BUB1/YGR188C Protein Information

Standard Name	Bub1p
Systematic Name	Ygr188cp
ORF Classification	Verified
Description	Protein kinase involved in the cell cycle checkpoint into anaphase; forms complex with Mad1p and Bub3p crucial to preventing cell cycle progression into anaphase in presence of spindle damage; CDC28-mediated phosphorylation at Bub1p-T566 is important for degradation in anaphase and adaptation of checkpoint to prolonged mitotic arrest; associates with centromere DNA via Skp1p; BUB1 has a paralog, MAD3, that arose from the whole genome duplication (1, 2, 3, 4, 5, 6)
Name Description	Budding Uninhibited by Benzimidazole 7

Experimental Data
Molecules/cell	414 8

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,021
Molecular Weight (Da)	117,867
Isoelectric Point (pI)	6.69

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Bub1p (InterPro)
Physical Interactions	There are 41 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000126B2E \| P41695 MIPS: YGR188C NCBI: 126030699 \| 126030701 \| 126030703 \| 1323334 \| 1430954 \| 1705511 \| 223674017 \| 223674018 \| 398366073 \| 475128 \| NP_011704.3 GenBank/EMBL/DDBJ: DAA08282.1 \| L32027 \| X99074 \| Z72973
External Classifications	EC: 2.7.11.1 [Non-specific serine/threonine protein kinase]

Amino Acid Sequence (or in FASTA format)
1 MNLDLGSTVR GYESDKDTFP QSKGVSSSQK EQHSQLNQTK IAYEQRLLND 51 LEDMDDPLDL FLDYMIWIST SYIEVDSESG QEVLRSTMER CLIYIQDMET 101 YRNDPRFLKI WIWYINLFLS NNFHESENTF KYMFNKGIGT KLSLFYEEFS 151 KLLENAQFFL EAKVLLELGA ENNCRPYNRL LRSLSNYEDR LREMNIVENQ 201 NSVPDSRERL KGRLIYRTAP FFIRKFLTSS LMTDDKENRA NLNSNVGVGK 251 SAPNVYQDSI VVADFKSETE RLNLNSSKQP SNQRLKNGNK KTSIYADQKQ 301 SNNPVYKLIN TPGRKPERIV FNFNLIYPEN DEEFNTEEIL AMIKGLYKVQ 351 RRGKKHTEDY TSDKNRKKRK LDVLVERRQD LPSSQPPVVP KSTRIEVFKD 401 DDNPSQSTHH KNTQVQVQTT TSILPLKPVV DGNLAHETPV KPSLTSNASR 451 SPTVTAFSKD AINEVFSMFN QHYSTPGALL DGDDTTTSKF NVFENFTQEF 501 TAKNIEDLTE VKDPKQETVS QQTTSTNETN DRYERLSNSS TRPEKADYMT 551 PIKETTETDV VPIIQTPKEQ IRTEDKKSGD NTETQTQLTS TTIQSSPFLT 601 QPEPQAEKLL QTAEHSEKSK EHYPTIIPPF TKIKNQPPVI IENPLSNNLR 651 AKFLSEISPP LFQYNTFYNY NQELKMSSLL KKIHRVSRNE NKNPIVDFKK 701 TGDLYCIRGE LGEGGYATVY LAESSQGHLR ALKVEKPASV WEYYIMSQVE 751 FRLRKSTILK SIINASALHL FLDESYLVLN YASQGTVLDL INLQREKAID 801 GNGIMDEYLC MFITVELMKV LEKIHEVGII HGDLKPDNCM IRLEKPGEPL 851 GAHYMRNGED GWENKGIYLI DFGRSFDMTL LPPGTKFKSN WKADQQDCWE 901 MRAGKPWSYE ADYYGLAGVI HSMLFGKFIE TIQLQNGRCK LKNPFKRYWK 951 KEIWGVIFDL LLNSGQASNQ ALPMTEKIVE IRNLIESHLE QHAENHLRNV 1001 ILSIEEELSH FQYKGKPSRR F*

Amino Acid Sequence (or in FASTA format)

       1  MNLDLGSTVR GYESDKDTFP QSKGVSSSQK EQHSQLNQTK IAYEQRLLND
      51  LEDMDDPLDL FLDYMIWIST SYIEVDSESG QEVLRSTMER CLIYIQDMET
     101  YRNDPRFLKI WIWYINLFLS NNFHESENTF KYMFNKGIGT KLSLFYEEFS
     151  KLLENAQFFL EAKVLLELGA ENNCRPYNRL LRSLSNYEDR LREMNIVENQ
     201  NSVPDSRERL KGRLIYRTAP FFIRKFLTSS LMTDDKENRA NLNSNVGVGK
     251  SAPNVYQDSI VVADFKSETE RLNLNSSKQP SNQRLKNGNK KTSIYADQKQ
     301  SNNPVYKLIN TPGRKPERIV FNFNLIYPEN DEEFNTEEIL AMIKGLYKVQ
     351  RRGKKHTEDY TSDKNRKKRK LDVLVERRQD LPSSQPPVVP KSTRIEVFKD
     401  DDNPSQSTHH KNTQVQVQTT TSILPLKPVV DGNLAHETPV KPSLTSNASR
     451  SPTVTAFSKD AINEVFSMFN QHYSTPGALL DGDDTTTSKF NVFENFTQEF
     501  TAKNIEDLTE VKDPKQETVS QQTTSTNETN DRYERLSNSS TRPEKADYMT
     551  PIKETTETDV VPIIQTPKEQ IRTEDKKSGD NTETQTQLTS TTIQSSPFLT
     601  QPEPQAEKLL QTAEHSEKSK EHYPTIIPPF TKIKNQPPVI IENPLSNNLR
     651  AKFLSEISPP LFQYNTFYNY NQELKMSSLL KKIHRVSRNE NKNPIVDFKK
     701  TGDLYCIRGE LGEGGYATVY LAESSQGHLR ALKVEKPASV WEYYIMSQVE
     751  FRLRKSTILK SIINASALHL FLDESYLVLN YASQGTVLDL INLQREKAID
     801  GNGIMDEYLC MFITVELMKV LEKIHEVGII HGDLKPDNCM IRLEKPGEPL
     851  GAHYMRNGED GWENKGIYLI DFGRSFDMTL LPPGTKFKSN WKADQQDCWE
     901  MRAGKPWSYE ADYYGLAGVI HSMLFGKFIE TIQLQNGRCK LKNPFKRYWK
     951  KEIWGVIFDL LLNSGQASNQ ALPMTEKIVE IRNLIESHLE QHAENHLRNV
    1001  ILSIEEELSH FQYKGKPSRR F*

external links for Bub1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Candida (CGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CandidaDB)	CYC2008 (complexes)	Pfam domains
YGOB	Complexome	YeastRC Structure Prediction (Seattle)
YOGY	DIP
	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Bub1p

1)	Farr KA and Hoyt MA (1998) Bub1p kinase activates the Saccharomyces cerevisiae spindle assembly checkpoint. Mol Cell Biol 18(5):2738-47
2)	Roberts BT, et al. (1994) The Saccharomyces cerevisiae checkpoint gene BUB1 encodes a novel protein kinase. Mol Cell Biol 14(12):8282-91
3)	Brady DM and Hardwick KG (2000) Complex formation between Mad1p, Bub1p and Bub3p is crucial for spindle checkpoint function. Curr Biol 10(11):675-8
4)	Kitagawa K, et al. (2003) Requirement of Skp1-Bub1 interaction for kinetochore-mediated activation of the spindle checkpoint. Mol Cell 11(5):1201-13
5)	Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
6)	Goto GH, et al. (2011) Bub1-mediated adaptation of the spindle checkpoint. PLoS Genet 7(1):e1001282
7)	Hoyt MA, et al. (1991) S. cerevisiae genes required for cell cycle arrest in response to loss of microtubule function. Cell 66(3):507-17
8)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41