CPLM-000754

Genbank Nucleotide ID

Mitotic checkpoint protein BUB3

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
8	MTGSNEFKLNQPPED	ubiquitination	[1, 2]
21	EDGISSVKFSPNTSQ	ubiquitination	[3]
52	PANSMRLKYQHTGAV	ubiquitination	[2, 4]
139	GTFSQPEKVYTLSVS	ubiquitination	[1, 2, 4]
179	QRRESSLKYQTRCIR	acetylation	[5]
179	QRRESSLKYQTRCIR	ubiquitination	[1, 2, 3]
191	CIRAFPNKQGYVLSS	ubiquitination	[1, 2, 3, 6, 7, 8]
216	DPSPEVQKKKYAFKC	ubiquitination	[1, 2, 3, 9, 10]
217	PSPEVQKKKYAFKCH	ubiquitination	[2]
218	SPEVQKKKYAFKCHR	ubiquitination	[2]
222	QKKKYAFKCHRLKEN	ubiquitination	[2]
322	QVTDAETKPKSPCT*	ubiquitination	[2, 3, 4]
324	TDAETKPKSPCT***	ubiquitination	[2]

[1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[9] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
Meierhofer D, Wang X, Huang L, Kaiser P.
J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
[10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]

Functional Description

Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1.

REPEAT 5 43 WD 1.
REPEAT 46 83 WD 2.
REPEAT 86 124 WD 3.
REPEAT 128 163 WD 4.
REPEAT 223 262 WD 5.
MOD_RES 179 179 N6-acetyllysine.
MOD_RES 211 211 Phosphoserine.
CROSSLNK 216 216 Glycyl lysine isopeptide (Lys-Gly)

Acetylation; ADP-ribosylation; Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition; Complete proteome; Isopeptide bond; Kinetochore; Meiosis; Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; WD repeat.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0000776; C:kinetochore; IDA:UniProtKB.
GO:0005634; C:nucleus; IDA:HPA.
GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:UniProtKB.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0007126; P:meiosis; IEA:UniProtKB-KW.
GO:0000070; P:mitotic sister chromatid segregation; IEA:Compara.
GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome.
GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO:0051983; P:regulation of chromosome segregation; IEA:Compara.

IPR020472; G-protein_beta_WD-40_rep.
IPR015943; WD40/YVTN_repeat-like_dom.
IPR001680; WD40_repeat.
IPR017986; WD40_repeat_dom.

PS00678; WD_REPEATS_1
PS50082; WD_REPEATS_2
PS50294; WD_REPEATS_REGION

PR00320; GPROTEINBRPT.