BUB1_HUMAN - dbPTM
BUB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUB1_HUMAN
UniProt AC O43683
Protein Name Mitotic checkpoint serine/threonine-protein kinase BUB1
Gene Name BUB1
Organism Homo sapiens (Human).
Sequence Length 1085
Subcellular Localization Nucleus. Chromosome, centromere, kinetochore. 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 localizatio
Protein Description 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. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 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..
Protein Sequence MDTPENVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPENKEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGIQNQAEPREFLQQQYRLFQTRLTETHLPAQARTSEPLHNVQVLNQMITSKSNPGNNMACISKNQGSELSGVISSACDKESNMERRVITISKSEYSVHSSLASKVDVEQVVMYCKEKLIRGESEFSFEELRAQKYNQRRKHEQWVNEDRHYMKRKEANAFEEQLLKQKMDELHKKLHQVVETSHEDLPASQERSEVNPARMGPSVGSQQELRAPCLPVTYQQTPVNMEKNPREAPPVVPPLANAISAALVSPATSQSIAPPVPLKAQTVTDSMFAVASKDAGCVNKSTHEFKPQSGAEIKEGCETHKVANTSSFHTTPNTSLGMVQATPSKVQPSPTVHTKEALGFIMNMFQAPTLPDISDDKDEWQSLDQNEDAFEAQFQKNVRSSGAWGVNKIISSLSSAFHVFEDGNKENYGLPQPKNKPTGARTFGERSVSRLPSKPKEEVPHAEEFLDDSTVWGIRCNKTLAPSPKSPGDFTSAAQLASTPFHKLPVESVHILEDKENVVAKQCTQATLDSCEENMVVPSRDGKFSPIQEKSPKQALSSHMYSASLLRLSQPAAGGVLTCEAELGVEACRLTDTDAAIAEDPPDAIAGLQAEWMQMSSLGTVDAPNFIVGNPWDDKLIFKLLSGLSKPVSSYPNTFEWQCKLPAIKPKTEFQLGSKLVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLVGELYSYGTLLNAINLYKNTPEKVMPQGLVISFAMRMLYMIEQVHDCEIIHGDIKPDNFILGNGFLEQDDEDDLSAGLALIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLPHLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRLIVLLLECKRSRK
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
3Phosphorylation-----MDTPENVLQM
-----CCCHHHHHHH		44.3428348404
17PhosphorylationMLEAHMQSYKGNDPL
HHHHHHHHCCCCCCC		22.6425159151
47PhosphorylationENKEYLITLLEHLMK
CCHHHHHHHHHHHHH		23.7724719451
60AcetylationMKEFLDKKKYHNDPR
HHHHHHHHCCCCCHH		59.227710301
148PhosphorylationRLFQTRLTETHLPAQ
HHHHHHHCCCCCCCC		35.23-
158PhosphorylationHLPAQARTSEPLHNV
CCCCCCCCCCCCCHH		40.2220860994
159PhosphorylationLPAQARTSEPLHNVQ
CCCCCCCCCCCCHHH		31.5020860994
173PhosphorylationQVLNQMITSKSNPGN
HHHHHHHHCCCCCCC		25.4328555341
174PhosphorylationVLNQMITSKSNPGNN
HHHHHHHCCCCCCCC		24.1420860994
175UbiquitinationLNQMITSKSNPGNNM
HHHHHHCCCCCCCCC		45.67-
175UbiquitinationLNQMITSKSNPGNNM
HHHHHHCCCCCCCCC		45.67-
176PhosphorylationNQMITSKSNPGNNMA
HHHHHCCCCCCCCCE		48.2825159151
187UbiquitinationNNMACISKNQGSELS
CCCEEEECCCCCCHH		33.12-
187UbiquitinationNNMACISKNQGSELS
CCCEEEECCCCCCHH		33.12-
191PhosphorylationCISKNQGSELSGVIS
EEECCCCCCHHHHHH		26.1221406692
194PhosphorylationKNQGSELSGVISSAC
CCCCCCHHHHHHHHC		27.2821815630
198PhosphorylationSELSGVISSACDKES
CCHHHHHHHHCCCCC		14.9621406692
199PhosphorylationELSGVISSACDKESN
CHHHHHHHHCCCCCC		23.0721406692
203UbiquitinationVISSACDKESNMERR
HHHHHCCCCCCCEEE		64.03-
203UbiquitinationVISSACDKESNMERR
HHHHHCCCCCCCEEE		64.03-
213PhosphorylationNMERRVITISKSEYS
CCEEEEEEEEHHHHC		19.15-
215PhosphorylationERRVITISKSEYSVH
EEEEEEEEHHHHCCC		22.8328555341
216UbiquitinationRRVITISKSEYSVHS
EEEEEEEHHHHCCCH		43.38-
216UbiquitinationRRVITISKSEYSVHS
EEEEEEEHHHHCCCH		43.38-
217PhosphorylationRVITISKSEYSVHSS
EEEEEEHHHHCCCHH		34.6728796482
219PhosphorylationITISKSEYSVHSSLA
EEEEHHHHCCCHHHC		24.0828796482
220PhosphorylationTISKSEYSVHSSLAS
EEEHHHHCCCHHHCC		14.8728796482
223PhosphorylationKSEYSVHSSLASKVD
HHHHCCCHHHCCCCC		25.5428555341
224PhosphorylationSEYSVHSSLASKVDV
HHHCCCHHHCCCCCH		17.0528555341
241UbiquitinationVVMYCKEKLIRGESE
HHHHHHHHHHCCCCC		34.41-
241UbiquitinationVVMYCKEKLIRGESE
HHHHHHHHHHCCCCC		34.41-
247PhosphorylationEKLIRGESEFSFEEL
HHHHCCCCCCCHHHH		46.92-
250PhosphorylationIRGESEFSFEELRAQ
HCCCCCCCHHHHHHH		27.9123186163
264UbiquitinationQKYNQRRKHEQWVNE
HHHHHHHHHHHHHHH		54.40-
264UbiquitinationQKYNQRRKHEQWVNE
HHHHHHHHHHHHHHH		54.40-
277UbiquitinationNEDRHYMKRKEANAF
HHHHHHHHHHHCHHH		53.83-
279UbiquitinationDRHYMKRKEANAFEE
HHHHHHHHHCHHHHH		56.51-
279UbiquitinationDRHYMKRKEANAFEE
HHHHHHHHHCHHHHH		56.51-
290UbiquitinationAFEEQLLKQKMDELH
HHHHHHHHHHHHHHH		57.37-
290UbiquitinationAFEEQLLKQKMDELH
HHHHHHHHHHHHHHH		57.37-
292UbiquitinationEEQLLKQKMDELHKK
HHHHHHHHHHHHHHH		46.89-
299UbiquitinationKMDELHKKLHQVVET
HHHHHHHHHHHHHHC		40.22-
299UbiquitinationKMDELHKKLHQVVET
HHHHHHHHHHHHHHC		40.22-
306PhosphorylationKLHQVVETSHEDLPA
HHHHHHHCCCCCCCH		24.6323401153
307PhosphorylationLHQVVETSHEDLPAS
HHHHHHCCCCCCCHH		16.0425159151
314PhosphorylationSHEDLPASQERSEVN
CCCCCCHHHCCCCCC		30.5417525332
318PhosphorylationLPASQERSEVNPARM
CCHHHCCCCCCHHHC		45.1828555341
328PhosphorylationNPARMGPSVGSQQEL
CHHHCCCCCCCHHHH		33.1228634120
331PhosphorylationRMGPSVGSQQELRAP
HCCCCCCCHHHHCCC		26.9119369195
347PhosphorylationLPVTYQQTPVNMEKN
CCCEECCCCCCCCCC		17.4328555341
353UbiquitinationQTPVNMEKNPREAPP
CCCCCCCCCCCCCCC		62.58-
353UbiquitinationQTPVNMEKNPREAPP
CCCCCCCCCCCCCCC		62.58-
370PhosphorylationPPLANAISAALVSPA
CHHHHHHHHHHCCCC		12.7027251275
375PhosphorylationAISAALVSPATSQSI
HHHHHHCCCCCCCCC		15.0725159151
378PhosphorylationAALVSPATSQSIAPP
HHHCCCCCCCCCCCC		30.5924732914
379PhosphorylationALVSPATSQSIAPPV
HHCCCCCCCCCCCCC		24.8424732914
381PhosphorylationVSPATSQSIAPPVPL
CCCCCCCCCCCCCCC		22.0824732914
392PhosphorylationPVPLKAQTVTDSMFA
CCCCCCEECCHHHHH		30.1725690035
394PhosphorylationPLKAQTVTDSMFAVA
CCCCEECCHHHHHHH		26.2429449344
396PhosphorylationKAQTVTDSMFAVASK
CCEECCHHHHHHHCC		13.3630278072
402PhosphorylationDSMFAVASKDAGCVN
HHHHHHHCCCCCCCC		25.1930576142
403UbiquitinationSMFAVASKDAGCVNK
HHHHHHCCCCCCCCC		41.69-
403UbiquitinationSMFAVASKDAGCVNK
HHHHHHCCCCCCCCC		41.69-
410UbiquitinationKDAGCVNKSTHEFKP
CCCCCCCCCCCCCCC		36.01-
410UbiquitinationKDAGCVNKSTHEFKP
CCCCCCCCCCCCCCC		36.01-
411PhosphorylationDAGCVNKSTHEFKPQ
CCCCCCCCCCCCCCC		29.7725849741
412PhosphorylationAGCVNKSTHEFKPQS
CCCCCCCCCCCCCCC		27.3425849741
416UbiquitinationNKSTHEFKPQSGAEI
CCCCCCCCCCCCCCC		38.88-
419PhosphorylationTHEFKPQSGAEIKEG
CCCCCCCCCCCCCCC		48.8028555341
435PhosphorylationETHKVANTSSFHTTP
HEECCCCCCCCCCCC		18.9322199227
436PhosphorylationTHKVANTSSFHTTPN
EECCCCCCCCCCCCC		30.7122199227
437PhosphorylationHKVANTSSFHTTPNT
ECCCCCCCCCCCCCC		21.0022199227
440PhosphorylationANTSSFHTTPNTSLG
CCCCCCCCCCCCCCC		41.7722199227
441PhosphorylationNTSSFHTTPNTSLGM
CCCCCCCCCCCCCCC		13.1322199227
444PhosphorylationSFHTTPNTSLGMVQA
CCCCCCCCCCCCEEC		26.9122199227
445PhosphorylationFHTTPNTSLGMVQAT
CCCCCCCCCCCEECC		29.5722199227
452PhosphorylationSLGMVQATPSKVQPS
CCCCEECCCCCCCCC		15.8225159151
454PhosphorylationGMVQATPSKVQPSPT
CCEECCCCCCCCCCC		40.9022199227
455UbiquitinationMVQATPSKVQPSPTV
CEECCCCCCCCCCCC		46.20-
455UbiquitinationMVQATPSKVQPSPTV
CEECCCCCCCCCCCC		46.20-
459PhosphorylationTPSKVQPSPTVHTKE
CCCCCCCCCCCCHHH		18.9930266825
461PhosphorylationSKVQPSPTVHTKEAL
CCCCCCCCCCHHHHH		29.2930266825
464PhosphorylationQPSPTVHTKEALGFI
CCCCCCCHHHHHHHH		26.6629396449
479PhosphorylationMNMFQAPTLPDISDD
HHHHCCCCCCCCCCC		54.6722468782
484PhosphorylationAPTLPDISDDKDEWQ
CCCCCCCCCCHHHHH		47.3322468782
506UbiquitinationAFEAQFQKNVRSSGA
HHHHHHHHHHHHCCH		59.71-
510PhosphorylationQFQKNVRSSGAWGVN
HHHHHHHHCCHHCHH		28.9219691289
511PhosphorylationFQKNVRSSGAWGVNK
HHHHHHHCCHHCHHH		23.2019691289
521PhosphorylationWGVNKIISSLSSAFH
HCHHHHHHHHHHHEE		28.7923186163
522PhosphorylationGVNKIISSLSSAFHV
CHHHHHHHHHHHEEE		23.1228555341
524PhosphorylationNKIISSLSSAFHVFE
HHHHHHHHHHEEEEC		22.9023186163
525PhosphorylationKIISSLSSAFHVFED
HHHHHHHHHEEEECC		40.0025159151
535UbiquitinationHVFEDGNKENYGLPQ
EEECCCCCCCCCCCC		53.52-
535UbiquitinationHVFEDGNKENYGLPQ
EEECCCCCCCCCCCC		53.52PubMed
538PhosphorylationEDGNKENYGLPQPKN
CCCCCCCCCCCCCCC		22.5625159151
552PhosphorylationNKPTGARTFGERSVS
CCCCCCCCCCCCCCC		35.1422210691
557PhosphorylationARTFGERSVSRLPSK
CCCCCCCCCCCCCCC		21.8320860994
559PhosphorylationTFGERSVSRLPSKPK
CCCCCCCCCCCCCCH		29.3728102081
563PhosphorylationRSVSRLPSKPKEEVP
CCCCCCCCCCHHHCC		67.2123898821
564UbiquitinationSVSRLPSKPKEEVPH
CCCCCCCCCHHHCCC		59.16-
564UbiquitinationSVSRLPSKPKEEVPH
CCCCCCCCCHHHCCC		59.16-
566UbiquitinationSRLPSKPKEEVPHAE
CCCCCCCHHHCCCHH		70.96-
566UbiquitinationSRLPSKPKEEVPHAE
CCCCCCCHHHCCCHH		70.96-
579PhosphorylationAEEFLDDSTVWGIRC
HHHHCCCCCEEEEEE		25.2420068231
580PhosphorylationEEFLDDSTVWGIRCN
HHHCCCCCEEEEEEC		27.5420068231
588UbiquitinationVWGIRCNKTLAPSPK
EEEEEECCCCCCCCC		48.84-
588UbiquitinationVWGIRCNKTLAPSPK
EEEEEECCCCCCCCC		48.84-
589PhosphorylationWGIRCNKTLAPSPKS
EEEEECCCCCCCCCC		17.7321712546
593PhosphorylationCNKTLAPSPKSPGDF
ECCCCCCCCCCCCCC		39.0825159151
595UbiquitinationKTLAPSPKSPGDFTS
CCCCCCCCCCCCCCH		73.88-
596PhosphorylationTLAPSPKSPGDFTSA
CCCCCCCCCCCCCHH		37.1829255136
601PhosphorylationPKSPGDFTSAAQLAS
CCCCCCCCHHHHHHC		23.3830266825
602PhosphorylationKSPGDFTSAAQLAST
CCCCCCCHHHHHHCC		22.9230266825
608PhosphorylationTSAAQLASTPFHKLP
CHHHHHHCCCCCCCC		45.2526055452
609PhosphorylationSAAQLASTPFHKLPV
HHHHHHCCCCCCCCC		25.1125159151
613UbiquitinationLASTPFHKLPVESVH
HHCCCCCCCCCCEEE		55.66-
618PhosphorylationFHKLPVESVHILEDK
CCCCCCCEEEEECCC		21.1628555341
625UbiquitinationSVHILEDKENVVAKQ
EEEEECCCCHHHHHH		41.64PubMed
634PhosphorylationNVVAKQCTQATLDSC
HHHHHHHHHHHHHHH		20.8129978859
637PhosphorylationAKQCTQATLDSCEEN
HHHHHHHHHHHHHHC		22.6829978859
640PhosphorylationCTQATLDSCEENMVV
HHHHHHHHHHHCCCC		26.9221815630
649PhosphorylationEENMVVPSRDGKFSP
HHCCCCCCCCCCCCC		31.2425159151
653UbiquitinationVVPSRDGKFSPIQEK
CCCCCCCCCCCCCCC		47.13-
653AcetylationVVPSRDGKFSPIQEK
CCCCCCCCCCCCCCC		47.1325953088
653UbiquitinationVVPSRDGKFSPIQEK
CCCCCCCCCCCCCCC		47.13-
655PhosphorylationPSRDGKFSPIQEKSP
CCCCCCCCCCCCCCH		25.2829255136
660UbiquitinationKFSPIQEKSPKQALS
CCCCCCCCCHHHHHH		56.54-
660UbiquitinationKFSPIQEKSPKQALS
CCCCCCCCCHHHHHH		56.54-
661PhosphorylationFSPIQEKSPKQALSS
CCCCCCCCHHHHHHH		36.2623401153
663UbiquitinationPIQEKSPKQALSSHM
CCCCCCHHHHHHHHH		56.12-
663UbiquitinationPIQEKSPKQALSSHM
CCCCCCHHHHHHHHH		56.12-
667PhosphorylationKSPKQALSSHMYSAS
CCHHHHHHHHHHHHH		22.6320860994
668PhosphorylationSPKQALSSHMYSASL
CHHHHHHHHHHHHHH		17.0829978859
671PhosphorylationQALSSHMYSASLLRL
HHHHHHHHHHHHHHH		8.8229978859
672PhosphorylationALSSHMYSASLLRLS
HHHHHHHHHHHHHHC		12.1028348404
674PhosphorylationSSHMYSASLLRLSQP
HHHHHHHHHHHHCCC		23.2329978859
679PhosphorylationSASLLRLSQPAAGGV
HHHHHHHCCCCCCCE		27.9022067460
752PhosphorylationKLIFKLLSGLSKPVS
HHHHHHHHCCCCCHH		48.3922199227
755PhosphorylationFKLLSGLSKPVSSYP
HHHHHCCCCCHHHCC		38.1422199227
756UbiquitinationKLLSGLSKPVSSYPN
HHHHCCCCCHHHCCC		55.25-
756UbiquitinationKLLSGLSKPVSSYPN
HHHHCCCCCHHHCCC		55.25-
761PhosphorylationLSKPVSSYPNTFEWQ
CCCCHHHCCCCEEEE		7.9322817900
770UbiquitinationNTFEWQCKLPAIKPK
CCEEEEECCCCCCCC		42.26-
777UbiquitinationKLPAIKPKTEFQLGS
CCCCCCCCCEEECCC		56.54-
777UbiquitinationKLPAIKPKTEFQLGS
CCCCCCCCCEEECCC		56.54-
778PhosphorylationLPAIKPKTEFQLGSK
CCCCCCCCEEECCCE		51.03-
785UbiquitinationTEFQLGSKLVYVHHL
CEEECCCEEEHHHHH		39.93-
813UbiquitinationQGDLNDAKNKQKFVL
CCCHHHCCCCCCEEE		68.49-
815UbiquitinationDLNDAKNKQKFVLKV
CHHHCCCCCCEEEEE		54.91-
815UbiquitinationDLNDAKNKQKFVLKV
CHHHCCCCCCEEEEE		54.91-
821UbiquitinationNKQKFVLKVQKPANP
CCCCEEEEECCCCCC		37.00-
869PhosphorylationSVLVGELYSYGTLLN
CEEEEEEHHHHHHHH		8.78-
870PhosphorylationVLVGELYSYGTLLNA
EEEEEEHHHHHHHHH		29.70-
901UbiquitinationVISFAMRMLYMIEQV
HHHHHHHHHHHHHHH		1.70-
950UbiquitinationALIDLGQSIDMKLFP
EEHHCCCCCCCEEEC		20.82-
957UbiquitinationSIDMKLFPKGTIFTA
CCCCEEECCCCEEEE		44.60-
958UbiquitinationIDMKLFPKGTIFTAK
CCCEEECCCCEEEEE		62.44-
960PhosphorylationMKLFPKGTIFTAKCE
CEEECCCCEEEEEEC		21.02-
968PhosphorylationIFTAKCETSGFQCVE
EEEEEECCCCCCHHH		43.5526074081
969PhosphorylationFTAKCETSGFQCVEM
EEEEECCCCCCHHHH		18.4726074081
999UbiquitinationAATVYCMLFGTYMKV
HHHHHHHHHCCEEEE		2.98-
1007UbiquitinationFGTYMKVKNEGGECK
HCCEEEEECCCCCCC		43.70-
1008UbiquitinationGTYMKVKNEGGECKP
CCEEEEECCCCCCCC		57.01-
1014MalonylationKNEGGECKPEGLFRR
ECCCCCCCCCCHHHC		41.6326320211
1014UbiquitinationKNEGGECKPEGLFRR
ECCCCCCCCCCHHHC		41.63-
1024UbiquitinationGLFRRLPHLDMWNEF
CHHHCCCCHHHHHHH		38.77-
1056UbiquitinationLLRQKLKKVFQQHYT
HHHHHHHHHHHHHHH		59.73-
1065UbiquitinationFQQHYTNKIRALRNR
HHHHHHHHHHHHHHH		26.26-
1081UbiquitinationIVLLLECKRSRK---
HHHHHHHHHHCC---		43.99-
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
148TPhosphorylationKinaseBUB1O43683
PSP
173TPhosphorylationKinaseBUB1O43683
PSP
176SPhosphorylationKinaseBUB1O43683
PSP
198SPhosphorylationKinaseBUB1O43683
PSP
213TPhosphorylationKinaseBUB1O43683
PSP
314SPhosphorylationKinaseATMQ13315
PSP
419SPhosphorylationKinaseBUB1O43683
PSP
454SPhosphorylationKinaseBUB1O43683
PSP
510SPhosphorylationKinaseBUB1O43683
PSP
511SPhosphorylationKinaseBUB1O43683
PSP
525SPhosphorylationKinaseBUB1O43683
PSP
552TPhosphorylationKinaseBUB1O43683
PSP
563SPhosphorylationKinaseBUB1O43683
PSP
589TPhosphorylationKinaseBUB1O43683
PSP
593SPhosphorylationKinaseCDK1P06493
PSP
609TPhosphorylationKinaseCDK1P06493
Uniprot
618SPhosphorylationKinaseBUB1O43683
PSP
667SPhosphorylationKinaseBUB1O43683
PSP
679SPhosphorylationKinaseBUB1O43683
PSP
752SPhosphorylationKinaseBUB1O43683
PSP
960TPhosphorylationKinaseBUB1O43683
PSP
969SPhosphorylationKinaseBUB1O43683
PSP
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:17158872
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
609TPhosphorylation

16760428
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 BUB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRK_HUMANCRKphysical
16189514
ARI2_HUMANARIH2physical
16189514
HDAC1_HUMANHDAC1physical
15388328
RAE1L_HUMANRAE1physical
11352911
APC_HUMANAPCphysical
11283619
KNL1_HUMANCASC5physical
20360068
UBR5_HUMANUBR5physical
20360068
NDC80_HUMANNDC80physical
20360068
MIS12_HUMANMIS12physical
20360068
DSN1_HUMANDSN1physical
20360068
SPC25_HUMANSPC25physical
20360068
BUB1B_HUMANBUB1Bphysical
20360068
SPC24_HUMANSPC24physical
20360068
ZWINT_HUMANZWINTphysical
20360068
NSL1_HUMANNSL1physical
20360068
NUF2_HUMANNUF2physical
20360068
BUB1_HUMANBUB1physical
20360068
NSL1_HUMANNSL1physical
20231385
KNL1_HUMANCASC5physical
22660415
PLK1_HUMANPLK1physical
16760428
BUB3_HUMANBUB3physical
16760428
BUB1B_HUMANBUB1Bphysical
9914370
CENPE_HUMANCENPEphysical
9914370
KNL1_HUMANCASC5physical
19141287
BUB3_HUMANBUB3physical
20220147
BUB1B_HUMANBUB1Bphysical
20220147
BUB3_HUMANBUB3physical
21988832
RDH12_HUMANRDH12physical
21988832
BUB3_HUMANBUB3physical
25416956
BUB1B_HUMANBUB1Bphysical
26186194
KNL1_HUMANCASC5physical
26186194
CDC20_HUMANCDC20physical
26186194
RAE1L_HUMANRAE1physical
26186194
RABL6_HUMANRABL6physical
26186194
BPTF_HUMANBPTFphysical
26186194
MIS12_HUMANMIS12physical
26186194
CDC20_HUMANCDC20physical
25669885
MD2L1_HUMANMAD2L1physical
25669885
CDC20_HUMANCDC20physical
26496610
PLEC_HUMANPLECphysical
26496610
BUB3_HUMANBUB3physical
26496610
RBPMS_HUMANRBPMSphysical
26496610
HPS5_HUMANHPS5physical
26496610
KI26B_HUMANKIF26Bphysical
26496610
KNL1_HUMANCASC5physical
26496610
APC_HUMANAPCphysical
25241761
4EBP1_HUMANEIF4EBP1physical
25241761
BUB1B_HUMANBUB1Bphysical
26148513
BUB3_HUMANBUB3physical
26148513
KNL1_HUMANCASC5physical
26148513
BUB1B_HUMANBUB1Bphysical
28514442
RAE1L_HUMANRAE1physical
28514442
KNL1_HUMANCASC5physical
28514442
MIS12_HUMANMIS12physical
28514442
CDC20_HUMANCDC20physical
28514442
BPTF_HUMANBPTFphysical
28514442
NDC80_HUMANNDC80physical
28514442
HNRC1_HUMANHNRNPCL1physical
28514442
HSF1_HUMANHSF1physical
27173435
CDC20_HUMANCDC20physical
26912231
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563; SER-593 ANDSER-596, AND MASS SPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-331; SER-375;SER-563; SER-596; SER-655 AND SER-661, AND MASS SPECTROMETRY.
"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-593; SER-596; SER-655AND SER-661, AND MASS 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 THR-461; SER-593; SER-596AND SER-655, AND MASS SPECTROMETRY.
"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-159 AND THR-452, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASSSPECTROMETRY.
"Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 isrequired for the kinetochore localization of Plk1.";
Qi W., Tang Z., Yu H.;
Mol. Biol. Cell 17:3705-3716(2006).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PLK1, PHOSPHORYLATIONAT THR-609, AND MUTAGENESIS OF THR-609.

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