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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
41 | N-linked_Glycosylation | ISCGSSQNITFQNRI EECCCCCCEEECCCE | 36.90 | - | |
64 | N-linked_Glycosylation | SLVLKIGNSSVATST EEEEEECCCCEEEEE | 34.29 | - | |
75 | N-linked_Glycosylation | ATSTTSNNSTNSIYQ EEEECCCCCCCCHHH | 50.40 | - | |
114 | N-linked_Glycosylation | LHFSPINNSTWNLTS EEEECCCCCCCCCCE | 41.35 | - | |
118 | N-linked_Glycosylation | PINNSTWNLTSASIT CCCCCCCCCCEEEEE | 33.26 | - | |
123 | Phosphorylation | TWNLTSASITVVTED CCCCCEEEEEEEECC | 20.68 | 28011693 | |
125 | Phosphorylation | NLTSASITVVTEDFV CCCEEEEEEEECCEE | 13.36 | 28011693 | |
136 | N-linked_Glycosylation | EDFVLLNNFSFNNFN CCEEEEECEEEECCC | 33.63 | - | |
143 | N-linked_Glycosylation | NFSFNNFNGSYIFKE CEEEECCCCCEEEEE | 40.39 | - | |
154 | N-linked_Glycosylation | IFKEYTVNVTSEFLT EEEEEEEEEECCEEE | 24.45 | - | |
168 | N-linked_Glycosylation | TLSFIPSNNSVVFVN EEEECCCCCEEEEEE | 39.17 | - | |
225 | N-linked_Glycosylation | GPLLTSQNDTLGRQW CCCCCCCCCCCCCCC | 43.96 | - | |
242 | N-linked_Glycosylation | DAEYLHVNSSVLVVT CCCEEEECCEEEEEE | 20.16 | - | |
288 | N-linked_Glycosylation | NVASPSFNVTWVLPV CCCCCCCEEEEEEEC | 34.35 | - | |
353 | N-linked_Glycosylation | YFKDFISNGSVESSG CCHHHHCCCCCCCCC | 41.78 | - | |
376 | N-linked_Glycosylation | DSQADITNATMNGLE CCHHHHCCCCCCCEE | 33.47 | - | |
398 | Phosphorylation | AKSLSGVSSVKSLLP CCCCCCCCHHHHCCC | 32.70 | 24894044 | |
399 | Phosphorylation | KSLSGVSSVKSLLPG CCCCCCCHHHHCCCC | 31.03 | 24894044 | |
469 | Phosphorylation | PLPLYGLSQTLTKST CCCCCCCCCCCCCCC | 19.43 | 17317660 | |
483 | Phosphorylation | TASHKSATASCISLA CCCCHHHHHHHHHHH | 26.62 | 25561503 | |
485 | Phosphorylation | SHKSATASCISLAST CCHHHHHHHHHHHHH | 13.97 | 25561503 | |
488 | Phosphorylation | SATASCISLASTHLG HHHHHHHHHHHHHHH | 23.39 | 17317660 | |
658 | Phosphorylation | ADFGLSKTGPSLDQT HHHCCCCCCCCCCCC | 51.45 | 25561503 | |
661 | Phosphorylation | GLSKTGPSLDQTHVS CCCCCCCCCCCCCHH | 46.02 | 25561503 | |
665 | Phosphorylation | TGPSLDQTHVSTAVK CCCCCCCCCHHHHHC | 24.74 | 30407730 | |
668 | Phosphorylation | SLDQTHVSTAVKGSF CCCCCCHHHHHCCCC | 11.75 | 30291188 | |
669 | Phosphorylation | LDQTHVSTAVKGSFG CCCCCHHHHHCCCCC | 34.09 | 23111157 | |
674 | Phosphorylation | VSTAVKGSFGYLDPE HHHHHCCCCCCCCHH | 15.13 | 15308754 | |
677 | Phosphorylation | AVKGSFGYLDPEYFR HHCCCCCCCCHHHHH | 13.11 | 30407730 | |
829 | Phosphorylation | IDRGGVNSGTGTDDD CCCCCCCCCCCCCCC | 35.01 | 17317660 | |
831 | Phosphorylation | RGGVNSGTGTDDDAE CCCCCCCCCCCCCHH | 36.41 | 15308754 | |
833 | Phosphorylation | GVNSGTGTDDDAEDA CCCCCCCCCCCHHHH | 35.77 | 15308754 | |
841 | Phosphorylation | DDDAEDATTSAVFSQ CCCHHHHHHHHHHHH | 33.34 | 15308754 | |
842 | Phosphorylation | DDAEDATTSAVFSQL CCHHHHHHHHHHHHH | 19.19 | 15308754 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of THE1_ARATH !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of THE1_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |