| UniProt ID | C3H33_ARATH | |
|---|---|---|
| UniProt AC | Q8GXX7 | |
| Protein Name | Zinc finger CCCH domain-containing protein 33 | |
| Gene Name | ZFN1 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 397 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | ||
| Protein Sequence | MDFNAGVPMSSLSPLMNQDAMWQMNLSSDETMETGSYPERPGEPDCSYYIRTGLCRFGSTCRFNHPRDRELVIATARMRGEYPERIGQPECEYYLKTGTCKFGVTCKFHHPRNKAGIAGRVSLNMLGYPLRSNEVDCAYFLRTGHCKFGGTCKFNHPQPQPTNMMVPTSGQQSYPWSRASFIASPRWQDPSSYASLIMPQGVVPVQGWNPYSGQLGSVSPSGTGNDQNYRNLQQNETIESGSQSQGSFSGYNPGSSVPLGGYYALPRENVFPERPGQPECQFYMKTGDCKFGTVCKFHHPRDRQAPPPDCLLSSIGLPLRPGEPLCVFYTRYGICKFGPSCKFDHPMRVFTYDNTASETDEVVETSTGKSRRLSVSETRQAATTSSGKDTTIDNTQQ | |
| 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 |
|---|---|---|---|---|---|
| 180 | Phosphorylation | SYPWSRASFIASPRW CCCCCCCCEEECCCC | 18.97 | 27545962 | |
| 184 | Phosphorylation | SRASFIASPRWQDPS CCCCEEECCCCCCHH | 15.35 | 30291188 | |
| 219 | Phosphorylation | SGQLGSVSPSGTGND CCCCCCCCCCCCCCC | 18.29 | 29654922 | |
| 221 | Phosphorylation | QLGSVSPSGTGNDQN CCCCCCCCCCCCCHH | 41.29 | 29654922 | |
| 223 | Phosphorylation | GSVSPSGTGNDQNYR CCCCCCCCCCCHHCC | 36.83 | 29654922 | |
| 313 | Phosphorylation | PPPDCLLSSIGLPLR CCCCCEEECCCCCCC | 13.63 | 25368622 | |
| 314 | Phosphorylation | PPDCLLSSIGLPLRP CCCCEEECCCCCCCC | 22.20 | 25368622 | |
| 329 | Phosphorylation | GEPLCVFYTRYGICK CCCEEEEEECCCCCC | 3.07 | 25368622 | |
| 330 | Phosphorylation | EPLCVFYTRYGICKF CCEEEEEECCCCCCC | 13.12 | 25368622 | |
| 332 | Phosphorylation | LCVFYTRYGICKFGP EEEEEECCCCCCCCC | 11.75 | 25368622 | |
| 351 | Phosphorylation | DHPMRVFTYDNTASE CCCEEEEEECCCCCC | 27.40 | 23776212 | |
| 352 | Phosphorylation | HPMRVFTYDNTASET CCEEEEEECCCCCCC | 8.84 | 23776212 | |
| 355 | Phosphorylation | RVFTYDNTASETDEV EEEEECCCCCCCCCE | 28.76 | 23776212 | |
| 357 | Phosphorylation | FTYDNTASETDEVVE EEECCCCCCCCCEEE | 38.70 | 30291188 | |
| 359 | Phosphorylation | YDNTASETDEVVETS ECCCCCCCCCEEECC | 34.66 | 27532006 | |
| 365 | Phosphorylation | ETDEVVETSTGKSRR CCCCEEECCCCCCCE | 21.70 | 23776212 | |
| 366 | Phosphorylation | TDEVVETSTGKSRRL CCCEEECCCCCCCEE | 22.96 | 23776212 | |
| 367 | Phosphorylation | DEVVETSTGKSRRLS CCEEECCCCCCCEEC | 56.92 | 23776212 | |
| 374 | Phosphorylation | TGKSRRLSVSETRQA CCCCCEECHHHHEHH | 23.06 | 19376835 | |
| 376 | Phosphorylation | KSRRLSVSETRQAAT CCCEECHHHHEHHHC | 29.85 | 19376835 | |
| 378 | Phosphorylation | RRLSVSETRQAATTS CEECHHHHEHHHCCC | 22.15 | 19376835 |
| 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 C3H33_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of C3H33_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 C3H33_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of C3H33_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-184; SER-374 ANDSER-376, AND MASS SPECTROMETRY. | |