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Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)

 BUB1B_HUMAN             Reviewed;        1050 AA.
O60566; B2R6U0; B4DL09; B4DLG3; O60501; O60627; O60758; O75389; Q59HH6;
Q8WV50; Q96KM4;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 3.
22-APR-2020, entry version 204.
RecName: Full=Mitotic checkpoint serine/threonine-protein kinase BUB1 beta;
EC=2.7.11.1;
AltName: Full=MAD3/BUB1-related protein kinase;
Short=hBUBR1;
AltName: Full=Mitotic checkpoint kinase MAD3L;
AltName: Full=Protein SSK1;
Name=BUB1B; Synonyms=BUBR1, MAD3L, SSK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-349.
TISSUE=Umbilical vein;
PubMed=9618306; DOI=10.1006/bbrc.1998.8713;
Donadelli R., Benatti L., Remuzzi A., Morigi M., Gullans S.R., Benigni A.,
Remuzzi G., Noris M.;
"Identification of a novel gene -- SSK1 -- in human endothelial cells
exposed to shear stress.";
Biochem. Biophys. Res. Commun. 246:881-887(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-349.
PubMed=9660858; DOI=10.1083/jcb.142.1.1;
Taylor S.S., Ha E., McKeon F.;
"The human homologue of Bub3 is required for kinetochore localization of
Bub1 and a Mad3/Bub1-related protein kinase.";
J. Cell Biol. 142:1-11(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CENPE, SUBCELLULAR
LOCATION, AND VARIANT GLN-349.
PubMed=9763420; DOI=10.1083/jcb.143.1.49;
Chan G.K.T., Schaar B.T., Yen T.J.;
"Characterization of the kinetochore binding domain of CENP-E reveals
interactions with the kinetochore proteins CENP-F and hBUBR1.";
J. Cell Biol. 143:49-63(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-15 AND GLN-349.
PubMed=9521327; DOI=10.1038/32688;
Cahill D.P., Lengauer C., Yu J., Riggins G.J., Willson J.K.V.,
Markowitz S.D., Kinzler K.W., Vogelstein B.;
"Mutations of mitotic checkpoint genes in human cancers.";
Nature 392:300-303(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9889005; DOI=10.1006/geno.1998.5629;
Davenport J.W., Fernandes E.R., Harris L.D., Neale G.A.M., Goorha R.;
"The mouse mitotic checkpoint gene bub1b, a novel bub1 family member, is
expressed in a cell cycle-dependent manner.";
Genomics 55:113-117(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-349.
Dai W., Ouyang B., Lan Z., Pan H.;
"Human MAD3-like protein kinase (hmad3).";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Seike M., Gemma A., Hosoya Y., Kurimoto F., Yoshimura A., Kudoh S.;
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
GLN-349.
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-349
AND SER-378.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PHOSPHORYLATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=10593653;
Li W., Lan Z., Wu H., Wu S., Meadows J., Chen J., Zhu V., Dai W.;
"BUBR1 phosphorylation is regulated during mitotic checkpoint activation.";
Cell Growth Differ. 10:769-775(1999).
[12]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION, AND INTERACTION
WITH APC/C.
PubMed=10477750; DOI=10.1083/jcb.146.5.941;
Chan G.K., Jablonski S.A., Sudakin V., Hittle J.C., Yen T.J.;
"Human BUBR1 is a mitotic checkpoint kinase that monitors CENP-E functions
at kinetochores and binds the cyclosome/APC.";
J. Cell Biol. 146:941-954(1999).
[13]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH CDC20 AND BUB3, AND MUTAGENESIS
OF LYS-795.
PubMed=11702782; DOI=10.1016/s1534-5807(01)00019-3;
Tang Z., Bharadwaj R., Li B., Yu H.;
"Mad2-independent inhibition of APC/Cdc20 by the mitotic checkpoint protein
BubR1.";
Dev. Cell 1:227-237(2001).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND DEGRADATION BY THE PROTEASOME.
PubMed=14706340; DOI=10.1016/s1535-6108(03)00302-7;
Shin H.J., Baek K.H., Jeon A.H., Park M.T., Lee S.J., Kang C.M., Lee H.S.,
Yoo S.H., Chung D.H., Sung Y.C., McKeon F., Lee C.W.;
"Dual roles of human BubR1, a mitotic checkpoint kinase, in the monitoring
of chromosomal instability.";
Cancer Cell 4:483-497(2003).
[15]
ACTIVITY REGULATION, INTERACTION WITH CENPE, AUTOPHOSPHORYLATION, AND
MUTAGENESIS OF LYS-795.
PubMed=12925705; DOI=10.1083/jcb.200303167;
Weaver B.A., Bonday Z.Q., Putkey F.R., Kops G.J., Silk A.D.,
Cleveland D.W.;
"Centromere-associated protein-E is essential for the mammalian mitotic
checkpoint to prevent aneuploidy due to single chromosome loss.";
J. Cell Biol. 162:551-563(2003).
[16]
FUNCTION.
PubMed=15020684; DOI=10.1242/jcs.01006;
Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S.;
"Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and
Mad2, and chromosome congression.";
J. Cell Sci. 117:1577-1589(2004).
[17]
PROTEOLYTIC CLEAVAGE AT ASP-579 AND ASP-610 BY CASPASE-3, INDUCTION, AND
MUTAGENESIS OF ASP-579 AND ASP-610.
PubMed=16227576; DOI=10.1128/mcb.25.21.9232-9248.2005;
Kim M., Murphy K., Liu F., Parker S.E., Dowling M.L., Baff W., Kao G.D.;
"Caspase-mediated specific cleavage of BubR1 is a determinant of mitotic
progression.";
Mol. Cell. Biol. 25:9232-9248(2005).
[18]
SUBCELLULAR LOCATION, AND INTERACTION WITH PLK1.
PubMed=16760428; DOI=10.1091/mbc.e06-03-0240;
Qi W., Tang Z., Yu H.;
"Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is
required for the kinetochore localization of Plk1.";
Mol. Biol. Cell 17:3705-3716(2006).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[20]
INTERACTION WITH KNL1, AND MUTAGENESIS OF ALA-159 AND PHE-175.
PubMed=17981135; DOI=10.1016/j.devcel.2007.09.005;
Kiyomitsu T., Obuse C., Yanagida M.;
"Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic
checkpoint through direct interaction with Bub1 and BubR1.";
Dev. Cell 13:663-676(2007).
[21]
INTERACTION WITH PLK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-676,
AND MUTAGENESIS OF THR-620.
PubMed=17785528; DOI=10.1101/gad.436007;
Elowe S., Huemmer S., Uldschmid A., Li X., Nigg E.A.;
"Tension-sensitive Plk1 phosphorylation on BubR1 regulates the stability of
kinetochore microtubule interactions.";
Genes Dev. 21:2205-2219(2007).
[22]
INTERACTION WITH PLK1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-792
AND THR-1008.
PubMed=17376779; DOI=10.1074/jbc.m611053200;
Matsumura S., Toyoshima F., Nishida E.;
"Polo-like kinase 1 facilitates chromosome alignment during prometaphase
through BubR1.";
J. Biol. Chem. 282:15217-15227(2007).
[23]
PHOSPHORYLATION AT SER-435; SER-543; SER-670 AND SER-1043.
PubMed=19015317; DOI=10.1083/jcb.200805163;
Huang H., Hittle J., Zappacosta F., Annan R.S., Hershko A., Yen T.J.;
"Phosphorylation sites in BubR1 that regulate kinetochore attachment,
tension, and mitotic exit.";
J. Cell Biol. 183:667-680(2008).
[24]
SUMOYLATION.
PubMed=18374647; DOI=10.1016/j.molcel.2008.01.013;
Zhang X.-D., Goeres J., Zhang H., Yen T.J., Porter A.C.G., Matunis M.J.;
"SUMO-2/3 modification and binding regulate the association of CENP-E with
kinetochores and progression through mitosis.";
Mol. Cell 29:729-741(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[28]
FUNCTION.
PubMed=19411850; DOI=10.4161/cc.8.11.8671;
Park S.-Y., Kim S., Cho H., Kwon S.-H., Chae S., Kang D., Seong Y.-S.,
Cho H.;
"Depletion of BubR1 promotes premature centrosomal localization of cyclin
B1 and accelerates mitotic entry.";
Cell Cycle 8:1754-1764(2009).
[29]
INTERACTION WITH CENPE, AND SUBCELLULAR LOCATION.
PubMed=19625775; DOI=10.4161/cc.8.16.9366;
Huang Y., Yao Y., Xu H.-Z., Wang Z.-G., Lu L., Dai W.;
"Defects in chromosome congression and mitotic progression in KIF18A-
deficient cells are partly mediated through impaired functions of CENP-E.";
Cell Cycle 8:2643-2649(2009).
[30]
INTERACTION WITH PCAF, ACETYLATION AT LYS-250, AND UBIQUITINATION.
PubMed=19407811; DOI=10.1038/emboj.2009.123;
Choi E., Choe H., Min J., Choi J.Y., Kim J., Lee H.;
"BubR1 acetylation at prometaphase is required for modulating APC/C
activity and timing of mitosis.";
EMBO J. 28:2077-2089(2009).
[31]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLK1.
PubMed=19503101; DOI=10.1038/onc.2009.141;
Izumi H., Matsumoto Y., Ikeuchi T., Saya H., Kajii T., Matsuura S.;
"BubR1 localizes to centrosomes and suppresses centrosome amplification via
regulating Plk1 activity in interphase cells.";
Oncogene 28:2806-2820(2009).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670 AND THR-1042, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-435; SER-543;
SER-665; SER-670 AND SER-697, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[36]
INTERACTION WITH RIPK3.
PubMed=29883609; DOI=10.1016/j.molcel.2018.05.016;
Choi S.W., Park H.H., Kim S., Chung J.M., Noh H.J., Kim S.K., Song H.K.,
Lee C.W., Morgan M.J., Kang H.C., Kim Y.S.;
"PELI1 selectively targets kinase-active RIP3 for ubiquitylation-dependent
proteasomal degradation.";
Mol. Cell 70:920-935(2018).
[37]
VARIANTS GLN-349 AND ALA-618.
PubMed=10366450; DOI=10.1006/geno.1999.5831;
Cahill D.P., da Costa L.T., Carson-Walter E.B., Kinzler K.W.,
Vogelstein B., Lengauer C.;
"Characterization of MAD2B and other mitotic spindle checkpoint genes.";
Genomics 58:181-187(1999).
[38]
VARIANTS MVA1 GLN-550; HIS-814; PHE-844; THR-909; HIS-921 AND PRO-1012.
PubMed=15475955; DOI=10.1038/ng1449;
Hanks S., Coleman K., Reid S., Plaja A., Firth H., Fitzpatrick D., Kidd A.,
Mehes K., Nash R., Robin N., Shannon N., Tolmie J., Swansbury J.,
Irrthum A., Douglas J., Rahman N.;
"Constitutional aneuploidy and cancer predisposition caused by biallelic
mutations in BUB1B.";
Nat. Genet. 36:1159-1161(2004).
[39]
VARIANT PCS GLN-36.
PubMed=16411201; DOI=10.1002/ajmg.a.31069;
Matsuura S., Matsumoto Y., Morishima K., Izumi H., Matsumoto H., Ito E.,
Tsutsui K., Kobayashi J., Tauchi H., Kajiwara Y., Hama S., Kurisu K.,
Tahara H., Oshimura M., Komatsu K., Ikeuchi T., Kajii T.;
"Monoallelic BUB1B mutations and defective mitotic-spindle checkpoint in
seven families with premature chromatid separation (PCS) syndrome.";
Am. J. Med. Genet. A 140:358-367(2006).
[40]
VARIANTS [LARGE SCALE ANALYSIS] MET-40; GLN-349; ASP-390 AND ALA-618.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Essential component of the mitotic checkpoint. Required for
normal mitosis progression. 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. May play a role for
tumor suppression. {ECO:0000269|PubMed:10477750,
ECO:0000269|PubMed:11702782, ECO:0000269|PubMed:14706340,
ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:19411850,
ECO:0000269|PubMed:19503101}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- ACTIVITY REGULATION: Kinase activity stimulated by CENPE.
{ECO:0000269|PubMed:12925705}.
-!- SUBUNIT: Interacts with CENPE, CENPF, mitosin, PLK1 and BUB3. Part of a
complex containing BUB3, CDC20 and BUB1B. Interacts with anaphase-
promoting complex/cyclosome (APC/C). Interacts with KNL1. Interacts
with RIPK3 (PubMed:29883609). {ECO:0000269|PubMed:10477750,
ECO:0000269|PubMed:11702782, ECO:0000269|PubMed:12925705,
ECO:0000269|PubMed:16760428, ECO:0000269|PubMed:17376779,
ECO:0000269|PubMed:17785528, ECO:0000269|PubMed:17981135,
ECO:0000269|PubMed:19407811, ECO:0000269|PubMed:19503101,
ECO:0000269|PubMed:19625775, ECO:0000269|PubMed:29883609,
ECO:0000269|PubMed:9763420}.
-!- INTERACTION:
O60566; O43683: BUB1; NbExp=3; IntAct=EBI-1001438, EBI-748936;
O60566; O43684: BUB3; NbExp=9; IntAct=EBI-1001438, EBI-1050987;
O60566; Q12834: CDC20; NbExp=32; IntAct=EBI-1001438, EBI-367462;
O60566; Q02224: CENPE; NbExp=4; IntAct=EBI-1001438, EBI-1375040;
O60566; P45481: Crebbp; Xeno; NbExp=3; IntAct=EBI-1001438, EBI-296306;
O60566; Q92831: KAT2B; NbExp=14; IntAct=EBI-1001438, EBI-477430;
O60566; Q8NG31-2: KNL1; NbExp=10; IntAct=EBI-1001438, EBI-10973816;
O60566; Q13257: MAD2L1; NbExp=14; IntAct=EBI-1001438, EBI-78203;
O60566; Q8IXJ6: SIRT2; NbExp=3; IntAct=EBI-1001438, EBI-477232;
O60566; P0CG48: UBC; NbExp=3; IntAct=EBI-1001438, EBI-3390054;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere,
kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome. Note=Cytoplasmic in interphase cells. Associates with the
kinetochores in early prophase. Kinetochore localization requires BUB1,
PLK1 and KNL1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O60566-1; Sequence=Displayed;
Name=2;
IsoId=O60566-2; Sequence=VSP_036474, VSP_036475, VSP_036476;
Name=3;
IsoId=O60566-3; Sequence=VSP_036473;
-!- TISSUE SPECIFICITY: Highly expressed in thymus followed by spleen.
Preferentially expressed in tissues with a high mitotic index.
{ECO:0000269|PubMed:10593653}.
-!- INDUCTION: Induced during mitosis. {ECO:0000269|PubMed:10477750,
ECO:0000269|PubMed:10593653, ECO:0000269|PubMed:16227576}.
-!- DOMAIN: The D-box targets the protein for rapid degradation by
ubiquitin-dependent proteolysis during the transition from mitosis to
interphase. {ECO:0000305}.
-!- DOMAIN: The BUB1 N-terminal domain directs kinetochore localization and
binding to BUB3.
-!- PTM: 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-610.
{ECO:0000269|PubMed:16227576}.
-!- PTM: Acetylation at Lys-250 regulates its degradation and timing in
anaphase entry. {ECO:0000269|PubMed:19407811}.
-!- PTM: Ubiquitinated. Degraded by the proteasome.
{ECO:0000269|PubMed:19407811}.
-!- PTM: Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the
association with CENPE at the kinetochore.
{ECO:0000269|PubMed:18374647}.
-!- PTM: Autophosphorylated in vitro. Intramolecular autophosphorylation is
stimulated by CENPE. Phosphorylated during mitosis and
hyperphosphorylated in mitotically arrested cells. Phosphorylation at
Ser-670 and Ser-1043 occurs at kinetochores upon mitotic entry with
dephosphorylation at the onset of anaphase.
{ECO:0000269|PubMed:10477750, ECO:0000269|PubMed:10593653,
ECO:0000269|PubMed:17376779, ECO:0000269|PubMed:17785528,
ECO:0000269|PubMed:19015317}.
-!- DISEASE: Note=Defects in BUB1B are associated with tumor formation.
-!- DISEASE: Premature chromatid separation trait (PCS) [MIM:176430]:
Consists of separate and splayed chromatids with discernible
centromeres and involves all or most chromosomes of a metaphase. It is
found in up to 2% of metaphases in cultured lymphocytes from
approximately 40% of normal individuals. When PCS is present in 5% or
more of cells, it is known as the heterozygous PCS trait and has no
obvious phenotypic effect, although some have reported decreased
fertility. Inheritance is autosomal dominant.
{ECO:0000269|PubMed:16411201}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Mosaic variegated aneuploidy syndrome 1 (MVA1) [MIM:257300]: A
severe developmental disorder characterized by mosaic aneuploidies,
predominantly trisomies and monosomies, involving multiple different
chromosomes and tissues. Affected individuals typically present with
severe intrauterine growth retardation and microcephaly. Eye anomalies,
mild dysmorphism, variable developmental delay, and a broad spectrum of
additional congenital abnormalities and medical conditions may also
occur. The risk of malignancy is high, with rhabdomyosarcoma, Wilms
tumor and leukemia reported in several cases.
{ECO:0000269|PubMed:15475955}. Note=The disease is caused by mutations
affecting the gene represented in this entry. MVA1 is caused by
biallelic mutations in the BUB1B gene.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
kinase family. BUB1 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92019.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BUB1BID854ch15q15.html";
---------------------------------------------------------------------------
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EMBL; AF053306; AAC06260.1; -; mRNA.
EMBL; AF046918; AAC33435.1; -; mRNA.
EMBL; AF046079; AAC12730.2; -; mRNA.
EMBL; AF107297; AAD11941.1; -; mRNA.
EMBL; AF035933; AAC23736.1; -; mRNA.
EMBL; AF068760; AAC19118.1; -; mRNA.
EMBL; AF310214; AAL10712.1; -; Genomic_DNA.
EMBL; AF310192; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310193; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310194; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310195; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310196; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310197; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310198; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310199; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310200; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310201; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310202; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310203; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310204; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310205; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310206; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310207; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310208; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310209; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310210; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310211; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310212; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AF310213; AAL10712.1; JOINED; Genomic_DNA.
EMBL; AK296795; BAG59371.1; -; mRNA.
EMBL; AK296984; BAG59525.1; -; mRNA.
EMBL; AK312709; BAG35587.1; -; mRNA.
EMBL; AB208782; BAD92019.1; ALT_INIT; mRNA.
EMBL; BC018739; AAH18739.1; -; mRNA.
CCDS; CCDS10053.1; -. [O60566-1]
PIR; JW0092; JW0092.
RefSeq; NP_001202.4; NM_001211.5. [O60566-1]
PDB; 2WVI; X-ray; 1.80 A; A=57-220.
PDB; 3SI5; X-ray; 2.20 A; A/B=57-220.
PDB; 4GGD; X-ray; 2.44 A; C/D=20-42.
PDB; 5JJA; X-ray; 2.35 A; C/D=647-720.
PDB; 5K6S; X-ray; 2.79 A; B=663-681.
PDB; 5KHU; EM; 4.80 A; Q=1-1050.
PDB; 5LCW; EM; 4.00 A; S=1-560.
PDB; 5SWF; X-ray; 2.82 A; B=668-676.
PDBsum; 2WVI; -.
PDBsum; 3SI5; -.
PDBsum; 4GGD; -.
PDBsum; 5JJA; -.
PDBsum; 5K6S; -.
PDBsum; 5KHU; -.
PDBsum; 5LCW; -.
PDBsum; 5SWF; -.
SMR; O60566; -.
BioGrid; 107166; 124.
ComplexPortal; CPX-3946; Mitotic Checkpoint Complex.
CORUM; O60566; -.
DIP; DIP-24203N; -.
ELM; O60566; -.
IntAct; O60566; 79.
MINT; O60566; -.
STRING; 9606.ENSP00000287598; -.
GlyConnect; 1516; -.
iPTMnet; O60566; -.
MetOSite; O60566; -.
PhosphoSitePlus; O60566; -.
BioMuta; BUB1B; -.
EPD; O60566; -.
jPOST; O60566; -.
MassIVE; O60566; -.
MaxQB; O60566; -.
PaxDb; O60566; -.
PeptideAtlas; O60566; -.
PRIDE; O60566; -.
ProteomicsDB; 49471; -. [O60566-1]
ProteomicsDB; 49472; -. [O60566-2]
ProteomicsDB; 49473; -. [O60566-3]
Antibodypedia; 1214; 688 antibodies.
DNASU; 701; -.
Ensembl; ENST00000287598; ENSP00000287598; ENSG00000156970. [O60566-1]
Ensembl; ENST00000412359; ENSP00000398470; ENSG00000156970. [O60566-3]
GeneID; 701; -.
KEGG; hsa:701; -.
UCSC; uc001zkx.5; human. [O60566-1]
CTD; 701; -.
DisGeNET; 701; -.
GeneCards; BUB1B; -.
HGNC; HGNC:1149; BUB1B.
HPA; ENSG00000156970; Tissue enhanced (lymphoid tissue, testis).
MalaCards; BUB1B; -.
MIM; 176430; phenotype.
MIM; 257300; phenotype.
MIM; 602860; gene.
neXtProt; NX_O60566; -.
OpenTargets; ENSG00000156970; -.
Orphanet; 1052; Mosaic variegated aneuploidy syndrome.
PharmGKB; PA82; -.
eggNOG; ENOG410IQA2; Eukaryota.
eggNOG; ENOG410XUW7; LUCA.
GeneTree; ENSGT00940000158912; -.
HOGENOM; CLU_010890_0_0_1; -.
InParanoid; O60566; -.
KO; K06637; -.
OMA; DNCMIRF; -.
OrthoDB; 1411806at2759; -.
PhylomeDB; O60566; -.
TreeFam; TF105456; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
SignaLink; O60566; -.
SIGNOR; O60566; -.
ChiTaRS; BUB1B; human.
EvolutionaryTrace; O60566; -.
GeneWiki; BUB1B; -.
GenomeRNAi; 701; -.
Pharos; O60566; Tbio.
PRO; PR:O60566; -.
Proteomes; UP000005640; Chromosome 15.
RNAct; O60566; protein.
Bgee; ENSG00000156970; Expressed in secondary oocyte and 146 other tissues.
ExpressionAtlas; O60566; baseline and differential.
Genevisible; O60566; HS.
GO; GO:0005680; C:anaphase-promoting complex; TAS:ProtInc.
GO; GO:0000777; C:condensed chromosome kinetochore; IDA:UniProtKB.
GO; GO:0000940; C:condensed chromosome outer kinetochore; IDA:UniProtKB.
GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IBA:GO_Central.
GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
GO; GO:0007093; P:mitotic cell cycle checkpoint; TAS:ProtInc.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IBA:GO_Central.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:Reactome.
DisProt; DP01117; -.
InterPro; IPR015661; Bub1/Mad3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR013212; Mad3/Bub1_I.
PANTHER; PTHR14030; PTHR14030; 1.
Pfam; PF08311; Mad3_BUB1_I; 1.
SMART; SM00777; Mad3_BUB1_I; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51489; BUB1_N; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis; ATP-binding;
Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
Disease mutation; Kinase; Kinetochore; Mitosis; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tumor suppressor;
Ubl conjugation.
CHAIN 1..1050
/note="Mitotic checkpoint serine/threonine-protein kinase
BUB1 beta"
/id="PRO_0000085673"
DOMAIN 62..226
/note="BUB1 N-terminal"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00822"
DOMAIN 766..1050
/note="Protein kinase"
NP_BIND 772..780
/note="ATP"
/evidence="ECO:0000250"
REGION 152..185
/note="Necessary for interaction with KNL1"
/evidence="ECO:0000269|PubMed:17981135"
MOTIF 111..118
/note="Nuclear localization signal"
/evidence="ECO:0000255"
MOTIF 224..232
/note="D-box"
COMPBIAS 209..215
/note="Poly-Glu"
ACT_SITE 882
/note="Proton acceptor"
/evidence="ECO:0000250"
BINDING 795
/note="ATP"
/evidence="ECO:0000250"
SITE 579..580
/note="Cleavage; by caspase-3"
/evidence="ECO:0000269|PubMed:16227576"
SITE 610..611
/note="Cleavage; by caspase-3"
/evidence="ECO:0000269|PubMed:16227576"
MOD_RES 250
/note="N6-acetyllysine; by PCAF"
/evidence="ECO:0000269|PubMed:19407811"
MOD_RES 367
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 435
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19015317"
MOD_RES 543
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:19015317"
MOD_RES 665
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 670
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:19015317"
MOD_RES 676
/note="Phosphoserine; by PLK1"
/evidence="ECO:0000269|PubMed:17785528"
MOD_RES 697
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 792
/note="Phosphothreonine; by PLK1"
/evidence="ECO:0000269|PubMed:17376779"
MOD_RES 1008
/note="Phosphothreonine; by PLK1"
/evidence="ECO:0000269|PubMed:17376779"
MOD_RES 1042
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:20068231"
MOD_RES 1043
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:19015317"
VAR_SEQ 80
/note="R -> RWVFLFHKDNRNINR (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_036473"
VAR_SEQ 113..166
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_036474"
VAR_SEQ 522
/note="K -> KVSLSL (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_036475"
VAR_SEQ 608..675
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_036476"
VARIANT 15
/note="M -> T (in a colorectal cancer cell line;
dbSNP:rs1392369693)"
/evidence="ECO:0000269|PubMed:9521327"
/id="VAR_008852"
VARIANT 36
/note="R -> Q (in PCS; dbSNP:rs534297115)"
/evidence="ECO:0000269|PubMed:16411201"
/id="VAR_028921"
VARIANT 40
/note="T -> M (in dbSNP:rs56079734)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_040402"
VARIANT 349
/note="R -> Q (in dbSNP:rs1801376)"
/evidence="ECO:0000269|PubMed:10366450,
ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:9521327,
ECO:0000269|PubMed:9618306, ECO:0000269|PubMed:9660858,
ECO:0000269|PubMed:9763420, ECO:0000269|Ref.6"
/id="VAR_008853"
VARIANT 378
/note="P -> S (in dbSNP:rs17851677)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_054549"
VARIANT 390
/note="E -> D (in dbSNP:rs1017842)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_028922"
VARIANT 550
/note="R -> Q (in MVA1; heterozygous compound with nonsense
mutation; dbSNP:rs28989187)"
/evidence="ECO:0000269|PubMed:15475955"
/id="VAR_028923"
VARIANT 618
/note="V -> A (in colorectal cancer; dbSNP:rs1801528)"
/evidence="ECO:0000269|PubMed:10366450,
ECO:0000269|PubMed:17344846"
/id="VAR_008854"
VARIANT 814
/note="R -> H (in MVA1; heterozygous compound with nonsense
mutation; dbSNP:rs28989182)"
/evidence="ECO:0000269|PubMed:15475955"
/id="VAR_028924"
VARIANT 844
/note="L -> F (in MVA1; associated with H-921; heterozygous
compound with nonsense mutation; dbSNP:rs28989181)"
/evidence="ECO:0000269|PubMed:15475955"
/id="VAR_028925"
VARIANT 909
/note="I -> T (in MVA1; heterozygous compound with nonsense
mutation; dbSNP:rs28989184)"
/evidence="ECO:0000269|PubMed:15475955"
/id="VAR_028926"
VARIANT 921
/note="Q -> H (in MVA1; associated with F-844; heterozygous
compound with nonsense mutation; dbSNP:rs28989183)"
/evidence="ECO:0000269|PubMed:15475955"
/id="VAR_028927"
VARIANT 1012
/note="L -> P (in MVA1; heterozygous compound with nonsense
mutation; dbSNP:rs28989185)"
/evidence="ECO:0000269|PubMed:15475955"
/id="VAR_028928"
MUTAGEN 159
/note="A->W: Loss of interaction with KNL1."
/evidence="ECO:0000269|PubMed:17981135"
MUTAGEN 175
/note="F->A: Loss of interaction with KNL1."
/evidence="ECO:0000269|PubMed:17981135"
MUTAGEN 579
/note="D->E: Abolishes the cleavage by caspase-3."
/evidence="ECO:0000269|PubMed:16227576"
MUTAGEN 610
/note="D->E: Abolishes the cleavage by caspase-3."
/evidence="ECO:0000269|PubMed:16227576"
MUTAGEN 620
/note="T->A: Induces chromosome congression defects and
mitotic delay."
/evidence="ECO:0000269|PubMed:17785528"
MUTAGEN 795
/note="K->A: Does not abolish the capacity to inhibit
APC/CDC20."
/evidence="ECO:0000269|PubMed:11702782,
ECO:0000269|PubMed:12925705"
MUTAGEN 795
/note="K->R: Inhibits kinase activity."
/evidence="ECO:0000269|PubMed:11702782,
ECO:0000269|PubMed:12925705"
CONFLICT 248..249
/note="AL -> VF (in Ref. 1; AAC23736)"
/evidence="ECO:0000305"
CONFLICT 283
/note="S -> P (in Ref. 8; BAG35587)"
/evidence="ECO:0000305"
CONFLICT 788
/note="S -> F (in Ref. 2; AAC06260)"
/evidence="ECO:0000305"
CONFLICT 1018
/note="E -> K (in Ref. 3; AAC33435)"
/evidence="ECO:0000305"
TURN 26..28
/evidence="ECO:0000244|PDB:4GGD"
HELIX 60..65
/evidence="ECO:0000244|PDB:2WVI"
HELIX 75..88
/evidence="ECO:0000244|PDB:2WVI"
HELIX 94..96
/evidence="ECO:0000244|PDB:3SI5"
HELIX 98..108
/evidence="ECO:0000244|PDB:2WVI"
TURN 109..111
/evidence="ECO:0000244|PDB:2WVI"
HELIX 113..115
/evidence="ECO:0000244|PDB:2WVI"
HELIX 119..131
/evidence="ECO:0000244|PDB:2WVI"
HELIX 135..144
/evidence="ECO:0000244|PDB:2WVI"
HELIX 152..164
/evidence="ECO:0000244|PDB:2WVI"
HELIX 168..180
/evidence="ECO:0000244|PDB:2WVI"
HELIX 186..218
/evidence="ECO:0000244|PDB:2WVI"
SEQUENCE 1050 AA; 119545 MW; F7871103A56E6B46 CRC64;
MAAVKKEGGA LSEAMSLEGD EWELSKENVQ PLRQGRIMST LQGALAQESA CNNTLQQQKR
AFEYEIRFYT GNDPLDVWDR YISWTEQNYP QGGKESNMST LLERAVEALQ GEKRYYSDPR
FLNLWLKLGR LCNEPLDMYS YLHNQGIGVS LAQFYISWAE EYEARENFRK ADAIFQEGIQ
QKAEPLERLQ SQHRQFQARV SRQTLLALEK EEEEEVFESS VPQRSTLAEL KSKGKKTARA
PIIRVGGALK APSQNRGLQN PFPQQMQNNS RITVFDENAD EASTAELSKP TVQPWIAPPM
PRAKENELQA GPWNTGRSLE HRPRGNTASL IAVPAVLPSF TPYVEETARQ PVMTPCKIEP
SINHILSTRK PGKEEGDPLQ RVQSHQQASE EKKEKMMYCK EKIYAGVGEF SFEEIRAEVF
RKKLKEQREA ELLTSAEKRA EMQKQIEEME KKLKEIQTTQ QERTGDQQEE TMPTKETTKL
QIASESQKIP GMTLSSSVCQ VNCCARETSL AENIWQEQPH SKGPSVPFSI FDEFLLSEKK
NKSPPADPPR VLAQRRPLAV LKTSESITSN EDVSPDVCDE FTGIEPLSED AIITGFRNVT
ICPNPEDTCD FARAARFVST PFHEIMSLKD LPSDPERLLP EEDLDVKTSE DQQTACGTIY
SQTLSIKKLS PIIEDSREAT HSSGFSGSSA SVASTSSIKC LQIPEKLELT NETSENPTQS
PWCSQYRRQL LKSLPELSAS AELCIEDRPM PKLEIEKEIE LGNEDYCIKR EYLICEDYKL
FWVAPRNSAE LTVIKVSSQP VPWDFYINLK LKERLNEDFD HFCSCYQYQD GCIVWHQYIN
CFTLQDLLQH SEYITHEITV LIIYNLLTIV EMLHKAEIVH GDLSPRCLIL RNRIHDPYDC
NKNNQALKIV DFSYSVDLRV QLDVFTLSGF RTVQILEGQK ILANCSSPYQ VDLFGIADLA
HLLLFKEHLQ VFWDGSFWKL SQNISELKDG ELWNKFFVRI LNANDEATVS VLGELAAEMN
GVFDTTFQSH LNKALWKVGK LTSPGALLFQ


Related products :

Catalog number Product name Quantity
BUB1_MOUSE ELISA Kit FOR Mitotic checkpoint serine per threonine-protein kinase BUB1; organism: Mouse; gene name: Bub1 96T
BUB1B_HUMAN Human ELISA Kit FOR Mitotic checkpoint serine per threonine-protein kinase BUB1 beta 96T
E1119d Mouse ELISA Kit FOR Mitotic checkpoint serine per threonine-protein kinase BUB1 beta 96T
CSB-EL002883MO Mouse Mitotic checkpoint serine per threonine-protein kinase BUB1 beta(BUB1B) ELISA kit 96T
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LF-PA41523 anti-Mitotic Checkpoint Kinase BUB1, Rabbit polyclonal to Mitotic Checkpoint Kinase BUB1, Isotype IgG, Host Rabbit 50 ug
CSB-EL002882HU Human Mitotic checkpoint serine_threonine-protein kinase BUB1(BUB1) ELISA kit 96T
CSB-EL002882MO Mouse Mitotic checkpoint serine_threonine-protein kinase BUB1(BUB1) ELISA kit 96T
CSB-EL002882HU Human Mitotic checkpoint serine_threonine-protein kinase BUB1(BUB1) ELISA kit SpeciesHuman 96T
CSB-EL002882MO Mouse Mitotic checkpoint serine_threonine-protein kinase BUB1(BUB1) ELISA kit SpeciesMouse 96T
CSB-EL002883MO Mouse Mitotic checkpoint serine_threonine-protein kinase BUB1 beta(BUB1B) ELISA kit 96T
CSB-EL002883HU Human Mitotic checkpoint serine_threonine-protein kinase BUB1 beta(BUB1B) ELISA kit 96T
CSB-EL002883HU Human Mitotic checkpoint serine_threonine-protein kinase BUB1 beta(BUB1B) ELISA kit SpeciesHuman 96T
CSB-EL002883MO Mouse Mitotic checkpoint serine_threonine-protein kinase BUB1 beta(BUB1B) ELISA kit SpeciesMouse 96T
GWB-462525 Mitotic Checkpoint Kinase BUB1 Rabbit anti-Human Polyclonal (N-Terminus) Antibody
20-373-85037 Checkpoint serine_threonine-protein kinase BUB1 - EC 2.7.11.1 Monoclonal 0.05 ml
20-373-85007 Checkpoint serine_threonine-protein kinase BUB1 - EC 2.7.11.1 Monoclonal 0.1 ml
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
LF-PA41523 anti_Mitotic Checkpoint Kinase BUB1 50 ug
26-354 PBK is a serine_threonine kinase related to the dual specific mitogen-activated protein kinase kinase (MAPKK) family. Evidence suggests that mitotic phosphorylation is required for its catalytic activ 0.05 mg
30-460 PBK is a serine_threonine kinase related to the dual specific mitogen-activated protein kinase kinase (MAPKK) family. Evidence suggests that mitotic phosphorylation is required for its catalytic activ 0.05 mg
EIAAB31333 Homo sapiens,Human,PAK1,PAK-1,PKN,PKN1,PRK1,PRKCL1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threo
EIAAB31331 PAK-1,Pkn,Pkn1,Prk1,Prkcl1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Rat,Rattus norvegicus,Serine_threonine-protein kinase N1,Seri
GWB-CEE83D Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
Pathways :
WP1493: Carbon assimilation C4 pathway
WP1659: Glycine, serine and threonine metabolism
WP2199: Seed Development
WP1566: Citrate cycle (TCA cycle)
WP2218: sGC
WP32: Translation Factors
WP210: Cytoplasmic Ribosomal Proteins
WP731: Sterol regulatory element binding protein related
WP2272: Pathogenic Escherichia coli infection
WP1654: gamma-Hexachlorocyclohexane degradation
WP232: G Protein Signaling Pathways
WP1502: Mitochondrial biogenesis
WP1690: Propanoate metabolism
WP1694: Pyrimidine metabolism
WP73: G Protein Signaling Pathways
WP1888: Post-translational protein modification
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1665: Limonene and pinene degradation
WP1613: 1,4-Dichlorobenzene degradation
WP1703: Streptomycin biosynthesis
WP1619: Amino sugar and nucleotide sugar metabolism
WP1371: G Protein Signaling Pathways
WP1675: Nitrogen metabolism
WP1909: Signal regulatory protein (SIRP) family interactions
WP253: Glycolysis

Related Genes :
[BUB1B BUBR1 MAD3L SSK1] Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC 2.7.11.1) (MAD3/BUB1-related protein kinase) (hBUBR1) (Mitotic checkpoint kinase MAD3L) (Protein SSK1)
[BUB1 BUB1L] Mitotic checkpoint serine/threonine-protein kinase BUB1 (hBUB1) (EC 2.7.11.1) (BUB1A)
[Bub1] Mitotic checkpoint serine/threonine-protein kinase BUB1 (mBUB1) (EC 2.7.11.1) (BUB1A)
[BUB1 YGR188C G7542] Checkpoint serine/threonine-protein kinase BUB1 (EC 2.7.11.1)
[bub1 SPCC1322.12c] Checkpoint serine/threonine-protein kinase bub1 (EC 2.7.11.1)
[BUB1 At2g20635 F23N11.4] Mitotic checkpoint serine/threonine-protein kinase BUB1 (AtBUB1) (EC 2.7.11.1) (Protein BUDDING UNINHIBITED BY BENZYMIDAZOL 1)
[BUB3] Mitotic checkpoint protein BUB3
[AURKB AIK2 AIM1 AIRK2 ARK2 STK1 STK12 STK5] Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (AIM-1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)
[Aurkb Aik2 Aim1 Airk2 Ark2 Stk1 Stk12 Stk5] Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)
[MAD1L1 MAD1 TXBP181] Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1) (Mitotic checkpoint MAD1 protein homolog) (HsMAD1) (hMAD1) (Tax-binding protein 181)
[Plk1 Plk] Serine/threonine-protein kinase PLK1 (EC 2.7.11.21) (Polo-like kinase 1) (PLK-1) (Serine/threonine-protein kinase 13) (STPK13)
[Aurkb Aik2 Aim1 Airk2 Ark2 Stk1 Stk12 Stk5] Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)
[AURKB AIK2 AIM1 AIRK2 ARK2 STK1 STK12 STK5] Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (AIM-1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)
[AURKB AIK2 AIM1 AIRK2 ARK2 STK1 STK12 STK5] Aurora kinase B (EC 2.7.11.1) (Aurora 1) (Aurora- and IPL1-like midbody-associated protein 1) (AIM-1) (Aurora/IPL1-related kinase 2) (ARK-2) (Aurora-related kinase 2) (STK-1) (Serine/threonine-protein kinase 12) (Serine/threonine-protein kinase 5) (Serine/threonine-protein kinase aurora-B)
[PLK1 PLK] Serine/threonine-protein kinase PLK1 (EC 2.7.11.21) (Polo-like kinase 1) (PLK-1) (Serine/threonine-protein kinase 13) (STPK13)
[MAD2L1 MAD2] Mitotic spindle assembly checkpoint protein MAD2A (HsMAD2) (Mitotic arrest deficient 2-like protein 1) (MAD2-like protein 1)
[CHEK2 CDS1 CHK2 RAD53] Serine/threonine-protein kinase Chk2 (EC 2.7.11.1) (CHK2 checkpoint homolog) (Cds1 homolog) (Hucds1) (hCds1) (Checkpoint kinase 2)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)
[MEC1 ESR1 SAD3 YBR136W YBR1012] Serine/threonine-protein kinase MEC1 (EC 2.7.11.1) (ATR homolog) (DNA-damage checkpoint kinase MEC1) (Mitosis entry checkpoint protein 1)
[mei-41 CG4252] Serine/threonine-protein kinase ATR (EC 2.7.11.1) (Ataxia telangiectasia and Rad3-related protein homolog) (ATR homolog) (dATR) (Meiotic protein 41)
[Plk1 Plk] Serine/threonine-protein kinase PLK1 (EC 2.7.11.21) (Polo-like kinase 1) (PLK-1)
[PLK1] Serine/threonine-protein kinase PLK1 (EC 2.7.11.21) (Polo-like kinase 1) (PLK-1)
[Chek1 Chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[chek1 chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1) (xChk1)
[air-2 stu-7 B0207.4] Aurora/IPL1-related protein kinase 2 (EC 2.7.11.1) (Serine/threonine-protein kinase aurora-B)
[Chek1 Chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[chk1 rad27 SPCC1259.13] Serine/threonine-protein kinase chk1 (EC 2.7.11.1) (Checkpoint kinase 1)
[Mad1l1 Mad1] Mitotic spindle assembly checkpoint protein MAD1 (Mitotic arrest deficient 1-like protein 1) (MAD1-like protein 1)
[AURKA AIK AIRK1 ARK1 AURA AYK1 BTAK IAK1 STK15 STK6] Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (hARK1) (Breast tumor-amplified kinase) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase aurora-A)

Bibliography :
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