UniProt ID | SINL4_ARATH | |
---|---|---|
UniProt AC | Q9C9M0 | |
Protein Name | E3 ubiquitin-protein ligase SINA-like 4 | |
Gene Name | At1g66650 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 329 | |
Subcellular Localization | ||
Protein Description | E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates.. | |
Protein Sequence | MTKLGRRNDGGGKSHRSSTKRQRRTSVSVDDPSPGEEEEKTLVVLTDDSDSEEDDKPLGDVLRTCRKRRVSSPKSVTLPNSNVLECPNCFDPLKKPIFQCNNGHLACFLCCIKLKKRCSFCKLPIGDVRCRAMEKVIKAGLVSCSNAIYGCKQSTTYGNQLQSHEKVCVFAPCSCPIKDCNYIGFYKDLINHFRATHKVSPGDINSFVFDRPVIFGLDLDSSDKMVIFVEEKQGNLFVVQGFIGSHGVYATVSHIAPMVPEVRKFSCSLARLRPYSTLRLGLEVKNIQKLRSQEEQPQEDFLLIPSYMVNGDHMKMEISIGDKNDYTHI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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 SINL4_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SINL4_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 SINL4_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CDF2_ARATH | CDF2 | physical | 24255109 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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