BZR2_ARATH - dbPTM
BZR2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BZR2_ARATH
UniProt AC Q9LN63
Protein Name Protein BRASSINAZOLE-RESISTANT 2 {ECO:0000303|PubMed:11970900}
Gene Name BZR2 {ECO:0000303|PubMed:11970900}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 335
Subcellular Localization Nucleus . Cytoplasm . Brassinosteroid treatment triggers nuclear accumulation.
Protein Description Positive regulator of brassinosteroid (BR) signaling. Transcription factor that activates target gene expression by binding specifically to the DNA sequence 5'-CANNTG-3'(E box) through its N-terminal domain. Can bind individually to the promoter as a homodimer or synergistically as a heterodimer with BIM1, BIM2 or BIM3. The C-terminal domain is probably involved in transcriptional activation. [PubMed: 12007405]
Protein Sequence MTSDGATSTSAAAAAAAMATRRKPSWRERENNRRRERRRRAVAAKIYTGLRAQGNYNLPKHCDNNEVLKALCSEAGWVVEEDGTTYRKGHKPLPGDMAGSSSRATPYSSHNQSPLSSTFDSPILSYQVSPSSSSFPSPSRVGDPHNISTIFPFLRNGGIPSSLPPLRISNSAPVTPPVSSPTSRNPKPLPTWESFTKQSMSMAAKQSMTSLNYPFYAVSAPASPTHHRQFHAPATIPECDESDSSTVDSGHWISFQKFAQQQPFSASMVPTSPTFNLVKPAPQQLSPNTAAIQEIGQSSEFKFENSQVKPWEGERIHDVAMEDLELTLGNGKAHS
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
2Phosphorylation------MTSDGATST
------CCCCCCHHH
35.2119376835
3Phosphorylation-----MTSDGATSTS
-----CCCCCCHHHH
32.5219376835
7Phosphorylation-MTSDGATSTSAAAA
-CCCCCCHHHHHHHH
37.7619376835
8PhosphorylationMTSDGATSTSAAAAA
CCCCCCHHHHHHHHH
21.6019376835
9PhosphorylationTSDGATSTSAAAAAA
CCCCCHHHHHHHHHH
20.3119376835
10PhosphorylationSDGATSTSAAAAAAA
CCCCHHHHHHHHHHH
18.7125561503
100PhosphorylationLPGDMAGSSSRATPY
CCCCCCCCCCCCCCC
18.6625561503
129PhosphorylationPILSYQVSPSSSSFP
CEEEEEECCCCCCCC
11.9829654922
137PhosphorylationPSSSSFPSPSRVGDP
CCCCCCCCCCCCCCC
33.2329654922
169PhosphorylationSLPPLRISNSAPVTP
CCCCCEECCCCCCCC
20.4930291188
171PhosphorylationPPLRISNSAPVTPPV
CCCEECCCCCCCCCC
27.4530291188
175PhosphorylationISNSAPVTPPVSSPT
ECCCCCCCCCCCCCC
22.3323776212
179PhosphorylationAPVTPPVSSPTSRNP
CCCCCCCCCCCCCCC
36.0523776212
180PhosphorylationPVTPPVSSPTSRNPK
CCCCCCCCCCCCCCC
32.2223776212
182PhosphorylationTPPVSSPTSRNPKPL
CCCCCCCCCCCCCCC
42.1223776212
183PhosphorylationPPVSSPTSRNPKPLP
CCCCCCCCCCCCCCC
33.1830291188
207PhosphorylationMSMAAKQSMTSLNYP
HHHHHHHHCHHCCCC
24.2623776212
209PhosphorylationMAAKQSMTSLNYPFY
HHHHHHCHHCCCCEE
35.0023776212
210PhosphorylationAAKQSMTSLNYPFYA
HHHHHCHHCCCCEEE
13.1323776212
213PhosphorylationQSMTSLNYPFYAVSA
HHCHHCCCCEEEEEC
10.4623776212
216PhosphorylationTSLNYPFYAVSAPAS
HHCCCCEEEEECCCC
11.1123776212
219PhosphorylationNYPFYAVSAPASPTH
CCCEEEEECCCCCCC
21.9923776212
223PhosphorylationYAVSAPASPTHHRQF
EEEECCCCCCCCCCC
29.3123776212
225PhosphorylationVSAPASPTHHRQFHA
EECCCCCCCCCCCCC
28.0223776212

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 BZR2_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BZR2_ARATH !!

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 BZR2_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BZR1_ARATHBZR1physical
12427989
HAT1_ARATHHAT1physical
24164091
HS902_ARATHHSP81-2physical
24374469
HS901_ARATHHSP90.1physical
23410833
MAX2_ARATHMAX2physical
24369836
ELF6_ARATHELF6physical
18467490
REF6_ARATHREF6physical
18467490

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BZR2_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASSSPECTROMETRY.

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