| UniProt ID | WWOX_MOUSE | |
|---|---|---|
| UniProt AC | Q91WL8 | |
| Protein Name | WW domain-containing oxidoreductase | |
| Gene Name | Wwox | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 414 | |
| Subcellular Localization | Cytoplasm . Nucleus . Mitochondrion . Partially localizes to the mitochondria (By similarity). Translocates to the nucleus in response to TGFB1 (PubMed:19366691). Translocates to the nucleus upon genotoxic stress or TNF stimulation (PubMed:11058590). | |
| Protein Description | Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm (By similarity). May also play a role in tumor necrosis factor (TNF)-mediated cell death. Required for normal bone development.. | |
| Protein Sequence | MAALRYAGLDDTDSEDELPPGWEERTTKDGWVYYANHTEEKTQWEHPKTGKRKRVAGDLPYGWEQETDENGQVFFVDHINKRTTYLDPRLAFTVDDNPTKPTTRQRYDGSTTAMEILQGRDFTGKVVLVTGANSGIGFETAKSFALHGAHVILACRNLSRASEAVSRILEEWHKAKVEAMTLDLAVLRSVQHFAEAFKAKNVSLHVLVCNAGTFALPWGLTKDGLETTFQVNHLGHFYLVQLLQDVLCRSSPARVIVVSSESHRFTDINDSSGKLDLSRLSPPRSDYWAMLAYNRSKLCNILFSNELHRRLSPRGVTSNAVHPGNMMYSAIHRNSWVYKLLFTLARPFTKSMQQGAATTVYCAVAPELEGLGGMYFNNCCRCLPSEEAQSEETARALWELSERLIQDRLGSPSS | |
| 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 | --MAALRYAGLDDTD --CCCCCCCCCCCCC | 13.08 | 27087446 | |
| 12 | Phosphorylation | RYAGLDDTDSEDELP CCCCCCCCCCCCCCC | 40.88 | 25521595 | |
| 14 | Phosphorylation | AGLDDTDSEDELPPG CCCCCCCCCCCCCCC | 49.38 | 25521595 | |
| 33 | Phosphorylation | TTKDGWVYYANHTEE ECCCEEEEEEECCCC | 7.14 | 22817900 | |
| 278 | Phosphorylation | SSGKLDLSRLSPPRS CCCCCCHHHCCCCCH | 30.73 | - | |
| 281 | Phosphorylation | KLDLSRLSPPRSDYW CCCHHHCCCCCHHHH | 31.57 | 24719451 | |
| 287 | Phosphorylation | LSPPRSDYWAMLAYN CCCCCHHHHHHHHHC | 9.05 | 16288044 | |
| 411 | Phosphorylation | LIQDRLGSPSS---- HHHHHHCCCCC---- | 26.63 | 21454597 | |
| 413 | Phosphorylation | QDRLGSPSS------ HHHHCCCCC------ | 50.83 | 24759943 | |
| 414 | Phosphorylation | DRLGSPSS------- HHHCCCCC------- | 47.85 | 24759943 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 287 | Y | Phosphorylation | Kinase | TNK2 | O54967 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of WWOX_MOUSE !! | ||||||
* 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 WWOX_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RUNX2_MOUSE | Runx2 | physical | 18487609 | |
| P53_MOUSE | Trp53 | physical | 15580310 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY. | |
| "Transforming growth factor beta1 signaling via interaction with cellsurface Hyal-2 and recruitment of WWOX/WOX1."; Hsu L.-J., Schultz L., Hong Q., Van Moer K., Heath J., Li M.-Y.,Lai F.-J., Lin S.-R., Lee M.-H., Lo C.-P., Lin Y.-S., Chen S.-T.,Chang N.-S.; J. Biol. Chem. 284:16049-16059(2009). Cited for: FUNCTION, PHOSPHORYLATION AT TYR-33, SUBCELLULAR LOCATION, ANDINTERACTION WITH HYAL2. | |