Q9Z1S0 · BUB1B_MOUSE
- ProteinMitotic checkpoint serine/threonine-protein kinase BUB1 beta
- GeneBub1b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1052 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential component of the mitotic checkpoint. Required for normal mitosis progression and tumor suppression. The mitotic checkpoint delays anaphase until all chromosomes are properly attached to the mitotic spindle. One of its checkpoint functions is to inhibit the activity of the anaphase-promoting complex/cyclosome (APC/C) by blocking the binding of CDC20 to APC/C, independently of its kinase activity. The other is to monitor kinetochore activities that depend on the kinetochore motor CENPE. Required for kinetochore localization of CENPE. Negatively regulates PLK1 activity in interphase cells and suppresses centrosome amplification. Also implicated in triggering apoptosis in polyploid cells that exit aberrantly from mitotic arrest. Essential for tumor suppression. May play a role in regulating aging and fertility (By similarity).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Kinase activity stimulated by CENPE.
Features
Showing features for site, binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | kinetochore | |
Cellular Component | mitotic checkpoint complex | |
Cellular Component | nucleus | |
Cellular Component | outer kinetochore | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | spindle | |
Molecular Function | ATP binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | apoptotic process | |
Biological Process | cell division | |
Biological Process | meiotic sister chromatid cohesion, centromeric | |
Biological Process | metaphase/anaphase transition of mitotic cell cycle | |
Biological Process | mitotic spindle assembly checkpoint signaling | |
Biological Process | protein localization to chromosome, centromeric region |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitotic checkpoint serine/threonine-protein kinase BUB1 beta
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9Z1S0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Cytoplasmic in interphase cells (By similarity).
Associates with the kinetochores in early prophase. Kinetochore localization requires BUB1, PLK1 and KNL1 (By similarity).
Associates with the kinetochores in early prophase. Kinetochore localization requires BUB1, PLK1 and KNL1 (By similarity).
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Disruption phenotype
Mice die in utero.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 71 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000085674 | 1-1052 | Mitotic checkpoint serine/threonine-protein kinase BUB1 beta | |||
Sequence: MAEASEAMCLEGAEWELSKENIQPLRHGRVMSTLQGALAKQESAGHTALQQQKRAFESEIRFYSGDDPLDVWDRYINWTEQNYPQGGKESNMSALVERAIEALQGETRYYNDPRFLSLWIKLGHLCNEPLDMYSYLQSQGIGVSLAQFYISWAEEYEARENFKKADIIFQEGIERKAEPLDRLQSQHRQFQSRVSRQAFLALGNEEEEALEPSEPQRSSLAELKSRGKKMARAPISRVGGALKAPGQSRGFLNAVPQPVHGNRRITVFDENADTASRTELSKPVAQPWMAPPVPRAKENELQPGPWSTDRPAGRRPHDNPASVTSIPSVLPSFTPYVEESAQQTVMTPCKIEPSINHVLSTRKPGREEGDPLQRVQSHQQGCEEKKEKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKERREAELLTSAKKREEMQKQIEEMERRLKAMQAVQQEGAGGQQEEKMPTEDPARLQIASGPQEMSGVPLSCSICPLSSNPREISPAENILQEQPDSKGSSMPFSIFDESLSDKKDKSPATGGPQVLNAQRRPLSVLKTTEVGTTNEDVSPDICDELTELEPLSEDAIITGFRNVTLCPNPEDTCDFARAARLASTPFHEILSSKGIAADPEGLLQEEDLDGKAAEAHHTVHHQALIIKKLSPIIEESREATHSSGFSRSSSSAPSTSSIKGFQLLEKLELTNDGAEDAIQSPWCSQYRLQLLKSLLELSAFAEFSVEDRPMPVLEIGKEIELGPEDYVIKQEHLTCDDYRLFWVAPRSSAELTMIKASSQPIPWDFYINLKLKERLNEDYDQLCSCCQYQDGHVVWYQYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRIHDPYDYVNKDDHAVRIMDFSYSVDLRVQLDAFAYSGFRTAQILEGQKILANCSSPYHVDLLGIADLAHLLLFKEHLHVFWDGLLWKLSQSTSELKDSELWNKFFVRILNASDKSTVSVLGELAAEMGGAFDATFHSHLNRALWKLGKTISPEALLTQQDKQPGGSQSPA | ||||||
Modified residue | 243 | N6-acetyllysine; by PCAF | ||||
Sequence: K | ||||||
Modified residue | 360 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 428 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 535 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 659 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 665 | Phosphoserine; by PLK1 | ||||
Sequence: S | ||||||
Modified residue | 686 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 781 | Phosphothreonine; by PLK1 | ||||
Sequence: T | ||||||
Modified residue | 998 | Phosphothreonine; by PLK1 | ||||
Sequence: T | ||||||
Modified residue | 1033 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1050 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Proteolytically cleaved by caspase-3 in a cell cycle specific manner. The cleavage might be involved in the durability of the cell cycle delay.
Acetylation at Lys-243 regulates its degradation and timing in anaphase entry.
Ubiquitinated. Degraded by the proteasome. Ubiquitinated by UBR5, promoting disassembly of the mitotic checkpoint complex from the APC/C complex.
Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the association with CENPE at the kinetochore (By similarity).
Autophosphorylated in vitro. Intramolecular autophosphorylation stimulated by CENPE. Phosphorylated during mitosis and hyperphosphorylated in mitotically arrested cells. Phosphorylation at Ser-659 and Ser-1033 occurs at kinetochores upon mitotic entry with dephosphorylation at the onset of anaphase.
Proteolytically cleaved by caspase-3 in a cell cycle specific manner. The cleavage might be involved in the durability of the cell cycle delay. Caspase-3 cleavage is associated with abrogation of the mitotic checkpoint. The major site of cleavage is at Asp-603.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with CENPE (PubMed:12925705).
Interacts with PLK1 (By similarity).
Part of a complex containing BUB3, CDC20 and BUB1B (By similarity).
Interacts with anaphase-promoting complex/cyclosome (APC/C) (By similarity).
Interacts with KNL1 (By similarity).
Interacts with KAT2B (By similarity).
Interacts with RIPK3 (By similarity).
Interacts with the closed conformation form of MAD2L1 (By similarity).
Interacts with CDC20 (By similarity).
Interacts with PLK1 (By similarity).
Part of a complex containing BUB3, CDC20 and BUB1B (By similarity).
Interacts with anaphase-promoting complex/cyclosome (APC/C) (By similarity).
Interacts with KNL1 (By similarity).
Interacts with KAT2B (By similarity).
Interacts with RIPK3 (By similarity).
Interacts with the closed conformation form of MAD2L1 (By similarity).
Interacts with CDC20 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 56-219 | BUB1 N-terminal | ||||
Sequence: FESEIRFYSGDDPLDVWDRYINWTEQNYPQGGKESNMSALVERAIEALQGETRYYNDPRFLSLWIKLGHLCNEPLDMYSYLQSQGIGVSLAQFYISWAEEYEARENFKKADIIFQEGIERKAEPLDRLQSQHRQFQSRVSRQAFLALGNEEEEALEPSEPQRSS | ||||||
Motif | 105-112 | Nuclear localization signal | ||||
Sequence: GETRYYND | ||||||
Region | 146-179 | Necessary for interaction with KNL1 | ||||
Sequence: AQFYISWAEEYEARENFKKADIIFQEGIERKAEP | ||||||
Region | 206-256 | Disordered | ||||
Sequence: EEEALEPSEPQRSSLAELKSRGKKMARAPISRVGGALKAPGQSRGFLNAVP | ||||||
Motif | 217-225 | D-box | ||||
Sequence: RSSLAELKS | ||||||
Region | 272-327 | Disordered | ||||
Sequence: ADTASRTELSKPVAQPWMAPPVPRAKENELQPGPWSTDRPAGRRPHDNPASVTSIP | ||||||
Region | 361-381 | Disordered | ||||
Sequence: TRKPGREEGDPLQRVQSHQQG | ||||||
Compositional bias | 496-524 | Polar residues | ||||
Sequence: SNPREISPAENILQEQPDSKGSSMPFSIF | ||||||
Region | 496-552 | Disordered | ||||
Sequence: SNPREISPAENILQEQPDSKGSSMPFSIFDESLSDKKDKSPATGGPQVLNAQRRPLS | ||||||
Domain | 756-1040 | Protein kinase | ||||
Sequence: VIKQEHLTCDDYRLFWVAPRSSAELTMIKASSQPIPWDFYINLKLKERLNEDYDQLCSCCQYQDGHVVWYQYINCSTLQNLLQHSEFVTHEIIVLIIYNLLTIVEKLHRAEIVHGDLSPRSLILRNRIHDPYDYVNKDDHAVRIMDFSYSVDLRVQLDAFAYSGFRTAQILEGQKILANCSSPYHVDLLGIADLAHLLLFKEHLHVFWDGLLWKLSQSTSELKDSELWNKFFVRILNASDKSTVSVLGELAAEMGGAFDATFHSHLNRALWKLGKTISPEALLTQ |
Domain
The D-box targets the protein for rapid degradation by ubiquitin-dependent proteolysis during the transition from mitosis to interphase.
The BUB1 N-terminal domain directs kinetochore localization and binding to BUB3.
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,052
- Mass (Da)118,392
- Last updated2011-07-27 v2
- Checksum9EF1ECF3735DD1F4
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 275 | in Ref. 1; AAD11940 | ||||
Sequence: A → T | ||||||
Sequence conflict | 278 | in Ref. 1; AAD11940 | ||||
Sequence: T → P | ||||||
Compositional bias | 496-524 | Polar residues | ||||
Sequence: SNPREISPAENILQEQPDSKGSSMPFSIF | ||||||
Sequence conflict | 664 | in Ref. 1; AAD11940 | ||||
Sequence: E → D | ||||||
Sequence conflict | 705 | in Ref. 1; AAD11940 | ||||
Sequence: D → N |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF107296 EMBL· GenBank· DDBJ | AAD11940.1 EMBL· GenBank· DDBJ | mRNA | ||
AL845470 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL929381 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |