| UniProt ID | SD18_ARATH | |
|---|---|---|
| UniProt AC | O81905 | |
| Protein Name | Receptor-like serine/threonine-protein kinase SD1-8 | |
| Gene Name | SD18 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 850 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein . |
|
| Protein Description | Involved in the regulation of cellular expansion and differentiation.. | |
| Protein Sequence | MRGLPNFYHSYTFFFFFLLILFPAYSISANTLSASESLTISSNNTIVSPGNVFELGFFKPGLDSRWYLGIWYKAISKRTYVWVANRDTPLSSSIGTLKISDSNLVVLDQSDTPVWSTNLTGGDVRSPLVAELLDNGNFVLRDSKNSAPDGVLWQSFDFPTDTLLPEMKLGWDAKTGFNRFIRSWKSPDDPSSGDFSFKLETEGFPEIFLWNRESRMYRSGPWNGIRFSGVPEMQPFEYMVFNFTTSKEEVTYSFRITKSDVYSRLSISSSGLLQRFTWIETAQNWNQFWYAPKDQCDEYKECGVYGYCDSNTSPVCNCIKGFKPRNPQVWGLRDGSDGCVRKTLLSCGGGDGFVRLKKMKLPDTTTASVDRGIGVKECEQKCLRDCNCTAFANTDIRGSGSGCVTWTGELFDIRNYAKGGQDLYVRLAATDLEDKRNRSAKIIGSSIGVSVLLLLSFIIFFLWKRKQKRSILIETPIVDHQLRSRDLLMNEVVISSRRHISRENNTDDLELPLMEFEEVAMATNNFSNANKLGQGGFGIVYKGKLLDGQEMAVKRLSKTSVQGTDEFKNEVKLIARLQHINLVRLLACCVDAGEKMLIYEYLENLSLDSHLFDKSRNSKLNWQMRFDIINGIARGLLYLHQDSRFRIIHRDLKASNILLDKYMTPKISDFGMARIFGRDETEANTRKVVGTYGYMSPEYAMDGIFSMKSDVFSFGVLLLEIISSKRNKGFYNSDRDLNLLGCVWRNWKEGKGLEIIDPIITDSSSTFRQHEILRCIQIGLLCVQERAEDRPTMSLVILMLGSESTTIPQPKAPGYCLERSLLDTDSSSSKQRDDESWTVNQITVSVLDAR | |
| 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 |
|---|---|---|---|---|---|
| 43 | N-linked_Glycosylation | ESLTISSNNTIVSPG CCEEECCCCEEECCC | 42.76 | - | |
| 118 | N-linked_Glycosylation | DTPVWSTNLTGGDVR CCCCEEECCCCCCCC | 30.04 | - | |
| 196 | Phosphorylation | DPSSGDFSFKLETEG CCCCCCCEEEEEECC | 26.64 | 23572148 | |
| 242 | N-linked_Glycosylation | PFEYMVFNFTTSKEE CEEEEEEEECCCCCE | 23.19 | - | |
| 387 | N-linked_Glycosylation | QKCLRDCNCTAFANT HHHHHHCCCCEEECC | 30.39 | - | |
| 437 | N-linked_Glycosylation | TDLEDKRNRSAKIIG CCCHHHHCHHHHHHH | 48.26 | - | |
| 495 | Phosphorylation | LMNEVVISSRRHISR HHHHHHHHCCCCCCC | 13.24 | 15308754 | |
| 496 | Phosphorylation | MNEVVISSRRHISRE HHHHHHHCCCCCCCC | 23.39 | 15308754 | |
| 681 | Phosphorylation | RIFGRDETEANTRKV CHHCCCCCHHHHCEE | 44.69 | 25561503 | |
| 685 | Phosphorylation | RDETEANTRKVVGTY CCCCHHHHCEEEEEE | 38.63 | 25561503 | |
| 827 | Phosphorylation | SLLDTDSSSSKQRDD HCCCCCCCCCCCCCC | 41.25 | 25561503 |
| 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 SD18_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SD18_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 SD18_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PUB38_ARATH | PUB38 | physical | 18552232 | |
| PUB9_ARATH | PUB9 | physical | 18552232 | |
| PUB14_ARATH | PUB14 | physical | 18552232 | |
| PUB13_ARATH | PUB13 | physical | 18552232 | |
| PUB45_ARATH | PUB45 | physical | 18552232 | |
| PUB29_ARATH | PUB29 | physical | 18552232 | |
| PUB44_ARATH | SAUL1 | physical | 18552232 | |
| CNG13_ARATH | CNGC13 | physical | 22737156 | |
| GCL1_ARATH | GCL1 | physical | 22737156 | |
| PUP3_ARATH | PUP3 | physical | 22737156 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-496, SUBCELLULARLOCATION, AND MASS SPECTROMETRY. | |