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Protein

Mitotic checkpoint serine/threonine-protein kinase BUB1 beta

Gene

BUB1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Kinase activity stimulated by CENPE.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei795ATPBy similarity1
Active sitei882Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi772 – 780ATPBy similarity9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS08163-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SignaLinkiO60566.
SIGNORiO60566.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitotic checkpoint serine/threonine-protein kinase BUB1 beta (EC:2.7.11.1)
Alternative name(s):
MAD3/BUB1-related protein kinase
Short name:
hBUBR1
Mitotic checkpoint kinase MAD3L
Protein SSK1
Gene namesi
Name:BUB1B
Synonyms:BUBR1, MAD3L, SSK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:1149. BUB1B.

Subcellular locationi

GO - Cellular componenti

  • anaphase-promoting complex Source: ProtInc
  • condensed chromosome kinetochore Source: UniProtKB
  • condensed chromosome outer kinetochore Source: UniProtKB
  • condensed nuclear chromosome kinetochore Source: Ensembl
  • cytoplasm Source: LIFEdb
  • cytosol Source: Reactome
  • kinetochore Source: UniProtKB
  • microtubule organizing center Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: BHF-UCL
  • spindle midzone Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in BUB1B are associated with tumor formation.

Premature chromatid separation trait (PCS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionConsists 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.
See also OMIM:176430
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02892136R → Q in PCS. 1 PublicationCorresponds to variant rs534297115dbSNPEnsembl.1
Mosaic variegated aneuploidy syndrome 1 (MVA1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. MVA1 is caused by biallelic mutations in the BUB1B gene.
Disease descriptionA 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.
See also OMIM:257300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_028923550R → Q in MVA1; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989187dbSNPEnsembl.1
Natural variantiVAR_028924814R → H in MVA1; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989182dbSNPEnsembl.1
Natural variantiVAR_028925844L → F in MVA1; associated with H-921; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989181dbSNPEnsembl.1
Natural variantiVAR_028926909I → T in MVA1; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989184dbSNPEnsembl.1
Natural variantiVAR_028927921Q → H in MVA1; associated with F-844; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989183dbSNPEnsembl.1
Natural variantiVAR_0289281012L → P in MVA1; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989185dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi159A → W: Loss of interaction with CASC5. 1 Publication1
Mutagenesisi175F → A: Loss of interaction with CASC5. 1 Publication1
Mutagenesisi579D → E: Abolishes the cleavage by caspase-3. 1 Publication1
Mutagenesisi610D → E: Abolishes the cleavage by caspase-3. 1 Publication1
Mutagenesisi620T → A: Induces chromosome congression defects and mitotic delay. 1 Publication1
Mutagenesisi795K → A: Does not abolish the capacity to inhibit APC/CDC20. 2 Publications1
Mutagenesisi795K → R: Inhibits kinase activity. 2 Publications1

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNETi701.
MalaCardsiBUB1B.
MIMi176430. phenotype.
257300. phenotype.
OpenTargetsiENSG00000156970.
Orphaneti1052. Mosaic variegated aneuploidy syndrome.
PharmGKBiPA82.

Polymorphism and mutation databases

BioMutaiBUB1B.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000856731 – 1050Mitotic checkpoint serine/threonine-protein kinase BUB1 betaAdd BLAST1050

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei250N6-acetyllysine; by PCAF1 Publication1
Modified residuei367PhosphoserineCombined sources1
Modified residuei435PhosphoserineCombined sources1 Publication1
Modified residuei543PhosphoserineCombined sources1 Publication1
Modified residuei665PhosphoserineCombined sources1
Modified residuei670PhosphoserineCombined sources1 Publication1
Modified residuei676Phosphoserine; by PLK11 Publication1
Modified residuei697PhosphoserineCombined sources1
Modified residuei792Phosphothreonine; by PLK11 Publication1
Modified residuei1008Phosphothreonine; by PLK11 Publication1
Modified residuei1042PhosphothreonineCombined sources1
Modified residuei1043Phosphoserine1 Publication1

Post-translational modificationi

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.
Acetylation at Lys-250 regulates its degradation and timing in anaphase entry.1 Publication
Ubiquitinated. Degraded by the proteasome.1 Publication
Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the association with CENPE at the kinetochore.1 Publication
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.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei579 – 580Cleavage; by caspase-32
Sitei610 – 611Cleavage; by caspase-32

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO60566.
MaxQBiO60566.
PaxDbiO60566.
PeptideAtlasiO60566.
PRIDEiO60566.

PTM databases

iPTMnetiO60566.
PhosphoSitePlusiO60566.

Expressioni

Tissue specificityi

Highly expressed in thymus followed by spleen. Preferentially expressed in tissues with a high mitotic index.1 Publication

Inductioni

Induced during mitosis.3 Publications

Gene expression databases

BgeeiENSG00000156970.
CleanExiHS_BUB1B.
ExpressionAtlasiO60566. baseline and differential.
GenevisibleiO60566. HS.

Organism-specific databases

HPAiHPA008419.

Interactioni

Subunit structurei

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 CASC5.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BUB3O436845EBI-1001438,EBI-1050987
CDC20Q1283416EBI-1001438,EBI-367462
CENPEQ022244EBI-1001438,EBI-1375040
CrebbpP454813EBI-1001438,EBI-296306From a different organism.
KAT2BQ9283114EBI-1001438,EBI-477430
SIRT2Q8IXJ63EBI-1001438,EBI-477232
UBCP0CG483EBI-1001438,EBI-3390054

Protein-protein interaction databases

BioGridi107166. 95 interactors.
DIPiDIP-24203N.
IntActiO60566. 68 interactors.
MINTiMINT-2796866.
STRINGi9606.ENSP00000287598.

Structurei

Secondary structure

11050
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni26 – 28Combined sources3
Helixi60 – 65Combined sources6
Helixi75 – 88Combined sources14
Helixi94 – 96Combined sources3
Helixi98 – 108Combined sources11
Turni109 – 111Combined sources3
Helixi113 – 115Combined sources3
Helixi119 – 131Combined sources13
Helixi135 – 144Combined sources10
Helixi152 – 164Combined sources13
Helixi168 – 180Combined sources13
Helixi186 – 218Combined sources33

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WVIX-ray1.80A57-220[»]
3SI5X-ray2.20A/B57-220[»]
4GGDX-ray2.44C/D20-42[»]
5JJAX-ray2.35C/D647-720[»]
5LCWelectron microscopy4.00S1-560[»]
ProteinModelPortaliO60566.
SMRiO60566.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60566.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini62 – 226BUB1 N-terminalPROSITE-ProRule annotationAdd BLAST165
Domaini766 – 1050Protein kinaseAdd BLAST285

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni152 – 185Necessary for interaction with CASC51 PublicationAdd BLAST34

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi111 – 118Nuclear localization signalSequence analysis8
Motifi224 – 232D-box9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi209 – 215Poly-Glu7

Domaini

The D-box targets the protein for rapid degradation by ubiquitin-dependent proteolysis during the transition from mitosis to interphase.Curated
The BUB1 N-terminal domain directs kinetochore localization and binding to BUB3.

Sequence similaritiesi

Contains 1 BUB1 N-terminal domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.Curated

Phylogenomic databases

eggNOGiENOG410IQA2. Eukaryota.
ENOG410XUW7. LUCA.
GeneTreeiENSGT00520000055622.
HOVERGENiHBG050748.
InParanoidiO60566.
KOiK06637.
OMAiATHSSGF.
OrthoDBiEOG091G01MC.
PhylomeDBiO60566.
TreeFamiTF105456.

Family and domain databases

InterProiIPR015661. Bub1/Mad3.
IPR011009. Kinase-like_dom.
IPR013212. Mad3/Bub1_I.
IPR000719. Prot_kinase_dom.
[Graphical view]
PANTHERiPTHR14030. PTHR14030. 1 hit.
PfamiPF08311. Mad3_BUB1_I. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00777. Mad3_BUB1_I. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51489. BUB1_N. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60566-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAVKKEGGA LSEAMSLEGD EWELSKENVQ PLRQGRIMST LQGALAQESA
60 70 80 90 100
CNNTLQQQKR AFEYEIRFYT GNDPLDVWDR YISWTEQNYP QGGKESNMST
110 120 130 140 150
LLERAVEALQ GEKRYYSDPR FLNLWLKLGR LCNEPLDMYS YLHNQGIGVS
160 170 180 190 200
LAQFYISWAE EYEARENFRK ADAIFQEGIQ QKAEPLERLQ SQHRQFQARV
210 220 230 240 250
SRQTLLALEK EEEEEVFESS VPQRSTLAEL KSKGKKTARA PIIRVGGALK
260 270 280 290 300
APSQNRGLQN PFPQQMQNNS RITVFDENAD EASTAELSKP TVQPWIAPPM
310 320 330 340 350
PRAKENELQA GPWNTGRSLE HRPRGNTASL IAVPAVLPSF TPYVEETARQ
360 370 380 390 400
PVMTPCKIEP SINHILSTRK PGKEEGDPLQ RVQSHQQASE EKKEKMMYCK
410 420 430 440 450
EKIYAGVGEF SFEEIRAEVF RKKLKEQREA ELLTSAEKRA EMQKQIEEME
460 470 480 490 500
KKLKEIQTTQ QERTGDQQEE TMPTKETTKL QIASESQKIP GMTLSSSVCQ
510 520 530 540 550
VNCCARETSL AENIWQEQPH SKGPSVPFSI FDEFLLSEKK NKSPPADPPR
560 570 580 590 600
VLAQRRPLAV LKTSESITSN EDVSPDVCDE FTGIEPLSED AIITGFRNVT
610 620 630 640 650
ICPNPEDTCD FARAARFVST PFHEIMSLKD LPSDPERLLP EEDLDVKTSE
660 670 680 690 700
DQQTACGTIY SQTLSIKKLS PIIEDSREAT HSSGFSGSSA SVASTSSIKC
710 720 730 740 750
LQIPEKLELT NETSENPTQS PWCSQYRRQL LKSLPELSAS AELCIEDRPM
760 770 780 790 800
PKLEIEKEIE LGNEDYCIKR EYLICEDYKL FWVAPRNSAE LTVIKVSSQP
810 820 830 840 850
VPWDFYINLK LKERLNEDFD HFCSCYQYQD GCIVWHQYIN CFTLQDLLQH
860 870 880 890 900
SEYITHEITV LIIYNLLTIV EMLHKAEIVH GDLSPRCLIL RNRIHDPYDC
910 920 930 940 950
NKNNQALKIV DFSYSVDLRV QLDVFTLSGF RTVQILEGQK ILANCSSPYQ
960 970 980 990 1000
VDLFGIADLA HLLLFKEHLQ VFWDGSFWKL SQNISELKDG ELWNKFFVRI
1010 1020 1030 1040 1050
LNANDEATVS VLGELAAEMN GVFDTTFQSH LNKALWKVGK LTSPGALLFQ
Length:1,050
Mass (Da):119,545
Last modified:April 3, 2007 - v3
Checksum:iF7871103A56E6B46
GO
Isoform 2 (identifier: O60566-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-166: Missing.
     522-522: K → KVSLSL
     608-675: Missing.

Note: No experimental confirmation available.
Show »
Length:933
Mass (Da):105,890
Checksum:i81D1307E360D7B67
GO
Isoform 3 (identifier: O60566-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     80-80: R → RWVFLFHKDNRNINR

Note: No experimental confirmation available.
Show »
Length:1,064
Mass (Da):121,386
Checksum:iFB6C9F104164FBEB
GO

Sequence cautioni

The sequence BAD92019 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti248 – 249AL → VF in AAC23736 (PubMed:9618306).Curated2
Sequence conflicti283S → P in BAG35587 (PubMed:14702039).Curated1
Sequence conflicti788S → F in AAC06260 (PubMed:9660858).Curated1
Sequence conflicti1018E → K in AAC33435 (PubMed:9763420).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00885215M → T in a colorectal cancer cell line. 1 Publication1
Natural variantiVAR_02892136R → Q in PCS. 1 PublicationCorresponds to variant rs534297115dbSNPEnsembl.1
Natural variantiVAR_04040240T → M.1 PublicationCorresponds to variant rs56079734dbSNPEnsembl.1
Natural variantiVAR_008853349R → Q.9 PublicationsCorresponds to variant rs1801376dbSNPEnsembl.1
Natural variantiVAR_054549378P → S.1 PublicationCorresponds to variant rs17851677dbSNPEnsembl.1
Natural variantiVAR_028922390E → D.1 PublicationCorresponds to variant rs1017842dbSNPEnsembl.1
Natural variantiVAR_028923550R → Q in MVA1; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989187dbSNPEnsembl.1
Natural variantiVAR_008854618V → A in colorectal cancer. 2 PublicationsCorresponds to variant rs1801528dbSNPEnsembl.1
Natural variantiVAR_028924814R → H in MVA1; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989182dbSNPEnsembl.1
Natural variantiVAR_028925844L → F in MVA1; associated with H-921; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989181dbSNPEnsembl.1
Natural variantiVAR_028926909I → T in MVA1; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989184dbSNPEnsembl.1
Natural variantiVAR_028927921Q → H in MVA1; associated with F-844; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989183dbSNPEnsembl.1
Natural variantiVAR_0289281012L → P in MVA1; heterozygous compound with nonsense mutation. 1 PublicationCorresponds to variant rs28989185dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03647380R → RWVFLFHKDNRNINR in isoform 3. 1 Publication1
Alternative sequenceiVSP_036474113 – 166Missing in isoform 2. 1 PublicationAdd BLAST54
Alternative sequenceiVSP_036475522K → KVSLSL in isoform 2. 1 Publication1
Alternative sequenceiVSP_036476608 – 675Missing in isoform 2. 1 PublicationAdd BLAST68

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053306 mRNA. Translation: AAC06260.1.
AF046918 mRNA. Translation: AAC33435.1.
AF046079 mRNA. Translation: AAC12730.2.
AF107297 mRNA. Translation: AAD11941.1.
AF035933 mRNA. Translation: AAC23736.1.
AF068760 mRNA. Translation: AAC19118.1.
AF310214
, AF310192, AF310193, AF310194, AF310195, AF310196, AF310197, AF310198, AF310199, AF310200, AF310201, AF310202, AF310203, AF310204, AF310205, AF310206, AF310207, AF310208, AF310209, AF310210, AF310211, AF310212, AF310213 Genomic DNA. Translation: AAL10712.1.
AK296795 mRNA. Translation: BAG59371.1.
AK296984 mRNA. Translation: BAG59525.1.
AK312709 mRNA. Translation: BAG35587.1.
AB208782 mRNA. Translation: BAD92019.1. Different initiation.
BC018739 mRNA. Translation: AAH18739.1.
CCDSiCCDS10053.1. [O60566-1]
PIRiJW0092.
RefSeqiNP_001202.4. NM_001211.5.
UniGeneiHs.513645.

Genome annotation databases

EnsembliENST00000287598; ENSP00000287598; ENSG00000156970. [O60566-1]
ENST00000412359; ENSP00000398470; ENSG00000156970. [O60566-3]
GeneIDi701.
KEGGihsa:701.
UCSCiuc001zkx.5. human. [O60566-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053306 mRNA. Translation: AAC06260.1.
AF046918 mRNA. Translation: AAC33435.1.
AF046079 mRNA. Translation: AAC12730.2.
AF107297 mRNA. Translation: AAD11941.1.
AF035933 mRNA. Translation: AAC23736.1.
AF068760 mRNA. Translation: AAC19118.1.
AF310214
, AF310192, AF310193, AF310194, AF310195, AF310196, AF310197, AF310198, AF310199, AF310200, AF310201, AF310202, AF310203, AF310204, AF310205, AF310206, AF310207, AF310208, AF310209, AF310210, AF310211, AF310212, AF310213 Genomic DNA. Translation: AAL10712.1.
AK296795 mRNA. Translation: BAG59371.1.
AK296984 mRNA. Translation: BAG59525.1.
AK312709 mRNA. Translation: BAG35587.1.
AB208782 mRNA. Translation: BAD92019.1. Different initiation.
BC018739 mRNA. Translation: AAH18739.1.
CCDSiCCDS10053.1. [O60566-1]
PIRiJW0092.
RefSeqiNP_001202.4. NM_001211.5.
UniGeneiHs.513645.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WVIX-ray1.80A57-220[»]
3SI5X-ray2.20A/B57-220[»]
4GGDX-ray2.44C/D20-42[»]
5JJAX-ray2.35C/D647-720[»]
5LCWelectron microscopy4.00S1-560[»]
ProteinModelPortaliO60566.
SMRiO60566.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107166. 95 interactors.
DIPiDIP-24203N.
IntActiO60566. 68 interactors.
MINTiMINT-2796866.
STRINGi9606.ENSP00000287598.

PTM databases

iPTMnetiO60566.
PhosphoSitePlusiO60566.

Polymorphism and mutation databases

BioMutaiBUB1B.

Proteomic databases

EPDiO60566.
MaxQBiO60566.
PaxDbiO60566.
PeptideAtlasiO60566.
PRIDEiO60566.

Protocols and materials databases

DNASUi701.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000287598; ENSP00000287598; ENSG00000156970. [O60566-1]
ENST00000412359; ENSP00000398470; ENSG00000156970. [O60566-3]
GeneIDi701.
KEGGihsa:701.
UCSCiuc001zkx.5. human. [O60566-1]

Organism-specific databases

CTDi701.
DisGeNETi701.
GeneCardsiBUB1B.
H-InvDBHIX0012121.
HGNCiHGNC:1149. BUB1B.
HPAiHPA008419.
MalaCardsiBUB1B.
MIMi176430. phenotype.
257300. phenotype.
602860. gene.
neXtProtiNX_O60566.
OpenTargetsiENSG00000156970.
Orphaneti1052. Mosaic variegated aneuploidy syndrome.
PharmGKBiPA82.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IQA2. Eukaryota.
ENOG410XUW7. LUCA.
GeneTreeiENSGT00520000055622.
HOVERGENiHBG050748.
InParanoidiO60566.
KOiK06637.
OMAiATHSSGF.
OrthoDBiEOG091G01MC.
PhylomeDBiO60566.
TreeFamiTF105456.

Enzyme and pathway databases

BioCyciZFISH:HS08163-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-141430. Inactivation of APC/C via direct inhibition of the APC/C complex.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-176409. APC/C:Cdc20 mediated degradation of mitotic proteins.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SignaLinkiO60566.
SIGNORiO60566.

Miscellaneous databases

EvolutionaryTraceiO60566.
GeneWikiiBUB1B.
GenomeRNAii701.
PROiO60566.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000156970.
CleanExiHS_BUB1B.
ExpressionAtlasiO60566. baseline and differential.
GenevisibleiO60566. HS.

Family and domain databases

InterProiIPR015661. Bub1/Mad3.
IPR011009. Kinase-like_dom.
IPR013212. Mad3/Bub1_I.
IPR000719. Prot_kinase_dom.
[Graphical view]
PANTHERiPTHR14030. PTHR14030. 1 hit.
PfamiPF08311. Mad3_BUB1_I. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00777. Mad3_BUB1_I. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51489. BUB1_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBUB1B_HUMAN
AccessioniPrimary (citable) accession number: O60566
Secondary accession number(s): B2R6U0
, B4DL09, B4DLG3, O60501, O60627, O60758, O75389, Q59HH6, Q8WV50, Q96KM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 3, 2007
Last modified: November 2, 2016
This is version 173 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.