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 | ||
* 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. |