BOREA_HUMAN - dbPTM
BOREA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BOREA_HUMAN
UniProt AC Q53HL2
Protein Name Borealin
Gene Name CDCA8
Organism Homo sapiens (Human).
Sequence Length 280
Subcellular Localization Nucleus, nucleolus . Cytoplasm . Cytoplasm, cytoskeleton, spindle . Chromosome, centromere . Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase thr
Protein Description Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment..
Protein Sequence MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK
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
5Acetylation---MAPRKGSSRVAK
---CCCCCCCCCHHC		63.1812435333
7Phosphorylation-MAPRKGSSRVAKTN
-CCCCCCCCCHHCCH		20.2923403867
8PhosphorylationMAPRKGSSRVAKTNS
CCCCCCCCCHHCCHH		39.1723403867
12UbiquitinationKGSSRVAKTNSLRRR
CCCCCHHCCHHHHHH		45.4429967540
13PhosphorylationGSSRVAKTNSLRRRK
CCCCHHCCHHHHHHH		21.9423403867
15PhosphorylationSRVAKTNSLRRRKLA
CCHHCCHHHHHHHHH		28.6017192257
20UbiquitinationTNSLRRRKLASFLKD
CHHHHHHHHHHHHHH		46.7429967540
23PhosphorylationLRRRKLASFLKDFDR
HHHHHHHHHHHHHCH		41.3617192257
37UbiquitinationREVEIRIKQIESDRQ
HHHHHHHHHHHHHHH		35.0633845483
48UbiquitinationSDRQNLLKEVDNLYN
HHHHHHHHHHHHHHH		59.8829967540
54PhosphorylationLKEVDNLYNIEILRL
HHHHHHHHHHHHHCC		21.9827642862
88PhosphorylationQALEEAATADLDITE
HHHHHHHHCCCCHHH		27.9623403867
94PhosphorylationATADLDITEINKLTA
HHCCCCHHHHHHHHH		30.4023403867
98UbiquitinationLDITEINKLTAEAIQ
CCHHHHHHHHHHHHH		53.5329967540
100PhosphorylationITEINKLTAEAIQTP
HHHHHHHHHHHHHCC		24.8624732914
106PhosphorylationLTAEAIQTPLKSAKT
HHHHHHHCCHHCCCC		25.1930266825
109UbiquitinationEAIQTPLKSAKTRKV
HHHHCCHHCCCCCCE		49.9621906983
110PhosphorylationAIQTPLKSAKTRKVI
HHHCCHHCCCCCCEE		42.5517192257
112UbiquitinationQTPLKSAKTRKVIQV
HCCHHCCCCCCEEEE		56.8222817900
115UbiquitinationLKSAKTRKVIQVDEM
HHCCCCCCEEEEEEE		49.2529967540
135UbiquitinationEEEENERKNLQTARV
HHHHHHHHHHHHHHH		56.6929967540
135SumoylationEEEENERKNLQTARV
HHHHHHHHHHHHHHH		56.6928112733
152PhosphorylationCPPSKKRTQSIQGKG
CCCCCCCCCCCCCCC		35.2320860994
154PhosphorylationPSKKRTQSIQGKGKG
CCCCCCCCCCCCCCC		19.1026055452
164PhosphorylationGKGKGKRSSRANTVT
CCCCCCCCCCCCCCC		27.8826055452
165PhosphorylationKGKGKRSSRANTVTP
CCCCCCCCCCCCCCC		39.1726055452
169PhosphorylationKRSSRANTVTPAVGR
CCCCCCCCCCCCCCE		25.4418243099
171PhosphorylationSSRANTVTPAVGRLE
CCCCCCCCCCCCEEE		11.9519691289
180PhosphorylationAVGRLEVSMVKPTPG
CCCEEEEEEECCCCC		14.4226055452
183UbiquitinationRLEVSMVKPTPGLTP
EEEEEEECCCCCCCC		34.2423000965
183AcetylationRLEVSMVKPTPGLTP
EEEEEEECCCCCCCC		34.2423236377
185PhosphorylationEVSMVKPTPGLTPRF
EEEEECCCCCCCCCC		25.0325159151
189PhosphorylationVKPTPGLTPRFDSRV
ECCCCCCCCCCCCCC		20.5225159151
194PhosphorylationGLTPRFDSRVFKTPG
CCCCCCCCCCCCCCC		27.8617192257
198UbiquitinationRFDSRVFKTPGLRTP
CCCCCCCCCCCCCCC		51.4527667366
199PhosphorylationFDSRVFKTPGLRTPA
CCCCCCCCCCCCCCC		15.8925159151
204PhosphorylationFKTPGLRTPAAGERI
CCCCCCCCCCCCCCE		23.4830266825
212PhosphorylationPAAGERIYNISGNGS
CCCCCCEEECCCCCC		16.8030266825
215PhosphorylationGERIYNISGNGSPLA
CCCEEECCCCCCCCC		23.6730266825
219PhosphorylationYNISGNGSPLADSKE
EECCCCCCCCCCCCE		22.2729255136
224PhosphorylationNGSPLADSKEIFLTV
CCCCCCCCCEEEEEE		26.9530266825
225UbiquitinationGSPLADSKEIFLTVP
CCCCCCCCEEEEEEE		56.2123503661
230PhosphorylationDSKEIFLTVPVGGGE
CCCEEEEEEECCCHH		16.4124732914
238PhosphorylationVPVGGGESLRLLASD
EECCCHHHHHHHHHH		23.2822817900
244PhosphorylationESLRLLASDLQRHSI
HHHHHHHHHHHHCCH		38.5325159151
250PhosphorylationASDLQRHSIAQLDPE
HHHHHHCCHHHCCHH		23.0825159151
263UbiquitinationPEALGNIKKLSNRLA
HHHHHHHHHHHHHHH		52.2232015554
264UbiquitinationEALGNIKKLSNRLAQ
HHHHHHHHHHHHHHH		54.0423503661
274PhosphorylationNRLAQICSSIRTHK-
HHHHHHHHHHHHCC-		30.3517192257
275PhosphorylationRLAQICSSIRTHK--
HHHHHHHHHHHCC--		16.2119691289
278PhosphorylationQICSSIRTHK-----
HHHHHHHHCC-----		32.1417483322
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
88TPhosphorylationKinaseMPS1P33981
GPS
94TPhosphorylationKinaseMPS1P33981
GPS
154SPhosphorylationKinaseAURKBQ96GD4
GPS
165SPhosphorylationKinaseAURBQ96GD4
PSP
169TPhosphorylationKinaseMPS1P33981
GPS
219SPhosphorylationKinaseAURKBQ96GD4
GPS
219SPhosphorylationKinaseCDK1P06493
PSP
230TPhosphorylationKinaseMPS1P33981
GPS
238SPhosphorylationKinaseMPS1P33981
GPS
275SPhosphorylationKinaseAURKBQ96GD4
GPS
278TPhosphorylationKinaseAURKBQ96GD4
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
88TPhosphorylation

19530738
169TPhosphorylation

19530738
230TPhosphorylation

19530738
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 BOREA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AURKB_HUMANAURKBphysical
15260989
BIRC5_HUMANBIRC5physical
15260989
INCE_HUMANINCENPphysical
15249581
RCC2_HUMANRCC2physical
15249581
AURKB_HUMANAURKBphysical
15249581
BIRC5_HUMANBIRC5physical
15249581
AURKB_HUMANAURKBphysical
19951914
UBC9_HUMANUBE2Iphysical
18946085
RBP2_HUMANRANBP2physical
18946085
XPO1_HUMANXPO1physical
17099693
AURKB_HUMANAURKBphysical
17099693
INCE_HUMANINCENPphysical
17099693
BIRC5_HUMANBIRC5physical
17099693
BIRC5_HUMANBIRC5physical
17956729
INCE_HUMANINCENPphysical
17956729
AURKB_HUMANAURKBphysical
17956729
INCE_HUMANINCENPphysical
16571674
BIRC5_HUMANBIRC5physical
16571674
BOREA_HUMANCDCA8physical
16571674
BIRC5_HUMANBIRC5physical
16291752
AURKB_HUMANAURKBphysical
18243099
BIRC5_HUMANBIRC5physical
18243099
NEK3_HUMANNEK3physical
21988832
DRB3_HUMANHLA-DRB3physical
21988832
MAPK5_HUMANMAPKAPK5physical
21988832
PIAS2_HUMANPIAS2physical
18946085
SENP3_HUMANSENP3physical
18946085
AURKB_HUMANAURKBphysical
18946085
INCE_HUMANINCENPphysical
18946085
BIRC5_HUMANBIRC5physical
18946085
ATP4A_HUMANATP4Aphysical
26186194
GPM6B_HUMANGPM6Bphysical
26186194
MYH3_HUMANMYH3physical
26186194
MYH7_HUMANMYH7physical
26186194
MYH4_HUMANMYH4physical
26186194
DPYL1_HUMANCRMP1physical
26186194
DPYL3_HUMANDPYSL3physical
26186194
DPYL2_HUMANDPYSL2physical
26186194
STXB1_HUMANSTXBP1physical
26186194
GBG2_HUMANGNG2physical
26186194
BIRC5_HUMANBIRC5physical
26186194
SYPH_HUMANSYPphysical
26186194
KCC2A_HUMANCAMK2Aphysical
26186194
VISL1_HUMANVSNL1physical
26186194
MTHR_HUMANMTHFRphysical
26186194
DCLK1_HUMANDCLK1physical
26186194
AP180_HUMANSNAP91physical
26186194
MYH3_HUMANMYH3physical
28514442
MYH7_HUMANMYH7physical
28514442
VISL1_HUMANVSNL1physical
28514442
MYH4_HUMANMYH4physical
28514442
ATP4A_HUMANATP4Aphysical
28514442
KCC2A_HUMANCAMK2Aphysical
28514442
DPYL1_HUMANCRMP1physical
28514442
DPYL3_HUMANDPYSL3physical
28514442
GBG2_HUMANGNG2physical
28514442
MTHR_HUMANMTHFRphysical
28514442
STXB1_HUMANSTXBP1physical
28514442
DCLK1_HUMANDCLK1physical
28514442
AP180_HUMANSNAP91physical
28514442
SYT1_HUMANSYT1physical
28514442
TAU_HUMANMAPTphysical
28514442
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 BOREA_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 THR-106 AND SER-219, ANDMASS 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 TYR-212; SER-219 ANDSER-224, AND MASS SPECTROMETRY.
"RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin.";
Klein U.R., Haindl M., Nigg E.A., Muller S.;
Mol. Biol. Cell 20:410-418(2009).
Cited for: INTERACTION WITH SENP3; UBE2I AND RANBP2, SUMOYLATION, SUBCELLULARLOCATION, MUTAGENESIS OF LYS-26, AND PHOSPHORYLATION AT THR-88; THR94;THR-169; THR-230 AND SER-238.
"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-219, AND MASSSPECTROMETRY.
"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 THR-106; THR-189; THR-204AND SER-219, 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 SER-15; SER-23; THR-106;SER-110; SER-154; SER-164; SER-165; THR-189; SER-194; THR-204;SER-219; SER-244 AND SER-274, 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 THR-106; SER-154; THR-169;THR-171; SER-180; THR-199; THR-204; SER-215 AND SER-219, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-106 AND SER-219, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASSSPECTROMETRY.
"Borealin: a novel chromosomal passenger required for stability of thebipolar mitotic spindle.";
Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F.,Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C.;
J. Cell Biol. 166:179-191(2004).
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE CPC COMPLEX,PHOSPHORYLATION AT SER-165, AND MUTAGENESIS OF SER-165.

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