Human,KIAA1995,Nek8,NEK8,NEK9,NERCC,Nercc1 kinase,Never in mitosis A-related kinase 9,NimA-related kinase 8,NimA-related protein kinase 9,Serine_threonine-protein kinase Nek9
EIAAB26890 Homo sapiens,HSPK 21,Human,NEK2,NEK2A,Never in mitosis A-related kinase 2,NimA-like protein kinase 1,NimA-related protein kinase 2,NLK1,Serine_threonine-protein kinase Nek2
EIAAB32397 cAMP-dependent protein kinase catalytic subunit PRKX,Mouse,Mus musculus,Pkare,PKA-related protein kinase,PrKX,Prkx,Protein kinase X,Protein kinase X-linked,Serine_threonine-protein kinase PRKX
EIAAB26908 Mouse,Mus musculus,Nek9,Nercc,Nercc1 kinase,Never in mitosis A-related kinase 9,NimA-related protein kinase 9,Serine_threonine-protein kinase Nek9
EIAAB31337 Homo sapiens,Human,PKN2,PRK2,PRKCL2,Protein kinase C-like 2,Protein-kinase C-related kinase 2,Serine_threonine-protein kinase N2
EIAAB31338 Homo sapiens,Human,PKN3,PKNBETA,Protein kinase PKN-beta,Protein-kinase C-related kinase 3,Serine_threonine-protein kinase N3
EIAAB31339 Mouse,Mus musculus,Pkn3,Pknbeta,Protein kinase PKN-beta,Protein-kinase C-related kinase 3,Serine_threonine-protein kinase N3
EIAAB06523 CAK-kinase p42,Ccrk,Cdch,Cdk20,CDK-activating kinase p42,CDK-related protein kinase PNQLARE,Cell cycle-related kinase,Cell division protein kinase 20,Cyclin-dependent kinase 20,Cyclin-dependent protei
EIAAB26895 Mouse,Mus musculus,Nek4,Never in mitosis A-related kinase 4,NimA-related protein kinase 4,Serine_threonine-protein kinase 2,Serine_threonine-protein kinase Nek4,Stk2


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur