| UniProt ID | PUP18_ARATH | |
|---|---|---|
| UniProt AC | Q9C508 | |
| Protein Name | Probable purine permease 18 | |
| Gene Name | PUP18 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 390 | |
| Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
| Protein Description | ||
| Protein Sequence | MEMTEASKQTTAEGSANPEPDQILSPRRSLELKQKKWWISVSLCIFLVLLGDSLVMLLLNFFYVQDNREDSDQDLQYRGTWLQALVQNAAFPLLIPLFFIFPSPKQNQETTNTRFLSFRLILLYISLGVLVAAHSKLFALGKLYANFGVFTLISATQLIFTAIFAAIINRFKFTRWIILSIIGSILIYVFGSPEFGGEPDENEEFYSIQAWLTFAASVAFALSLCLFQLCFEKVLVKTKRYGNKKVFRMVIEMQICVSFVATVVCLVGLFASGENKELQGDSHRFKKGETYYVLSLIGLALSWQVWAVGLMGLVLYVSGVFGDVVHMCTSPLVALFVVLAFDFMDDEFSWPRIGTLIATVVALGSYFYTLHKRNKKKMVELYQTENNIDV | |
| 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 |
|---|---|---|---|---|---|
| 10 | Phosphorylation | MTEASKQTTAEGSAN CCHHHCCCCCCCCCC | 31.54 | 23776212 | |
| 11 | Phosphorylation | TEASKQTTAEGSANP CHHHCCCCCCCCCCC | 21.88 | 23776212 | |
| 15 | Phosphorylation | KQTTAEGSANPEPDQ CCCCCCCCCCCCHHH | 19.17 | 23776212 | |
| 25 | Phosphorylation | PEPDQILSPRRSLEL CCHHHCCCCCCCHHH | 20.28 | 30291188 |
| 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 PUP18_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PUP18_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 PUP18_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| HHP4_ARATH | HHP4 | physical | 24833385 | |
| UBC34_ARATH | UBC34 | physical | 24833385 | |
| CLH1_ARATH | CLH1 | physical | 24833385 | |
| CNIH1_ARATH | AT3G12180 | physical | 24833385 | |
| WNK3_ARATH | WNK3 | physical | 24833385 | |
| CP21D_ARATH | AT3G66654 | physical | 24833385 | |
| SPCS1_ARATH | AT2G22425 | physical | 24833385 | |
| PAM74_ARATH | AT5G59650 | physical | 24833385 | |
| BETL2_ARATH | AT1G29060 | physical | 24833385 | |
| BET12_ARATH | ATBET12 | physical | 24833385 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-25, AND MASSSPECTROMETRY. | |
| "Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY. | |
| "Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis."; Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.; Mol. Cell. Proteomics 6:1711-1726(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY. | |
| "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identifyphosphorylation sites in secondary active transporters."; Hem S., Rofidal V., Sommerer N., Rossignol M.; Biochem. Biophys. Res. Commun. 363:375-380(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY. | |
| "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-25, AND MASSSPECTROMETRY. | |