Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein BRASSINOSTEROID INSENSITIVE 1  

UniProtKB / Swiss-Prot ID :  BRI1_ARATH

Gene Name (Synonyms) : 
BRI1 At4g39400 F23K16.30  

Species :  Arabidopsis thaliana (Mouse-ear cress). 

Subcellular Localization :  Cell membrane; Single-pass type I membrane protein. Endosome membrane; Single-pass type I membrane protein. 

Protein 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. 

Transmembrane Topology (topPTM) : BRI1_ARATH 

Protein Sequence MKTFSSFFLSVTTLFFFSFFSLSFQASPSQSLYREIHQLISFKDVLPDKNLLPDWSSNKNPCTFDGVTCR...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCEEEEECC...
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
831Phosphotyrosine.ELEMYAEGH
HHCCCCCCC
7.66UniProtKB
Link-
838Phosphoserine.GHGNSGDRT
CCCCCCCCC
46.81UniProtKB
Link-
842Phosphothreonine.SGDRTANNT
CCCCCCCCC
38.18UniProtKB
Link-
846Phosphothreonine.TANNTNWKL
CCCCCCCCC
42.11UniProtKB
Link-
858Phosphoserine.KEALSINLA
CCCCCCCCC
19.24UniProtKB
Link-
872Phosphothreonine.LRKLTFADL
HHCCCHHHH
21.58UniProtKB
Link-
880Phosphothreonine.LLQATNGFH
HHCCHHHEE
23.94UniProtKB
Link-
887Phosphoserine.FHNDSLIGS
EEEEEEEEE
27.49UniProtKB
Link-
956Phosphotyrosine.RLLVYEFMK
EEEEEEECC
11.92UniProtKB
Link-
982Phosphothreonine.LNWSTRRKI
CCHHHHHHH
26.55UniProtKB
Link-
1166Phosphoserine.SGIDSQSTI
CCCCCCCCC
24.90UniProtKB
Link-
1168Phosphoserine.IDSQSTIRS
CCCCCCCCC
29.74UniProtKB
Link-
1180Phosphothreonine.GGFSTIEMV
CCCCEEEEC
20.78UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Drug Reference
- top -
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Sequential transphosphorylation of the BRI1/BAK1 receptor kinasecomplex impacts early events in brassinosteroid signaling.";
Wang X., Kota U., He K., Blackburn K., Li J., Goshe M.B., Huber S.C.,Clouse S.D.;
Dev. Cell 15:220-235(2008).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-838; THR-846; SER-858; SER-1166 ANDTHR-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 ANDTHR-1180.
"Identification of in vitro phosphorylation sites in the Arabidopsisthaliana somatic embryogenesis receptor-like kinases.";
Karlova R., Boeren S., van Dongen W., Kwaaitaal M., Aker J.,Vervoort J., de Vries S.C.;
Proteomics 9:368-379(2009).
Cited for: PHOSPHORYLATION AT SER-887, AND PHOSPHORYLATION OF SERK1.
"Tyrosine phosphorylation of the BRI1 receptor kinase emerges as acomponent of brassinosteroid signaling in Arabidopsis.";
Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.;
Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009).
Cited for: 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.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures