ID BUB1B_MOUSE Reviewed; 1052 AA. AC Q9Z1S0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 28-NOV-2006, entry version 50. DE Mitotic checkpoint serine/threonine-protein kinase BUB1 beta DE (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (Mitotic checkpoint DE kinase MAD3L). GN Name=Bub1b; Synonyms=Mad3l; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NIH Swiss; TISSUE=Embryo; RX MEDLINE=99107817; PubMed=9889005; DOI=10.1006/geno.1998.5629; RA Davenport J.W., Fernandes E.R., Harris L.D., Neale G.A.M., Goorha R.; RT "The mouse mitotic checkpoint gene bub1b, a novel bub1 family member, RT is expressed in a cell cycle-dependent manner."; RL Genomics 55:113-117(1999). RN [2] RP FUNCTION. RX PubMed=14744753; DOI=10.1158/0008-5472.CAN-03-3119; RA Dai W., Wang Q., Liu T., Swamy M., Fang Y., Xie S., Mahmood R., RA Yang Y.M., Xu M., Rao C.V.; RT "Slippage of mitotic arrest and enhanced tumor development in mice RT with BubR1 haploinsufficiency."; RL Cancer Res. 64:440-445(2004). RN [3] RP FUNCTION. RX PubMed=15208629; DOI=10.1038/ng1382; RA Baker D.J., Jeganathan K.B., Cameron J.D., Thompson M., Juneja S., RA Kopecka A., Kumar R., Jenkins R.B., de Groen P.C., Roche P., RA van Deursen J.M.; RT "BubR1 insufficiency causes early onset of aging-associated phenotypes RT and infertility in mice."; RL Nat. Genet. 36:744-749(2004). CC -!- FUNCTION: Essential component of the mitotic checkpoint. Required CC for normal mitosis progression and tumor suppression. The mitotic CC checkpoint delays anaphase until all chromosomes are properly CC attached to the mitotic spindle. One of its checkpoint functions CC is to inhibit the activity of the anaphase-promoting CC complex/cyclosome (APC/C) by blocking the binding of CDC20 to CC APC/C, independently of its kinase activity. The other is to CC monitor kinetochore activities that depend on the kinetochore CC motor CENPE. Also implicated in triggering apoptosis in polyploid CC cells that exit aberrantly from mitotic arrest. Essential for CC tumor suppression. May play a role in regulating aging and CC fertility. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with CENPE, CENPF, mitosin and BUB3. Part of a CC complex containing BUB3, CDC20 and BUB1B. Interact with anaphase- CC promoting complex/cyclosome (APC/C) (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic in interphase cells CC (By similarity). Nucleus. Associates with the kinetochores (By CC similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in thymus followed by spleen. CC -!- DOMAIN: The CD1 domain directs kinetochore localization and CC binding to BUB3. CC -!- DOMAIN: The D-box targets the protein for rapid degradation by CC ubiquitin-dependent proteolysis during the transition from mitosis CC to interphase (Potential). CC -!- PTM: Proteolytically cleaved by caspase-3 in a cell cycle specific CC manner (By similarity). The cleavage might be involved in the CC durability of the cell cycle delay (By similarity). CC -!- PTM: Ubiquitinated. Degradated by the proteasome (By similarity). CC -!- PTM: Phosphorylated during mitosis and hyperphosphorylated in CC mitotically arrested cells (By similarity). CC -!- DISEASE: Defects in Bub1b are involved in the development of lung CC and intestinal adenocarcinomas after exposure to a carcinogen. CC -!- MISCELLANEOUS: Mice lacking BUB1B die in utero. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. BUB1 CC subfamily. CC -!- SIMILARITY: Contains 1 CD1 domain. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF107296; AAD11940.1; -; mRNA. DR UniGene; Mm.29133; -. DR Ensembl; ENSMUSG00000040084; Mus musculus. DR KEGG; mmu:12236; -. DR MGI; MGI:1333889; Bub1b. DR ArrayExpress; Q9Z1S0; -. DR GO; GO:0000776; C:kinetochore; IDA:MGI. DR GO; GO:0000940; C:outer kinetochore of condensed chromosome; IDA:MGI. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR013212; Mad3_BUB1_I. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF08311; Mad3_BUB1_I; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00777; Mad3_BUB1_I; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. KW Anti-oncogene; Apoptosis; ATP-binding; Cell cycle; Cell division; KW Kinase; Mitosis; Nuclear protein; Nucleotide-binding; Phosphorylation; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT CHAIN 1 1052 Mitotic checkpoint serine/threonine- FT protein kinase BUB1 beta. FT /FTId=PRO_0000085674. FT DOMAIN 56 207 CD1. FT DOMAIN 756 1040 Protein kinase. FT NP_BIND 762 770 ATP (By similarity). FT MOTIF 105 112 Nuclear localization signal (Potential). FT MOTIF 217 225 D-box. FT COMPBIAS 205 208 Poly-Glu. FT COMPBIAS 675 680 Poly-Ser. FT ACT_SITE 871 871 Proton acceptor (By similarity). FT BINDING 784 784 ATP (By similarity). FT SITE 572 573 Cleavage (by caspase-3) (By similarity). FT SITE 603 604 Cleavage (by caspase-3) (By similarity). SQ SEQUENCE 1052 AA; 118403 MW; 5FE3D00EA114CCD8 CRC64; MAEASEAMCL EGAEWELSKE NIQPLRHGRV MSTLQGALAK QESAGHTALQ QQKRAFESEI RFYSGDDPLD VWDRYINWTE QNYPQGGKES NMSALVERAI EALQGETRYY NDPRFLSLWI KLGHLCNEPL DMYSYLQSQG IGVSLAQFYI SWAEEYEARE NFKKADIIFQ EGIERKAEPL DRLQSQHRQF QSRVSRQAFL ALGNEEEEAL EPSEPQRSSL AELKSRGKKM ARAPISRVGG ALKAPGQSRG FLNAVPQPVH GNRRITVFDE NADTTSRPEL SKPVAQPWMA PPVPRAKENE LQPGPWSTDR PAGRRPHDNP ASVTSIPSVL PSFTPYVEES AQQTVMTPCK IEPSINHVLS TRKPGREEGD PLQRVQSHQQ GCEEKKEKMM YCKEKIYAGV GEFSFEEIRA EVFRKKLKER REAELLTSAK KREEMQKQIE EMERRLKAMQ AVQQEGAGGQ QEEKMPTEDP ARLQIASGPQ EMSGVPLSCS ICPLSSNPRE ISPAENILQE QPDSKGSSMP FSIFDESLSD KKDKSPATGG PQVLNAQRRP LSVLKTTEVG TTNEDVSPDI CDELTELEPL SEDAIITGFR NVTLCPNPED TCDFARAARL ASTPFHEILS SKGIAADPEG LLQEEDLDGK AAEAHHTVHH QALIIKKLSP IIEDSREATH SSGFSRSSSS APSTSSIKGF QLLEKLELTN DGAENAIQSP WCSQYRLQLL KSLLELSAFA EFSVEDRPMP VLEIGKEIEL GPEDYVIKQE HLTCDDYRLF WVAPRSSAEL TMIKASSQPI PWDFYINLKL KERLNEDYDQ LCSCCQYQDG HVVWYQYINC STLQNLLQHS EFVTHEIIVL IIYNLLTIVE KLHRAEIVHG DLSPRSLILR NRIHDPYDYV NKDDHAVRIM DFSYSVDLRV QLDAFAYSGF RTAQILEGQK ILANCSSPYH VDLLGIADLA HLLLFKEHLH VFWDGLLWKL SQSTSELKDS ELWNKFFVRI LNASDKSTVS VLGELAAEMG GAFDATFHSH LNRALWKLGK TISPEALLTQ QDKQPGGSQS PA //