BUB3_HUMAN - dbPTM
BUB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BUB3_HUMAN
UniProt AC O43684
Protein Name Mitotic checkpoint protein BUB3
Gene Name BUB3
Organism Homo sapiens (Human).
Sequence Length 328
Subcellular Localization Nucleus. Chromosome, centromere, kinetochore. Starts to localize at kinetochores in prometaphase I (Pro-MI) stage and maintains the localization until the metaphase I-anaphase I (MI-AI) transition..
Protein Description Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1..
Protein Sequence MTGSNEFKLNQPPEDGISSVKFSPNTSQFLLVSSWDTSVRLYDVPANSMRLKYQHTGAVLDCAFYDPTHAWSGGLDHQLKMHDLNTDQENLVGTHDAPIRCVEYCPEVNVMVTGSWDQTVKLWDPRTPCNAGTFSQPEKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSPEVQKKKYAFKCHRLKENNIEQIYPVNAISFHNIHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGTTLAIASSYMYEMDDTEHPEDGIFIRQVTDAETKPKSPCT
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
2Phosphorylation------MTGSNEFKL
------CCCCCCCCC		49.6823312004
4Phosphorylation----MTGSNEFKLNQ
----CCCCCCCCCCC		24.8223312004
8SumoylationMTGSNEFKLNQPPED
CCCCCCCCCCCCCCC		40.11-
8SumoylationMTGSNEFKLNQPPED
CCCCCCCCCCCCCCC		40.11-
8UbiquitinationMTGSNEFKLNQPPED
CCCCCCCCCCCCCCC		40.11-
18PhosphorylationQPPEDGISSVKFSPN
CCCCCCCCCEEECCC		34.3121712546
19PhosphorylationPPEDGISSVKFSPNT
CCCCCCCCEEECCCC		27.6620057499
21UbiquitinationEDGISSVKFSPNTSQ
CCCCCCEEECCCCCC		41.9121906983
23PhosphorylationGISSVKFSPNTSQFL
CCCCEEECCCCCCEE		16.1228348404
26PhosphorylationSVKFSPNTSQFLLVS
CEEECCCCCCEEEEE		27.5628348404
27PhosphorylationVKFSPNTSQFLLVSS
EEECCCCCCEEEEEE		26.1028348404
33PhosphorylationTSQFLLVSSWDTSVR
CCCEEEEEECCCEEE		26.19-
42PhosphorylationWDTSVRLYDVPANSM
CCCEEEEEECCCCCC		12.3427642862
48PhosphorylationLYDVPANSMRLKYQH
EEECCCCCCEEEEEE		13.85-
52UbiquitinationPANSMRLKYQHTGAV
CCCCCEEEEEECCCE		32.2821906983
52AcetylationPANSMRLKYQHTGAV
CCCCCEEEEEECCCE		32.2825953088
80UbiquitinationGGLDHQLKMHDLNTD
CCHHHEEEECCCCCC		27.84-
86PhosphorylationLKMHDLNTDQENLVG
EEECCCCCCCHHCCC		46.48-
126MethylationTVKLWDPRTPCNAGT
EEEEECCCCCCCCCC		49.15-
127PhosphorylationVKLWDPRTPCNAGTF
EEEECCCCCCCCCCC		37.2727273156
129S-nitrosylationLWDPRTPCNAGTFSQ
EECCCCCCCCCCCCC		5.572212679
139AcetylationGTFSQPEKVYTLSVS
CCCCCCCEEEEEEEC		47.4225953088
139UbiquitinationGTFSQPEKVYTLSVS
CCCCCCCEEEEEEEC		47.4221906983
141PhosphorylationFSQPEKVYTLSVSGD
CCCCCEEEEEEECCC		17.0328152594
142PhosphorylationSQPEKVYTLSVSGDR
CCCCEEEEEEECCCE		18.6228152594
144PhosphorylationPEKVYTLSVSGDRLI
CCEEEEEEECCCEEE		13.3628152594
146PhosphorylationKVYTLSVSGDRLIVG
EEEEEEECCCEEEEE		31.4428152594
149MethylationTLSVSGDRLIVGTAG
EEEECCCEEEEECCC		29.82-
154PhosphorylationGDRLIVGTAGRRVLV
CCEEEEECCCCEEEE		18.2922817900
169NitrationWDLRNMGYVQQRRES
EECCCCCHHHHHHHC		5.59-
179UbiquitinationQRRESSLKYQTRCIR
HHHHCCCHHHHHEEE		36.9419608861
1792-HydroxyisobutyrylationQRRESSLKYQTRCIR
HHHHCCCHHHHHEEE		36.94-
179AcetylationQRRESSLKYQTRCIR
HHHHCCCHHHHHEEE		36.9419608861
179 (in isoform 2)Ubiquitination-36.94-
186MethylationKYQTRCIRAFPNKQG
HHHHHEEECCCCCCC		33.53-
191UbiquitinationCIRAFPNKQGYVLSS
EEECCCCCCCEEEEE		45.3921906983
191UbiquitinationCIRAFPNKQGYVLSS
EEECCCCCCCEEEEE		45.3921890473
1912-HydroxyisobutyrylationCIRAFPNKQGYVLSS
EEECCCCCCCEEEEE		45.39-
191 (in isoform 2)Ubiquitination-45.39-
191AcetylationCIRAFPNKQGYVLSS
EEECCCCCCCEEEEE		45.3926051181
194PhosphorylationAFPNKQGYVLSSIEG
CCCCCCCEEEEEEEC		8.8424043423
197PhosphorylationNKQGYVLSSIEGRVA
CCCCEEEEEEECEEE		21.1624043423
198PhosphorylationKQGYVLSSIEGRVAV
CCCEEEEEEECEEEE		22.0924043423
207PhosphorylationEGRVAVEYLDPSPEV
ECEEEEEECCCCHHH		15.1430266825
207NitrationEGRVAVEYLDPSPEV
ECEEEEEECCCCHHH		15.14-
211PhosphorylationAVEYLDPSPEVQKKK
EEEECCCCHHHHHHH		33.1019664994
216AcetylationDPSPEVQKKKYAFKC
CCCHHHHHHHHEEEC		57.3123954790
216MalonylationDPSPEVQKKKYAFKC
CCCHHHHHHHHEEEC		57.3126320211
216 (in isoform 2)Ubiquitination-57.31-
2162-HydroxyisobutyrylationDPSPEVQKKKYAFKC
CCCHHHHHHHHEEEC		57.31-
216UbiquitinationDPSPEVQKKKYAFKC
CCCHHHHHHHHEEEC		57.3118781797
217UbiquitinationPSPEVQKKKYAFKCH
CCHHHHHHHHEEECC		33.65-
218UbiquitinationSPEVQKKKYAFKCHR
CHHHHHHHHEEECCC		49.17-
222UbiquitinationQKKKYAFKCHRLKEN
HHHHHEEECCCCCCC		22.44-
222AcetylationQKKKYAFKCHRLKEN
HHHHHEEECCCCCCC		22.4425953088
2222-HydroxyisobutyrylationQKKKYAFKCHRLKEN
HHHHHEEECCCCCCC		22.44-
227UbiquitinationAFKCHRLKENNIEQI
EEECCCCCCCCCEEE		59.35-
227 (in isoform 2)Ubiquitination-59.35-
227SumoylationAFKCHRLKENNIEQI
EEECCCCCCCCCEEE		59.35-
227AcetylationAFKCHRLKENNIEQI
EEECCCCCCCCCEEE		59.3526051181
266UbiquitinationNIWDPFNKKRLCQFH
CCCCCCCCCCCCHHC		39.38-
317PhosphorylationGIFIRQVTDAETKPK
CEEEEEECCCCCCCC		22.5823403867
321PhosphorylationRQVTDAETKPKSPCT
EEECCCCCCCCCCCC		55.1323403867
322UbiquitinationQVTDAETKPKSPCT-
EECCCCCCCCCCCC-		41.7921906983
322SumoylationQVTDAETKPKSPCT-
EECCCCCCCCCCCC-		41.79-
322SumoylationQVTDAETKPKSPCT-
EECCCCCCCCCCCC-		41.79-
322AcetylationQVTDAETKPKSPCT-
EECCCCCCCCCCCC-		41.7923749302
322 (in isoform 2)Ubiquitination-41.79-
324UbiquitinationTDAETKPKSPCT---
CCCCCCCCCCCC---		69.46-
324 (in isoform 2)Ubiquitination-69.46-
325PhosphorylationDAETKPKSPCT----
CCCCCCCCCCC----		33.4623401153
328PhosphorylationTKPKSPCT-------
CCCCCCCC-------		45.0623403867
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
19SPhosphorylationKinaseBUB1O43683
PSP
207YPhosphorylationKinasePKMP14618
PSP
211SPhosphorylationKinaseP38AQ16539
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BUB3_HUMAN !!
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 BUB3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
15388328
HDAC2_HUMANHDAC2physical
15388328
BUB1B_HUMANBUB1Bphysical
9660858
APC_HUMANAPCphysical
11283619
ZN207_HUMANZNF207physical
22939629
SEPT2_HUMANSEPT2physical
22939629
ZN207_HUMANZNF207physical
22365833
NKAP_HUMANNKAPphysical
22365833
BUB1B_HUMANBUB1Bphysical
20220147
SGT1_HUMANSUGT1physical
21988832
CPNE1_HUMANCPNE1physical
21988832
UBA1_HUMANUBA1physical
21988832
RL37A_HUMANRPL37Aphysical
21988832
THA_HUMANTHRAphysical
21988832
ZN207_HUMANZNF207physical
21988832
EXOC3_HUMANEXOC3physical
21988832
CLIP1_HUMANCLIP1physical
22863883
TCPH_HUMANCCT7physical
26186194
BUB1B_HUMANBUB1Bphysical
26186194
TCPB_HUMANCCT2physical
26186194
BUB1_HUMANBUB1physical
26186194
BTBDA_HUMANBTBD10physical
26186194
KCD20_HUMANKCTD20physical
26186194
ZN207_HUMANZNF207physical
26186194
ZC3H1_HUMANZFC3H1physical
26186194
APC16_HUMANANAPC16physical
26186194
UBR5_HUMANUBR5physical
25833949
HXK2_HUMANHK2physical
26344197
BUB1_HUMANBUB1physical
26496610
BUB1B_HUMANBUB1Bphysical
26496610
DYN2_HUMANDNM2physical
26496610
ZN207_HUMANZNF207physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPB_HUMANCCT2physical
26496610
TCPE_HUMANCCT5physical
26496610
INT7_HUMANINTS7physical
26496610
RAIN_HUMANRASIP1physical
26496610
K1109_HUMANKIAA1109physical
26496610
UBR5_HUMANUBR5physical
26438829
IMB1_HUMANKPNB1physical
26438829
ZN207_HUMANZNF207physical
26438829
BUB1_HUMANBUB1physical
28514442
BUB1B_HUMANBUB1Bphysical
28514442
ZC3H1_HUMANZFC3H1physical
28514442
KCD20_HUMANKCTD20physical
28514442
BTBDA_HUMANBTBD10physical
28514442
ZN207_HUMANZNF207physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
CDC27_HUMANCDC27physical
28514442
TCPD_HUMANCCT4physical
28514442
KNL1_HUMANCASC5physical
28514442
CDC23_HUMANCDC23physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPE_HUMANCCT5physical
28514442
TCPA_HUMANTCP1physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
ACTBL_HUMANACTBL2physical
28514442
TCPQ_HUMANCCT8physical
28514442
ACTA_HUMANACTA2physical
28514442
LZTL1_HUMANLZTFL1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BUB3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-211, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-216, AND MASSSPECTROMETRY.

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