BRI1_ARATH - dbPTM
BRI1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRI1_ARATH
UniProt AC O22476
Protein Name Protein BRASSINOSTEROID INSENSITIVE 1 {ECO:0000303|PubMed:9298904}
Gene Name BRI1 {ECO:0000303|PubMed:9298904}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1196
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Endosome membrane
Single-pass type I membrane protein.
Protein Description 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]
Protein Sequence MKTFSSFFLSVTTLFFFSFFSLSFQASPSQSLYREIHQLISFKDVLPDKNLLPDWSSNKNPCTFDGVTCRDDKVTSIDLSSKPLNVGFSAVSSSLLSLTGLESLFLSNSHINGSVSGFKCSASLTSLDLSRNSLSGPVTTLTSLGSCSGLKFLNVSSNTLDFPGKVSGGLKLNSLEVLDLSANSISGANVVGWVLSDGCGELKHLAISGNKISGDVDVSRCVNLEFLDVSSNNFSTGIPFLGDCSALQHLDISGNKLSGDFSRAISTCTELKLLNISSNQFVGPIPPLPLKSLQYLSLAENKFTGEIPDFLSGACDTLTGLDLSGNHFYGAVPPFFGSCSLLESLALSSNNFSGELPMDTLLKMRGLKVLDLSFNEFSGELPESLTNLSASLLTLDLSSNNFSGPILPNLCQNPKNTLQELYLQNNGFTGKIPPTLSNCSELVSLHLSFNYLSGTIPSSLGSLSKLRDLKLWLNMLEGEIPQELMYVKTLETLILDFNDLTGEIPSGLSNCTNLNWISLSNNRLTGEIPKWIGRLENLAILKLSNNSFSGNIPAELGDCRSLIWLDLNTNLFNGTIPAAMFKQSGKIAANFIAGKRYVYIKNDGMKKECHGAGNLLEFQGIRSEQLNRLSTRNPCNITSRVYGGHTSPTFDNNGSMMFLDMSYNMLSGYIPKEIGSMPYLFILNLGHNDISGSIPDEVGDLRGLNILDLSSNKLDGRIPQAMSALTMLTEIDLSNNNLSGPIPEMGQFETFPPAKFLNNPGLCGYPLPRCDPSNADGYAHHQRSHGRRPASLAGSVAMGLLFSFVCIFGLILVGREMRKRRRKKEAELEMYAEGHGNSGDRTANNTNWKLTGVKEALSINLAAFEKPLRKLTFADLLQATNGFHNDSLIGSGGFGDVYKAILKDGSAVAIKKLIHVSGQGDREFMAEMETIGKIKHRNLVPLLGYCKVGDERLLVYEFMKYGSLEDVLHDPKKAGVKLNWSTRRKIAIGSARGLAFLHHNCSPHIIHRDMKSSNVLLDENLEARVSDFGMARLMSAMDTHLSVSTLAGTPGYVPPEYYQSFRCSTKGDVYSYGVVLLELLTGKRPTDSPDFGDNNLVGWVKQHAKLRISDVFDPELMKEDPALEIELLQHLKVAVACLDDRAWRRPTMVQVMAMFKEIQAGSGIDSQSTIRSIEDGGFSTIEMVDMSIKEVPEGKL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
112N-linked_GlycosylationFLSNSHINGSVSGFK
HCCCCCCCCCCCCCC		31.1221666665
154N-linked_GlycosylationCSGLKFLNVSSNTLD
CCCCEEEEECCCCCC		34.4524461462
233N-linked_GlycosylationFLDVSSNNFSTGIPF
EEECCCCCCCCCCCC		33.9121666665
275N-linked_GlycosylationCTELKLLNISSNQFV
CCEEEEEECCCCCCC		42.4024461462
351N-linked_GlycosylationSLALSSNNFSGELPM
HHHHCCCCCCCCCCH		34.1121666665
387N-linked_GlycosylationELPESLTNLSASLLT
CCCHHHHHHCHHHHE		36.97-
401N-linked_GlycosylationTLDLSSNNFSGPILP
EEECCCCCCCCCCCH		34.11-
438N-linked_GlycosylationKIPPTLSNCSELVSL
CCCCCCCCHHHHHHH		36.12-
510N-linked_GlycosylationEIPSGLSNCTNLNWI
CCCCCCCCCCCCCEE		41.4921666666
545N-linked_GlycosylationLAILKLSNNSFSGNI
EEEEECCCCCCCCCC		59.6124461462
573N-linked_GlycosylationDLNTNLFNGTIPAAM
ECCCCCCCCCCCHHH		50.2721666666
636N-linked_GlycosylationLSTRNPCNITSRVYG
HHCCCCCCCCCCCCC		41.66-
653N-linked_GlycosylationTSPTFDNNGSMMFLD
CCCCCCCCCCEEEEE		45.84-
737N-linked_GlycosylationEIDLSNNNLSGPIPE
EEECCCCCCCCCCCC		39.57-
831PhosphorylationKEAELEMYAEGHGNS
HHHHHHHHHCCCCCC		7.6619124768
838PhosphorylationYAEGHGNSGDRTANN
HHCCCCCCCCCCCCC		46.8118694562
842PhosphorylationHGNSGDRTANNTNWK
CCCCCCCCCCCCCCE		38.1811027724
846PhosphorylationGDRTANNTNWKLTGV
CCCCCCCCCCEECCH		42.1118694562
851PhosphorylationNNTNWKLTGVKEALS
CCCCCEECCHHHHHH		35.88-
858PhosphorylationTGVKEALSINLAAFE
CCHHHHHHCCHHHHC		19.2418694562
872PhosphorylationEKPLRKLTFADLLQA
CCHHHHCCHHHHHHH		21.5824243849
880PhosphorylationFADLLQATNGFHNDS
HHHHHHHHCCCCCCC		23.9424243849
887PhosphorylationTNGFHNDSLIGSGGF
HCCCCCCCCCCCCCC		27.4924243849
891PhosphorylationHNDSLIGSGGFGDVY
CCCCCCCCCCCHHHH		28.84-
917PhosphorylationIKKLIHVSGQGDREF
EEEEEECCCCCCHHH		15.9625561503
956PhosphorylationGDERLLVYEFMKYGS
CCCEEEEEEHHHHCC		11.9219124768
981PhosphorylationAGVKLNWSTRRKIAI
HCCCCCCCCCCCEEC		15.80-
982PhosphorylationGVKLNWSTRRKIAIG
CCCCCCCCCCCEECC		26.5524243849
1035PhosphorylationFGMARLMSAMDTHLS
HHHHHHHHHHCCCEE		25.65-
1039PhosphorylationRLMSAMDTHLSVSTL
HHHHHHCCCEEHHHH		16.19-
1042PhosphorylationSAMDTHLSVSTLAGT
HHHCCCEEHHHHCCC		13.35-
1044PhosphorylationMDTHLSVSTLAGTPG
HCCCEEHHHHCCCCC		17.8324243849
1045PhosphorylationDTHLSVSTLAGTPGY
CCCEEHHHHCCCCCC		20.6224243849
1049PhosphorylationSVSTLAGTPGYVPPE
EHHHHCCCCCCCCHH		14.1324243849
1052PhosphorylationTLAGTPGYVPPEYYQ
HHCCCCCCCCHHHHH		15.81-
1060PhosphorylationVPPEYYQSFRCSTKG
CCHHHHHCCCCCCCC		9.87-
1072PhosphorylationTKGDVYSYGVVLLEL
CCCCHHHHHHHHHHH		9.03-
1166PhosphorylationQAGSGIDSQSTIRSI
HCCCCCCCCHHEEEE		24.9018694562
1168PhosphorylationGSGIDSQSTIRSIED
CCCCCCCHHEEEECC		29.7424243849
1169PhosphorylationSGIDSQSTIRSIEDG
CCCCCCHHEEEECCC		16.87-
1172PhosphorylationDSQSTIRSIEDGGFS
CCCHHEEEECCCCCE		26.86-
1179PhosphorylationSIEDGGFSTIEMVDM
EECCCCCEEEEEEEC		31.58-
1180PhosphorylationIEDGGFSTIEMVDMS
ECCCCCEEEEEEECC		20.7818694562
1187PhosphorylationTIEMVDMSIKEVPEG
EEEEEECCCCCCCCC		26.50-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of BRI1_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
838SPhosphorylation

11027724
846TPhosphorylation

11027724
858SPhosphorylation

11027724
887SPhosphorylation

19105183
1166SPhosphorylation

18694562
1166SPhosphorylation

18694562
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BRI1_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAK1_ARATHBAK1genetic
12150929
BAK1_ARATHBAK1physical
12150929
P2C70_ARATHKAPPphysical
17302430
BAK1_ARATHBAK1physical
18694562
SERK1_ARATHSERK1physical
19105183
BAK1_ARATHBAK1physical
15894717
BAK1_ARATHBAK1physical
15548744
BAK1_ARATHBAK1physical
12150928
TTHL_ARATHTTLphysical
15319482
EIF3I_ARATHTRIP-1physical
15998311
BAK1_ARATHBAK1physical
21593986
Y4523_ARATHBSK1physical
23496207
Y5126_ARATHAT5G41260physical
23496207
BIK1_ARATHBIK1physical
23818580
CLAH1_ARATHAT3G11130physical
23975899
CCI1_ARATHCPI1physical
23776660
BAK1_ARATHBAK1physical
19532123
CALR3_ARATHCRT3physical
19597144
VA727_ARATHVAMP727physical
24833385
SYP22_ARATHVAM3physical
24833385
BAK1_ARATHBAK1physical
21464298
BAK1_ARATHBAK1physical
20876109
BRI1_ARATHBRI1physical
25602612
SERK1_ARATHSERK1physical
23929946
BAK1_ARATHBAK1physical
24126715
BAK1_ARATHBAK1physical
19277500
BAK1_ARATHBAK1genetic
19277500
BRI1_ARATHBRI1physical
18332904
TTHL_ARATHTTLphysical
18332904
BAK1_ARATHBAK1physical
18332904
U503A_ARATHAT3G09070genetic
26387715
BKI1_ARATHBKI1physical
25331450
HRD3A_ARATHAT1G18260physical
26371323
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BRI1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.

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