| UniProt ID | AKRCA_ARATH | |
|---|---|---|
| UniProt AC | Q84TF0 | |
| Protein Name | Aldo-keto reductase family 4 member C10 | |
| Gene Name | AKR4C10 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 314 | |
| Subcellular Localization | ||
| Protein Description | Oxidoreductase that may act on a broad range of substrates such as ketosteroids, aldehydes, ketones and sugars.. | |
| Protein Sequence | MAEEIRFFELNTGAKIPSVGLGTWQADPGLVGNAVDAAVKIGYRHIDCAQIYGNEKEIGLVLKKLFDGGVVKREEMFITSKLWCTYHDPQEVPEALNRTLQDLQLDYVDLYLIHWPVSLKKGSTGFKPENILPTDIPSTWKAMESLFDSGKARAIGVSNFSSKKLADLLVVARVPPAVNQVECHPSWQQNVLRDFCKSKGVHLSGYSPLGSPGTTWLTSDVLKNPILGGVAEKLGKTPAQVALRWGLQMGQSVLPKSTHEDRIKQNFDVFNWSIPEDMLSKFSEIGQGRLVRGMSFVHETSPYKSLEELWDGEI | |
| 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 | ------MAEEIRFFE ------CCCEEEEEE | 24.11 | - | |
| 145 | Phosphorylation | STWKAMESLFDSGKA HHHHHHHHHHHHCCE | 22.66 | 24894044 | |
| 149 | Phosphorylation | AMESLFDSGKARAIG HHHHHHHHCCEEEEE | 34.55 | 24894044 | |
| 295 | Phosphorylation | GRLVRGMSFVHETSP CCCCCCCEEEECCCC | 27.26 | 30291188 | |
| 300 | Phosphorylation | GMSFVHETSPYKSLE CCEEEECCCCCCCHH | 21.81 | 23776212 | |
| 301 | Phosphorylation | MSFVHETSPYKSLEE CEEEECCCCCCCHHH | 24.21 | 23776212 | |
| 303 | Phosphorylation | FVHETSPYKSLEELW EEECCCCCCCHHHHH | 16.99 | 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 AKRCA_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AKRCA_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 AKRCA_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of AKRCA_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-295, AND MASSSPECTROMETRY. | |
| "Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASSSPECTROMETRY. | |