Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein kinase BRI1-like 1

Gene

BRL1

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

Functioni

Receptor with a serine/threonine-protein kinase activity. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development. Binds brassinolide. May be involved in cell growth and vascular differentiation.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei887 – 8871ATPPROSITE-ProRule annotation
Active sitei987 – 9871Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi865 – 8739ATPPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding, Steroid-binding

Enzyme and pathway databases

BioCyciARA:AT1G55610-MONOMER.
ARA:GQT-104-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase BRI1-like 1 (EC:2.7.11.1)
Alternative name(s):
BRASSINOSTEROID INSENSITIVE 1-like protein 1
Gene namesi
Name:BRL1
Ordered Locus Names:At1g55610
ORF Names:F20N2.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G55610.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 776755ExtracellularSequence analysisAdd
BLAST
Transmembranei777 – 79721HelicalSequence analysisAdd
BLAST
Topological domaini798 – 1166369CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 11661145Serine/threonine-protein kinase BRI1-like 1PRO_0000024308Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence analysis
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence analysis
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence analysis
Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence analysis
Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence analysis
Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence analysis
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence analysis
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence analysis
Glycosylationi451 – 4511N-linked (GlcNAc...)Sequence analysis
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence analysis
Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence analysis
Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence analysis
Glycosylationi558 – 5581N-linked (GlcNAc...)Sequence analysis
Glycosylationi638 – 6381N-linked (GlcNAc...)Sequence analysis
Glycosylationi722 – 7221N-linked (GlcNAc...)Sequence analysis
Glycosylationi743 – 7431N-linked (GlcNAc...)Sequence analysis
Modified residuei848 – 8481PhosphothreonineBy similarity
Modified residuei856 – 8561PhosphothreonineBy similarity
Modified residuei932 – 9321PhosphotyrosineBy similarity
Modified residuei1030 – 10301PhosphotyrosineBy similarity
Modified residuei1141 – 11411PhosphothreonineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9ZWC8.
PRIDEiQ9ZWC8.

PTM databases

iPTMnetiQ9ZWC8.

Expressioni

Tissue specificityi

Predominantly expressed in vascular tissues. From 7 day old seedlings, it is expressed in the columella cells of the root tip, in the vascular initials in the meristematic region of the root and in vascular tissues. After germination, it is expressed in the stele cell and in the early differentiation zone of the root, where the expression continues from the root to the hypocotyls and cotyledons following the midvein. In mature plants, it is expressed in the vasculature of the leaf, predominantly in the midvein, and in the vascular bundles of inflorescence stems. Localizes to procambial cells of the vascular bundles located between the differentiating xylem and the phloem.2 Publications

Gene expression databases

GenevisibleiQ9ZWC8. AT.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
BAK1Q94F625EBI-590903,EBI-617138
BKI1Q9FMZ04EBI-590903,EBI-1111615

Protein-protein interaction databases

BioGridi27235. 2 interactions.
IntActiQ9ZWC8. 3 interactions.
STRINGi3702.AT1G55610.1.

Structurei

Secondary structure

1
1166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 4412Combined sources
Beta strandi46 – 483Combined sources
Turni53 – 564Combined sources
Helixi65 – 673Combined sources
Beta strandi71 – 733Combined sources
Beta strandi79 – 835Combined sources
Beta strandi90 – 934Combined sources
Helixi95 – 995Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi111 – 1166Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi134 – 1374Combined sources
Helixi140 – 14910Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi184 – 1907Combined sources
Turni193 – 1986Combined sources
Beta strandi205 – 2073Combined sources
Beta strandi214 – 2163Combined sources
Helixi217 – 2193Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi235 – 2395Combined sources
Helixi247 – 2493Combined sources
Beta strandi255 – 2573Combined sources
Turni270 – 2756Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi290 – 2923Combined sources
Helixi295 – 3028Combined sources
Beta strandi305 – 3084Combined sources
Helixi320 – 3245Combined sources
Beta strandi330 – 3323Combined sources
Beta strandi335 – 3384Combined sources
Helixi342 – 3454Combined sources
Helixi347 – 3493Combined sources
Beta strandi355 – 3573Combined sources
Beta strandi364 – 3663Combined sources
Helixi369 – 3735Combined sources
Beta strandi379 – 3813Combined sources
Beta strandi384 – 3896Combined sources
Beta strandi395 – 3984Combined sources
Beta strandi406 – 4083Combined sources
Helixi420 – 4245Combined sources
Beta strandi430 – 4323Combined sources
Beta strandi439 – 4413Combined sources
Helixi444 – 4474Combined sources
Beta strandi454 – 4563Combined sources
Beta strandi459 – 4646Combined sources
Turni468 – 4725Combined sources
Beta strandi478 – 4814Combined sources
Helixi493 – 4975Combined sources
Beta strandi503 – 5053Combined sources
Helixi517 – 5215Combined sources
Beta strandi527 – 5293Combined sources
Helixi541 – 5455Combined sources
Beta strandi551 – 5533Combined sources
Beta strandi556 – 5594Combined sources
Helixi565 – 5684Combined sources
Turni569 – 5735Combined sources
Turni578 – 5814Combined sources
Beta strandi583 – 5908Combined sources
Turni594 – 5974Combined sources
Beta strandi598 – 6036Combined sources
Helixi609 – 6146Combined sources
Turni616 – 6205Combined sources
Beta strandi623 – 6308Combined sources
Beta strandi636 – 6394Combined sources
Beta strandi642 – 6454Combined sources
Beta strandi652 – 6543Combined sources
Helixi657 – 6615Combined sources
Beta strandi667 – 6693Combined sources
Helixi681 – 6855Combined sources
Beta strandi690 – 6934Combined sources
Beta strandi696 – 7016Combined sources
Helixi705 – 7095Combined sources
Beta strandi715 – 7173Combined sources
Beta strandi720 – 7234Combined sources
Helixi733 – 7353Combined sources
Helixi738 – 7414Combined sources
Beta strandi745 – 7495Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4J0MX-ray2.50A/B25-758[»]
ProteinModelPortaliQ9ZWC8.
SMRiQ9ZWC8. Positions 31-757, 810-1139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati78 – 9922LRR 1Add
BLAST
Repeati103 – 12422LRR 2Add
BLAST
Repeati126 – 14722LRR 3Add
BLAST
Repeati152 – 17322LRR 4Add
BLAST
Repeati176 – 19722LRR 5Add
BLAST
Repeati202 – 22423LRR 6Add
BLAST
Repeati227 – 24822LRR 7Add
BLAST
Repeati252 – 27423LRR 8Add
BLAST
Repeati278 – 30023LRR 9Add
BLAST
Repeati303 – 32523LRR 10Add
BLAST
Repeati327 – 34923LRR 11Add
BLAST
Repeati352 – 37524LRR 12Add
BLAST
Repeati376 – 39722LRR 13Add
BLAST
Repeati403 – 42422LRR 14Add
BLAST
Repeati427 – 44923LRR 15Add
BLAST
Repeati451 – 47323LRR 16Add
BLAST
Repeati476 – 49823LRR 17Add
BLAST
Repeati500 – 52223LRR 18Add
BLAST
Repeati524 – 54724LRR 19Add
BLAST
Repeati548 – 57023LRR 20Add
BLAST
Repeati664 – 68623LRR 21Add
BLAST
Repeati688 – 71023LRR 22Add
BLAST
Repeati712 – 73423LRR 23Add
BLAST
Domaini859 – 1147289Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi66 – 738Cys pair 1
Motifi748 – 7558Cys pair 2

Domaini

Contains two pairs of conservatively spaced Cys (Cys pair 1 and 2) possibly involved in forming some heterodimers.By similarity
A 70 amino acid island between the 19th and the 20th LRR is essential for the binding of brassinosteroids.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 23 LRR (leucine-rich) repeats.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IJWH. Eukaryota.
COG0515. LUCA.
COG4886. LUCA.
HOGENOMiHOG000116551.
InParanoidiQ9ZWC8.
OMAiCPATRIY.
PhylomeDBiQ9ZWC8.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13516. LRR_6. 4 hits.
PF13855. LRR_8. 1 hit.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 4 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51450. LRR. 16 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ZWC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQRWLLVLI LCFFTTSLVM GIHGKHLIND DFNETALLLA FKQNSVKSDP
60 70 80 90 100
NNVLGNWKYE SGRGSCSWRG VSCSDDGRIV GLDLRNSGLT GTLNLVNLTA
110 120 130 140 150
LPNLQNLYLQ GNYFSSGGDS SGSDCYLQVL DLSSNSISDY SMVDYVFSKC
160 170 180 190 200
SNLVSVNISN NKLVGKLGFA PSSLQSLTTV DLSYNILSDK IPESFISDFP
210 220 230 240 250
ASLKYLDLTH NNLSGDFSDL SFGICGNLTF FSLSQNNLSG DKFPITLPNC
260 270 280 290 300
KFLETLNISR NNLAGKIPNG EYWGSFQNLK QLSLAHNRLS GEIPPELSLL
310 320 330 340 350
CKTLVILDLS GNTFSGELPS QFTACVWLQN LNLGNNYLSG DFLNTVVSKI
360 370 380 390 400
TGITYLYVAY NNISGSVPIS LTNCSNLRVL DLSSNGFTGN VPSGFCSLQS
410 420 430 440 450
SPVLEKILIA NNYLSGTVPM ELGKCKSLKT IDLSFNELTG PIPKEIWMLP
460 470 480 490 500
NLSDLVMWAN NLTGTIPEGV CVKGGNLETL ILNNNLLTGS IPESISRCTN
510 520 530 540 550
MIWISLSSNR LTGKIPSGIG NLSKLAILQL GNNSLSGNVP RQLGNCKSLI
560 570 580 590 600
WLDLNSNNLT GDLPGELASQ AGLVMPGSVS GKQFAFVRNE GGTDCRGAGG
610 620 630 640 650
LVEFEGIRAE RLERLPMVHS CPATRIYSGM TMYTFSANGS MIYFDISYNA
660 670 680 690 700
VSGFIPPGYG NMGYLQVLNL GHNRITGTIP DSFGGLKAIG VLDLSHNNLQ
710 720 730 740 750
GYLPGSLGSL SFLSDLDVSN NNLTGPIPFG GQLTTFPVSR YANNSGLCGV
760 770 780 790 800
PLRPCGSAPR RPITSRIHAK KQTVATAVIA GIAFSFMCFV MLVMALYRVR
810 820 830 840 850
KVQKKEQKRE KYIESLPTSG SCSWKLSSVP EPLSINVATF EKPLRKLTFA
860 870 880 890 900
HLLEATNGFS AETMVGSGGF GEVYKAQLRD GSVVAIKKLI RITGQGDREF
910 920 930 940 950
MAEMETIGKI KHRNLVPLLG YCKVGEERLL VYEYMKWGSL ETVLHEKSSK
960 970 980 990 1000
KGGIYLNWAA RKKIAIGAAR GLAFLHHSCI PHIIHRDMKS SNVLLDEDFE
1010 1020 1030 1040 1050
ARVSDFGMAR LVSALDTHLS VSTLAGTPGY VPPEYYQSFR CTAKGDVYSY
1060 1070 1080 1090 1100
GVILLELLSG KKPIDPGEFG EDNNLVGWAK QLYREKRGAE ILDPELVTDK
1110 1120 1130 1140 1150
SGDVELFHYL KIASQCLDDR PFKRPTMIQL MAMFKEMKAD TEEDESLDEF
1160
SLKETPLVEE SRDKEP
Length:1,166
Mass (Da):127,424
Last modified:May 1, 1999 - v1
Checksum:i8C4DD9231A466AF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ708660 mRNA. Translation: ACN59256.1.
AC002328 Genomic DNA. Translation: AAF79510.1.
CP002684 Genomic DNA. Translation: AEE33271.1.
CP002684 Genomic DNA. Translation: AEE33272.1.
PIRiF96598.
RefSeqiNP_001117501.1. NM_001124029.1.
NP_175957.1. NM_104437.2.
UniGeneiAt.66034.

Genome annotation databases

EnsemblPlantsiAT1G55610.1; AT1G55610.1; AT1G55610.
AT1G55610.2; AT1G55610.2; AT1G55610.
GeneIDi842010.
GrameneiAT1G55610.1; AT1G55610.1; AT1G55610.
AT1G55610.2; AT1G55610.2; AT1G55610.
KEGGiath:AT1G55610.

Cross-referencesi

Web resourcesi

PlantP kinase Classification PPC

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ708660 mRNA. Translation: ACN59256.1.
AC002328 Genomic DNA. Translation: AAF79510.1.
CP002684 Genomic DNA. Translation: AEE33271.1.
CP002684 Genomic DNA. Translation: AEE33272.1.
PIRiF96598.
RefSeqiNP_001117501.1. NM_001124029.1.
NP_175957.1. NM_104437.2.
UniGeneiAt.66034.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4J0MX-ray2.50A/B25-758[»]
ProteinModelPortaliQ9ZWC8.
SMRiQ9ZWC8. Positions 31-757, 810-1139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27235. 2 interactions.
IntActiQ9ZWC8. 3 interactions.
STRINGi3702.AT1G55610.1.

PTM databases

iPTMnetiQ9ZWC8.

Proteomic databases

PaxDbiQ9ZWC8.
PRIDEiQ9ZWC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G55610.1; AT1G55610.1; AT1G55610.
AT1G55610.2; AT1G55610.2; AT1G55610.
GeneIDi842010.
GrameneiAT1G55610.1; AT1G55610.1; AT1G55610.
AT1G55610.2; AT1G55610.2; AT1G55610.
KEGGiath:AT1G55610.

Organism-specific databases

TAIRiAT1G55610.

Phylogenomic databases

eggNOGiENOG410IJWH. Eukaryota.
COG0515. LUCA.
COG4886. LUCA.
HOGENOMiHOG000116551.
InParanoidiQ9ZWC8.
OMAiCPATRIY.
PhylomeDBiQ9ZWC8.

Enzyme and pathway databases

BioCyciARA:AT1G55610-MONOMER.
ARA:GQT-104-MONOMER.

Miscellaneous databases

PROiQ9ZWC8.

Gene expression databases

GenevisibleiQ9ZWC8. AT.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.80.10.10. 4 hits.
InterProiIPR013320. ConA-like_dom.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR013210. LRR_N_plant-typ.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13516. LRR_6. 4 hits.
PF13855. LRR_8. 1 hit.
PF08263. LRRNT_2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 8 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 4 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51450. LRR. 16 hits.
PS00107. 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. "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana."
    Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.
    BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry."
    Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
    Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. La-0.
  5. "BRL1 and BRL3 are novel brassinosteroid receptors that function in vascular differentiation in Arabidopsis."
    Cano-Delgado A., Yin Y., Yu C., Vafeados D., Mora-Garcia S., Cheng J.-C., Nam K.H., Li J., Chory J.
    Development 131:5341-5351(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, STEROID-BINDING, TISSUE SPECIFICITY.
  6. "Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database."
    Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
    Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "BRL1, a leucine-rich repeat receptor-like protein kinase, is functionally redundant with BRI1 in regulating Arabidopsis brassinosteroid signaling."
    Zhou A., Wang H., Walker J.C., Li J.
    Plant J. 40:399-409(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiBRL1_ARATH
AccessioniPrimary (citable) accession number: Q9ZWC8
Secondary accession number(s): C0LGH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.