ID BUB1B_MOUSE STANDARD; PRT; 1052 AA. AC Q9Z1S0; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 07-FEB-2006 (Rel. 49, Last annotation update) DE Mitotic checkpoint serine/threonine-protein kinase BUB1 beta DE (EC 2.7.1.37) (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). CC -!- FUNCTION: Probable component of the mitotic checkpoint that delays CC anaphase until all chromosomes are properly attached to the CC mitotic spindle. Can interact with BUB3, CENP-F, CENP-E and CC mitosin (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with CENP-E, BUB3 and mitosin (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic in interphase cells. Bound to CC BUB3 or CENP-E, it can be localized to nuclear kinetochores (By CC similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in thymus followed by spleen. CC -!- DOMAIN: CD1 domain directs kinetochore localization and binding to CC 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 -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. BUB1 CC subfamily. CC -!- SIMILARITY: Contains 1 CD1 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 Ensembl; ENSMUSG00000040084; Mus musculus. DR MGI; MGI:1333889; Bub1b. DR GO; GO:0000776; C:kinetochore; IDA. DR GO; GO:0000940; C:outer kinetochore of condensed chromosome; IDA. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR ProDom; PD000001; Prot_kinase; 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 ATP-binding; Cell cycle; Cell division; Kinase; Mitosis; KW Nuclear protein; Nucleotide-binding; Serine/threonine-protein kinase; KW Transferase. 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). 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 //