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O43683 (BUB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitotic checkpoint serine/threonine-protein kinase BUB1

Short name=hBUB1
EC=2.7.11.1
Alternative name(s):
BUB1A
Gene names
Name:BUB1
Synonyms:BUB1L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1085 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Plays an important role in defining SGOL1 localization and thereby affects sister chromatid cohesion. Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of 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. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. Ref.4 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.21

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Autophosphorylated when the cells enters mitosis.

Subunit structure

Interacts with BUB3 and CASC5. Interacts (when phosphorylated) with PLK1. The BUB1-BUB3 complex interacts with MAD1L1. Interacts with SV40 Large T antigen; this interaction induces activation of a DNA damage response and promotes p53/TP53 stabilization and phosphorylation Probable. Ref.4 Ref.11 Ref.13 Ref.14 Ref.20

Subcellular location

Nucleus. Chromosomecentromerekinetochore. Note: Nuclear in interphase cells. Accumulates gradually during G1 and S phase of the cell cycle, peaks at G2/M, and drops dramatically after mitosis. Localizes to the outer kinetochore. Kinetochore localization is required for normal mitotic timing and checkpoint response to spindle damage and occurs very early in prophase. AURKB, CASC5 and INCENP are required for kinetochore localization By similarity. Ref.10 Ref.13 Ref.14 Ref.15

Tissue specificity

High expression in testis and thymus, less in colon, spleen, lung and small intestine. Expressed in fetal thymus, bone marrow, heart, liver, spleen and thymus. Expression is associated with cells/tissues with a high mitotic index.

Induction

Inhibited by phorbol 12-myristate 13-acetate (PMA).

Domain

The KEN box is required for its ubiquitination and degradation. Ref.15

BUB1 N-terminal domain directs kinetochore localization and binding to BUB3. Ref.15

Post-translational modification

Upon spindle-assembly checkpoint activation it is hyperphosphorylated and its kinase activity toward CDC20 is stimulated. Phosphorylation at Thr-609 is required for interaction with PLK1, phosphorylation at this site probably creates a binding site for the POLO-box domain of PLK1, thus enhancing the PLK1-BUB1 interaction. Ref.4 Ref.11 Ref.13

Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1. Ref.15

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. BUB1 subfamily.

Contains 1 BUB1 N-terminal domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Cell division
Chromosome partition
Host-virus interaction
Mitosis
   Cellular componentCentromere
Chromosome
Kinetochore
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from electronic annotation. Source: Ensembl

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle checkpoint

Traceable author statement Ref.1. Source: ProtInc

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic spindle assembly checkpoint

Traceable author statement Ref.2. Source: ProtInc

positive regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of chromosome segregation

Inferred from mutant phenotype Ref.21. Source: UniProtKB

regulation of sister chromatid cohesion

Inferred from direct assay Ref.12. Source: UniProtKB

spindle assembly checkpoint

Inferred from direct assay Ref.10Ref.11. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcondensed chromosome kinetochore

Inferred from direct assay PubMed 19465021. Source: UniProtKB

condensed nuclear chromosome, centromeric region

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay Ref.10Ref.13. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.4Ref.11Ref.13Ref.14. Source: UniProtKB

protein kinase activity

Traceable author statement Ref.4. Source: ProtInc

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P030702EBI-748936,EBI-617698From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43683-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43683-2)

The sequence of this isoform differs from the canonical sequence as follows:
     876-932: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.
Isoform 3 (identifier: O43683-3)

The sequence of this isoform differs from the canonical sequence as follows:
     10-29: Missing.
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10851085Mitotic checkpoint serine/threonine-protein kinase BUB1
PRO_0000085671

Regions

Domain11 – 182172BUB1 N-terminal
Domain787 – 1085299Protein kinase
Nucleotide binding793 – 8019ATP By similarity
Region1 – 146146Necessary for kinetochore localization
Region99 – 13234Necessary for interaction with CASC5
Region229 – 25628Necessary for interaction with BUB3
Region458 – 47619Essential for loading of BUBR1, MAD1L1 and MAD2L1 to kinetochores
Motif58 – 658Nuclear localization signal Potential
Motif535 – 5373KEN box 1
Motif625 – 6273KEN box 2

Sites

Active site9171Proton acceptor By similarity
Binding site8211ATP By similarity

Amino acid modifications

Modified residue3141Phosphoserine Ref.16 Ref.22
Modified residue3751Phosphoserine Ref.22
Modified residue5631Phosphoserine Ref.22 Ref.23
Modified residue5931Phosphoserine Ref.18 Ref.23 Ref.24
Modified residue5961Phosphoserine Ref.17 Ref.18 Ref.22 Ref.23 Ref.24 Ref.26
Modified residue6091Phosphothreonine; by CDK1 Ref.13
Modified residue6551Phosphoserine Ref.17 Ref.22

Natural variations

Alternative sequence10 – 2920Missing in isoform 3.
VSP_054760
Alternative sequence876 – 93257Missing in isoform 2.
VSP_054761
Natural variant201G → D. Ref.28
Corresponds to variant rs35890336 [ dbSNP | Ensembl ].
VAR_040400
Natural variant361E → D in colorectal cancer. Ref.5
Corresponds to variant rs1801328 [ dbSNP | Ensembl ].
VAR_008849
Natural variant2591Y → C in pancreatic cancer; associated with N-265; failure to rescue the spindle-assembly checkpoint activity as a result of a deficient recruitment of MAD2L1 and BUBR1 to kinetochores; efficient restoration of chromosome congression; reduced binding to BUB3; rescue of the ability of kinetochores to bind SGOL1 and CENPF but not MCAK. Ref.21 Ref.27
VAR_015687
Natural variant2651H → N in pancreatic cancer; associated with C-259; complete rescue of the spindle-assembly checkpoint activity; increased rate of chromosome congression errors. Ref.21 Ref.27
VAR_015688
Natural variant4921S → Y in colorectal cancer. Ref.1
VAR_008850
Natural variant5341N → D. Ref.28
Corresponds to variant rs36109304 [ dbSNP | Ensembl ].
VAR_040401
Natural variant6481P → R in colorectal cancer. Ref.5
VAR_008851

Experimental info

Mutagenesis1061A → D or W: Loss of interaction with CASC5. Ref.14
Mutagenesis1221L → G: Loss of interaction with CASC5. Ref.14
Mutagenesis1301A → S: Partial rescue of the spindle-assembly checkpoint activity. Increased rate of chromosome congression errors. Impaired localization to kinetochores and loss of kinetochore binding of CENPF, SGOL1 and BUBR1 but not of MCAK, MAD1L1 or MAD2L1. Ref.21
Mutagenesis5351K → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-536 and A-537. Ref.15
Mutagenesis5361E → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-535 and A-537. Ref.15
Mutagenesis5371N → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-535 and A-536. Ref.15
Mutagenesis6091T → A: Diminished interaction with PLK1. Ref.13
Mutagenesis6251K → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-626 and A-627. Ref.15
Mutagenesis6261E → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-625 and A-627. Ref.15
Mutagenesis6271N → A: Loss of ubiquitination and CDH1-dependent degradation; when associated with A-625 and A-626. Ref.15
Mutagenesis8211K → A: Loss of activity. Ref.4
Sequence conflict701S → T in AAC06259. Ref.5
Sequence conflict276 – 2794MKRK → IRHE in AAC39546. Ref.9

Secondary structure

.......................................................................... 1085
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 38AE5E1F88C53BDC

FASTA1,085122,375
        10         20         30         40         50         60 
MDTPENVLQM LEAHMQSYKG NDPLGEWERY IQWVEENFPE NKEYLITLLE HLMKEFLDKK 

        70         80         90        100        110        120 
KYHNDPRFIS YCLKFAEYNS DLHQFFEFLY NHGIGTLSSP LYIAWAGHLE AQGELQHASA 

       130        140        150        160        170        180 
VLQRGIQNQA EPREFLQQQY RLFQTRLTET HLPAQARTSE PLHNVQVLNQ MITSKSNPGN 

       190        200        210        220        230        240 
NMACISKNQG SELSGVISSA CDKESNMERR VITISKSEYS VHSSLASKVD VEQVVMYCKE 

       250        260        270        280        290        300 
KLIRGESEFS FEELRAQKYN QRRKHEQWVN EDRHYMKRKE ANAFEEQLLK QKMDELHKKL 

       310        320        330        340        350        360 
HQVVETSHED LPASQERSEV NPARMGPSVG SQQELRAPCL PVTYQQTPVN MEKNPREAPP 

       370        380        390        400        410        420 
VVPPLANAIS AALVSPATSQ SIAPPVPLKA QTVTDSMFAV ASKDAGCVNK STHEFKPQSG 

       430        440        450        460        470        480 
AEIKEGCETH KVANTSSFHT TPNTSLGMVQ ATPSKVQPSP TVHTKEALGF IMNMFQAPTL 

       490        500        510        520        530        540 
PDISDDKDEW QSLDQNEDAF EAQFQKNVRS SGAWGVNKII SSLSSAFHVF EDGNKENYGL 

       550        560        570        580        590        600 
PQPKNKPTGA RTFGERSVSR LPSKPKEEVP HAEEFLDDST VWGIRCNKTL APSPKSPGDF 

       610        620        630        640        650        660 
TSAAQLASTP FHKLPVESVH ILEDKENVVA KQCTQATLDS CEENMVVPSR DGKFSPIQEK 

       670        680        690        700        710        720 
SPKQALSSHM YSASLLRLSQ PAAGGVLTCE AELGVEACRL TDTDAAIAED PPDAIAGLQA 

       730        740        750        760        770        780 
EWMQMSSLGT VDAPNFIVGN PWDDKLIFKL LSGLSKPVSS YPNTFEWQCK LPAIKPKTEF 

       790        800        810        820        830        840 
QLGSKLVYVH HLLGEGAFAQ VYEATQGDLN DAKNKQKFVL KVQKPANPWE FYIGTQLMER 

       850        860        870        880        890        900 
LKPSMQHMFM KFYSAHLFQN GSVLVGELYS YGTLLNAINL YKNTPEKVMP QGLVISFAMR 

       910        920        930        940        950        960 
MLYMIEQVHD CEIIHGDIKP DNFILGNGFL EQDDEDDLSA GLALIDLGQS IDMKLFPKGT 

       970        980        990       1000       1010       1020 
IFTAKCETSG FQCVEMLSNK PWNYQIDYFG VAATVYCMLF GTYMKVKNEG GECKPEGLFR 

      1030       1040       1050       1060       1070       1080 
RLPHLDMWNE FFHVMLNIPD CHHLPSLDLL RQKLKKVFQQ HYTNKIRALR NRLIVLLLEC 


KRSRK 

« Hide

Isoform 2 [UniParc].

Checksum: 9D5F967383751D9C
Show »

FASTA1,028115,843
Isoform 3 [UniParc].

Checksum: E6BD9A1AA4ADAA71
Show »

FASTA1,065120,002

References

« Hide 'large scale' references
[1]"Mutations of mitotic checkpoint genes in human cancers."
Cahill D.P., Lengauer C., Yu J., Riggins G.J., Willson J.K.V., Markowitz S.D., Kinzler K.W., Vogelstein B.
Nature 392:300-303(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT TYR-492.
[2]"Human Bub1: a putative spindle checkpoint kinase closely linked to cell proliferation."
Ouyang B., Lan Z., Meadows J., Pan H., Fukasawa K., Li W., Dai W.
Cell Growth Differ. 9:877-885(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The human homologue of Bub3 is required for kinetochore localization of Bub1 and a Mad3/Bub1-related protein kinase."
Taylor S.S., Ha E., McKeon F.
J. Cell Biol. 142:1-11(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Phosphorylation of human MAD1 by the BUB1 kinase in vitro."
Seeley T.W., Wang L., Zhen J.Y.
Biochem. Biophys. Res. Commun. 257:589-595(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, INTERACTION WITH BUB3 AND MAD1L1, MUTAGENESIS OF LYS-821.
Tissue: Testis.
[5]"Characterization of MAD2B and other mitotic spindle checkpoint genes."
Cahill D.P., da Costa L.T., Carson-Walter E.B., Kinzler K.W., Vogelstein B., Lengauer C.
Genomics 58:181-187(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ASP-36 AND ARG-648.
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[9]"Mammalian BUB1 protein kinases: map positions and in vivo expression."
Pangilinan F., Li Q., Weaver T., Lewis B.C., Dang C.V., Spencer F.
Genomics 46:379-388(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 276-1085.
[10]"Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression."
Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S.
J. Cell Sci. 117:1577-1589(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C inhibition by the spindle checkpoint."
Tang Z., Shu H., Oncel D., Chen S., Yu H.
Mol. Cell 16:387-397(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH BUB3.
[12]"Human Bub1 defines the persistent cohesion site along the mitotic chromosome by affecting Shugoshin localization."
Kitajima T.S., Hauf S., Ohsugi M., Yamamoto T., Watanabe Y.
Curr. Biol. 15:353-359(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is required for the kinetochore localization of Plk1."
Qi W., Tang Z., Yu H.
Mol. Biol. Cell 17:3705-3716(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLK1, PHOSPHORYLATION AT THR-609, MUTAGENESIS OF THR-609.
[14]"Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic checkpoint through direct interaction with Bub1 and BubR1."
Kiyomitsu T., Obuse C., Yanagida M.
Dev. Cell 13:663-676(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CASC5, MUTAGENESIS OF ALA-106 AND LEU-122.
[15]"KEN-box-dependent degradation of the Bub1 spindle checkpoint kinase by the anaphase-promoting complex/cyclosome."
Qi W., Yu H.
J. Biol. Chem. 282:3672-3679(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, DOMAIN KEN BOX, MUTAGENESIS OF LYS-535; GLU-536; ASN-537; LYS-625; GLU-626 AND ASN-627.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593 AND SER-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Simian virus 40 large T antigen disrupts genome integrity and activates a DNA damage response via Bub1 binding."
Hein J., Boichuk S., Wu J., Cheng Y., Freire R., Jat P.S., Roberts T.M., Gjoerup O.V.
J. Virol. 83:117-127(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[21]"Bub1 regulates chromosome segregation in a kinetochore-independent manner."
Klebig C., Korinth D., Meraldi P.
J. Cell Biol. 185:841-858(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ALA-130, CHARACTERIZATION OF VARIANTS CYS-259 AND ASN-265.
[22]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-375; SER-563; SER-596 AND SER-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563; SER-593 AND SER-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[24]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593 AND SER-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"A double missense variation of the BUB1 gene and a defective mitotic spindle checkpoint in the pancreatic cancer cell line Hs766T."
Hempen P.M., Kurpad H., Calhoun E.S., Abraham S., Kern S.E.
Hum. Mutat. 21:445-445(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PANCREATIC CANCER CYS-259 AND ASN-265.
[28]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-20 AND ASP-534.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF046078 mRNA. Translation: AAC12729.1.
AF043294 mRNA. Translation: AAB97855.2.
AF053305 mRNA. Translation: AAC06259.1.
AF047471 mRNA. Translation: AAC03122.1.
AF139363 expand/collapse EMBL AC list , AF139349, AF139350, AF139351, AF139352, AF139353, AF139354, AF139355, AF139356, AF139357, AF139358, AF139359, AF139360, AF139361, AF139362 Genomic DNA. Translation: AAD43675.1.
AC114776 Genomic DNA. Translation: AAY14706.1.
AC226101 Genomic DNA. No translation available.
CH471237 Genomic DNA. Translation: EAW50355.1.
BC028201 mRNA. Translation: AAH28201.1.
AF011387 mRNA. Translation: AAC39546.1.
CCDSCCDS33273.1.
RefSeqNP_001265546.1. NM_001278617.1. [O43683-2]
NP_004327.1. NM_004336.4. [O43683-1]
UniGeneHs.469649.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LAHNMR-A1-150[»]
3E7EX-ray2.31A724-1085[»]
4A1GX-ray2.60A/B/C/D1-150[»]
ProteinModelPortalO43683.
SMRO43683. Positions 1-150, 735-1080.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107164. 32 interactions.
DIPDIP-24206N.
IntActO43683. 28 interactions.
MINTMINT-1460788.
STRING9606.ENSP00000302530.

Chemistry

BindingDBO43683.
ChEMBLCHEMBL1772932.

PTM databases

PhosphoSiteO43683.

Proteomic databases

MaxQBO43683.
PaxDbO43683.
PRIDEO43683.

Protocols and materials databases

DNASU699.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302759; ENSP00000302530; ENSG00000169679.
ENST00000409311; ENSP00000386701; ENSG00000169679.
ENST00000535254; ENSP00000441013; ENSG00000169679.
GeneID699.
KEGGhsa:699.
UCSCuc002tgc.3. human. [O43683-1]

Organism-specific databases

CTD699.
GeneCardsGC02M111395.
HGNCHGNC:1148. BUB1.
HPAHPA006123.
MIM602452. gene.
neXtProtNX_O43683.
Orphanet1052. Mosaic variegated aneuploidy syndrome.
PharmGKBPA81.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG317001.
HOGENOMHOG000231751.
HOVERGENHBG003709.
InParanoidO43683.
KOK02178.
OMADPLDVYD.
PhylomeDBO43683.
TreeFamTF105455.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkO43683.

Gene expression databases

ArrayExpressO43683.
BgeeO43683.
CleanExHS_BUB1.
GenevestigatorO43683.

Family and domain databases

InterProIPR015661. Bub1/Mad3.
IPR011009. Kinase-like_dom.
IPR013212. Mad3_BUB1_I.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR14030. PTHR14030. 1 hit.
PfamPF08311. Mad3_BUB1_I. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00777. Mad3_BUB1_I. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51489. BUB1_N. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBub1. human.
EvolutionaryTraceO43683.
GeneWikiBUB1.
GenomeRNAi699.
NextBio2860.
PROO43683.
SOURCESearch...

Entry information

Entry nameBUB1_HUMAN
AccessionPrimary (citable) accession number: O43683
Secondary accession number(s): E9PC26 expand/collapse secondary AC list , F5GXI5, O43430, O43643, O60626, Q53QE4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM