UniProt Accession

 AURKB_HUMAN; Q96GD4; B4DNM4; C7G533; C7G534; C7G535; D3DTR4; O14630; O60446; O95083; Q96DV5; Q9UQ46 

Genbank Protein ID

 AF008552; AB011450; AB011446; AF004022; AF015254; AB519677; AB519678; AB519679; BT019534; AK297976; AC135178; CH471108; CH471108; CH471108; BC000442; BC009751; BC013300; BC080581 

Genbank Nucleotide ID

 AAC12709.1; BAA32136.1; BAA82709.1; AAB65786.1; AAC98891.1; BAI23190.1; BAI23191.1; BAI23192.1; AAV38341.1; BAG60286.1; EAW90075.1; EAW90077.1; EAW90078.1; AAH00442.3; AAH09751.1; AAH13300.2; AAH80581.1 

Protein Name

 Aurora kinase B 

Protein Synonyms/Alias

 Aurora 1; Aurora- and IPL1-like midbody-associated protein 1; AIM-1; Aurora/IPL1-related kinase 2; ARK-2; Aurora-related kinase 2; STK-1; Serine/threonine-protein kinase 12; Serine/threonine-protein kinase 5; Serine/threonine-protein kinase aurora-B 

Gene Name

 AURKB 

Gene Synonyms/Alias

 AIK2; AIM1; AIRK2; ARK2; STK1; STK12; STK5 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
4	****MAQKENSYPWP	ubiquitination	[1]
31	LPQRVLRKEPVTPSA	ubiquitination	[1]
56	PTAAPGQKVMENSSG	ubiquitination	[1, 2, 3, 4, 5, 6]
85	EIGRPLGKGKFGNVY	ubiquitination	[1, 2, 3, 6]
87	GRPLGKGKFGNVYLA	ubiquitination	[1, 2, 3, 4]
110	VALKVLFKSQIEKEG	ubiquitination	[1, 3]
115	LFKSQIEKEGVEHQL	ubiquitination	[1, 3]
164	APRGELYKELQKSCT	ubiquitination	[1, 2, 3]
168	ELYKELQKSCTFDEQ	ubiquitination	[1, 3, 4]
194	ALMYCHGKKVIHRDI	ubiquitination	[1]
195	LMYCHGKKVIHRDIK	ubiquitination	[1]
202	KVIHRDIKPENLLLG	sumoylation	[7, 8]
202	KVIHRDIKPENLLLG	ubiquitination	[1, 3]
211	ENLLLGLKGELKIAD	ubiquitination	[1, 2, 3, 6, 9]
215	LGLKGELKIADFGWS	ubiquitination	[1, 2, 3]
231	HAPSLRRKTMCGTLD	ubiquitination	[1]
287	ETYRRIVKVDLKFPA	ubiquitination	[1, 2]
291	RIVKVDLKFPASVPM	ubiquitination	[3]
306	GAQDLISKLLRHNPS	ubiquitination	[3, 10]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Mitotic kinase Aurora-B is regulated by SUMO-2/3 conjugation/deconjugation during mitosis.
 Ban R, Nishida T, Urano T.
 Genes Cells. 2011 Jun;16(6):652-69. [PMID: 21554500]
 [8] SUMOylation in control of accurate chromosome segregation during mitosis.
 Wan J, Subramonian D, Zhang XD.
 Curr Protein Pept Sci. 2012 Aug;13(5):467-81. [PMID: 22812528]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [10] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 77 327 Protein kinase.
 NP_BIND 83 91 ATP (By similarity).
 ACT_SITE 200 200 Proton acceptor (By similarity).
 BINDING 106 106 ATP (By similarity).
 MOD_RES 35 35 Phosphothreonine.
 MOD_RES 62 62 Phosphoserine.
 MOD_RES 64 64 Phosphothreonine.
 MOD_RES 232 232 Phosphothreonine; by autocatalysis.  

Keyword

 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 344 AA 

Protein Sequence

Gene Ontology

 GO:0010369; C:chromocenter; IEA:Compara.
 GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
 GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:BHF-UCL.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030496; C:midbody; TAS:UniProtKB.
 GO:0005819; C:spindle; TAS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
 GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
 GO:0007568; P:aging; IEA:Compara.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 GO:0008608; P:attachment of spindle microtubules to kinetochore; TAS:UniProtKB.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0034644; P:cellular response to UV; IDA:UniProtKB.
 GO:0036089; P:cleavage furrow formation; IDA:UniProtKB.
 GO:0016570; P:histone modification; TAS:UniProtKB.
 GO:0002903; P:negative regulation of B cell apoptotic process; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
 GO:0046777; P:protein autophosphorylation; TAS:UniProtKB.
 GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
 GO:0051983; P:regulation of chromosome segregation; TAS:UniProtKB.
 GO:0051256; P:spindle midzone assembly involved in mitosis; IMP:UniProtKB. 

Interpro

 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 

Pfam

 PF00069; Pkinase 

SMART

 SM00220; S_TKc 

PROSITE

 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 

PRINTS