| UniProt ID | CML27_ARATH | |
|---|---|---|
| UniProt AC | Q9LE22 | |
| Protein Name | Probable calcium-binding protein CML27 | |
| Gene Name | CML27 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 170 | |
| Subcellular Localization | ||
| Protein Description | Potential calcium sensor.. | |
| Protein Sequence | MASANPETAKPTPATVDMANPEELKKVFDQFDSNGDGKISVLELGGVFKAMGTSYTETELNRVLEEVDTDRDGYINLDEFSTLCRSSSSAAEIRDAFDLYDQDKNGLISASELHQVLNRLGMSCSVEDCTRMIGPVDADGDGNVNFEEFQKMMTSSSLLNSNGSAAPPST | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MASANPETA ------CCCCCCCCC | 19.83 | 22223895 | |
| 3 | Phosphorylation | -----MASANPETAK -----CCCCCCCCCC | 27.55 | 23111157 | |
| 12 | Phosphorylation | NPETAKPTPATVDMA CCCCCCCCCCCCCCC | 25.50 | 24894044 | |
| 53 | Phosphorylation | GVFKAMGTSYTETEL HHHHHCCCCCCHHHH | 12.89 | 23776212 | |
| 54 | Phosphorylation | VFKAMGTSYTETELN HHHHCCCCCCHHHHH | 25.07 | 30291188 | |
| 55 | Phosphorylation | FKAMGTSYTETELNR HHHCCCCCCHHHHHH | 14.40 | 23776212 | |
| 56 | Phosphorylation | KAMGTSYTETELNRV HHCCCCCCHHHHHHH | 35.88 | 23776212 | |
| 58 | Phosphorylation | MGTSYTETELNRVLE CCCCCCHHHHHHHHH | 37.66 | 23776212 | |
| 86 | Phosphorylation | EFSTLCRSSSSAAEI HHHHHHCCCCCHHHH | 33.31 | 23776212 | |
| 87 | Phosphorylation | FSTLCRSSSSAAEIR HHHHHCCCCCHHHHH | 14.68 | 23776212 | |
| 88 | Phosphorylation | STLCRSSSSAAEIRD HHHHCCCCCHHHHHH | 25.83 | 23776212 | |
| 89 | Phosphorylation | TLCRSSSSAAEIRDA HHHCCCCCHHHHHHH | 33.18 | 23776212 | |
| 125 | Phosphorylation | NRLGMSCSVEDCTRM HHHCCCCCHHHHCHH | 22.64 | 23572148 | |
| 132 | Sulfoxidation | SVEDCTRMIGPVDAD CHHHHCHHCCCCCCC | 1.93 | 23289948 |
| 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 CML27_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CML27_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 CML27_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CML27_ARATH !! | ||||
| 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-88, 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-54, AND MASSSPECTROMETRY. | |