THE1_ARATH - dbPTM
THE1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THE1_ARATH
UniProt AC Q9LK35
Protein Name Receptor-like protein kinase THESEUS 1
Gene Name THE1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 855
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Receptor-like protein kinase required for cell elongation during vegetative growth, mostly in a brassinosteroid-(BR-) independent manner. Mediates the response of growing plant cells to the perturbation of cellulose synthesis and may act as a cell-wall-integrity sensor. Controls ectopic-lignin accumulation in cellulose-deficient mutant backgrounds..
Protein Sequence MVFTKSLLVLLWFLSCYTTTTSSALFNPPDNYLISCGSSQNITFQNRIFVPDSLHSSLVLKIGNSSVATSTTSNNSTNSIYQTARVFSSLASYRFKITSLGRHWIRLHFSPINNSTWNLTSASITVVTEDFVLLNNFSFNNFNGSYIFKEYTVNVTSEFLTLSFIPSNNSVVFVNAIEVVSVPDNLIPDQALALNPSTPFSGLSLLAFETVYRLNMGGPLLTSQNDTLGRQWDNDAEYLHVNSSVLVVTANPSSIKYSPSVTQETAPNMVYATADTMGDANVASPSFNVTWVLPVDPDFRYFVRVHFCDIVSQALNTLVFNLYVNDDLALGSLDLSTLTNGLKVPYFKDFISNGSVESSGVLTVSVGPDSQADITNATMNGLEVLKISNEAKSLSGVSSVKSLLPGGSGSKSKKKAVIIGSLVGAVTLILLIAVCCYCCLVASRKQRSTSPQEGGNGHPWLPLPLYGLSQTLTKSTASHKSATASCISLASTHLGRCFMFQEIMDATNKFDESSLLGVGGFGRVYKGTLEDGTKVAVKRGNPRSEQGMAEFRTEIEMLSKLRHRHLVSLIGYCDERSEMILVYEYMANGPLRSHLYGADLPPLSWKQRLEICIGAARGLHYLHTGASQSIIHRDVKTTNILLDENLVAKVADFGLSKTGPSLDQTHVSTAVKGSFGYLDPEYFRRQQLTEKSDVYSFGVVLMEVLCCRPALNPVLPREQVNIAEWAMAWQKKGLLDQIMDSNLTGKVNPASLKKFGETAEKCLAEYGVDRPSMGDVLWNLEYALQLEETSSALMEPDDNSTNHIPGIPMAPMEPFDNSMSIIDRGGVNSGTGTDDDAEDATTSAVFSQLVHPRGR
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
41N-linked_GlycosylationISCGSSQNITFQNRI
EECCCCCCEEECCCE
36.90-
64N-linked_GlycosylationSLVLKIGNSSVATST
EEEEEECCCCEEEEE
34.29-
75N-linked_GlycosylationATSTTSNNSTNSIYQ
EEEECCCCCCCCHHH
50.40-
114N-linked_GlycosylationLHFSPINNSTWNLTS
EEEECCCCCCCCCCE
41.35-
118N-linked_GlycosylationPINNSTWNLTSASIT
CCCCCCCCCCEEEEE
33.26-
123PhosphorylationTWNLTSASITVVTED
CCCCCEEEEEEEECC
20.6828011693
125PhosphorylationNLTSASITVVTEDFV
CCCEEEEEEEECCEE
13.3628011693
136N-linked_GlycosylationEDFVLLNNFSFNNFN
CCEEEEECEEEECCC
33.63-
143N-linked_GlycosylationNFSFNNFNGSYIFKE
CEEEECCCCCEEEEE
40.39-
154N-linked_GlycosylationIFKEYTVNVTSEFLT
EEEEEEEEEECCEEE
24.45-
168N-linked_GlycosylationTLSFIPSNNSVVFVN
EEEECCCCCEEEEEE
39.17-
225N-linked_GlycosylationGPLLTSQNDTLGRQW
CCCCCCCCCCCCCCC
43.96-
242N-linked_GlycosylationDAEYLHVNSSVLVVT
CCCEEEECCEEEEEE
20.16-
288N-linked_GlycosylationNVASPSFNVTWVLPV
CCCCCCCEEEEEEEC
34.35-
353N-linked_GlycosylationYFKDFISNGSVESSG
CCHHHHCCCCCCCCC
41.78-
376N-linked_GlycosylationDSQADITNATMNGLE
CCHHHHCCCCCCCEE
33.47-
398PhosphorylationAKSLSGVSSVKSLLP
CCCCCCCCHHHHCCC
32.7024894044
399PhosphorylationKSLSGVSSVKSLLPG
CCCCCCCHHHHCCCC
31.0324894044
469PhosphorylationPLPLYGLSQTLTKST
CCCCCCCCCCCCCCC
19.4317317660
483PhosphorylationTASHKSATASCISLA
CCCCHHHHHHHHHHH
26.6225561503
485PhosphorylationSHKSATASCISLAST
CCHHHHHHHHHHHHH
13.9725561503
488PhosphorylationSATASCISLASTHLG
HHHHHHHHHHHHHHH
23.3917317660
658PhosphorylationADFGLSKTGPSLDQT
HHHCCCCCCCCCCCC
51.4525561503
661PhosphorylationGLSKTGPSLDQTHVS
CCCCCCCCCCCCCHH
46.0225561503
665PhosphorylationTGPSLDQTHVSTAVK
CCCCCCCCCHHHHHC
24.7430407730
668PhosphorylationSLDQTHVSTAVKGSF
CCCCCCHHHHHCCCC
11.7530291188
669PhosphorylationLDQTHVSTAVKGSFG
CCCCCHHHHHCCCCC
34.0923111157
674PhosphorylationVSTAVKGSFGYLDPE
HHHHHCCCCCCCCHH
15.1315308754
677PhosphorylationAVKGSFGYLDPEYFR
HHCCCCCCCCHHHHH
13.1130407730
829PhosphorylationIDRGGVNSGTGTDDD
CCCCCCCCCCCCCCC
35.0117317660
831PhosphorylationRGGVNSGTGTDDDAE
CCCCCCCCCCCCCHH
36.4115308754
833PhosphorylationGVNSGTGTDDDAEDA
CCCCCCCCCCCHHHH
35.7715308754
841PhosphorylationDDDAEDATTSAVFSQ
CCCHHHHHHHHHHHH
33.3415308754
842PhosphorylationDDAEDATTSAVFSQL
CCHHHHHHHHHHHHH
19.1915308754

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 THE1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THE1_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 THE1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of THE1_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THE1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis.";
Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.;
Mol. Cell. Proteomics 6:1198-1214(2007).
Cited for: PHOSPHORYLATION AT SER-469; SER-488; SER-668; SER-829 AND THR-833,IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], ANDSUBCELLULAR LOCATION.
"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 SER-829; THR-831 ANDTHR-833, AND MASS SPECTROMETRY.
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829; THR-831; THR-833;THR-841 AND THR-842, AND MASS SPECTROMETRY.

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