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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-NOV-2017, entry version 182.
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]
ENZYME 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]
CASPASE-3 CLEAVAGE AT ASP-579 AND ASP-610, 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]
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).
[37]
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).
[38]
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).
[39]
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: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME 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.
{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:9763420}.
-!- INTERACTION:
O43684:BUB3; NbExp=9; IntAct=EBI-1001438, EBI-1050987;
Q12834:CDC20; NbExp=30; IntAct=EBI-1001438, EBI-367462;
Q02224:CENPE; NbExp=4; IntAct=EBI-1001438, EBI-1375040;
P45481:Crebbp (xeno); NbExp=3; IntAct=EBI-1001438, EBI-296306;
Q92831:KAT2B; NbExp=14; IntAct=EBI-1001438, EBI-477430;
Q8NG31-2:KNL1; NbExp=10; IntAct=EBI-1001438, EBI-10973816;
Q13257:MAD2L1; NbExp=14; IntAct=EBI-1001438, EBI-78203;
Q8IXJ6:SIRT2; NbExp=3; IntAct=EBI-1001438, EBI-477232;
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;
Note=No experimental confirmation available.;
Name=3;
IsoId=O60566-3; Sequence=VSP_036473;
Note=No experimental confirmation available.;
-!- 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.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
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.
UniGene; Hs.513645; -.
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; -.
ProteinModelPortal; O60566; -.
SMR; O60566; -.
BioGrid; 107166; 98.
CORUM; O60566; -.
DIP; DIP-24203N; -.
ELM; O60566; -.
IntAct; O60566; 69.
MINT; MINT-2796866; -.
STRING; 9606.ENSP00000287598; -.
iPTMnet; O60566; -.
PhosphoSitePlus; O60566; -.
BioMuta; BUB1B; -.
EPD; O60566; -.
MaxQB; O60566; -.
PaxDb; O60566; -.
PeptideAtlas; O60566; -.
PRIDE; O60566; -.
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; -.
EuPathDB; HostDB:ENSG00000156970.12; -.
GeneCards; BUB1B; -.
H-InvDB; HIX0012121; -.
HGNC; HGNC:1149; BUB1B.
HPA; HPA008419; -.
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; ENSGT00520000055622; -.
HOVERGEN; HBG050748; -.
InParanoid; O60566; -.
KO; K06637; -.
OMA; ATHSSGF; -.
OrthoDB; EOG091G01MC; -.
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.
SignaLink; O60566; -.
SIGNOR; O60566; -.
EvolutionaryTrace; O60566; -.
GeneWiki; BUB1B; -.
GenomeRNAi; 701; -.
PRO; PR:O60566; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000156970; -.
CleanEx; HS_BUB1B; -.
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:0051233; C:spindle midzone; NAS: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:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IBA:GO_Central.
GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IEA:Ensembl.
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:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0034501; P:protein localization to kinetochore; IPI:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR015661; Bub1/Mad3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR013212; Mad3/Bub1_I.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
PANTHER; PTHR14030; PTHR14030; 1.
Pfam; PF08311; Mad3_BUB1_I; 1.
Pfam; PF00069; Pkinase; 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;
Complete proteome; 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 Mitotic checkpoint serine/threonine-
protein kinase BUB1 beta.
/FTId=PRO_0000085673.
DOMAIN 62 226 BUB1 N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00822}.
DOMAIN 766 1050 Protein kinase.
NP_BIND 772 780 ATP. {ECO:0000250}.
REGION 152 185 Necessary for interaction with KNL1.
{ECO:0000269|PubMed:17981135}.
MOTIF 111 118 Nuclear localization signal.
{ECO:0000255}.
MOTIF 224 232 D-box.
COMPBIAS 209 215 Poly-Glu.
ACT_SITE 882 882 Proton acceptor. {ECO:0000250}.
BINDING 795 795 ATP. {ECO:0000250}.
SITE 579 580 Cleavage; by caspase-3.
SITE 610 611 Cleavage; by caspase-3.
MOD_RES 250 250 N6-acetyllysine; by PCAF.
{ECO:0000269|PubMed:19407811}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19015317}.
MOD_RES 543 543 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19015317}.
MOD_RES 665 665 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 670 670 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19015317}.
MOD_RES 676 676 Phosphoserine; by PLK1.
{ECO:0000269|PubMed:17785528}.
MOD_RES 697 697 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 792 792 Phosphothreonine; by PLK1.
{ECO:0000269|PubMed:17376779}.
MOD_RES 1008 1008 Phosphothreonine; by PLK1.
{ECO:0000269|PubMed:17376779}.
MOD_RES 1042 1042 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1043 1043 Phosphoserine.
{ECO:0000269|PubMed:19015317}.
VAR_SEQ 80 80 R -> RWVFLFHKDNRNINR (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036473.
VAR_SEQ 113 166 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036474.
VAR_SEQ 522 522 K -> KVSLSL (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036475.
VAR_SEQ 608 675 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036476.
VARIANT 15 15 M -> T (in a colorectal cancer cell
line). {ECO:0000269|PubMed:9521327}.
/FTId=VAR_008852.
VARIANT 36 36 R -> Q (in PCS; dbSNP:rs534297115).
{ECO:0000269|PubMed:16411201}.
/FTId=VAR_028921.
VARIANT 40 40 T -> M (in dbSNP:rs56079734).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040402.
VARIANT 349 349 R -> Q (in dbSNP:rs1801376).
{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}.
/FTId=VAR_008853.
VARIANT 378 378 P -> S (in dbSNP:rs17851677).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_054549.
VARIANT 390 390 E -> D (in dbSNP:rs1017842).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_028922.
VARIANT 550 550 R -> Q (in MVA1; heterozygous compound
with nonsense mutation;
dbSNP:rs28989187).
{ECO:0000269|PubMed:15475955}.
/FTId=VAR_028923.
VARIANT 618 618 V -> A (in colorectal cancer;
dbSNP:rs1801528).
{ECO:0000269|PubMed:10366450,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_008854.
VARIANT 814 814 R -> H (in MVA1; heterozygous compound
with nonsense mutation;
dbSNP:rs28989182).
{ECO:0000269|PubMed:15475955}.
/FTId=VAR_028924.
VARIANT 844 844 L -> F (in MVA1; associated with H-921;
heterozygous compound with nonsense
mutation; dbSNP:rs28989181).
{ECO:0000269|PubMed:15475955}.
/FTId=VAR_028925.
VARIANT 909 909 I -> T (in MVA1; heterozygous compound
with nonsense mutation;
dbSNP:rs28989184).
{ECO:0000269|PubMed:15475955}.
/FTId=VAR_028926.
VARIANT 921 921 Q -> H (in MVA1; associated with F-844;
heterozygous compound with nonsense
mutation; dbSNP:rs28989183).
{ECO:0000269|PubMed:15475955}.
/FTId=VAR_028927.
VARIANT 1012 1012 L -> P (in MVA1; heterozygous compound
with nonsense mutation;
dbSNP:rs28989185).
{ECO:0000269|PubMed:15475955}.
/FTId=VAR_028928.
MUTAGEN 159 159 A->W: Loss of interaction with KNL1.
{ECO:0000269|PubMed:17981135}.
MUTAGEN 175 175 F->A: Loss of interaction with KNL1.
{ECO:0000269|PubMed:17981135}.
MUTAGEN 579 579 D->E: Abolishes the cleavage by caspase-
3. {ECO:0000269|PubMed:16227576}.
MUTAGEN 610 610 D->E: Abolishes the cleavage by caspase-
3. {ECO:0000269|PubMed:16227576}.
MUTAGEN 620 620 T->A: Induces chromosome congression
defects and mitotic delay.
{ECO:0000269|PubMed:17785528}.
MUTAGEN 795 795 K->A: Does not abolish the capacity to
inhibit APC/CDC20.
{ECO:0000269|PubMed:11702782,
ECO:0000269|PubMed:12925705}.
MUTAGEN 795 795 K->R: Inhibits kinase activity.
{ECO:0000269|PubMed:11702782,
ECO:0000269|PubMed:12925705}.
CONFLICT 248 249 AL -> VF (in Ref. 1; AAC23736).
{ECO:0000305}.
CONFLICT 283 283 S -> P (in Ref. 8; BAG35587).
{ECO:0000305}.
CONFLICT 788 788 S -> F (in Ref. 2; AAC06260).
{ECO:0000305}.
CONFLICT 1018 1018 E -> K (in Ref. 3; AAC33435).
{ECO:0000305}.
TURN 26 28 {ECO:0000244|PDB:4GGD}.
HELIX 60 65 {ECO:0000244|PDB:2WVI}.
HELIX 75 88 {ECO:0000244|PDB:2WVI}.
HELIX 94 96 {ECO:0000244|PDB:3SI5}.
HELIX 98 108 {ECO:0000244|PDB:2WVI}.
TURN 109 111 {ECO:0000244|PDB:2WVI}.
HELIX 113 115 {ECO:0000244|PDB:2WVI}.
HELIX 119 131 {ECO:0000244|PDB:2WVI}.
HELIX 135 144 {ECO:0000244|PDB:2WVI}.
HELIX 152 164 {ECO:0000244|PDB:2WVI}.
HELIX 168 180 {ECO:0000244|PDB:2WVI}.
HELIX 186 218 {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


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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


 

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