BAK1_ARATH - dbPTM
BAK1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BAK1_ARATH
UniProt AC Q94F62
Protein Name BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1 {ECO:0000303|PubMed:12150929}
Gene Name BAK1 {ECO:0000303|PubMed:12150929}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 615
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Endosome membrane
Single-pass type I membrane protein. Endocytosis enhanced upon interaction with MSBP1.
Protein Description Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Controls the expression of genes associated with innate immunity in the absence of pathogens or elicitors. Involved in brassinosteroid (BR) signal transduction. Phosphorylates BRI1. May be involved in changing the equilibrium between plasma membrane-located BRI1 homodimers and endocytosed BRI1-BAK1 heterodimers. Interaction with MSBP1 stimulates the endocytosis of BAK1 and suppresses brassinosteroid signaling. Acts in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) via its interactions with FLS2 and EFR, and the phosphorylation of BIK1. Involved in programmed cell death (PCD) control. Positively regulates the BR-dependent plant growth pathway and negatively regulates the BR-independent cell-death pathway. [PubMed: 17583510]
Protein Sequence MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANLSGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSLTAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSNRITGAIAGGVAAGAALLFAVPAIALAWWRRKKPQDHFFDVPAEEDPEVHLGQLKRFSLRELQVASDNFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTQGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPESQPPLDWPKRQRIALGSARGLAYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGVMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEALVDVDLQGNYKDEEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAERWEEWQKEEMFRQDFNYPTHHPAVSGWIIGDSTSQIENEYPSGPR
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
79N-linked_GlycosylationRVDLGNANLSGQLVM
EEECCCCCCHHHHHH		38.45-
103N-linked_GlycosylationYLELYSNNITGTIPE
EEEEHHCCCCCCCHH		27.53-
114N-linked_GlycosylationTIPEQLGNLTELVSL
CCHHHHCCHHHHHHH		53.00-
127N-linked_GlycosylationSLDLYLNNLSGPIPS
HHHHHHCCCCCCCCC		32.75-
149N-linked_GlycosylationLRFLRLNNNSLSGEI
HHEEEECCCCCCCCC		44.02-
159PhosphorylationLSGEIPRSLTAVLTL
CCCCCCCHHHHHEEE		25.3925368622
161PhosphorylationGEIPRSLTAVLTLQV
CCCCCHHHHHEEEEE		18.9025368622
165PhosphorylationRSLTAVLTLQVLDLS
CHHHHHEEEEEEECC		14.4625368622
172PhosphorylationTLQVLDLSNNPLTGD
EEEEEECCCCCCCCC		33.9425368622
177PhosphorylationDLSNNPLTGDIPVNG
ECCCCCCCCCCCCCC		33.7825368622
183N-linked_GlycosylationLTGDIPVNGSFSLFT
CCCCCCCCCEEEEEE		34.73-
185PhosphorylationGDIPVNGSFSLFTPI
CCCCCCCEEEEEEEE		13.3725368622
187PhosphorylationIPVNGSFSLFTPISF
CCCCCEEEEEEEEEE		25.0325368622
190PhosphorylationNGSFSLFTPISFANT
CCEEEEEEEEEECCC		25.6325368622
193PhosphorylationFSLFTPISFANTKLT
EEEEEEEEECCCCCC		21.3625368622
197PhosphorylationTPISFANTKLTPLPA
EEEEECCCCCCCCCC		24.8125368622
278PhosphorylationLGQLKRFSLRELQVA
HHHHCCCCHHHHHHH		30.4624243849
286PhosphorylationLRELQVASDNFSNKN
HHHHHHHCCCCCCCC		33.9418694562
290PhosphorylationQVASDNFSNKNILGR
HHHCCCCCCCCCCCC		53.8218694562
312PhosphorylationKGRLADGTLVAVKRL
CCEECCCCEEEEEEH		20.7118694562
333PhosphorylationGGELQFQTEVEMISM
CCCEEEHHHHHHHHH		43.2024243849
339PhosphorylationQTEVEMISMAVHRNL
HHHHHHHHHHHHHHH		10.2024243849
370PhosphorylationYPYMANGSVASCLRE
EHHHCCCCHHHHHHC		17.8324243849
373PhosphorylationMANGSVASCLRERPE
HCCCCHHHHHHCCCC		16.13-
443PhosphorylationGLAKLMDYKDTHVTT
HHHHHHCCCCCCCHH		9.2215308754
446PhosphorylationKLMDYKDTHVTTAVR
HHHCCCCCCCHHHHH		17.6930291188
449PhosphorylationDYKDTHVTTAVRGTI
CCCCCCCHHHHHCCC		11.0530291188
450PhosphorylationYKDTHVTTAVRGTIG
CCCCCCHHHHHCCCC		23.2830291188
455PhosphorylationVTTAVRGTIGHIAPE
CHHHHHCCCCCCCHH		17.1418694562
463PhosphorylationIGHIAPEYLSTGKSS
CCCCCHHHHHCCCCC		12.6125561503
465PhosphorylationHIAPEYLSTGKSSEK
CCCHHHHHCCCCCCC		33.9219880383
466PhosphorylationIAPEYLSTGKSSEKT
CCHHHHHCCCCCCCC		46.1425561503
470PhosphorylationYLSTGKSSEKTDVFG
HHHCCCCCCCCCCCH		46.7424243849
546PhosphorylationIQVALLCTQSSPMER
HHHHHHHCCCCCCCC		31.30-
589PhosphorylationRQDFNYPTHHPAVSG
HHCCCCCCCCCCCCE		23.5819105183
595PhosphorylationPTHHPAVSGWIIGDS
CCCCCCCCEEECCCC		30.4324243849
602PhosphorylationSGWIIGDSTSQIENE
CEEECCCCHHHHCCC		25.4224243849
604PhosphorylationWIIGDSTSQIENEYP
EECCCCHHHHCCCCC		32.8619105183
610PhosphorylationTSQIENEYPSGPR--
HHHHCCCCCCCCC--		17.8020876109
612PhosphorylationQIENEYPSGPR----
HHCCCCCCCCC----		61.6012150929
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 BAK1_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
286SPhosphorylation

18694562
290SPhosphorylation

15894717
290SPhosphorylation

15894717
312TPhosphorylation

17302430
446TPhosphorylation

15894717
446TPhosphorylation

15894717
449TPhosphorylation

15894717
449TPhosphorylation

15894717
455TPhosphorylation

15894717
589TPhosphorylation

19105183
595SPhosphorylation

19105183
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 BAK1_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRI1_ARATHBRI1physical
12150929
P2C70_ARATHKAPPphysical
17302430
FLS2_ARATHFLS2physical
18621007
PEPR1_ARATHPEPR1physical
20018402
PEPR2_ARATHPEPR2physical
20018402
BON1_ARATHBON1physical
21623975
Y5838_ARATHBIR1physical
21623975
PUB13_ARATHPUB13physical
21680842
RM16L_ARATHPUB12physical
21680842
FLS2_ARATHFLS2physical
22427336
FLS2_ARATHFLS2physical
23637603
FLS2_ARATHFLS2physical
24114786
MSBP1_ARATHMSBP1physical
19532123
BRI1_ARATHBRI1physical
19532123
FLS2_ARATHFLS2physical
20103591
BAK1_ARATHBAK1physical
20876109
BRI1_ARATHBRI1physical
20876109
BRI1_ARATHBRI1physical
21350342
Y1719_ARATHAT1G27190physical
24388849
FLS2_ARATHFLS2physical
24388849
BAK1_ARATHBAK1physical
24550926
BRI1_ARATHBRI1physical
24550926
BSL2_ARATHBSL2physical
24924143
BIK1_ARATHBIK1physical
20018686
BAK1_ARATHBAK1physical
20018686
PUB13_ARATHPUB13physical
25873653
BAK1_ARATHBAK1physical
25873653
FLS2_ARATHFLS2physical
25944825
FLS2_ARATHFLS2genetic
25944825
EFR_ARATHEFRgenetic
25944825
EFR_ARATHEFRphysical
24443525
FLS2_ARATHFLS2physical
24443525
BRI1_ARATHBRI1physical
19277500
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BAK1_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: AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT SER-290; THR-446; THR-449;THR-450; THR-455; THR-589; SER-595; SER-604 AND SER-612.
"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-286; SER-290; THR-312; THR-446;THR-449; THR-450 AND THR-455, INTERACTION WITH BRI1, AND MUTAGENESISOF THR-455.
"Identification and functional analysis of in vivo phosphorylationsites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptorkinase.";
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.;
Plant Cell 17:1685-1703(2005).
Cited for: PHOSPHORYLATION AT SER-290; THR-446; THR-449 AND THR-455, ANDINTERACTION WITH BRI1.
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Plant Cell 16:2394-2405(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-449 AND THR-450, ANDMASS SPECTROMETRY.
"Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays arole in brassinosteroid signaling and basal defense gene expression.";
Oh M.H., Wang X., Wu X., Zhao Y., Clouse S.D., Huber S.C.;
Proc. Natl. Acad. Sci. U.S.A. 107:17827-17832(2010).
Cited for: MUTAGENESIS OF TYR-304; TYR-363; TYR-365; TYR-403; TYR-443; TYR-463;TYR-478; TYR-530; TYR-587 AND TYR-610, AUTOPHOSPHORYLATION, ANDPHOSPHORYLATION AT TYR-610.

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