AURKB
entrez
9212
canonical
uniprot
Q96GD4
canonical
ensembl
ENSG00000178999
resolver
ensp
ENSP00000313950
resolver
ensp
ENSP00000443869
resolver
ensp
ENSP00000462207
resolver
ensp
ENSP00000463999
resolver
ensp
ENSP00000602627
resolver
genesymbol
AURKB
resolver
genesymbol_syn
AIK2
resolver
genesymbol_syn
AIM1
resolver
genesymbol_syn
AIRK2
resolver
genesymbol_syn
ARK2
resolver
genesymbol_syn
STK1
resolver
genesymbol_syn
STK12
resolver
genesymbol_syn
STK5
resolver
hgnc
HGNC:11390
resolver
uniprot
B4DNM4
resolver
uniprot
C7G533
resolver
uniprot
C7G534
resolver
uniprot
C7G535
resolver
uniprot
D3DTR4
resolver
uniprot
J9JID1
resolver
uniprot
O14630
resolver
uniprot
O60446
resolver
uniprot
O95083
resolver
uniprot
Q96DV5
resolver
uniprot
Q9UQ46
resolver
uniprot_entry
AURKB_HUMAN
resolver
uniprot_sec
B4DNM4
resolver
uniprot_sec
C7G533
resolver
uniprot_sec
C7G534
resolver
uniprot_sec
C7G535
resolver
uniprot_sec
D3DTR4
resolver
uniprot_sec
J9JID1
resolver
uniprot_sec
O14630
resolver
uniprot_sec
O60446
resolver
uniprot_sec
O95083
resolver
uniprot_sec
Q96DV5
resolver
uniprot_sec
Q9UQ46
resolver
activity_regulation
ACTIVITY REGULATION: Activity is greatly increased when AURKB is within the CPC complex (PubMed:12925766, PubMed:14722118, PubMed:15249581). In particular, AURKB-phosphorylated INCENP acts as an activator of AURKB (PubMed:14722118, PubMed:15249581). Positive feedback between HASPIN and AURKB contributes to CPC localization (PubMed:14722118, PubMed:15249581). Inhibited by ZM447439 (PubMed:25666058). {ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:25666058}.
uniprot
proteins
amino_acid_sequence
MAQKENSYPWPYGRQTAPSGLSTLPQRVLRKEPVTPSALVLMSRSNVQPTAAPGQKVMENSSGTPDILTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA
uniprot
proteins
disease_involvement
DISEASE: Note=Disruptive regulation of expression is a possible mechanism of the perturbation of chromosomal integrity in cancer cells through its dominant-negative effect on cytokinesis. {ECO:0000305|PubMed:9809983}.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (PubMed:11516652, PubMed:12925766, PubMed:14610074, PubMed:14722118, PubMed:29449677). 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 (PubMed:11516652, PubMed:12925766, PubMed:14610074, PubMed:14722118, PubMed:26829474). Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis (PubMed:15249581). Required for central/midzone spindle assembly and cleavage furrow formation (PubMed:12458200, PubMed:12686604). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP (PubMed:11516652, PubMed:12925766, PubMed:14610074). Phosphorylation of INCENP leads to increased AURKB activity (PubMed:11516652, PubMed:12925766, PubMed:14610074). Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histones H1.4 and H3 (PubMed:11756469, PubMed:11784863, PubMed:11856369, PubMed:12689593, PubMed:14602875, PubMed:16103226, PubMed:21511733, PubMed:21658950). A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres (PubMed:21658950). Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively) (PubMed:11784863, PubMed:11856369). AURKB is also required for kinetochore localization of BUB1 and SGO1 (PubMed:15020684, PubMed:17617734). Phosphorylation of p53/TP53 negatively regulates its transcriptional activity (PubMed:20959462). Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes (By similarity). Acts as an inhibitor of CGAS during mitosis: catalyzes phosphorylation of the N-terminus of CGAS during the G2-M transition, blocking CGAS liquid phase separation and activation, and thereby preventing CGAS-induced autoimmunity (PubMed:33542149). Phosphorylates KRT5 during anaphase and telophase (By similarity). Phosphorylates ATXN10 which promotes phosphorylation of ATXN10 by PLK1 and may play a role in the regulation of cytokinesis and stimulating the proteasomal degradation of ATXN10 (PubMed:25666058). {ECO:0000250|UniProtKB:O70126, ECO:0000269|PubMed:11516652, ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:11784863, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12458200, ECO:0000269|PubMed:12686604, ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:15249581, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21658950, ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:24814515, ECO:0000269|PubMed:25666058, ECO:0000269|PubMed:26829474, ECO:0000269|PubMed:29449677, ECO:0000269|PubMed:33542149}.
uniprot
proteins
mass_dalton
39311
uniprot
proteins
mutagenesis
MUTAGEN 106; /note="K->R: Leads to loss of kinase activity and severely impairs mitotic progression."; /evidence="ECO:0000269|PubMed:12686604, ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:16179162"; MUTAGEN 215; /note="K->Q: Mimics acetylation, promoting accurate chromosome segregation."; /evidence="ECO:0000269|PubMed:26829474"; MUTAGEN 215; /note="K->R: Abolished acetylation by KAT5, leading to impaired chromosome segregation."; /evidence="ECO:0000269|PubMed:26829474
uniprot
proteins
post_translational_modification
PTM: The phosphorylation of Thr-232 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism (PubMed:14722118). Thr-232 phosphorylation is indispensable for the AURKB kinase activity (PubMed:14722118, PubMed:26829474). {ECO:0000269|PubMed:14722118, ECO:0000269|PubMed:26829474}.; PTM: Acetylated at Lys-215 by KAT5 at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis. {ECO:0000269|PubMed:26829474}.; PTM: Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complexes (PubMed:17543862, PubMed:19995937). Ubiquitinated by the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, ubiquitination leads to removal from mitotic chromosomes and is required for cytokinesis (PubMed:17543862). During anaphase, the BCR(KLHL21) E3 ubiquitin ligase complex recruits the CPC complex from chromosomes to the spindle midzone and mediates the ubiquitination of AURKB (PubMed:17543862). Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome (PubMed:19995937). Deubiquitinated by USP35; inhibiting CDH1-mediated degradation of AURKB (PubMed:29449677). {ECO:0000269|PubMed:17543862, ECO:0000269|PubMed:19995937, ECO:0000269|PubMed:29449677}.
uniprot
proteins
protein_family
Aurora subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Ser/Thr protein kinase family
uniprot
proteins
pubmed
11413462
uniprot
proteins
pubmed
11471245
uniprot
proteins
pubmed
11516652
uniprot
proteins
pubmed
11756469
uniprot
proteins
pubmed
11784863
uniprot
proteins
pubmed
11856369
uniprot
proteins
pubmed
12458200
uniprot
proteins
pubmed
12686604
uniprot
proteins
pubmed
12689593
uniprot
proteins
pubmed
12925766
uniprot
proteins
pubmed
14602875
uniprot
proteins
pubmed
14610074
uniprot
proteins
pubmed
14674694
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14722118
uniprot
proteins
pubmed
15020684
uniprot
proteins
pubmed
15064709
uniprot
proteins
pubmed
15249581
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16103226
uniprot
proteins
pubmed
16179162
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16762494
uniprot
proteins
pubmed
16764853
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17543862
uniprot
proteins
pubmed
17617734
uniprot
proteins
pubmed
17726514
uniprot
proteins
pubmed
18591255
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19134008
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19995937
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20562864
uniprot
proteins
pubmed
20605920
uniprot
proteins
pubmed
20929775
uniprot
proteins
pubmed
20959462
uniprot
proteins
pubmed
21225229
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21511733
uniprot
proteins
pubmed
21658950
uniprot
proteins
pubmed
22422861
uniprot
proteins
pubmed
22920039
uniprot
proteins
pubmed
23036704
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24814515
uniprot
proteins
pubmed
25666058
uniprot
proteins
pubmed
26829474
uniprot
proteins
pubmed
27332895
uniprot
proteins
pubmed
29449677
uniprot
proteins
pubmed
33542149
uniprot
proteins
pubmed
9514916
uniprot
proteins
pubmed
9809983
uniprot
proteins
pubmed
9858806
uniprot
proteins
sequence_length
344
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20959462}. Chromosome {ECO:0000269|PubMed:20929775}. Chromosome, centromere {ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:20929775}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:26829474}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11516652, ECO:0000269|PubMed:12458200, ECO:0000269|PubMed:12925766, ECO:0000269|PubMed:20605920}. Midbody {ECO:0000269|PubMed:16179162, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:23036704}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis (PubMed:20929775). Colocalized with gamma tubulin in the midbody (PubMed:17726514). Proper localization of the active, Thr-232-phosphorylated form during metaphase may be dependent upon interaction with SPDYC (PubMed:20605920). Colocalized with SIRT2 during cytokinesis with the midbody (PubMed:17726514). Localization (and probably targeting of the CPC) to the inner centromere occurs predominantly in regions with overlapping mitosis-specific histone phosphorylations H3pT3 and H2ApT12 (PubMed:20929775). {ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:20605920, ECO:0000269|PubMed:20929775}.
uniprot
proteins