Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q96GD4 (AURKB_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Aurora kinase B

Gene

AURKB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. 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. 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, HASPIN, and histone H3. A positive feedback loop involving HASPIN 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 (H3S10ph and H3S28ph, respectively). A positive feedback between HASPIN and AURKB contributes to CPC localization. AURKB is also required for kinetochore localization of BUB1 and SGO1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. 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.19 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+

Enzyme regulationi

Activity is greatly increased when AURKB is within the CPC complex. In particular, AURKB-phosphorylated INCENP acts as an activator of AURKB. Positive feedback between HASPIN and AURKB contributes to CPC localization.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei106ATPPROSITE-ProRule annotation1
Active sitei200Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi83 – 91ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • histone serine kinase activity Source: UniProtKB
  • kinase binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: FlyBase
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • abscission Source: UniProtKB
  • aging Source: Ensembl
  • anaphase-promoting complex-dependent catabolic process Source: Reactome
  • attachment of spindle microtubules to kinetochore Source: UniProtKB
  • cell proliferation Source: Ensembl
  • cellular response to UV Source: UniProtKB
  • cleavage furrow formation Source: UniProtKB
  • histone H3-S28 phosphorylation Source: UniProtKB
  • histone modification Source: UniProtKB
  • mitotic cytokinesis checkpoint Source: UniProtKB
  • mitotic spindle midzone assembly Source: UniProtKB
  • negative regulation of B cell apoptotic process Source: UniProtKB
  • negative regulation of cytokinesis Source: UniProtKB
  • negative regulation of protein binding Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: UniProtKB
  • positive regulation of cytokinesis Source: UniProtKB
  • positive regulation of telomerase activity Source: BHF-UCL
  • positive regulation of telomere capping Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • protein autophosphorylation Source: UniProtKB
  • protein localization to kinetochore Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of chromosome segregation Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • spindle checkpoint Source: InterPro
  • spindle organization Source: UniProtKB
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-68877 Mitotic Prometaphase
SignaLinkiQ96GD4
SIGNORiQ96GD4

Names & Taxonomyi

Protein namesi
Recommended name:
Aurora kinase B (EC:2.7.11.1)
Alternative name(s):
Aurora 1
Aurora- and IPL1-like midbody-associated protein 1
Short name:
AIM-1
Aurora/IPL1-related kinase 2
Short name:
ARK-2
Short name:
Aurora-related kinase 2
STK-1
Serine/threonine-protein kinase 12
Serine/threonine-protein kinase 5
Serine/threonine-protein kinase aurora-B
Gene namesi
Name:AURKB
Synonyms:AIK2, AIM1, AIRK2, ARK2, STK1, STK12, STK5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000178999.12
HGNCiHGNC:11390 AURKB
MIMi604970 gene
neXtProtiNX_Q96GD4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Disruptive regulation of expression is a possible mechanism of the perturbation of chromosomal integrity in cancer cells through its dominant-negative effect on cytokinesis.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi106K → R: Leads to loss of kinase activity and severely impairs mitotic progression. 4 Publications1

Organism-specific databases

DisGeNETi9212
OpenTargetsiENSG00000178999
PharmGKBiPA36199

Chemistry databases

ChEMBLiCHEMBL2185
DrugBankiDB05169 AT9283
DB04703 HESPERIDIN
GuidetoPHARMACOLOGYi1937

Polymorphism and mutation databases

BioMutaiAURKB
DMDMi317373473

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000856561 – 344Aurora kinase BAdd BLAST344

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35PhosphothreonineCombined sources1
Modified residuei62PhosphoserineCombined sources1
Modified residuei64PhosphothreonineCombined sources1
Modified residuei227PhosphoserineCombined sources1
Modified residuei232Phosphothreonine; by autocatalysis1 Publication1

Post-translational modificationi

The phosphorylation of Thr-232 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-232 phosphorylation is indispensable for the AURKB kinase activity.1 Publication
Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complexes. Ubiquitinated by the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, ubiquitination leads to removal from mitotic chromosomes and is required for cytokinesis. 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. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96GD4
MaxQBiQ96GD4
PaxDbiQ96GD4
PeptideAtlasiQ96GD4
PRIDEiQ96GD4
ProteomicsDBi76623

PTM databases

iPTMnetiQ96GD4
PhosphoSitePlusiQ96GD4
SwissPalmiQ96GD4

Expressioni

Tissue specificityi

High level expression seen in the thymus. It is also expressed in the spleen, lung, testis, colon, placenta and fetal liver. Expressed during S and G2/M phase and expression is up-regulated in cancer cells during M phase.2 Publications

Inductioni

Expression is cell cycle-regulated, with a low in G1/S, an increase during G2 and M. Expression decreases again after M phase.1 Publication

Gene expression databases

BgeeiENSG00000178999
CleanExiHS_AIM1
HS_AURKB
ExpressionAtlasiQ96GD4 baseline and differential
GenevisibleiQ96GD4 HS

Organism-specific databases

HPAiCAB005862
HPA037708

Interactioni

Subunit structurei

Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; predominantly independent AURKB- and AURKC-containing complexes exist. Associates with RACGAP1 during M phase. Interacts with CDCA1, EVI5, JTB, NDC80, PSMA3, SEPT1, SIRT2 and TACC1. Interacts with SPDYC; this interaction may be required for proper localization of active, Thr-232-phosphorylated AURKB form during prometaphase and metaphase. Interacts with p53/TP53. Interacts (via the middle kinase domain) with NOC2L (via the N- and C-terminus domains). Interacts with TTC28. Interacts with RNF2/RING1B.19 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • kinase binding Source: UniProtKB
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi114646, 164 interactors
ComplexPortaliCPX-116 Chromosomal passenger complex
CORUMiQ96GD4
DIPiDIP-34530N
ELMiQ96GD4
IntActiQ96GD4, 90 interactors
MINTiQ96GD4
STRINGi9606.ENSP00000463999

Chemistry databases

BindingDBiQ96GD4

Structurei

Secondary structure

1344
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi74 – 76Combined sources3
Beta strandi77 – 82Combined sources6
Beta strandi89 – 96Combined sources8
Turni97 – 99Combined sources3
Beta strandi102 – 109Combined sources8
Helixi110 – 116Combined sources7
Helixi119 – 130Combined sources12
Beta strandi140 – 145Combined sources6
Beta strandi147 – 155Combined sources9
Helixi162 – 169Combined sources8
Helixi174 – 193Combined sources20
Helixi203 – 205Combined sources3
Beta strandi206 – 208Combined sources3
Beta strandi214 – 216Combined sources3
Helixi242 – 245Combined sources4
Helixi253 – 268Combined sources16
Helixi278 – 286Combined sources9
Helixi298 – 307Combined sources10
Helixi312 – 314Combined sources3
Helixi318 – 322Combined sources5
Helixi325 – 330Combined sources6

3D structure databases

ProteinModelPortaliQ96GD4
SMRiQ96GD4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini77 – 327Protein kinasePROSITE-ProRule annotationAdd BLAST251

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0580 Eukaryota
ENOG410XNRB LUCA
GeneTreeiENSGT00910000144066
HOVERGENiHBG108519
InParanoidiQ96GD4
KOiK11479
OMAiPYGRQTT
OrthoDBiEOG091G0EU2
PhylomeDBiQ96GD4
TreeFamiTF351439

Family and domain databases

InterProiView protein in InterPro
IPR030616 Aur
IPR028772 AURKB
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24350 PTHR24350, 1 hit
PTHR24350:SF4 PTHR24350:SF4, 1 hit
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96GD4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQKENSYPW PYGRQTAPSG LSTLPQRVLR KEPVTPSALV LMSRSNVQPT 
        60         70         80         90        100
AAPGQKVMEN SSGTPDILTR HFTIDDFEIG RPLGKGKFGN VYLAREKKSH 
       110        120        130        140        150
FIVALKVLFK SQIEKEGVEH QLRREIEIQA HLHHPNILRL YNYFYDRRRI 
       160        170        180        190        200
YLILEYAPRG ELYKELQKSC TFDEQRTATI MEELADALMY CHGKKVIHRD 
       210        220        230        240        250
IKPENLLLGL KGELKIADFG WSVHAPSLRR KTMCGTLDYL PPEMIEGRMH 
       260        270        280        290        300
NEKVDLWCIG VLCYELLVGN PPFESASHNE TYRRIVKVDL KFPASVPMGA 
       310        320        330        340 
QDLISKLLRH NPSERLPLAQ VSAHPWVRAN SRRVLPPSAL QSVA
Length:344
Mass (Da):39,311
Last modified:January 11, 2011 - v3
Checksum:iA5ED13EF5A1FAFBF
GO
Isoform 2 (identifier: Q96GD4-2) [UniParc]FASTAAdd to basket
Also known as: aurkb-sv1

The sequence of this isoform differs from the canonical sequence as follows:
     86-134: GKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHH → ALLCLWPEASSVSSPSH

Show »
Length:312
Mass (Da):35,302
Checksum:i9499DAE479793112
GO
Isoform 3 (identifier: Q96GD4-3) [UniParc]FASTAAdd to basket
Also known as: aurkb-sv2

The sequence of this isoform differs from the canonical sequence as follows:
     69-69: T → TR
     133-141: HHPNILRLY → QSWRSWQML
     142-344: Missing.

Note: Not expressed in normal liver, high expression in metastatic liver.
Show »
Length:142
Mass (Da):16,211
Checksum:iD8AB62DA2CCFA385
GO
Isoform 4 (identifier: Q96GD4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.

Show »
Length:303
Mass (Da):34,760
Checksum:i301BAFF2494B3650
GO
Isoform 5 (identifier: Q96GD4-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-69: T → TR

Show »
Length:345
Mass (Da):39,467
Checksum:iACB05C191F35F38C
GO

Sequence cautioni

The sequence AAH13300 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 15RQ → DK in AAC98891 (Ref. 5) Curated2
Sequence conflicti161E → M in AAB65786 (PubMed:11471245).Curated1
Sequence conflicti161E → M in AAC98891 (Ref. 5) Curated1
Sequence conflicti167 – 169QKS → HKT in AAB65786 (PubMed:11471245).Curated3
Sequence conflicti179T → TVRR in AAB65786 (PubMed:11471245).Curated1
Sequence conflicti180I → VRAV in AAC98891 (Ref. 5) Curated1
Sequence conflicti226P → T in BAA82709 (PubMed:9858806).Curated1
Sequence conflicti249 – 250MH → ID in BAA82709 (PubMed:9858806).Curated2
Sequence conflicti271Missing in BAA82709 (PubMed:9858806).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04038352A → V1 PublicationCorresponds to variant dbSNP:rs55878091Ensembl.1
Natural variantiVAR_027970100H → Q. Corresponds to variant dbSNP:rs3027254Ensembl.1
Natural variantiVAR_040384179T → M1 PublicationCorresponds to variant dbSNP:rs55871613Ensembl.1
Natural variantiVAR_027971298M → T8 PublicationsCorresponds to variant dbSNP:rs1059476Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0471031 – 41Missing in isoform 4. 1 PublicationAdd BLAST41
Alternative sequenceiVSP_04438469T → TR in isoform 3 and isoform 5. 2 Publications1
Alternative sequenceiVSP_04438586 – 134GKFGN…AHLHH → ALLCLWPEASSVSSPSH in isoform 2. 1 PublicationAdd BLAST49
Alternative sequenceiVSP_044386133 – 141HHPNILRLY → QSWRSWQML in isoform 3. 1 Publication9
Alternative sequenceiVSP_044387142 – 344Missing in isoform 3. 1 PublicationAdd BLAST203

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008552 mRNA Translation: AAC12709.1
AB011450 mRNA Translation: BAA32136.1
AB011446 mRNA Translation: BAA82709.1
AF004022 mRNA Translation: AAB65786.1
AF015254 mRNA Translation: AAC98891.1
AB519677 mRNA Translation: BAI23190.1
AB519678 mRNA Translation: BAI23191.1
AB519679 mRNA Translation: BAI23192.1
BT019534 mRNA Translation: AAV38341.1
AK297976 mRNA Translation: BAG60286.1
AC135178 Genomic DNA No translation available.
CH471108 Genomic DNA Translation: EAW90075.1
CH471108 Genomic DNA Translation: EAW90077.1
CH471108 Genomic DNA Translation: EAW90078.1
BC000442 mRNA Translation: AAH00442.3
BC009751 mRNA Translation: AAH09751.1
BC013300 mRNA Translation: AAH13300.2 Different initiation.
BC080581 mRNA Translation: AAH80581.1
CCDSiCCDS11134.1 [Q96GD4-1]
CCDS58514.1 [Q96GD4-4]
CCDS67162.1 [Q96GD4-5]
CCDS82065.1 [Q96GD4-2]
RefSeqiNP_001243763.1, NM_001256834.2 [Q96GD4-4]
NP_001271455.1, NM_001284526.1 [Q96GD4-5]
NP_001300879.1, NM_001313950.1 [Q96GD4-1]
NP_001300880.1, NM_001313951.1 [Q96GD4-4]
NP_001300881.1, NM_001313952.1
NP_001300882.1, NM_001313953.1 [Q96GD4-2]
NP_001300883.1, NM_001313954.1
NP_001300884.1, NM_001313955.1
NP_004208.2, NM_004217.3 [Q96GD4-1]
XP_011522372.1, XM_011524070.2
XP_011522374.1, XM_011524072.2 [Q96GD4-4]
XP_016880796.1, XM_017025307.1 [Q96GD4-4]
UniGeneiHs.442658

Genome annotation databases

EnsembliENST00000316199; ENSP00000313950; ENSG00000178999 [Q96GD4-5]
ENST00000534871; ENSP00000443869; ENSG00000178999 [Q96GD4-4]
ENST00000578549; ENSP00000462207; ENSG00000178999 [Q96GD4-2]
ENST00000585124; ENSP00000463999; ENSG00000178999 [Q96GD4-1]
GeneIDi9212
KEGGihsa:9212
UCSCiuc002gkm.5 human [Q96GD4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiAURKB_HUMAN
AccessioniPrimary (citable) accession number: Q96GD4
Secondary accession number(s): B4DNM4
, C7G533, C7G534, C7G535, D3DTR4, J9JID1, O14630, O60446, O95083, Q96DV5, Q9UQ46
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 11, 2011
Last modified: July 18, 2018
This is version 199 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health