| UniProt ID | MND2_YEAST | |
|---|---|---|
| UniProt AC | P40577 | |
| Protein Name | Anaphase-promoting complex subunit MND2 | |
| Gene Name | MND2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 368 | |
| Subcellular Localization | ||
| Protein Description | Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.. | |
| Protein Sequence | MARALRDISLFNDIRKDQNSAGAKHERYNMRDLRSKKNQHVNGIDDYEDDSLDRFIRRKKSRVVKYIPSLSAYNVFNEFPYYPTSASQLLDGKLDEFLMLSEQYKSRLPKIRKLGWNRFKPIGINKTMYELEMLRSRARAQNAEGNNEEDFRQHDSREEDPRNNGSIGRVILPHILQENEEYDTGEGVTGLHSMPNDSMAILANNSANNSQNEEVSEEDEISYDYDAEFDHVVDEDDNEEGEVPGEGVEGIEVQRERIVPDDLLMRPTSLSRSLQQFVEEAHHLDRNPYDIDSDNDGEDSKVELDMNPDFEDDVGREHDYNSEYSQEPTSYGGITPDLASNWRNWTRERITSLDELMERRARQQRGQD | |
| 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 |
|---|---|---|---|---|---|
| 268 | Phosphorylation | DDLLMRPTSLSRSLQ HHHHCCCCHHHHHHH | 31.75 | 23749301 | |
| 289 | Phosphorylation | HHLDRNPYDIDSDND HHCCCCCCCCCCCCC | 29.13 | 19795423 | |
| 293 | Phosphorylation | RNPYDIDSDNDGEDS CCCCCCCCCCCCCCC | 38.35 | 25704821 | |
| 300 | Phosphorylation | SDNDGEDSKVELDMN CCCCCCCCCEEECCC | 34.01 | 19779198 | |
| 352 | Phosphorylation | WTRERITSLDELMER HHHHHCCCHHHHHHH | 31.30 | 28152593 |
| 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 MND2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MND2_YEAST !! | ||||||
* 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 MND2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
