UniProt ID | Y1164_ARATH | |
---|---|---|
UniProt AC | Q9LQ95 | |
Protein Name | BTB/POZ domain-containing protein At1g01640 | |
Gene Name | At1g01640 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 207 | |
Subcellular Localization | ||
Protein Description | May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.. | |
Protein Sequence | MTEAEQKAAFLGGLVVSFKEQMHTDVLVKPGEEAPPIPTHKAVLAARSKVFRNMLDSDECKTSPEESITLPDLSHDELKSLLEFLYSGNLKAPYNQYRSLYLAADKYDISYLQDVCRNHFIASLSSRNVLDILELASIPCDTILKDAAINHIVKHMEEVVVPMKYETFVQRNPDLSVEITRAYLRETKAKAKDHGAPLNGNTRPRIW | |
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 |
|
---|---|---|---|---|---|---|
Oops, there are no PTM records of Y1164_ARATH !! |
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 Y1164_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of Y1164_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 Y1164_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
UEV1D_ARATH | UEV1D-4 | physical | 21798944 | |
CUL1_ARATH | CUL1 | physical | 21798944 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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