| UniProt ID | RLK5_ARATH | |
|---|---|---|
| UniProt AC | P47735 | |
| Protein Name | Receptor-like protein kinase 5 | |
| Gene Name | RLK5 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 999 | |
| Subcellular Localization |
Cell 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 that controls floral organ abscission. May interact with the 'INFLORESCENCE DEFICIENT IN ABSCISSION' (IDA) ligands family.. | |
| Protein Sequence | MLYCLILLLCLSSTYLPSLSLNQDATILRQAKLGLSDPAQSLSSWSDNNDVTPCKWLGVSCDATSNVVSVDLSSFMLVGPFPSILCHLPSLHSLSLYNNSINGSLSADDFDTCHNLISLDLSENLLVGSIPKSLPFNLPNLKFLEISGNNLSDTIPSSFGEFRKLESLNLAGNFLSGTIPASLGNVTTLKELKLAYNLFSPSQIPSQLGNLTELQVLWLAGCNLVGPIPPSLSRLTSLVNLDLTFNQLTGSIPSWITQLKTVEQIELFNNSFSGELPESMGNMTTLKRFDASMNKLTGKIPDNLNLLNLESLNLFENMLEGPLPESITRSKTLSELKLFNNRLTGVLPSQLGANSPLQYVDLSYNRFSGEIPANVCGEGKLEYLILIDNSFSGEISNNLGKCKSLTRVRLSNNKLSGQIPHGFWGLPRLSLLELSDNSFTGSIPKTIIGAKNLSNLRISKNRFSGSIPNEIGSLNGIIEISGAENDFSGEIPESLVKLKQLSRLDLSKNQLSGEIPRELRGWKNLNELNLANNHLSGEIPKEVGILPVLNYLDLSSNQFSGEIPLELQNLKLNVLNLSYNHLSGKIPPLYANKIYAHDFIGNPGLCVDLDGLCRKITRSKNIGYVWILLTIFLLAGLVFVVGIVMFIAKCRKLRALKSSTLAASKWRSFHKLHFSEHEIADCLDEKNVIGFGSSGKVYKVELRGGEVVAVKKLNKSVKGGDDEYSSDSLNRDVFAAEVETLGTIRHKSIVRLWCCCSSGDCKLLVYEYMPNGSLADVLHGDRKGGVVLGWPERLRIALDAAEGLSYLHHDCVPPIVHRDVKSSNILLDSDYGAKVADFGIAKVGQMSGSKTPEAMSGIAGSCGYIAPEYVYTLRVNEKSDIYSFGVVLLELVTGKQPTDSELGDKDMAKWVCTALDKCGLEPVIDPKLDLKFKEEISKVIHIGLLCTSPLPLNRPSMRKVVIMLQEVSGAVPCSSPNTSKRSKTGGKLSPYYTEDLNSV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 98 | N-linked_Glycosylation | LHSLSLYNNSINGSL CCHHCCCCCCCCCCC | 40.86 | 27058169 | |
| 102 | N-linked_Glycosylation | SLYNNSINGSLSADD CCCCCCCCCCCCCCC | 33.55 | 27058169 | |
| 150 | N-linked_Glycosylation | FLEISGNNLSDTIPS EEEEECCCHHHCCCC | 44.43 | 27058169 | |
| 185 | N-linked_Glycosylation | TIPASLGNVTTLKEL CCCCCCCCCCCHHHH | 33.00 | 27058169 | |
| 210 | N-linked_Glycosylation | QIPSQLGNLTELQVL HCCHHHCCCCHHHHH | 53.00 | - | |
| 269 | N-linked_Glycosylation | VEQIELFNNSFSGEL HHHHHHHCCCCCCCC | 56.72 | 27058169 | |
| 282 | N-linked_Glycosylation | ELPESMGNMTTLKRF CCCHHHCCCHHHHHH | 18.91 | 27058169 | |
| 452 | N-linked_Glycosylation | KTIIGAKNLSNLRIS CEEECCCCCCCCEEC | 48.44 | - | |
| 576 | N-linked_Glycosylation | NLKLNVLNLSYNHLS HCEEEEEEECHHHCC | 23.74 | 27058169 | |
| 766 | Phosphorylation | GDCKLLVYEYMPNGS CCEEEEEEEECCCCC | 11.00 | - | |
| 806 | Phosphorylation | DAAEGLSYLHHDCVP HHHHCHHHHCCCCCC | 18.33 | - | |
| 856 | Phosphorylation | SKTPEAMSGIAGSCG CCCHHHHHCCCCCCC | 33.81 | - | |
| 864 | Phosphorylation | GIAGSCGYIAPEYVY CCCCCCCEECCEEEE | 9.76 | - | |
| 871 | Phosphorylation | YIAPEYVYTLRVNEK EECCEEEEEEEECCC | 10.11 | - | |
| 872 | Phosphorylation | IAPEYVYTLRVNEKS ECCEEEEEEEECCCC | 9.69 | - |
| 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 RLK5_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RLK5_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 RLK5_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CNG10_ARATH | CNGC10 | physical | 22737156 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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