ID BU1B_MOUSE STANDARD; PRT; 1052 AA. AC Q9Z1S0; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 05-JUL-2004 (Rel. 44, 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; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. 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: Cyclin destruction box sequence, which targets protein for CC rapid degradation by ubiquitin-dependent proteolysis during the CC transition from mitosis to interphase. 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; -. DR MGD; MGI:1333889; Bub1b. DR InterPro; IPR011009; Kinase_like. 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; Mitosis; Nuclear protein; KW Serine/threonine-protein kinase; Transferase. FT DOMAIN 56 207 CD1. FT DOMAIN 105 112 Nuclear localization signal (Potential). FT DOMAIN 756 1040 Protein kinase. FT NP_BIND 762 770 ATP (By similarity). FT BINDING 784 784 ATP (By similarity). FT ACT_SITE 871 871 Proton acceptor (By similarity). FT DOMAIN 205 208 Poly-Glu. FT DOMAIN 675 680 Poly-Ser. FT DOMAIN 217 225 CYCLIN DESTRUCTION BOX. 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 //