| UniProt ID | BUB3_MOUSE | |
|---|---|---|
| UniProt AC | Q9WVA3 | |
| Protein Name | Mitotic checkpoint protein BUB3 | |
| Gene Name | Bub3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 326 | |
| Subcellular Localization | Nucleus. Chromosome, centromere, kinetochore . Starts to localize at kinetochores in prometaphase I (Pro-MI) stage and maintains the localization until the metaphase I-anaphase I (MI-AI) transition.. | |
| Protein Description | Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1 (By similarity). Regulates chromosome segregation during oocyte meiosis.. | |
| Protein Sequence | MTGSNEFKLNQPPEDGISSVKFSPNTSQFLLVSSWDTSVRLYDVPANSMRLKYQHTGAVLDCAFYDPTHAWSGGLDHQLKMHDLNTDQENLVGTHDAPIRCVEYCPEVNVMVTGSWDQTVKLWDPRTPCNAGTFSQPEKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSPEVQKKKYAFKCHRLKENNIEQIYPVNAISFHNIHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGTTLAIASSYMYEMDDTEHPEDGIFIRQVTDAETKPKST | |
| 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 |
|---|---|---|---|---|---|
| 81 | Ubiquitination | GLDHQLKMHDLNTDQ CHHHEEEECCCCCCC | 3.96 | 27667366 | |
| 106 | Ubiquitination | IRCVEYCPEVNVMVT EEEEEECCCCCEEEE | 47.90 | 27667366 | |
| 127 | Phosphorylation | VKLWDPRTPCNAGTF EEEECCCCCCCCCCC | 37.27 | 26745281 | |
| 129 | S-nitrosocysteine | LWDPRTPCNAGTFSQ EECCCCCCCCCCCCC | 5.57 | - | |
| 129 | Glutathionylation | LWDPRTPCNAGTFSQ EECCCCCCCCCCCCC | 5.57 | 24333276 | |
| 129 | S-nitrosylation | LWDPRTPCNAGTFSQ EECCCCCCCCCCCCC | 5.57 | 21278135 | |
| 179 | Acetylation | QRRESSLKYQTRCIR HHHHCCCHHHHHEEE | 36.94 | 23954790 | |
| 191 | Ubiquitination | CIRAFPNKQGYVLSS EEECCCCCCCEEEEE | 45.39 | 27667366 | |
| 211 | Phosphorylation | AVEYLDPSPEVQKKK EEEECCCCHHHHHHH | 33.10 | 27180971 | |
| 216 | Acetylation | DPSPEVQKKKYAFKC CCCHHHHHHHHEEEC | 57.31 | 23236377 | |
| 216 | Ubiquitination | DPSPEVQKKKYAFKC CCCHHHHHHHHEEEC | 57.31 | 22790023 | |
| 217 | Ubiquitination | PSPEVQKKKYAFKCH CCHHHHHHHHEEECC | 33.65 | - |
| 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 BUB3_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BUB3_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 BUB3_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of BUB3_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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