Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Aurora kinase B  

UniProtKB / Swiss-Prot ID :  AURKB_HUMAN

Gene Name (Synonyms) : 
AURKB, AIK2, AIM1, AIRK2, ARK2, STK1, STK12, STK5  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Chromosome. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokine 

Protein Function :  Serine/threonine-protein kinase 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. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, GSG2/Haspin, and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis. A positive feedback between GSG2 and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. 

Protein Sequence MAQKENSYPWPYGRQTAPSGLSTLPQRVLRKEPVTPSALVLMSRSNVQPTAAPGQKVMENSSGTPDILTR...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
52A -> V. VAR_040383
100H -> Q (in dbSNP:rs3027254). VAR_027970
179T -> M. VAR_040384
298M -> T (in dbSNP:rs1059476). VAR_027971
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAQKEN
---CCCCCC
29.20UniProtKB
Link-
7PhosphoserineQKENSYPWP
CCCCCCCCC
33.39HPRD
Link-
7PhosphoserineQKENSYPWP
CCCCCCCCC
33.39PhosphoELM
Link-
7PhosphoserineQKENSYPWP
CCCCCCCCC
33.39Phosphositeplus
Link-
7PhosphoserineQKENSYPWP
CCCCCCCCC
33.39SysPTM
Link-
7Phosphoserine.QKENSYPWP
CCCCCCCCC
33.39UniProtKB
Link-
8PhosphotyrosineKENSYPWPY
CCCCCCCCC
22.39Phosphositeplus
Link-
12PhosphotyrosineYPWPYGRQT
CCCCCCCCC
22.52HPRD
Link-
12PhosphotyrosineYPWPYGRQT
CCCCCCCCC
22.52PhosphoELM
Link-
12PhosphotyrosineYPWPYGRQT
CCCCCCCCC
22.52Phosphositeplus
Link-
12PhosphotyrosineYPWPYGRQT
CCCCCCCCC
22.52SysPTM
Link-
12Phosphotyrosine.YPWPYGRQT
CCCCCCCCC
22.52UniProtKB
Link-
16PhosphothreonineYGRQTAPSG
CCCCCCCCC
38.89HPRD
Link-
16Phosphothreonine.YGRQTAPSG
CCCCCCCCC
38.89UniProtKB
Link-
35PhosphothreonineKEPVTPSAL
CCCCCCCCH
23.42HPRD
Link-
35PhosphothreonineKEPVTPSAL
CCCCCCCCH
23.42PhosphoELM
Link-
35PhosphothreonineKEPVTPSAL
CCCCCCCCH
23.42Phosphositeplus
Link-
35PhosphothreonineKEPVTPSAL
CCCCCCCCH
23.42SysPTM
Link-
35Phosphothreonine.KEPVTPSAL
CCCCCCCCH
23.42UniProtKB
Link-
45PhosphoserineLMSRSNVQP
CCCCCCCCC
33.76HPRD
Link-
45PhosphoserineLMSRSNVQP
CCCCCCCCC
33.76Phosphositeplus
Link-
45PhosphoserineLMSRSNVQP
CCCCCCCCC
33.76SysPTM
Link-
45Phosphoserine.LMSRSNVQP
CCCCCCCCC
33.76UniProtKB
Link-
56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)APGQKVMEN
CCCCCCCCC
49.84Phosphositeplus
Link-
61PhosphoserineVMENSSGTP
CCCCCCCCC
19.48HPRD
Link-
61PhosphoserineVMENSSGTP
CCCCCCCCC
19.48Phosphositeplus
Link-
61PhosphoserineVMENSSGTP
CCCCCCCCC
19.48SysPTM
Link-
61Phosphoserine.VMENSSGTP
CCCCCCCCC
19.48UniProtKB
Link-
62PhosphoserineMENSSGTPD
CCCCCCCCC
59.26HPRD
Link-
62PhosphoserineMENSSGTPD
CCCCCCCCC
59.26Phosphositeplus
Link-
62Phosphoserine.MENSSGTPD
CCCCCCCCC
59.26UniProtKB
Link-
64PhosphothreonineNSSGTPDIL
CCCCCCCCC
21.53HPRD
Link-
64PhosphothreonineNSSGTPDIL
CCCCCCCCC
21.53Phosphositeplus
Link-
64PhosphothreonineNSSGTPDIL
CCCCCCCCC
21.53SysPTM
Link-
64Phosphothreonine.NSSGTPDIL
CCCCCCCCC
21.53UniProtKB
Link-
85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)RPLGKGKFG
EEEEECCCE
67.61Phosphositeplus
Link
85Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RPLGKGKFG
EEEEECCCE
67.61Phosphositeplus
Link
87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)LGKGKFGNV
EEECCCEEE
54.29Phosphositeplus
Link
92PhosphotyrosineFGNVYLARE
CEEEEEEEE
9.92HPRD
Link
92PhosphotyrosineFGNVYLARE
CEEEEEEEE
9.92SysPTM
Link
92Phosphotyrosine.FGNVYLARE
CEEEEEEEE
9.92UniProtKB
Link
115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SQIEKEGVE
HHCCCHHHH
62.49Phosphositeplus
Link
202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)HRDIKPENL
EEECCCCCE
51.04Phosphositeplus
Link
202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HRDIKPENL
EEECCCCCE
51.04Phosphositeplus
Link
211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LLGLKGELK
EECCCCCEE
48.84Phosphositeplus
Link
215Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KGELKIADF
CCCEEEEEE
31.39Phosphositeplus
Link
227PhosphoserineVHAPSLRRK
EEECCCEEE
34.98HPRD
Link-
227PhosphoserineVHAPSLRRK
EEECCCEEE
34.98Phosphositeplus
Link-
227PhosphoserineVHAPSLRRK
EEECCCEEE
34.98SysPTM
Link-
227Phosphoserine.VHAPSLRRK
EEECCCEEE
34.98UniProtKB
Link-
232PhosphothreonineLRRKTMCGT
CEEEEEEEC
18.84HPRD
Link-
232PhosphothreonineLRRKTMCGT
CEEEEEEEC
18.84Phosphositeplus
Link-
232PhosphothreonineLRRKTMCGT
CEEEEEEEC
18.84SysPTM
Link-
232Phosphothreonine (Aurora B)LRRKTMCGT
CEEEEEEEC
18.84PhosphoELM
Link-
232Phosphothreonine; by autocatalysis.LRRKTMCGT
CEEEEEEEC
18.84UniProtKB
Link-
236PhosphothreonineTMCGTLDYL
EEEECHHHC
16.13HPRD
Link
236PhosphothreonineTMCGTLDYL
EEEECHHHC
16.13PhosphoELM
Link
236PhosphothreonineTMCGTLDYL
EEEECHHHC
16.13Phosphositeplus
Link
236PhosphothreonineTMCGTLDYL
EEEECHHHC
16.13SysPTM
Link
236Phosphothreonine.TMCGTLDYL
EEEECHHHC
16.13UniProtKB
Link
287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RRIVKVDLK
HHHHCCCCC
27.88Phosphositeplus
Link
291Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KVDLKFPAS
CCCCCCCCC
44.85Phosphositeplus
Link
306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DLISKLLRH
HHHHHHCCC
44.54Phosphositeplus
Link
313PhosphoserineRHNPSERLP
CCCCCCCCC
40.44HPRD
Link
313PhosphoserineRHNPSERLP
CCCCCCCCC
40.44Phosphositeplus
Link
313PhosphoserineRHNPSERLP
CCCCCCCCC
40.44SysPTM
Link
313Phosphoserine.RHNPSERLP
CCCCCCCCC
40.44UniProtKB
Link
331PhosphoserineVRANSRRVL
CCCCCCCCC
22.07Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
BIRC5_HUMANphysical interactionMINT-4509580MINT17099693
BIRC5_HUMANdirect interactionMINT-4509558MINT17099693
TBL3_HUMANphysical interactionMINT-65154MINT16169070
PP1A_HUMANphysical interactionEBI-1206808
intact17274640
BIRC5_HUMANphysical interactionEBI-1397794
intact17681274
INCE_HUMANphysical interaction
physical interaction
EBI-1555366
EBI-1555353
intact17956729
17956729
TACC1_HUMANphysical interaction
colocalization
EBI-624334
EBI-624347
intact15064709
15064709
TBL3_HUMANphysical interactionEBI-736328
intact16169070
SEPT1_HUMANphysical interaction
phosphorylation
physical interaction
colocalization
physical interaction
EBI-693011
EBI-693058
EBI-693
intact16179162
16179162
16179162
16179162
16179162
CENPA_HUMANin vitroHPRD:05397HPRD11756469
DESM_HUMANin vitroHPRD:05397HPRD12686604
RASA1_HUMANin vivo
yeast 2-hybrid
HPRD:05397HPRD11976319
BIRC5_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:05397HPRD12419797
11516652
16291752
INCE_HUMANin vitroHPRD:05397HPRD12925766
RGAP1_HUMANin vitro
in vivo
HPRD:05397HPRD12689593
14744859
TGFR1_HUMANin vivoHPRD:05397HPRD15761153
SEPT1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:05397HPRD16179162
TBL3_HUMANyeast 2-hybridHPRD:05397HPRD16169070
ANKZ1_HUMANyeast 2-hybridHPRD:05397HPRD16169070
CDC27_HUMANENSP00000313950STRING
UB2D1_HUMANENSP00000313950STRING
CDC23_HUMANENSP00000313950STRING
PSA3_HUMANENSP00000313950STRING
ESPL1_HUMANENSP00000313950STRING
KIF23_HUMANENSP00000313950STRING
ANC5_HUMANENSP00000313950STRING
PLK1_HUMANENSP00000313950STRING
BUB1_HUMANENSP00000313950STRING
UB2E1_HUMANENSP00000313950STRING
CDC20_HUMANENSP00000313950STRING
APC10_HUMANENSP00000313950STRING
ANC2_HUMANENSP00000313950STRING
BOREA_HUMANENSP00000313950STRING
ANC4_HUMANENSP00000313950STRING
STK6_HUMANENSP00000313950STRING
ANC1_HUMANENSP00000313950STRING
APC11_HUMANENSP00000313950STRING
PTTG1_HUMANENSP00000313950STRING
PTTG2_HUMANENSP00000313950STRING
APC7_HUMANENSP00000313950STRING
CDC16_HUMANENSP00000313950STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-7; THR-16; THR-35;SER-45; SER-61; SER-62 AND THR-64, ACETYLATION [LARGE SCALE ANALYSIS]AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Autophosphorylation of a newly identified site of Aurora-B isindispensable for cytokinesis.";
Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H.,Furukawa K., Takahashi T., Izawa I., Inagaki M.;
J. Biol. Chem. 279:12997-13003(2004).
Cited for: AUTOPHOSPHORYLATION AT THR-232, FUNCTION, INTERACTION WITH INCENP,ENZYME REGULATION, AND MUTAGENESIS OF LYS-106.
"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-7; TYR-12 AND THR-232,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-7; THR-16; THR-35;SER-45; SER-61; SER-62 AND THR-64, ACETYLATION [LARGE SCALE ANALYSIS]AT ALA-2, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND MASSSPECTROMETRY.
"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-7; THR-35; SER-45;SER-61; THR-64; TYR-92; SER-227; THR-232; THR-236 AND SER-313, ANDMASS 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 THR-35, AND MASSSPECTROMETRY.
"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-61, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures