UniProt ID | WEE1B_XENLA | |
---|---|---|
UniProt AC | Q8QGV2 | |
Protein Name | Wee1-like protein kinase 1-B | |
Gene Name | wee1-b | |
Organism | Xenopus laevis (African clawed frog). | |
Sequence Length | 595 | |
Subcellular Localization | Nucleus. | |
Protein Description | Acts as a zygotic negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed cdk1 before the onset of mitosis by mediating phosphorylation of cdk1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed cdk1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-cdk1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric cdk1 does not occur.. | |
Protein Sequence | MNVQPRNMNVQPRNMNVQPVRHKLFFSDTDEEEEDGHSTGEDSAFQESDSPVSRQREKQEGKPPGGTWEELEEEEGFGSSPIKSPGDFFMSDSPSYRQLAPASPTRSPQGPTSPIPECPGTPPHKTFRKLRLFDTPHTPKSLLSKARGIGSSALRFRGGTLFREAEKAPKPEFVYSTPQVNINPFTPDSLEIQSSAGLCRGRKRALLNDSCGEDMEGSDCELEDEDIRPAKRIPITESNMKSRYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHPHVVRYYSAWAEDDHMLIQNEYCNGGSLSDVISENYRTMQYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISRTTLPNTAVEEADDEECGSGKVIYKIGDLGHVTRVSSPQVEEGDSRFLANEVLQENYTHLAKADIFALALTVWSAAGAEPFPTNGDQWHEIRQGKLPRVPQLLSQEFVDLIKLMISPDPEKRPSSVALVKHSVLLSASRKSAEQLRIELDAEKFKNALLQKELKKAQIAKAAAEERAHFPDRIATRSTTQNNRTTRLIGKKMNRSVSLTIY | |
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 |
---|---|---|---|---|---|
186 | Phosphorylation | QVNINPFTPDSLEIQ CCCCCCCCCCCCHHH | 27.69 | 17360425 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
186 | T | Phosphorylation | Kinase | CDK1 | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of WEE1B_XENLA !! |
* 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 WEE1B_XENLA !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of WEE1B_XENLA !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Mechanism for inactivation of the mitotic inhibitory kinase Wee1 at Mphase."; Okamoto K., Sagata N.; Proc. Natl. Acad. Sci. U.S.A. 104:3753-3758(2007). Cited for: PHOSPHORYLATION AT THR-186, INTERACTION WITH PIN1, AND MUTAGENESIS OF181-ASN--ASN-183 AND THR-186. |