BUB1B_HUMAN - dbPTM
BUB1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUB1B_HUMAN
UniProt AC O60566
Protein Name Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
Gene Name BUB1B
Organism Homo sapiens (Human).
Sequence Length 1050
Subcellular Localization Cytoplasm. Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic in interphase cells. Associates with the kinetochores in early prophase. Kinetochore localization requires BUB1,
Protein Description 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..
Protein Sequence MAAVKKEGGALSEAMSLEGDEWELSKENVQPLRQGRIMSTLQGALAQESACNNTLQQQKRAFEYEIRFYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNEPLDMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEGIQQKAEPLERLQSQHRQFQARVSRQTLLALEKEEEEEVFESSVPQRSTLAELKSKGKKTARAPIIRVGGALKAPSQNRGLQNPFPQQMQNNSRITVFDENADEASTAELSKPTVQPWIAPPMPRAKENELQAGPWNTGRSLEHRPRGNTASLIAVPAVLPSFTPYVEETARQPVMTPCKIEPSINHILSTRKPGKEEGDPLQRVQSHQQASEEKKEKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKEQREAELLTSAEKRAEMQKQIEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQKIPGMTLSSSVCQVNCCARETSLAENIWQEQPHSKGPSVPFSIFDEFLLSEKKNKSPPADPPRVLAQRRPLAVLKTSESITSNEDVSPDVCDEFTGIEPLSEDAIITGFRNVTICPNPEDTCDFARAARFVSTPFHEIMSLKDLPSDPERLLPEEDLDVKTSEDQQTACGTIYSQTLSIKKLSPIIEDSREATHSSGFSGSSASVASTSSIKCLQIPEKLELTNETSENPTQSPWCSQYRRQLLKSLPELSASAELCIEDRPMPKLEIEKEIELGNEDYCIKREYLICEDYKLFWVAPRNSAELTVIKVSSQPVPWDFYINLKLKERLNEDFDHFCSCYQYQDGCIVWHQYINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDCNKNNQALKIVDFSYSVDLRVQLDVFTLSGFRTVQILEGQKILANCSSPYQVDLFGIADLAHLLLFKEHLQVFWDGSFWKLSQNISELKDGELWNKFFVRILNANDEATVSVLGELAAEMNGVFDTTFQSHLNKALWKVGKLTSPGALLFQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
12PhosphorylationKKEGGALSEAMSLEG
CCCCCCHHHHHCCCC
23.8328555341
16PhosphorylationGALSEAMSLEGDEWE
CCHHHHHCCCCCCEE
30.2530624053
26UbiquitinationGDEWELSKENVQPLR
CCCEEHHHHCCHHHH
66.9729967540
39PhosphorylationLRQGRIMSTLQGALA
HHHCCHHHHHHHHHH
24.48-
40PhosphorylationRQGRIMSTLQGALAQ
HHCCHHHHHHHHHHH
13.0128555341
49PhosphorylationQGALAQESACNNTLQ
HHHHHHHHHHCCHHH
26.4924043423
54PhosphorylationQESACNNTLQQQKRA
HHHHHCCHHHHHHHH
16.3822817900
59UbiquitinationNNTLQQQKRAFEYEI
CCHHHHHHHHHEEEE
41.16-
59 (in isoform 3)Ubiquitination-41.16-
64PhosphorylationQQKRAFEYEIRFYTG
HHHHHHEEEEEEECC
15.3723898821
83PhosphorylationDVWDRYISWTEQNYP
CHHHHHHHCHHHCCC
21.00-
113UbiquitinationVEALQGEKRYYSDPR
HHHHHCCCHHCCCHH
53.1533845483
127 (in isoform 3)Ubiquitination-37.00-
156 (in isoform 2)Ubiquitination-2.6821890473
170UbiquitinationEARENFRKADAIFQE
HHHHHHHHHHHHHHH
46.62-
182UbiquitinationFQEGIQQKAEPLERL
HHHHHHHHHHHHHHH
38.0432015554
196 (in isoform 3)Ubiquitination-6.55-
201PhosphorylationRQFQARVSRQTLLAL
HHHHHHHHHHHHHHH
17.0828674151
204PhosphorylationQARVSRQTLLALEKE
HHHHHHHHHHHHHHH
23.7228555341
210UbiquitinationQTLLALEKEEEEEVF
HHHHHHHHHHHHHHH
71.8722817900
210 (in isoform 1)Ubiquitination-71.8721890473
220PhosphorylationEEEVFESSVPQRSTL
HHHHHHCCCCCCCHH
30.5328555341
224 (in isoform 3)Ubiquitination-26.0721890473
231UbiquitinationRSTLAELKSKGKKTA
CCHHHHHHHCCCCCC
41.4433845483
232PhosphorylationSTLAELKSKGKKTAR
CHHHHHHHCCCCCCC
60.3020860994
237PhosphorylationLKSKGKKTARAPIIR
HHHCCCCCCCCCEEE
25.5124719451
250SumoylationIRVGGALKAPSQNRG
EEECCEECCCCCCCC
58.69-
250AcetylationIRVGGALKAPSQNRG
EEECCEECCCCCCCC
58.6919407811
250SumoylationIRVGGALKAPSQNRG
EEECCEECCCCCCCC
58.6919407811
250UbiquitinationIRVGGALKAPSQNRG
EEECCEECCCCCCCC
58.6919407811
264 (in isoform 3)Ubiquitination-52.32-
266SulfoxidationQNPFPQQMQNNSRIT
CCCCCHHHHCCCCEE
3.7621406390
270PhosphorylationPQQMQNNSRITVFDE
CHHHHCCCCEEEECC
32.3926425664
304UbiquitinationAPPMPRAKENELQAG
CCCCCCCCCCCCCCC
63.4529967540
315PhosphorylationLQAGPWNTGRSLEHR
CCCCCCCCCCCCCCC
30.06-
318PhosphorylationGPWNTGRSLEHRPRG
CCCCCCCCCCCCCCC
39.1828555341
361PhosphorylationTPCKIEPSINHILST
CCCCCCCCHHHHHCC
24.1922673903
367PhosphorylationPSINHILSTRKPGKE
CCHHHHHCCCCCCCC
26.0925159151
368PhosphorylationSINHILSTRKPGKEE
CHHHHHCCCCCCCCC
38.9928555341
370UbiquitinationNHILSTRKPGKEEGD
HHHHCCCCCCCCCCC
59.2029967540
373UbiquitinationLSTRKPGKEEGDPLQ
HCCCCCCCCCCCHHH
62.2124816145
384PhosphorylationDPLQRVQSHQQASEE
CHHHHHHHHHHHCHH
22.0230576142
384 (in isoform 3)Ubiquitination-22.02-
404PhosphorylationMYCKEKIYAGVGEFS
HHHHHHHHCCCCCCC
14.3628674419
418 (in isoform 3)Phosphorylation-32.1327642862
421 (in isoform 2)Ubiquitination-40.1321890473
434PhosphorylationQREAELLTSAEKRAE
HHHHHHHHHHHHHHH
38.2229255136
435PhosphorylationREAELLTSAEKRAEM
HHHHHHHHHHHHHHH
34.1129255136
438UbiquitinationELLTSAEKRAEMQKQ
HHHHHHHHHHHHHHH
57.5324816145
451AcetylationKQIEEMEKKLKEIQT
HHHHHHHHHHHHHHH
63.197432055
452UbiquitinationQIEEMEKKLKEIQTT
HHHHHHHHHHHHHHH
52.0329967540
454UbiquitinationEEMEKKLKEIQTTQQ
HHHHHHHHHHHHHHH
62.7529967540
464PhosphorylationQTTQQERTGDQQEET
HHHHHHHHCCCCCCC
44.3421406692
468 (in isoform 3)Ubiquitination-56.06-
471PhosphorylationTGDQQEETMPTKETT
HCCCCCCCCCCCHHC
27.9121406692
474PhosphorylationQQEETMPTKETTKLQ
CCCCCCCCCHHCHHE
30.5921406692
475UbiquitinationQEETMPTKETTKLQI
CCCCCCCCHHCHHEC
47.3921906983
475 (in isoform 1)Ubiquitination-47.3921890473
479UbiquitinationMPTKETTKLQIASES
CCCCHHCHHECCCCC
45.9022817900
488UbiquitinationQIASESQKIPGMTLS
ECCCCCCCCCCCEEC
61.21-
489 (in isoform 3)Ubiquitination-2.5021890473
496PhosphorylationIPGMTLSSSVCQVNC
CCCCEECCCCHHHHC
29.8728555341
497PhosphorylationPGMTLSSSVCQVNCC
CCCEECCCCHHHHCC
24.4428555341
502 (in isoform 3)Ubiquitination-6.83-
508PhosphorylationVNCCARETSLAENIW
HHCCCCCCHHHHHHH
24.4023186163
509PhosphorylationNCCARETSLAENIWQ
HCCCCCCHHHHHHHH
22.3430576142
521PhosphorylationIWQEQPHSKGPSVPF
HHHCCCCCCCCCCCC
46.0925159151
522UbiquitinationWQEQPHSKGPSVPFS
HHCCCCCCCCCCCCC
72.3329967540
537PhosphorylationIFDEFLLSEKKNKSP
HHHHHHHHHCCCCCC
49.9024719451
539UbiquitinationDEFLLSEKKNKSPPA
HHHHHHHCCCCCCCC
59.2732015554
540UbiquitinationEFLLSEKKNKSPPAD
HHHHHHCCCCCCCCC
66.61-
542UbiquitinationLLSEKKNKSPPADPP
HHHHCCCCCCCCCCC
73.5429967540
543PhosphorylationLSEKKNKSPPADPPR
HHHCCCCCCCCCCCH
45.5730266825
554 (in isoform 3)Ubiquitination-37.44-
563PhosphorylationRPLAVLKTSESITSN
CCEEEEECCCCCCCC
33.3029116813
564PhosphorylationPLAVLKTSESITSNE
CEEEEECCCCCCCCC
27.9728464451
566PhosphorylationAVLKTSESITSNEDV
EEEECCCCCCCCCCC
30.8229802988
568PhosphorylationLKTSESITSNEDVSP
EECCCCCCCCCCCCH
34.4828102081
569PhosphorylationKTSESITSNEDVSPD
ECCCCCCCCCCCCHH
36.2329116813
574PhosphorylationITSNEDVSPDVCDEF
CCCCCCCCHHHCCCC
27.9229496963
582PhosphorylationPDVCDEFTGIEPLSE
HHHCCCCCCCCCCCC
34.8928464451
600PhosphorylationITGFRNVTICPNPED
EECCCCEEECCCHHH
22.0228555341
608PhosphorylationICPNPEDTCDFARAA
ECCCHHHCCHHHHHH
16.5928555341
619PhosphorylationARAARFVSTPFHEIM
HHHHHHHCCCHHHHC
27.8722199227
620PhosphorylationRAARFVSTPFHEIMS
HHHHHHCCCHHHHCC
25.3622199227
627PhosphorylationTPFHEIMSLKDLPSD
CCHHHHCCCCCCCCC
37.6228555341
629UbiquitinationFHEIMSLKDLPSDPE
HHHHCCCCCCCCCHH
50.3321906983
629 (in isoform 1)Ubiquitination-50.3321890473
633PhosphorylationMSLKDLPSDPERLLP
CCCCCCCCCHHHHCC
73.4330576142
643 (in isoform 3)Ubiquitination-46.6521890473
658PhosphorylationDQQTACGTIYSQTLS
HHCHHCHHHHEEECC
19.3421945579
660PhosphorylationQTACGTIYSQTLSIK
CHHCHHHHEEECCCC
8.4521945579
661PhosphorylationTACGTIYSQTLSIKK
HHCHHHHEEECCCCC
16.9121945579
665PhosphorylationTIYSQTLSIKKLSPI
HHHEEECCCCCCCCC
35.4323186163
667AcetylationYSQTLSIKKLSPIIE
HEEECCCCCCCCCCC
44.2625953088
667UbiquitinationYSQTLSIKKLSPIIE
HEEECCCCCCCCCCC
44.2629967540
668UbiquitinationSQTLSIKKLSPIIED
EEECCCCCCCCCCCC
53.1529967540
670PhosphorylationTLSIKKLSPIIEDSR
ECCCCCCCCCCCCHH
23.9629255136
676PhosphorylationLSPIIEDSREATHSS
CCCCCCCHHHHHCCC
21.1623927012
680PhosphorylationIEDSREATHSSGFSG
CCCHHHHHCCCCCCC
19.9630576142
682PhosphorylationDSREATHSSGFSGSS
CHHHHHCCCCCCCCC
28.0023186163
682 (in isoform 3)Ubiquitination-28.00-
683PhosphorylationSREATHSSGFSGSSA
HHHHHCCCCCCCCCC
35.9330576142
686PhosphorylationATHSSGFSGSSASVA
HHCCCCCCCCCCCCC
41.0923186163
688PhosphorylationHSSGFSGSSASVAST
CCCCCCCCCCCCCCC
22.8723186163
689PhosphorylationSSGFSGSSASVASTS
CCCCCCCCCCCCCCC
28.2623186163
691PhosphorylationGFSGSSASVASTSSI
CCCCCCCCCCCCCCC
21.8423186163
694PhosphorylationGSSASVASTSSIKCL
CCCCCCCCCCCCEEE
27.0223186163
695PhosphorylationSSASVASTSSIKCLQ
CCCCCCCCCCCEEEE
19.4323186163
696PhosphorylationSASVASTSSIKCLQI
CCCCCCCCCCEEEEC
27.8023186163
697PhosphorylationASVASTSSIKCLQIP
CCCCCCCCCEEEECC
26.5923312004
699UbiquitinationVASTSSIKCLQIPEK
CCCCCCCEEEECCCC
30.7329967540
706UbiquitinationKCLQIPEKLELTNET
EEEECCCCEECCCCC
41.7429967540
710PhosphorylationIPEKLELTNETSENP
CCCCEECCCCCCCCC
22.9521815630
713PhosphorylationKLELTNETSENPTQS
CEECCCCCCCCCCCC
43.3325627689
714PhosphorylationLELTNETSENPTQSP
EECCCCCCCCCCCCH
29.2428555341
718PhosphorylationNETSENPTQSPWCSQ
CCCCCCCCCCHHHHH
53.9421815630
720PhosphorylationTSENPTQSPWCSQYR
CCCCCCCCHHHHHHH
23.8921815630
724PhosphorylationPTQSPWCSQYRRQLL
CCCCHHHHHHHHHHH
26.7829396449
726PhosphorylationQSPWCSQYRRQLLKS
CCHHHHHHHHHHHHH
7.4729396449
733PhosphorylationYRRQLLKSLPELSAS
HHHHHHHHCHHHHHC
49.4822067460
757UbiquitinationMPKLEIEKEIELGNE
CCCEEEEEEEECCCC
70.4329967540
766PhosphorylationIELGNEDYCIKREYL
EECCCCCCEEEEEEE
7.0122817900
769UbiquitinationGNEDYCIKREYLICE
CCCCCEEEEEEEEEC
35.3029967540
771 (in isoform 3)Ubiquitination-39.42-
783 (in isoform 3)Ubiquitination-4.04-
792PhosphorylationPRNSAELTVIKVSSQ
CCCCCEEEEEEEECC
16.2217376779
797PhosphorylationELTVIKVSSQPVPWD
EEEEEEEECCCCCCE
20.46-
878 (in isoform 2)Ubiquitination-3.1121890473
884PhosphorylationEIVHGDLSPRCLILR
CHHCCCCCCCEEEEE
18.2925159151
902UbiquitinationHDPYDCNKNNQALKI
CCCCCCCCCCCEEEE
64.7029967540
912 (in isoform 3)Phosphorylation-5.2427642862
919DimethylationFSYSVDLRVQLDVFT
EECEEEEEEEEEEEE
15.07-
919MethylationFSYSVDLRVQLDVFT
EECEEEEEEEEEEEE
15.07-
988UbiquitinationSQNISELKDGELWNK
CCCHHHCCCCHHHHH
60.6829967540
995UbiquitinationKDGELWNKFFVRILN
CCCHHHHHHHHHHHC
28.7021890473
995 (in isoform 1)Ubiquitination-28.7021890473
1008PhosphorylationLNANDEATVSVLGEL
HCCCCCHHHHHHHHH
15.9717376779
1009 (in isoform 3)Ubiquitination-4.8621890473
1037UbiquitinationHLNKALWKVGKLTSP
HHHHHHHHHHCCCCC
41.79-
1040AcetylationKALWKVGKLTSPGAL
HHHHHHHCCCCCCEE
52.1325953088
1040UbiquitinationKALWKVGKLTSPGAL
HHHHHHHCCCCCCEE
52.1329967540
1042PhosphorylationLWKVGKLTSPGALLF
HHHHHCCCCCCEECC
36.0430266825
1043PhosphorylationWKVGKLTSPGALLFQ
HHHHCCCCCCEECCC
31.6030266825
1051 (in isoform 3)Ubiquitination--
1054 (in isoform 3)Ubiquitination--

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
435SPhosphorylationKinaseTTKP33981
PSP
543SPhosphorylationKinaseCDK1P06493
PSP
543SPhosphorylationKinaseTTKP33981
PSP
670SPhosphorylationKinaseCDK1P06493
PSP
670SPhosphorylationKinaseTTKP33981
PSP
676SPhosphorylationKinasePLK1P53350
Uniprot
680TPhosphorylationKinasePLK1P53350
PSP
792TPhosphorylationKinasePLK1P53350
Uniprot
1008TPhosphorylationKinasePLK1P53350
Uniprot
1043SPhosphorylationKinaseCDK1P06493
PSP
1043SPhosphorylationKinaseTTKP33981
PSP
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:23091007
-KUbiquitinationE3 ubiquitin ligaseCDC20Q12834
PMID:16856867

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
250KAcetylation

19407811
670SPhosphorylation

19015317
1043SPhosphorylation

19015317

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of BUB1B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
15388328
CDC20_HUMANCDC20physical
11030144
CDC20_HUMANCDC20physical
11535616
BUB3_HUMANBUB3physical
11535616
MD2L1_HUMANMAD2L1physical
11535616
CENPE_HUMANCENPEphysical
9763420
BUB3_HUMANBUB3physical
12419313
APC_HUMANAPCphysical
11283619
CDC27_HUMANCDC27physical
10477750
CDC16_HUMANCDC16physical
10477750
APC7_HUMANANAPC7physical
10477750
CDC20_HUMANCDC20physical
11274370
PARP1_HUMANPARP1physical
16449973
CDC20_HUMANCDC20physical
20512932
CDC20_HUMANCDC20physical
20360068
CDC27_HUMANCDC27physical
20360068
APC4_HUMANANAPC4physical
20360068
BUB1B_HUMANBUB1Bphysical
20360068
APC7_HUMANANAPC7physical
20360068
CDC20_HUMANCDC20physical
20733051
NSL1_HUMANNSL1physical
20231385
BUB3_HUMANBUB3physical
21937719
MXI1_HUMANMXI1physical
21937719
CDC20_HUMANCDC20physical
18591651
CDC20_HUMANCDC20physical
21335556
CDC20_HUMANCDC20physical
22566641
MDM2_HUMANMDM2physical
22566641
MD2BP_HUMANMAD2L1BPphysical
22566641
CDC20_HUMANCDC20physical
11702782
BUB3_HUMANBUB3physical
11702782
PLK1_HUMANPLK1physical
19503101
TBB5_HUMANTUBBphysical
19503101
KNL1_HUMANCASC5physical
22000412
CDC20_HUMANCDC20physical
22000412
MD2L1_HUMANMAD2L1physical
22000412
BUB3_HUMANBUB3physical
22000412
P73_HUMANTP73physical
19139399
CENPE_HUMANCENPEphysical
20237434
MD2L1_HUMANMAD2L1physical
21525009
PLK1_HUMANPLK1physical
17376779
MD2BP_HUMANMAD2L1BPphysical
22100920
CDC20_HUMANCDC20physical
22100920
MD2L1_HUMANMAD2L1physical
22100920
BUB1B_HUMANBUB1Bphysical
22100920
BUB3_HUMANBUB3physical
22100920
PTTG1_HUMANPTTG1physical
19117984
SGO1_HUMANSGOL1physical
22374677
CDC20_HUMANCDC20physical
23091007
BUB3_HUMANBUB3physical
20220147
MD2L1_HUMANMAD2L1physical
23791783
CDC20_HUMANCDC20physical
23791783
BUB3_HUMANBUB3physical
23791783
BUB3_HUMANBUB3physical
21988832
COMD4_HUMANCOMMD4physical
21988832
PNMA2_HUMANPNMA2physical
22863883
UGPA_HUMANUGP2physical
22863883
CDC27_HUMANCDC27physical
25012665
CDC20_HUMANCDC20physical
25012665
BUB3_HUMANBUB3physical
25012665
MD2L1_HUMANMAD2L1physical
25012665
PCH2_HUMANTRIP13physical
25012665
BUB3_HUMANBUB3physical
25246557
CDC20_HUMANCDC20physical
25246557
CDC27_HUMANCDC27physical
25246557
CDC20_HUMANCDC20physical
25383541
APC1_HUMANANAPC1physical
25852190
ANC2_HUMANANAPC2physical
25852190
BAG2_HUMANBAG2physical
25852190
BUB1_HUMANBUB1physical
25852190
BUB3_HUMANBUB3physical
25852190
DSN1_HUMANDSN1physical
25852190
KNL1_HUMANCASC5physical
25852190
ZC3H1_HUMANZFC3H1physical
25852190
TCPB_HUMANCCT2physical
25852190
CDC20_HUMANCDC20physical
25852190
CDC27_HUMANCDC27physical
25852190
EF2_HUMANEEF2physical
25852190
HSPB1_HUMANHSPB1physical
25852190
HS105_HUMANHSPH1physical
25852190
NDC80_HUMANNDC80physical
25852190
MD2L1_HUMANMAD2L1physical
25852190
MIS12_HUMANMIS12physical
25852190
NUF2_HUMANNUF2physical
25852190
PMF1_HUMANPMF1physical
25852190
PSA3_HUMANPSMA3physical
25852190
PSA4_HUMANPSMA4physical
25852190
PSA6_HUMANPSMA6physical
25852190
PSB5_HUMANPSMB5physical
25852190
PSMD6_HUMANPSMD6physical
25852190
RL39_HUMANRPL39physical
25852190
SK2L2_HUMANSKIV2L2physical
25852190
UBR5_HUMANUBR5physical
25833949
BUB3_HUMANBUB3physical
25833949
CDC20_HUMANCDC20physical
25833949
CDC20_HUMANCDC20physical
25505175
FZR1_HUMANFZR1physical
25505175
BUB3_HUMANBUB3physical
25505175
MXI1_HUMANMXI1physical
25505175
CDC20_HUMANCDC20physical
25669885
MD2L1_HUMANMAD2L1physical
25669885
CCNA2_HUMANCCNA2physical
25669885
BUB3_HUMANBUB3physical
25669885
APC4_HUMANANAPC4physical
25669885
CDC20_HUMANCDC20physical
25482201
APC1_HUMANANAPC1physical
25482201
BUB3_HUMANBUB3physical
25482201
MD2L1_HUMANMAD2L1physical
25482201
BUB3_HUMANBUB3physical
24151075
CDC20_HUMANCDC20physical
24151075
MD2L1_HUMANMAD2L1physical
24151075
CDC16_HUMANCDC16physical
24151075
CDC27_HUMANCDC27physical
25673878
APC4_HUMANANAPC4physical
25673878
APC10_HUMANANAPC10physical
25673878
NEK2_HUMANNEK2physical
25673878
CDC20_HUMANCDC20physical
25673878
MD2L1_HUMANMAD2L1physical
25673878
APC7_HUMANANAPC7physical
26986935
CDC20_HUMANCDC20physical
26986935
MD2L1_HUMANMAD2L1physical
26986935
HDAC2_HUMANHDAC2physical
28985013
HDAC3_HUMANHDAC3physical
28985013
CDC20_HUMANCDC20physical
28096334

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=Defects in BUB1B are associated with tumor formation.
176430
257300Mosaic variegated aneuploidy syndrome 1 (MVA1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUB1B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"BubR1 acetylation at prometaphase is required for modulating APC/Cactivity and timing of mitosis.";
Choi E., Choe H., Min J., Choi J.Y., Kim J., Lee H.;
EMBO J. 28:2077-2089(2009).
Cited for: INTERACTION WITH PCAF, ACETYLATION AT LYS-250, AND UBIQUITINATION.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1043, AND MASSSPECTROMETRY.
"Phosphorylation sites in BubR1 that regulate kinetochore attachment,tension, and mitotic exit.";
Huang H., Hittle J., Zappacosta F., Annan R.S., Hershko A., Yen T.J.;
J. Cell Biol. 183:667-680(2008).
Cited for: PHOSPHORYLATION AT SER-435; SER-543; SER-670 AND SER-1043.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-670, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543, AND MASSSPECTROMETRY.
"Tension-sensitive Plk1 phosphorylation on BubR1 regulates thestability of kinetochore microtubule interactions.";
Elowe S., Huemmer S., Uldschmid A., Li X., Nigg E.A.;
Genes Dev. 21:2205-2219(2007).
Cited for: INTERACTION WITH PLK1, SUBCELLULAR LOCATION, PHOSPHORYLATION ATSER-676, AND MUTAGENESIS OF THR-620.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54, AND MASSSPECTROMETRY.
"Polo-like kinase 1 facilitates chromosome alignment duringprometaphase through BubR1.";
Matsumura S., Toyoshima F., Nishida E.;
J. Biol. Chem. 282:15217-15227(2007).
Cited for: INTERACTION WITH PLK1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION ATTHR-792 AND THR-1008.

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