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Protein BRASSINOSTEROID INSENSITIVE 1 (AtBRI1) (EC 2.7.10.1) (EC 2.7.11.1) (Brassinosteroid LRR receptor kinase)

 BRI1_ARATH              Reviewed;        1196 AA.
O22476; C0LGS4;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
05-DEC-2018, entry version 177.
RecName: Full=Protein BRASSINOSTEROID INSENSITIVE 1 {ECO:0000303|PubMed:9298904};
Short=AtBRI1 {ECO:0000303|PubMed:9298904};
EC=2.7.10.1 {ECO:0000305};
EC=2.7.11.1 {ECO:0000305};
AltName: Full=Brassinosteroid LRR receptor kinase {ECO:0000303|PubMed:9298904};
Flags: Precursor;
Name=BRI1 {ECO:0000303|PubMed:9298904}; OrderedLocusNames=At4g39400;
ORFNames=F23K16.30;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND MUTANTS
BRI1-101; BRI1-104; BRI1-113 AND BRI1-115.
STRAIN=cv. Columbia;
PubMed=9298904; DOI=10.1016/S0092-8674(00)80357-8;
Li J., Chory J.;
"A putative leucine-rich repeat receptor kinase involved in
brassinosteroid signal transduction.";
Cell 90:929-938(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTANTS BRI1-5/DWF2-W41;
BRI1-6/BRI1-119/DWF2-399; BRI1-7/DWF2-WM3-2; BRI1-8/DWF2-WM6-2 AND
BRI1-9/DWF2-WMB19, AND DISRUPTION PHENOTYPE.
STRAIN=cv. En-2, and cv. Wassilewskija-2;
PubMed=10557222; DOI=10.1104/pp.121.3.743;
Noguchi T., Fujioka S., Choe S., Takatsuto S., Yoshida S., Yuan H.,
Feldmann K.A., Tax F.E.;
"Brassinosteroid-insensitive dwarf mutants of Arabidopsis accumulate
brassinosteroids.";
Plant Physiol. 121:743-752(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, AND MUTANTS BRI1-1; BRI1-108; BRI1-117 AND
BRI1-102.
STRAIN=cv. Columbia;
PubMed=10938344; DOI=10.1104/pp.123.4.1247;
Friedrichsen D.M., Joazeiro C.A.P., Li J., Hunter T., Chory J.;
"BRASSINOSTEROID-INSENSITIVE-1 is a ubiquitously expressed leucine-
rich repeat receptor serine/threonine kinase.";
Plant Physiol. 123:1247-1256(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=20064227; DOI=10.1186/1471-2164-11-19;
Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
"Genome-wide cloning and sequence analysis of leucine-rich repeat
receptor-like protein kinase genes in Arabidopsis thaliana.";
BMC Genomics 11:19-19(2010).
[5]
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).
[6]
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).
[7]
PHOSPHORYLATION AT SER-838; THR-842; THR-846; SER-858 AND THR-872, AND
MUTAGENESIS OF LYS-911.
PubMed=11027724; DOI=10.1104/pp.124.2.751;
Oh M.-H., Ray W.K., Huber S.C., Asara J.M., Gage D.A., Clouse S.D.;
"Recombinant BRASSINOSTEROID INSENSITIVE 1 receptor-like kinase
autophosphorylates on serine and threonine residues and phosphorylates
a conserved peptide motif in vitro.";
Plant Physiol. 124:751-766(2000).
[8]
STEROID-BINDING.
PubMed=10875920; DOI=10.1126/science.288.5475.2360;
He Z., Wang Z.-Y., Li J., Zhu Q., Lamb C., Ronald P., Chory J.;
"Perception of brassinosteroids by the extracellular domain of the
receptor kinase BRI1.";
Science 288:2360-2363(2000).
[9]
SUBCELLULAR LOCATION, STEROID-BINDING, AND AUTOPHOSPHORYLATION.
PubMed=11268216; DOI=10.1038/35066597;
Wang Z.-Y., Seto H., Fujioka S., Yoshida S., Chory J.;
"BRI1 is a critical component of a plasma-membrane receptor for plant
steroids.";
Nature 410:380-383(2001).
[10]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH BAK1.
PubMed=12150928; DOI=10.1016/S0092-8674(02)00814-0;
Nam K.H., Li J.;
"BRI1/BAK1, a receptor kinase pair mediating brassinosteroid
signaling.";
Cell 110:203-212(2002).
[11]
PHOSPHORYLATION, AND INTERACTION WITH BAK1.
PubMed=12150929; DOI=10.1016/S0092-8674(02)00812-7;
Li J., Wen J., Lease K.A., Doke J.T., Tax F.E., Walker J.C.;
"BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with
BRI1 and modulates brassinosteroid signaling.";
Cell 110:213-222(2002).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH BAK1.
PubMed=15548744; DOI=10.1105/tpc.104.025387;
Russinova E., Borst J.-W., Kwaaitaal M., Cano-Delgado A., Yin Y.,
Chory J., de Vries S.C.;
"Heterodimerization and endocytosis of Arabidopsis brassinosteroid
receptors BRI1 and AtSERK3 (BAK1).";
Plant Cell 16:3216-3229(2004).
[13]
INTERACTION WITH TTL.
PubMed=15319482; DOI=10.1105/tpc.104.023903;
Nam K.H., Li J.;
"The Arabidopsis transthyretin-like protein is a potential substrate
of BRASSINOSTEROID-INSENSITIVE 1.";
Plant Cell 16:2406-2417(2004).
[14]
PHOSPHORYLATION AT SER-838; SER-858; THR-872; THR-880; THR-982 AND
SER-1168, INTERACTION WITH BAK1, AND MUTAGENESIS OF SER-838; THR-842;
THR-846; SER-858; THR-872; THR-1039; SER-1044; THR-1045; THR-1049;
SER-1168; SER-1172; 1179-SER-THR-1180 AND SER-1187.
PubMed=15894717; DOI=10.1105/tpc.105.031393;
Wang X., Goshe M.B., Soderblom E.J., Phinney B.S., Kuchar J.A., Li J.,
Asami T., Yoshida S., Huber S.C., Clouse S.D.;
"Identification and functional analysis of in vivo phosphorylation
sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor
kinase.";
Plant Cell 17:1685-1703(2005).
[15]
INTERACTION WITH SERK1.
PubMed=16473966; DOI=10.1105/tpc.105.039412;
Karlova R., Boeren S., Russinova E., Aker J., Vervoort J.,
de Vries S.C.;
"The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein
complex includes BRASSINOSTEROID-INSENSITIVE1.";
Plant Cell 18:626-638(2006).
[16]
FUNCTION.
PubMed=17138891; DOI=10.1126/science.1134040;
Belkhadir Y., Chory J.;
"Brassinosteroid signaling: a paradigm for steroid hormone signaling
from the cell surface.";
Science 314:1410-1411(2006).
[17]
SUBCELLULAR LOCATION.
PubMed=17578906; DOI=10.1101/gad.1561307;
Geldner N., Hyman D.L., Wang X., Schumacher K., Chory J.;
"Endosomal signaling of plant steroid receptor kinase BRI1.";
Genes Dev. 21:1598-1602(2007).
[18]
GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=17588517; DOI=10.1016/j.molcel.2007.05.015;
Jin H., Yan Z., Nam K.H., Li J.;
"Allele-specific suppression of a defective brassinosteroid receptor
reveals a physiological role of UGGT in ER quality control.";
Mol. Cell 26:821-830(2007).
[19]
FUNCTION, AND DOMAIN.
PubMed=17520012; DOI=10.1371/journal.pone.0000449;
Kwezi L., Meier S., Mungur L., Ruzvidzo O., Irving H., Gehring C.;
"The Arabidopsis thaliana brassinosteroid receptor (AtBRI1) contains a
domain that functions as a guanylyl cyclase in vitro.";
PLoS ONE 2:E449-E449(2007).
[20]
SUBUNIT.
PubMed=17905839; DOI=10.1529/biophysj.107.112003;
Hink M.A., Shah K., Russinova E., de Vries S.C., Visser A.J.;
"Fluorescence fluctuation analysis of Arabidopsis thaliana somatic
embryogenesis receptor-like kinase and brassinosteroid insensitive 1
receptor oligomerization.";
Biophys. J. 94:1052-1062(2008).
[21]
MUTAGENESIS OF GLY-989.
PubMed=18332904; DOI=10.1038/cr.2008.36;
Xu W., Huang J., Li B., Li J., Wang Y.;
"Is kinase activity essential for biological functions of BRI1?";
Cell Res. 18:472-478(2008).
[22]
FUNCTION, PHOSPHORYLATION AT SER-838; THR-846; SER-858; SER-1166 AND
THR-1180, INTERACTION WITH BAK1, AND MUTAGENESIS OF SER-838; THR-842;
THR-846; SER-858; THR-1049; SER-1166; SER-1168; SER-1172; SER-1179 AND
THR-1180.
PubMed=18694562; DOI=10.1016/j.devcel.2008.06.011;
Wang X., Kota U., He K., Blackburn K., Li J., Goshe M.B., Huber S.C.,
Clouse S.D.;
"Sequential transphosphorylation of the BRI1/BAK1 receptor kinase
complex impacts early events in brassinosteroid signaling.";
Dev. Cell 15:220-235(2008).
[23]
FUNCTION, AND INTERACTION WITH BSK1 AND BSK3.
PubMed=18653891; DOI=10.1126/science.1156973;
Tang W., Kim T.W., Oses-Prieto J.A., Sun Y., Deng Z., Zhu S., Wang R.,
Burlingame A.L., Wang Z.Y.;
"BSKs mediate signal transduction from the receptor kinase BRI1 in
Arabidopsis.";
Science 321:557-560(2008).
[24]
PHOSPHORYLATION AT SER-887, AND PHOSPHORYLATION OF SERK1.
PubMed=19105183; DOI=10.1002/pmic.200701059;
Karlova R., Boeren S., van Dongen W., Kwaaitaal M., Aker J.,
Vervoort J., de Vries S.C.;
"Identification of in vitro phosphorylation sites in the Arabidopsis
thaliana somatic embryogenesis receptor-like kinases.";
Proteomics 9:368-379(2009).
[25]
FUNCTION, MUTAGENESIS OF TYR-831; TYR-898; TYR-945; TYR-956; TYR-961;
TYR-1052; TYR-1057; TYR-1058; TYR-1070 AND TYR-1072,
AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT TYR-831 AND TYR-956.
PubMed=19124768; DOI=10.1073/pnas.0810249106;
Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.;
"Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a
component of brassinosteroid signaling in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009).
[26]
INTERACTION WITH CDG1.
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).
[27]
FUNCTION, AND INTERACTION WITH BSK5; BSK6 AND BSK11.
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).
[28]
INTERACTION WITH BIK1.
PubMed=23818580; DOI=10.1073/pnas.1302154110;
Lin W., Lu D., Gao X., Jiang S., Ma X., Wang Z., Mengiste T., He P.,
Shan L.;
"Inverse modulation of plant immune and brassinosteroid signaling
pathways by the receptor-like cytoplasmic kinase BIK1.";
Proc. Natl. Acad. Sci. U.S.A. 110:12114-12119(2013).
[29]
LACK OF INTERACTION WITH CNGC17 AND PSKR1, AND SUBCELLULAR LOCATION.
PubMed=26071421; DOI=10.1105/tpc.15.00306;
Ladwig F., Dahlke R.I., Stuehrwohldt N., Hartmann J., Harter K.,
Sauter M.;
"Phytosulfokine regulates growth in Arabidopsis through a response
module at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED
CHANNEL17, H+-ATPase, and BAK1.";
Plant Cell 27:1718-1729(2015).
[30]
INTERACTION WITH B'ALPHA; B'BETA; B'GAMMA AND B'ETA.
PubMed=26517938; DOI=10.1016/j.molp.2015.10.007;
Wang R., Liu M., Yuan M., Oses-Prieto J.A., Cai X., Sun Y.,
Burlingame A.L., Wang Z.Y., Tang W.;
"The brassinosteroid-activated BRI1 receptor kinase is switched off by
dephosphorylation mediated by cytoplasm-localized PP2A B' subunits.";
Mol. Plant 9:148-157(2016).
[31]
X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 29-788 IN COMPLEX WITH
BRASSINOLIDE, AND GLYCOSYLATION AT ASN-112; ASN-154; ASN-233; ASN-275;
ASN-351 AND ASN-545.
PubMed=21666665; DOI=10.1038/nature10153;
Hothorn M., Belkhadir Y., Dreux M., Dabi T., Noel J.P., Wilson I.A.,
Chory J.;
"Structural basis of steroid hormone perception by the receptor kinase
BRI1.";
Nature 474:467-471(2011).
[32]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 23-784 IN COMPLEX WITH
BRASSINOLIDE, AND GLYCOSYLATION AT ASN-112; ASN-154; ASN-233; ASN-275;
ASN-351; ASN-510; ASN-545 AND ASN-573.
PubMed=21666666; DOI=10.1038/nature10178;
She J., Han Z., Kim T.W., Wang J., Cheng W., Chang J., Shi S.,
Wang J., Yang M., Wang Z.Y., Chai J.;
"Structural insight into brassinosteroid perception by BRI1.";
Nature 474:472-476(2011).
[33]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 29-788 IN COMPLEX WITH
BRASSINOLIDE, AND GLYCOSYLATION AT ASN-112; ASN-154; ASN-233; ASN-275;
ASN-351; ASN-545 AND ASN-573.
PubMed=23929946; DOI=10.1126/science.1242468;
Santiago J., Henzler C., Hothorn M.;
"Molecular mechanism for plant steroid receptor activation by somatic
embryogenesis co-receptor kinases.";
Science 341:889-892(2013).
[34]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 865-1160 IN COMPLEX WITH
ATP, AND GLYCOSYLATION AT ASN-154; ASN-275 AND ASN-545.
PubMed=24461462; DOI=10.1111/tpj.12445;
Bojar D., Martinez J., Santiago J., Rybin V., Bayliss R., Hothorn M.;
"Crystal structures of the phosphorylated BRI1 kinase domain and
implications for brassinosteroid signal initiation.";
Plant J. 78:31-43(2014).
-!- FUNCTION: Receptor with a dual specificity kinase activity acting
on both serine/threonine- and tyrosine-containing substrates.
Regulates, in response to brassinosteroid binding, a signaling
cascade involved in plant development, including expression of
light- and stress-regulated genes, promotion of cell elongation,
normal leaf and chloroplast senescence, and flowering. Binds
brassinolide, and less effectively castasterone, but not
2,3,22,23-O-tetramethylbrassinolide or ecdysone. May be involved
in a feedback regulation of brassinosteroid biosynthesis.
Phosphorylates BRI1-associated receptor kinase 1 (BAK1),
Transthyretin-Like protein (TTL) and SERK1 on 'Ser-299' and 'Thr-
462' in vitro. May have a guanylyl cyclase activity
(PubMed:10557222, PubMed:10938344, PubMed:17138891,
PubMed:17520012, PubMed:18694562, PubMed:19124768). Phosphorylates
BSK1, BSK2 and BSK3 in vitro (PubMed:18653891). Phosphorylates
BSK1, BSK3, BSK5, BSK6, BSK8 AND BSK11 in vitro (PubMed:23496207).
{ECO:0000269|PubMed:10557222, ECO:0000269|PubMed:10938344,
ECO:0000269|PubMed:17138891, ECO:0000269|PubMed:17520012,
ECO:0000269|PubMed:18653891, ECO:0000269|PubMed:18694562,
ECO:0000269|PubMed:19124768, ECO:0000269|PubMed:23496207}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000305};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1; Evidence={ECO:0000305};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
-!- ACTIVITY REGULATION: Activated by Ser and Thr phosphorylation.
-!- SUBUNIT: Monomer or homodimer in the plasma membrane. Heterodimer
with BAK1 in the endosomes. Interacts with SERK1 and TTL in a
kinase-dependent manner. Component of the SERK1 signaling complex,
composed of KAPP, CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1
and BRI1. Interacts with CDG1 (PubMed:21855796). No interactions
with PSKR1 or CNGC17 (PubMed:26071421). Interacts with BIK1
(PubMed:23818580). Interacts with B'ALPHA, B'BETA, B'GAMMA and
B'ETA (PubMed:26517938). Interacts with BSK1 and BSK3
(PubMed:18653891). Interacts with BSK5, BSK6 and BSK11
(PubMed:23496207). {ECO:0000269|PubMed:12150928,
ECO:0000269|PubMed:12150929, ECO:0000269|PubMed:15319482,
ECO:0000269|PubMed:15548744, ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:16473966, ECO:0000269|PubMed:17905839,
ECO:0000269|PubMed:18653891, ECO:0000269|PubMed:18694562,
ECO:0000269|PubMed:21855796, ECO:0000269|PubMed:23496207,
ECO:0000269|PubMed:23818580, ECO:0000269|PubMed:26071421,
ECO:0000269|PubMed:26517938}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1797828, EBI-1797828;
Q94F62:BAK1; NbExp=9; IntAct=EBI-1797828, EBI-617138;
O65440-2:BAM3; NbExp=3; IntAct=EBI-1797828, EBI-20653325;
Q944A7:BSK1; NbExp=4; IntAct=EBI-1797828, EBI-1797846;
Q8W4L3:BSK3; NbExp=2; IntAct=EBI-1797828, EBI-1797930;
Q6XAT2:ERL2; NbExp=2; IntAct=EBI-1797828, EBI-16895926;
Q9ZVD4:LRR-RLK; NbExp=2; IntAct=EBI-1797828, EBI-20651739;
Q9S7I6:RPK2; NbExp=2; IntAct=EBI-1797828, EBI-16940204;
Q94AG2:SERK1; NbExp=7; IntAct=EBI-1797828, EBI-1555537;
Q8RWZ1:SUB; NbExp=2; IntAct=EBI-1797828, EBI-17072125;
Q9LVM5:TTL; NbExp=3; IntAct=EBI-1797828, EBI-1803584;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26071421};
Single-pass type I membrane protein {ECO:0000305}. Endosome
membrane; Single-pass type I membrane protein.
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
{ECO:0000269|PubMed:10938344, ECO:0000269|PubMed:9298904}.
-!- DEVELOPMENTAL STAGE: Expressed constitutively in either dark- or
light-grown seedlings.
-!- DOMAIN: Contains one leucine-zipper motif and two pairs of
conservatively spaced Cys (Cys pair 1 and 2) involved in forming
heterodimers. {ECO:0000269|PubMed:17520012}.
-!- DOMAIN: A 70 amino acid island between the 21th and the 22th LRR
is essential for the binding of brassinosteroids.
{ECO:0000269|PubMed:21666665}.
-!- DOMAIN: The JM domain (815-883) is a positive regulator of kinase
activity and is required for Tyr phosphorylation.
{ECO:0000269|PubMed:17520012}.
-!- DOMAIN: A guanylyl cyclase domain (1021-1134) having an in vitro
activity is included in the C-terminal kinase domain.
{ECO:0000269|PubMed:17520012}.
-!- PTM: Autophosphorylated on Tyr-831, Tyr-956 and maybe Tyr-1072.
Phosphorylated on at least 12 sites, with a preference for Ser
residues. Transphosphorylated on Ser-887 by SERK1 and on Ser-838,
Thr-846, Ser-858 and Ser-1166 by BAK1. Phosphorylation on Ser-1166
enhances the kinase activity. {ECO:0000269|PubMed:11027724,
ECO:0000269|PubMed:12150928, ECO:0000269|PubMed:12150929,
ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562,
ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:19124768}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:17588517}.
-!- DISRUPTION PHENOTYPE: Dwarf phenotype and aberrant leaf shape.
{ECO:0000269|PubMed:10557222}.
-!- MISCELLANEOUS: Binding of brassinosteroid induces intramolecular
autophosphorylation of BRI1. Interaction with BAK1 activates both
receptor kinases and the full activation of either receptor kinase
requires transphosphorylation by their partners. Optimum in vitro
phosphorylation of the substrate requires Arg or Lys residues at
P-3, P-4, and P+5 (relative to the phosphorylated amino acid at
P=0). Homodimerizes in the absence of ligand and binds
brassinosteroid in the absence of its coreceptor BAK1.
-!- MISCELLANEOUS: The bri1-9 mutation produces a fully active protein
with a subtle conformational change that is recognized for
reglucosylation by UGGT, resulting in its endoplasmic reticulum
retention via Glc(1)Man(9)GlcNAc(2)-calreticulin/calnexin
interaction. {ECO:0000305|PubMed:17588517}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
-----------------------------------------------------------------------
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EMBL; AF017056; AAC49810.1; -; Genomic_DNA.
EMBL; FJ708766; ACN59359.1; -; mRNA.
EMBL; AL078620; CAB44675.1; -; Genomic_DNA.
EMBL; AL161595; CAB80603.1; -; Genomic_DNA.
EMBL; CP002687; AEE87069.1; -; Genomic_DNA.
PIR; T09356; T09356.
RefSeq; NP_195650.1; NM_120100.3.
UniGene; At.27898; -.
UniGene; At.69020; -.
PDB; 3RGX; X-ray; 2.47 A; A=23-784.
PDB; 3RGZ; X-ray; 2.28 A; A=23-784.
PDB; 3RIZ; X-ray; 2.52 A; A=29-788.
PDB; 3RJ0; X-ray; 2.54 A; A=29-788.
PDB; 4LSA; X-ray; 2.50 A; A=29-788.
PDB; 4LSX; X-ray; 3.30 A; A/B=29-788.
PDB; 4M7E; X-ray; 3.60 A; A/B=24-784.
PDB; 4OH4; X-ray; 2.25 A; A/B=863-1172.
PDB; 4Q5J; X-ray; 2.77 A; A/B=863-1180.
PDB; 5LPB; X-ray; 1.98 A; A=865-1160.
PDB; 5LPV; X-ray; 2.70 A; A=865-1160.
PDB; 5LPW; X-ray; 2.43 A; A=865-1160.
PDB; 5LPY; X-ray; 2.30 A; A=865-1160.
PDB; 5LPZ; X-ray; 2.48 A; A=865-1196.
PDB; 6FIF; X-ray; 2.54 A; A=1-788.
PDBsum; 3RGX; -.
PDBsum; 3RGZ; -.
PDBsum; 3RIZ; -.
PDBsum; 3RJ0; -.
PDBsum; 4LSA; -.
PDBsum; 4LSX; -.
PDBsum; 4M7E; -.
PDBsum; 4OH4; -.
PDBsum; 4Q5J; -.
PDBsum; 5LPB; -.
PDBsum; 5LPV; -.
PDBsum; 5LPW; -.
PDBsum; 5LPY; -.
PDBsum; 5LPZ; -.
PDBsum; 6FIF; -.
ProteinModelPortal; O22476; -.
SMR; O22476; -.
BioGrid; 15375; 30.
DIP; DIP-45997N; -.
IntAct; O22476; 17.
STRING; 3702.AT4G39400.1; -.
iPTMnet; O22476; -.
PaxDb; O22476; -.
PRIDE; O22476; -.
EnsemblPlants; AT4G39400.1; AT4G39400.1; AT4G39400.
GeneID; 830095; -.
Gramene; AT4G39400.1; AT4G39400.1; AT4G39400.
KEGG; ath:AT4G39400; -.
Araport; AT4G39400; -.
TAIR; locus:2005498; AT4G39400.
eggNOG; ENOG410IF0B; Eukaryota.
eggNOG; COG0515; LUCA.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000116551; -.
InParanoid; O22476; -.
KO; K13415; -.
OMA; DHQSHRR; -.
OrthoDB; EOG093600TU; -.
PhylomeDB; O22476; -.
EvolutionaryTrace; O22476; -.
PRO; PR:O22476; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; O22476; baseline and differential.
Genevisible; O22476; AT.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
GO; GO:0005496; F:steroid binding; IDA:TAIR.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0048657; P:anther wall tapetum cell differentiation; IMP:TAIR.
GO; GO:0010268; P:brassinosteroid homeostasis; IEP:TAIR.
GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IMP:TAIR.
GO; GO:0009729; P:detection of brassinosteroid stimulus; IMP:TAIR.
GO; GO:0048366; P:leaf development; IMP:TAIR.
GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
GO; GO:0009911; P:positive regulation of flower development; IGI:TAIR.
GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
GO; GO:1900140; P:regulation of seedling development; IMP:UniProtKB.
GO; GO:0010224; P:response to UV-B; IGI:TAIR.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR013210; LRR_N_plant-typ.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00560; LRR_1; 2.
Pfam; PF13855; LRR_8; 2.
Pfam; PF08263; LRRNT_2; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00369; LRR_TYP; 7.
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;
3D-structure; ATP-binding; Brassinosteroid signaling pathway;
Cell membrane; Complete proteome; Endosome; Glycoprotein; Kinase;
Leucine-rich repeat; Lipid-binding; Membrane; Nucleotide-binding;
Phosphoprotein; Receptor; Reference proteome; Repeat;
Serine/threonine-protein kinase; Signal; Steroid-binding; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 1196 Protein BRASSINOSTEROID INSENSITIVE 1.
/FTId=PRO_0000024305.
TRANSMEM 793 813 Helical. {ECO:0000255}.
REPEAT 71 98 LRR 1. {ECO:0000255}.
REPEAT 99 121 LRR 2. {ECO:0000255}.
REPEAT 122 146 LRR 3. {ECO:0000255}.
REPEAT 148 169 LRR 4. {ECO:0000255}.
REPEAT 172 197 LRR 5. {ECO:0000255}.
REPEAT 199 221 LRR 6. {ECO:0000255}.
REPEAT 222 244 LRR 7. {ECO:0000255}.
REPEAT 245 268 LRR 8. {ECO:0000255}.
REPEAT 269 290 LRR 9. {ECO:0000255}.
REPEAT 291 314 LRR 10. {ECO:0000255}.
REPEAT 316 338 LRR 11. {ECO:0000255}.
REPEAT 339 363 LRR 12. {ECO:0000255}.
REPEAT 364 388 LRR 13. {ECO:0000255}.
REPEAT 390 413 LRR 14. {ECO:0000255}.
REPEAT 415 439 LRR 15. {ECO:0000255}.
REPEAT 441 463 LRR 16. {ECO:0000255}.
REPEAT 464 487 LRR 17. {ECO:0000255}.
REPEAT 488 511 LRR 18. {ECO:0000255}.
REPEAT 513 535 LRR 19. {ECO:0000255}.
REPEAT 536 559 LRR 20. {ECO:0000255}.
REPEAT 561 583 LRR 21. {ECO:0000255}.
REPEAT 653 677 LRR 22. {ECO:0000255}.
REPEAT 678 701 LRR 23. {ECO:0000255}.
REPEAT 702 725 LRR 24. {ECO:0000255}.
REPEAT 727 750 LRR 25. {ECO:0000255}.
DOMAIN 883 1158 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 889 897 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 957 959 ATP. {ECO:0000269|PubMed:24461462}.
NP_BIND 963 966 ATP. {ECO:0000269|PubMed:24461462}.
NP_BIND 1009 1014 ATP. {ECO:0000269|PubMed:24461462}.
MOTIF 62 69 Cys pair 1.
MOTIF 763 770 Cys pair 2.
ACT_SITE 1009 1009 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 597 597 Brassinolide.
{ECO:0000269|PubMed:21666666,
ECO:0000269|PubMed:23929946}.
BINDING 642 642 Brassinolide.
{ECO:0000269|PubMed:23929946}.
BINDING 647 647 Brassinolide; via amide nitrogen.
{ECO:0000269|PubMed:21666665,
ECO:0000269|PubMed:21666666,
ECO:0000269|PubMed:23929946}.
BINDING 705 705 Brassinolide.
{ECO:0000269|PubMed:21666666}.
BINDING 911 911 ATP. {ECO:0000269|PubMed:24461462}.
BINDING 1027 1027 ATP. {ECO:0000269|PubMed:24461462}.
MOD_RES 831 831 Phosphotyrosine.
{ECO:0000269|PubMed:19124768}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000269|PubMed:11027724,
ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MOD_RES 842 842 Phosphothreonine.
{ECO:0000269|PubMed:11027724}.
MOD_RES 846 846 Phosphothreonine.
{ECO:0000269|PubMed:11027724,
ECO:0000269|PubMed:18694562}.
MOD_RES 851 851 Phosphothreonine. {ECO:0000255}.
MOD_RES 858 858 Phosphoserine.
{ECO:0000269|PubMed:11027724,
ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MOD_RES 872 872 Phosphothreonine.
{ECO:0000269|PubMed:11027724,
ECO:0000269|PubMed:15894717}.
MOD_RES 880 880 Phosphothreonine.
{ECO:0000269|PubMed:15894717}.
MOD_RES 887 887 Phosphoserine.
{ECO:0000269|PubMed:19105183}.
MOD_RES 891 891 Phosphoserine. {ECO:0000255}.
MOD_RES 956 956 Phosphotyrosine.
{ECO:0000269|PubMed:19124768}.
MOD_RES 981 981 Phosphoserine. {ECO:0000255}.
MOD_RES 982 982 Phosphothreonine.
{ECO:0000269|PubMed:15894717}.
MOD_RES 1035 1035 Phosphoserine. {ECO:0000255}.
MOD_RES 1039 1039 Phosphothreonine. {ECO:0000255}.
MOD_RES 1042 1042 Phosphoserine. {ECO:0000255}.
MOD_RES 1044 1044 Phosphoserine.
{ECO:0000250|UniProtKB:Q9M0G7,
ECO:0000255}.
MOD_RES 1045 1045 Phosphothreonine. {ECO:0000255}.
MOD_RES 1049 1049 Phosphothreonine. {ECO:0000255}.
MOD_RES 1052 1052 Phosphotyrosine.
{ECO:0000250|UniProtKB:C0LGT6}.
MOD_RES 1060 1060 Phosphoserine. {ECO:0000255}.
MOD_RES 1072 1072 Phosphotyrosine. {ECO:0000255}.
MOD_RES 1166 1166 Phosphoserine.
{ECO:0000269|PubMed:18694562}.
MOD_RES 1168 1168 Phosphoserine.
{ECO:0000269|PubMed:15894717}.
MOD_RES 1169 1169 Phosphothreonine. {ECO:0000255}.
MOD_RES 1172 1172 Phosphoserine. {ECO:0000255}.
MOD_RES 1179 1179 Phosphoserine. {ECO:0000255}.
MOD_RES 1180 1180 Phosphothreonine.
{ECO:0000269|PubMed:18694562}.
MOD_RES 1187 1187 Phosphoserine. {ECO:0000255}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21666665,
ECO:0000269|PubMed:21666666,
ECO:0000269|PubMed:23929946}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21666665,
ECO:0000269|PubMed:21666666,
ECO:0000269|PubMed:23929946,
ECO:0000269|PubMed:24461462}.
CARBOHYD 233 233 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21666665,
ECO:0000269|PubMed:21666666,
ECO:0000269|PubMed:23929946}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21666665,
ECO:0000269|PubMed:21666666,
ECO:0000269|PubMed:23929946,
ECO:0000269|PubMed:24461462}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21666665,
ECO:0000269|PubMed:21666666,
ECO:0000269|PubMed:23929946}.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 438 438 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 510 510 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21666666}.
CARBOHYD 545 545 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21666665,
ECO:0000269|PubMed:21666666,
ECO:0000269|PubMed:23929946,
ECO:0000269|PubMed:24461462}.
CARBOHYD 573 573 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21666666,
ECO:0000269|PubMed:23929946}.
CARBOHYD 636 636 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 653 653 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 737 737 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 69 69 C->Y: In bri1-5; brassinosteroid-
insensitive semi-dwarf mutant.
MUTAGEN 611 611 G->E: In bri1-113; brassinosteroid-
insensitive semi-dwarf mutant.
MUTAGEN 613 613 G->S: In bri1-7; brassinosteroid-
insensitive semi-dwarf mutant.
MUTAGEN 644 644 G->D: In bri1-6; brassinosteroid-
insensitive semi-dwarf mutant.
MUTAGEN 662 662 S->F: In bri1-9; brassinosteroid-
insensitive semi-dwarf mutant.
MUTAGEN 750 750 T->I: In bri1-102; brassinosteroid-
insensitive dwarf mutant.
MUTAGEN 831 831 Y->D,E: No effect on kinase activity,
flowering time or leaf size, but altered
leaf shape.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 831 831 Y->F: No effect on kinase activity but
altered flowering time and leaf size and
shape. {ECO:0000269|PubMed:19124768}.
MUTAGEN 838 838 S->A: Decreases peptide phosphorylation,
but no effect on autophosphorylation.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 838 838 S->D: Increased kinase activity; when
associated with D-842; D-846 and D-858.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 842 842 T->A: Decreases peptide phosphorylation,
but no effect on autophosphorylation.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 842 842 T->D: Increased kinase activity; when
associated with D-838; D-846 and D-858.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 846 846 T->A: Decreases peptide phosphorylation,
but no effect on autophosphorylation.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 846 846 T->D: Increased kinase activity; when
associated with D-838; D-842 and D-858.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 858 858 S->A: Decreases peptide phosphorylation,
but no effect on autophosphorylation.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 858 858 S->D: Increased kinase activity; when
associated with D-838; D-842 and D-846.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 872 872 T->A: 10-fold increase in peptide
phosphorylation.
{ECO:0000269|PubMed:15894717}.
MUTAGEN 898 898 Y->F: No effect on kinase activity.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 909 909 A->T: In bri1-1; brassinosteroid-
insensitive dwarf mutant.
MUTAGEN 911 911 K->E: Loss of kinase activity; dwarf
mutant. {ECO:0000269|PubMed:11027724}.
MUTAGEN 945 945 Y->F: No effect on kinase activity.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 956 956 Y->F: Loss of kinase activity.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 961 961 Y->F: No effect on kinase activity.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 983 983 R->N: In bri1-8; brassinosteroid-
insensitive dwarf mutant.
MUTAGEN 983 983 R->Q: In bri1-108; brassinosteroid-
insensitive dwarf mutant.
MUTAGEN 989 989 G->I: In bri1-301; impaired kinase
activity and loss of autophosphorylation.
{ECO:0000269|PubMed:18332904}.
MUTAGEN 1031 1031 A->W: In bri1-104; brassinosteroid-
insensitive dwarf mutant, but no effect
on interaction with TTL.
MUTAGEN 1039 1039 T->A: Abolishes peptide phosphorylation,
and to a lower level autophosphorylation.
{ECO:0000269|PubMed:15894717}.
MUTAGEN 1042 1042 S->A: Abolishes peptide phosphorylation,
and to a lower level autophosphorylation.
MUTAGEN 1044 1044 S->A: Abolishes peptide phosphorylation,
and autophosphorylation.
{ECO:0000269|PubMed:15894717}.
MUTAGEN 1045 1045 T->A: Abolishes peptide phosphorylation,
and autophosphorylation.
{ECO:0000269|PubMed:15894717}.
MUTAGEN 1048 1048 G->D: In bri1-115; brassinosteroid-
insensitive dwarf mutant and no
interaction with TTL.
MUTAGEN 1049 1049 T->A: Abolishes peptide phosphorylation,
and autophosphorylation.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 1049 1049 T->D: Loss of kinase activity and
brassinosteroid signaling.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 1052 1052 Y->F: Loss of kinase activity.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 1057 1057 Y->F: Loss of kinase activity.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 1058 1058 Y->F: No effect on kinase activity.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 1070 1070 Y->F: No effect on kinase activity.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 1072 1072 Y->F: Loss of kinase activity.
{ECO:0000269|PubMed:19124768}.
MUTAGEN 1078 1078 E->K: In bri1-101; brassinosteroid-
insensitive dwarf mutant and no
interaction with TTL.
MUTAGEN 1139 1139 D->N: In bri1-117; brassinosteroid-
insensitive dwarf mutant.
MUTAGEN 1166 1166 S->D: Increased kinase activity; when
associated with D-1168; D-1172; D-1179
and D-1180.
{ECO:0000269|PubMed:18694562}.
MUTAGEN 1168 1168 S->A: Decreases peptide phosphorylation,
but no effect on autophosphorylation.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 1168 1168 S->D: Increased kinase activity; when
associated with D-1166; D-1172; D-1179
and D-1180. {ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 1172 1172 S->A: Decreases peptide phosphorylation,
but no effect on autophosphorylation.
{ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 1172 1172 S->D: Increased kinase activity; when
associated with D-1166; D-1168; D-1179
and D-1180. {ECO:0000269|PubMed:15894717,
ECO:0000269|PubMed:18694562}.
MUTAGEN 1179 1180 ST->A: Decreases peptide phosphorylation,
but no effect on autophosphorylation.
{ECO:0000269|PubMed:15894717}.
MUTAGEN 1179 1179 S->D: Increased kinase activity; when
associated with D-1166; D-1168; D-1172
and D-1180.
{ECO:0000269|PubMed:18694562}.
MUTAGEN 1180 1180 T->D: Increased kinase activity; when
associated with D-1166; D-1168; D-1172
and D-1179.
{ECO:0000269|PubMed:18694562}.
MUTAGEN 1187 1187 S->A: Decreases peptide phosphorylation,
but no effect on autophosphorylation.
{ECO:0000269|PubMed:15894717}.
HELIX 32 43 {ECO:0000244|PDB:3RGZ}.
HELIX 49 51 {ECO:0000244|PDB:3RIZ}.
STRAND 57 59 {ECO:0000244|PDB:3RGX}.
HELIX 61 63 {ECO:0000244|PDB:3RGZ}.
STRAND 67 70 {ECO:0000244|PDB:3RGZ}.
STRAND 73 78 {ECO:0000244|PDB:3RGZ}.
HELIX 88 94 {ECO:0000244|PDB:3RGZ}.
TURN 95 97 {ECO:0000244|PDB:3RGZ}.
STRAND 103 105 {ECO:0000244|PDB:3RGZ}.
STRAND 111 113 {ECO:0000244|PDB:3RGZ}.
STRAND 126 128 {ECO:0000244|PDB:3RGZ}.
STRAND 131 137 {ECO:0000244|PDB:3RGZ}.
HELIX 138 146 {ECO:0000244|PDB:3RGZ}.
STRAND 152 154 {ECO:0000244|PDB:3RGZ}.
STRAND 157 161 {ECO:0000244|PDB:3RGZ}.
STRAND 176 179 {ECO:0000244|PDB:3RGZ}.
STRAND 182 184 {ECO:0000244|PDB:3RGX}.
STRAND 186 188 {ECO:0000244|PDB:3RGZ}.
HELIX 190 195 {ECO:0000244|PDB:3RGZ}.
STRAND 204 206 {ECO:0000244|PDB:3RGZ}.
STRAND 209 214 {ECO:0000244|PDB:3RGZ}.
STRAND 226 228 {ECO:0000244|PDB:3RGZ}.
STRAND 249 251 {ECO:0000244|PDB:3RGZ}.
HELIX 261 264 {ECO:0000244|PDB:3RGZ}.
TURN 265 267 {ECO:0000244|PDB:3RGZ}.
STRAND 273 275 {ECO:0000244|PDB:3RGZ}.
STRAND 282 284 {ECO:0000244|PDB:3RGZ}.
STRAND 295 297 {ECO:0000244|PDB:3RGZ}.
STRAND 300 306 {ECO:0000244|PDB:3RGZ}.
HELIX 309 314 {ECO:0000244|PDB:3RGX}.
TURN 315 317 {ECO:0000244|PDB:3RGX}.
STRAND 319 322 {ECO:0000244|PDB:3RGZ}.
STRAND 325 330 {ECO:0000244|PDB:3RGZ}.
HELIX 334 338 {ECO:0000244|PDB:3RGZ}.
STRAND 344 346 {ECO:0000244|PDB:3RGZ}.
STRAND 349 355 {ECO:0000244|PDB:3RGZ}.
HELIX 358 361 {ECO:0000244|PDB:3RGZ}.
STRAND 369 371 {ECO:0000244|PDB:3RGZ}.
STRAND 374 379 {ECO:0000244|PDB:3RGZ}.
HELIX 385 388 {ECO:0000244|PDB:3RGZ}.
TURN 389 391 {ECO:0000244|PDB:3RGX}.
STRAND 393 396 {ECO:0000244|PDB:3RGZ}.
STRAND 399 405 {ECO:0000244|PDB:3RGZ}.
TURN 408 411 {ECO:0000244|PDB:3RGZ}.
STRAND 413 415 {ECO:0000244|PDB:4LSA}.
STRAND 420 422 {ECO:0000244|PDB:3RGZ}.
STRAND 425 431 {ECO:0000244|PDB:3RGZ}.
HELIX 434 438 {ECO:0000244|PDB:3RGZ}.
STRAND 444 446 {ECO:0000244|PDB:3RGZ}.
STRAND 449 454 {ECO:0000244|PDB:3RGZ}.
HELIX 458 462 {ECO:0000244|PDB:3RGZ}.
STRAND 468 470 {ECO:0000244|PDB:3RGZ}.
HELIX 482 486 {ECO:0000244|PDB:3RGZ}.
STRAND 492 494 {ECO:0000244|PDB:3RGZ}.
STRAND 497 500 {ECO:0000244|PDB:3RIZ}.
HELIX 506 510 {ECO:0000244|PDB:3RGZ}.
STRAND 516 518 {ECO:0000244|PDB:3RGZ}.
STRAND 525 527 {ECO:0000244|PDB:3RIZ}.
HELIX 530 534 {ECO:0000244|PDB:3RGZ}.
STRAND 540 542 {ECO:0000244|PDB:3RGZ}.
STRAND 549 551 {ECO:0000244|PDB:3RGZ}.
HELIX 554 558 {ECO:0000244|PDB:3RGZ}.
STRAND 564 566 {ECO:0000244|PDB:3RGZ}.
STRAND 569 575 {ECO:0000244|PDB:3RGZ}.
HELIX 578 581 {ECO:0000244|PDB:3RGZ}.
TURN 582 585 {ECO:0000244|PDB:3RGZ}.
TURN 591 594 {ECO:0000244|PDB:4LSA}.
STRAND 596 601 {ECO:0000244|PDB:3RGZ}.
STRAND 611 617 {ECO:0000244|PDB:3RGZ}.
HELIX 623 631 {ECO:0000244|PDB:3RGZ}.
STRAND 641 645 {ECO:0000244|PDB:3RGZ}.
STRAND 651 654 {ECO:0000244|PDB:3RGZ}.
STRAND 658 660 {ECO:0000244|PDB:3RGZ}.
STRAND 663 668 {ECO:0000244|PDB:3RGZ}.
HELIX 672 676 {ECO:0000244|PDB:3RGZ}.
STRAND 682 684 {ECO:0000244|PDB:3RGZ}.
STRAND 687 693 {ECO:0000244|PDB:3RGX}.
HELIX 696 700 {ECO:0000244|PDB:3RGZ}.
STRAND 706 708 {ECO:0000244|PDB:3RGZ}.
STRAND 715 717 {ECO:0000244|PDB:3RGX}.
HELIX 720 724 {ECO:0000244|PDB:3RGZ}.
STRAND 729 732 {ECO:0000244|PDB:3RGZ}.
STRAND 735 741 {ECO:0000244|PDB:3RGZ}.
STRAND 744 747 {ECO:0000244|PDB:3RGZ}.
HELIX 748 750 {ECO:0000244|PDB:3RGZ}.
HELIX 753 756 {ECO:0000244|PDB:3RGZ}.
STRAND 761 764 {ECO:0000244|PDB:3RGZ}.
HELIX 873 879 {ECO:0000244|PDB:5LPB}.
TURN 880 883 {ECO:0000244|PDB:5LPB}.
HELIX 885 887 {ECO:0000244|PDB:5LPB}.
STRAND 888 892 {ECO:0000244|PDB:5LPB}.
STRAND 895 901 {ECO:0000244|PDB:5LPB}.
STRAND 907 913 {ECO:0000244|PDB:5LPB}.
TURN 916 918 {ECO:0000244|PDB:5LPB}.
HELIX 919 929 {ECO:0000244|PDB:5LPB}.
HELIX 931 933 {ECO:0000244|PDB:5LPB}.
STRAND 942 948 {ECO:0000244|PDB:5LPB}.
STRAND 951 957 {ECO:0000244|PDB:5LPB}.
HELIX 964 969 {ECO:0000244|PDB:5LPB}.
HELIX 971 973 {ECO:0000244|PDB:5LPY}.
HELIX 980 999 {ECO:0000244|PDB:5LPB}.
STRAND 1001 1006 {ECO:0000244|PDB:5LPB}.
HELIX 1012 1014 {ECO:0000244|PDB:5LPB}.
STRAND 1015 1017 {ECO:0000244|PDB:5LPB}.
STRAND 1023 1025 {ECO:0000244|PDB:5LPB}.
STRAND 1032 1034 {ECO:0000244|PDB:5LPB}.
TURN 1050 1052 {ECO:0000244|PDB:5LPB}.
HELIX 1055 1058 {ECO:0000244|PDB:5LPB}.
STRAND 1060 1063 {ECO:0000244|PDB:5LPB}.
HELIX 1065 1081 {ECO:0000244|PDB:5LPB}.
TURN 1089 1093 {ECO:0000244|PDB:4OH4}.
HELIX 1096 1103 {ECO:0000244|PDB:5LPB}.
HELIX 1108 1110 {ECO:0000244|PDB:5LPB}.
HELIX 1114 1117 {ECO:0000244|PDB:5LPB}.
HELIX 1121 1123 {ECO:0000244|PDB:5LPB}.
HELIX 1124 1137 {ECO:0000244|PDB:5LPB}.
HELIX 1142 1144 {ECO:0000244|PDB:5LPB}.
HELIX 1148 1159 {ECO:0000244|PDB:5LPB}.
SEQUENCE 1196 AA; 130543 MW; C7FBA1C21294E600 CRC64;
MKTFSSFFLS VTTLFFFSFF SLSFQASPSQ SLYREIHQLI SFKDVLPDKN LLPDWSSNKN
PCTFDGVTCR DDKVTSIDLS SKPLNVGFSA VSSSLLSLTG LESLFLSNSH INGSVSGFKC
SASLTSLDLS RNSLSGPVTT LTSLGSCSGL KFLNVSSNTL DFPGKVSGGL KLNSLEVLDL
SANSISGANV VGWVLSDGCG ELKHLAISGN KISGDVDVSR CVNLEFLDVS SNNFSTGIPF
LGDCSALQHL DISGNKLSGD FSRAISTCTE LKLLNISSNQ FVGPIPPLPL KSLQYLSLAE
NKFTGEIPDF LSGACDTLTG LDLSGNHFYG AVPPFFGSCS LLESLALSSN NFSGELPMDT
LLKMRGLKVL DLSFNEFSGE LPESLTNLSA SLLTLDLSSN NFSGPILPNL CQNPKNTLQE
LYLQNNGFTG KIPPTLSNCS ELVSLHLSFN YLSGTIPSSL GSLSKLRDLK LWLNMLEGEI
PQELMYVKTL ETLILDFNDL TGEIPSGLSN CTNLNWISLS NNRLTGEIPK WIGRLENLAI
LKLSNNSFSG NIPAELGDCR SLIWLDLNTN LFNGTIPAAM FKQSGKIAAN FIAGKRYVYI
KNDGMKKECH GAGNLLEFQG IRSEQLNRLS TRNPCNITSR VYGGHTSPTF DNNGSMMFLD
MSYNMLSGYI PKEIGSMPYL FILNLGHNDI SGSIPDEVGD LRGLNILDLS SNKLDGRIPQ
AMSALTMLTE IDLSNNNLSG PIPEMGQFET FPPAKFLNNP GLCGYPLPRC DPSNADGYAH
HQRSHGRRPA SLAGSVAMGL LFSFVCIFGL ILVGREMRKR RRKKEAELEM YAEGHGNSGD
RTANNTNWKL TGVKEALSIN LAAFEKPLRK LTFADLLQAT NGFHNDSLIG SGGFGDVYKA
ILKDGSAVAI KKLIHVSGQG DREFMAEMET IGKIKHRNLV PLLGYCKVGD ERLLVYEFMK
YGSLEDVLHD PKKAGVKLNW STRRKIAIGS ARGLAFLHHN CSPHIIHRDM KSSNVLLDEN
LEARVSDFGM ARLMSAMDTH LSVSTLAGTP GYVPPEYYQS FRCSTKGDVY SYGVVLLELL
TGKRPTDSPD FGDNNLVGWV KQHAKLRISD VFDPELMKED PALEIELLQH LKVAVACLDD
RAWRRPTMVQ VMAMFKEIQA GSGIDSQSTI RSIEDGGFST IEMVDMSIKE VPEGKL


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