| UniProt ID | ADF1_ARATH | |
|---|---|---|
| UniProt AC | Q39250 | |
| Protein Name | Actin-depolymerizing factor 1 | |
| Gene Name | ADF1 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 139 | |
| Subcellular Localization | Cytoplasm, cytoskeleton . | |
| Protein Description | Actin-depolymerizing protein. Stimulates F-actin depolymerization. Involved in plant development, cell organ expansion and flowering by controlling breakdown of thick actin cables. [PubMed: 11402164 Severs actin filaments or bundles and promotes actin cytoskeleton disassembly] | |
| Protein Sequence | MANAASGMAVHDDCKLRFLELKAKRTHRFIVYKIEEKQKQVVVEKVGQPIQTYEEFAACLPADECRYAIYDFDFVTAENCQKSKIFFIAWCPDIAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVFRSRAN | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MANAASGMAVHDD --CCCCCCCCCCCCC | 27.04 | 14593172 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 6 | S | Phosphorylation | Kinase | CPK3 | Q42479 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 6 | S | Phosphorylation |
| 23903947 |
* 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 ADF1_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ADF1_ARATH !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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