| UniProt ID | DUS1_RAT | |
|---|---|---|
| UniProt AC | Q64623 | |
| Protein Name | Dual specificity protein phosphatase 1 {ECO:0000305} | |
| Gene Name | Dusp1 {ECO:0000312|RGD:620897} | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 367 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle.. | |
| Protein Sequence | MVMEVGILDAGGLRALLRERAAQCLLLDCRSFFAFNAGHIVGSVNVRFSTIVRRRAKGAMGLEHIVPNTELRGRLLAGAYHAVVLLDERSAALDGAKRDGTLALAAGALCREARSTQVFFLQGGYEAFSASCPELCSKQSTPMGLSLPLSTSVPDSAESGCSSCSTPLYDQGGPVEILSFLYLGSAYHASRKDMLDALGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFIDSIKDAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPHCSAEAGSPAMAVLDRGTSTTTVFNFPVSIPVHPTNSALNYLQSPITTSPSC | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 359 | S | Phosphorylation | Kinase | MAPK1 | P63086 | Uniprot |
| 359 | S | Phosphorylation | Kinase | MAPK3 | P21708 | Uniprot |
| 364 | S | Phosphorylation | Kinase | MAPK1 | P63086 | Uniprot |
| 364 | S | Phosphorylation | Kinase | MAPK3 | P21708 | Uniprot |
| - | K | Ubiquitination | E3 ubiquitin ligase | Fbxo32 | Q91Z62 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 359 | S | Phosphorylation |
| - |
| 364 | S | Phosphorylation |
| - |
* 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 DUS1_RAT !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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