UniProt ID | CASP_ARATH | |
---|---|---|
UniProt AC | Q9LS42 | |
Protein Name | Protein CASP | |
Gene Name | CASP | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 689 | |
Subcellular Localization |
Golgi apparatus membrane Single-pass type IV membrane protein . |
|
Protein Description | May be involved in intra-Golgi transport.. | |
Protein Sequence | MEVSQDGSERDKTPPPSSSSSSSSPIPVVTNFWKEFDLEKEKSLLDEQGLRIAENQENSQKNRRKLAESTRDFKKASPENKLSMFNSLLKGYQEEVDNITKRAKFGENAFLNIYQKLYEAPDPFPALASIAEQDRKLSEVESENRKMKVELEEFRTEATHLKNQQATIRRLEERNRQLEQQMEEKIKEVVEIKQRNLAEENQKTMELLKDREQALQDQLRQAKDSVSTMQKLHELAQNQLFELRAQSDEETAGKQSEVSLLMDEVERAQTRLLTLEREKGHLRSQLQTANEDTDNKKSDNIDSNSMLENSLTAKEKIISELNMEIHNVETALANERESHVAEIKKLNSLLNKKDTIIEEMKKELQERPSAKLVDDLRKKVKILQAVGYNSIEAEDWDAATTGEEMSKMESLLLDKNRKMEHEVTQLKVQLSEKASLLEKAEAKGEELTAKVNEQQRLIQKLEDDILKGYGSKERKGALFDEWEFSEAGVAEQSEPMDQKHVPSEQDQSSMLKVICSQRDRFRARLRETEEEIRRLKEKIGFLTDELEKTKADNVKLYGKIRYVQDYNHDKVVSRGSKKYVEDLESGFSSDVESKYKKIYEDDINPFAAFSKKEREQRIKDLGIRDRITLSSGRFLLGNKYARTFAFFYTIGLHVLVFTCLYRMSAYSYLSHGAEETLMTEATTNLPHGL | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MEVSQDGS -------CCCCCCCC | 11.79 | 22223895 | |
247 | Phosphorylation | LFELRAQSDEETAGK HHHHHHCCCHHHCCH | 46.10 | 25561503 | |
579 | Phosphorylation | VSRGSKKYVEDLESG EECCCHHHHHHHHHC | 16.89 | 19376835 | |
585 | Phosphorylation | KYVEDLESGFSSDVE HHHHHHHHCCCCHHH | 53.05 | 23776212 | |
588 | Phosphorylation | EDLESGFSSDVESKY HHHHHCCCCHHHHHH | 29.20 | 23776212 | |
589 | Phosphorylation | DLESGFSSDVESKYK HHHHCCCCHHHHHHH | 43.33 | 30291188 | |
593 | Phosphorylation | GFSSDVESKYKKIYE CCCCHHHHHHHHHHH | 40.93 | 23776212 |
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 CASP_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CASP_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 CASP_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
STP1_ARATH | STP1 | physical | 24833385 | |
CNIH1_ARATH | AT3G12180 | physical | 24833385 | |
PPA3_ARATH | PAP3 | physical | 24833385 | |
RAA5A_ARATH | RABA5a | physical | 24833385 | |
WAK3_ARATH | WAK3 | physical | 24833385 | |
BETL2_ARATH | AT1G29060 | physical | 24833385 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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-589, 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-589, AND MASSSPECTROMETRY. |