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Q96GD4

- AURKB_HUMAN

UniProt

Q96GD4 - AURKB_HUMAN

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Protein

Aurora kinase B

Gene
AURKB, AIK2, AIM1, AIRK2, ARK2, STK1, STK12, STK5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - 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 (1 Publication, 1 Publication). 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 (H3S10ph and H3S28ph, respectively). 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. 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

Magnesium.

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 GSG2 and AURKB contributes to CPC localization.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061ATP By similarity
Active sitei200 – 2001Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi83 – 919ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. histone serine kinase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding Source: UniProtKB
  5. protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  6. protein serine/threonine kinase activity Source: FlyBase

GO - Biological processi

  1. abscission Source: UniProtKB
  2. aging Source: Ensembl
  3. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  4. attachment of spindle microtubules to kinetochore Source: UniProtKB
  5. cell proliferation Source: Ensembl
  6. cellular response to UV Source: UniProtKB
  7. cleavage furrow formation Source: UniProtKB
  8. cytokinesis checkpoint Source: UniProtKB
  9. histone H3-S28 phosphorylation Source: UniProtKB
  10. histone modification Source: UniProtKB
  11. mitotic cell cycle Source: Reactome
  12. negative regulation of B cell apoptotic process Source: UniProtKB
  13. negative regulation of cytokinesis Source: UniProtKB
  14. negative regulation of protein binding Source: UniProtKB
  15. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  16. positive regulation of cytokinesis Source: UniProtKB
  17. protein autophosphorylation Source: UniProtKB
  18. protein localization to kinetochore Source: UniProtKB
  19. protein phosphorylation Source: UniProtKB
  20. regulation of chromosome segregation Source: UniProtKB
  21. spindle checkpoint Source: InterPro
  22. spindle midzone assembly involved in mitosis Source: UniProtKB
  23. spindle stabilization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_682. Mitotic Prometaphase.
SignaLinkiQ96GD4.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:11390. AURKB.

Subcellular locationi

Nucleus. Chromosome. Chromosomecentromere. Cytoplasmcytoskeletonspindle. Midbody
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. Colocalized with gamma tubulin in the mid-body. Proper localization of the active, Thr-232-phosphorylated form during metaphase may be dependent upon interaction with SPDYC. Colocalized with SIRT2 during cytokinesis with the midbody.8 Publications

GO - Cellular componenti

  1. chromocenter Source: Ensembl
  2. chromosome passenger complex Source: UniProtKB
  3. condensed chromosome, centromeric region Source: UniProtKB
  4. condensed nuclear chromosome, centromeric region Source: BHF-UCL
  5. cytosol Source: Reactome
  6. intercellular bridge Source: HPA
  7. midbody Source: UniProtKB
  8. nucleus Source: UniProtKB
  9. spindle Source: UniProtKB
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061K → R: Leads to loss of kinase activity and severely impairs mitotic progression. 4 Publications

Organism-specific databases

PharmGKBiPA36199.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Aurora kinase BPRO_0000085656Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351Phosphothreonine1 Publication
Modified residuei62 – 621Phosphoserine1 Publication
Modified residuei64 – 641Phosphothreonine1 Publication
Modified residuei232 – 2321Phosphothreonine; by autocatalysis1 Publication

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.
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

MaxQBiQ96GD4.
PaxDbiQ96GD4.
PRIDEiQ96GD4.

PTM databases

PhosphoSiteiQ96GD4.

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.3 Publications

Gene expression databases

ArrayExpressiQ96GD4.
BgeeiQ96GD4.
CleanExiHS_AIM1.
HS_AURKB.
GenevestigatoriQ96GD4.

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 and AURKC. 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.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BIRC5O153927EBI-624291,EBI-518823
BIRC5O15392-12EBI-624291,EBI-518838
BIRC5O15392-22EBI-624291,EBI-518842
GAS2L3Q86XJ14EBI-624291,EBI-9248152
HSP90AB1P082382EBI-624291,EBI-352572
INCENPQ9NQS77EBI-624291,EBI-307907
NPM1P067485EBI-624291,EBI-78579
SEPT1Q8WYJ66EBI-624291,EBI-693002
TACC1O75410-62EBI-624291,EBI-624278

Protein-protein interaction databases

BioGridi114646. 81 interactions.
DIPiDIP-34530N.
IntActiQ96GD4. 32 interactions.
MINTiMINT-1413997.
STRINGi9606.ENSP00000313950.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi74 – 763
Beta strandi77 – 826
Beta strandi89 – 968
Turni97 – 993
Beta strandi102 – 1098
Helixi110 – 1167
Helixi119 – 13012
Beta strandi140 – 1456
Beta strandi147 – 1559
Helixi162 – 1698
Helixi174 – 19320
Helixi203 – 2053
Beta strandi206 – 2083
Beta strandi214 – 2163
Helixi242 – 2454
Helixi253 – 26816
Helixi278 – 2869
Helixi298 – 30710
Helixi312 – 3143
Helixi318 – 3225
Helixi325 – 3306

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AF3X-ray2.75A55-344[»]
ProteinModelPortaliQ96GD4.
SMRiQ96GD4. Positions 70-338.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 327251Protein kinaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG108519.
InParanoidiQ96GD4.
KOiK11479.
OMAiHPWVRAN.
PhylomeDBiQ96GD4.
TreeFamiTF351439.

Family and domain databases

InterProiIPR028772. AURKB.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24350:SF4. PTHR24350:SF4. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

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

MAQKENSYPW PYGRQTAPSG LSTLPQRVLR KEPVTPSALV LMSRSNVQPT    50
AAPGQKVMEN SSGTPDILTR HFTIDDFEIG RPLGKGKFGN VYLAREKKSH 100
FIVALKVLFK SQIEKEGVEH QLRREIEIQA HLHHPNILRL YNYFYDRRRI 150
YLILEYAPRG ELYKELQKSC TFDEQRTATI MEELADALMY CHGKKVIHRD 200
IKPENLLLGL KGELKIADFG WSVHAPSLRR KTMCGTLDYL PPEMIEGRMH 250
NEKVDLWCIG VLCYELLVGN PPFESASHNE TYRRIVKVDL KFPASVPMGA 300
QDLISKLLRH NPSERLPLAQ VSAHPWVRAN SRRVLPPSAL QSVA 344
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 AAH13300.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521A → V.1 Publication
Corresponds to variant rs55878091 [ dbSNP | Ensembl ].
VAR_040383
Natural varianti100 – 1001H → Q.
Corresponds to variant rs3027254 [ dbSNP | Ensembl ].
VAR_027970
Natural varianti179 – 1791T → M.1 Publication
VAR_040384
Natural varianti298 – 2981M → T.8 Publications
Corresponds to variant rs1059476 [ dbSNP | Ensembl ].
VAR_027971

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4141Missing in isoform 4. VSP_047103Add
BLAST
Alternative sequencei69 – 691T → TR in isoform 3 and isoform 5. VSP_044384
Alternative sequencei86 – 13449GKFGN…AHLHH → ALLCLWPEASSVSSPSH in isoform 2. VSP_044385Add
BLAST
Alternative sequencei133 – 1419HHPNILRLY → QSWRSWQML in isoform 3. VSP_044386
Alternative sequencei142 – 344203Missing in isoform 3. VSP_044387Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 152RQ → DK in AAC98891. 1 Publication
Sequence conflicti161 – 1611E → M in AAB65786. 1 Publication
Sequence conflicti161 – 1611E → M in AAC98891. 1 Publication
Sequence conflicti167 – 1693QKS → HKT in AAB65786. 1 Publication
Sequence conflicti179 – 1791T → TVRR in AAB65786. 1 Publication
Sequence conflicti180 – 1801I → VRAV in AAC98891. 1 Publication
Sequence conflicti226 – 2261P → T in BAA82709. 1 Publication
Sequence conflicti249 – 2502MH → ID in BAA82709. 1 Publication
Sequence conflicti271 – 2711Missing in BAA82709. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
RefSeqiNP_001243763.1. NM_001256834.1. [Q96GD4-4]
NP_001271455.1. NM_001284526.1. [Q96GD4-5]
NP_004208.2. NM_004217.3. [Q96GD4-1]
XP_005256911.1. XM_005256854.2. [Q96GD4-1]
UniGeneiHs.442658.

Genome annotation databases

EnsembliENST00000316199; ENSP00000313950; ENSG00000178999.
ENST00000534871; ENSP00000443869; ENSG00000178999. [Q96GD4-4]
ENST00000535053; ENSP00000445866; ENSG00000178999. [Q96GD4-3]
ENST00000578549; ENSP00000462207; ENSG00000178999. [Q96GD4-2]
ENST00000585124; ENSP00000463999; ENSG00000178999. [Q96GD4-1]
GeneIDi9212.
KEGGihsa:9212.
UCSCiuc002gkm.4. human. [Q96GD4-1]
uc021tpy.1. human. [Q96GD4-2]

Polymorphism databases

DMDMi317373473.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11134.1. [Q96GD4-1 ]
CCDS58514.1. [Q96GD4-4 ]
CCDS67162.1. [Q96GD4-5 ]
RefSeqi NP_001243763.1. NM_001256834.1. [Q96GD4-4 ]
NP_001271455.1. NM_001284526.1. [Q96GD4-5 ]
NP_004208.2. NM_004217.3. [Q96GD4-1 ]
XP_005256911.1. XM_005256854.2. [Q96GD4-1 ]
UniGenei Hs.442658.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AF3 X-ray 2.75 A 55-344 [» ]
ProteinModelPortali Q96GD4.
SMRi Q96GD4. Positions 70-338.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114646. 81 interactions.
DIPi DIP-34530N.
IntActi Q96GD4. 32 interactions.
MINTi MINT-1413997.
STRINGi 9606.ENSP00000313950.

Chemistry

BindingDBi Q96GD4.
ChEMBLi CHEMBL2185.
GuidetoPHARMACOLOGYi 1937.

PTM databases

PhosphoSitei Q96GD4.

Polymorphism databases

DMDMi 317373473.

Proteomic databases

MaxQBi Q96GD4.
PaxDbi Q96GD4.
PRIDEi Q96GD4.

Protocols and materials databases

DNASUi 9212.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316199 ; ENSP00000313950 ; ENSG00000178999 .
ENST00000534871 ; ENSP00000443869 ; ENSG00000178999 . [Q96GD4-4 ]
ENST00000535053 ; ENSP00000445866 ; ENSG00000178999 . [Q96GD4-3 ]
ENST00000578549 ; ENSP00000462207 ; ENSG00000178999 . [Q96GD4-2 ]
ENST00000585124 ; ENSP00000463999 ; ENSG00000178999 . [Q96GD4-1 ]
GeneIDi 9212.
KEGGi hsa:9212.
UCSCi uc002gkm.4. human. [Q96GD4-1 ]
uc021tpy.1. human. [Q96GD4-2 ]

Organism-specific databases

CTDi 9212.
GeneCardsi GC17M008108.
H-InvDB HIX0019005.
HGNCi HGNC:11390. AURKB.
HPAi CAB005862.
HPA037708.
MIMi 604970. gene.
neXtProti NX_Q96GD4.
PharmGKBi PA36199.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG108519.
InParanoidi Q96GD4.
KOi K11479.
OMAi HPWVRAN.
PhylomeDBi Q96GD4.
TreeFami TF351439.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_682. Mitotic Prometaphase.
SignaLinki Q96GD4.

Miscellaneous databases

GeneWikii Aurora_B_kinase.
GenomeRNAii 9212.
NextBioi 34535.
PROi Q96GD4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96GD4.
Bgeei Q96GD4.
CleanExi HS_AIM1.
HS_AURKB.
Genevestigatori Q96GD4.

Family and domain databases

InterProi IPR028772. AURKB.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24350:SF4. PTHR24350:SF4. 1 hit.
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, expression, subcellular localization, and chromosomal assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1 and 2."
    Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D.J., Jenkins N.A., Copeland N.G., Yagita H., Okumura K.
    Biochem. Biophys. Res. Commun. 244:285-292(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-298.
  2. "Multinuclearity and increased ploidy caused by overexpression of the aurora- and Ipl1-like midbody-associated protein mitotic kinase in human cancer cells."
    Tatsuka M., Katayama H., Ota T., Tanaka T., Odashima S., Suzuki F., Terada Y.
    Cancer Res. 58:4811-4816(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT THR-298.
  3. "Identification and characterization of STK12/Aik2: a human gene related to aurora of Drosophila and yeast IPL1."
    Kimura M., Matsuda Y., Yoshioka T., Sumi N., Okano Y.
    Cytogenet. Cell Genet. 82:147-152(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT THR-298.
    Tissue: Liver and Spleen.
  4. "In silico cloning of a new protein kinase, Aik2, related to Drosophila aurora using the new tool: EST Blast."
    Prigent C., Gill R., Trower M., Sanseau P.
    In Silico Biol. 1:123-128(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-298.
  5. "Cloning of a novel human gene homologous to mouse STK-1."
    Zhang Q., Yu L., Bi A.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-298.
  6. "Expression of Aurora B and alternative variant forms in hepatocellular carcinoma and adjacent tissue."
    Yasen M., Mizushima H., Mogushi K., Obulhasim G., Miyaguchi K., Inoue K., Nakahara I., Ohta T., Aihara A., Tanaka S., Arii S., Tanaka H.
    Cancer Sci. 100:472-480(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING.
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-298.
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
  9. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), VARIANT THR-298.
    Tissue: Lung, Lymph and Muscle.
  12. "INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis."
    Wheatley S.P., Carvalho A., Vagnarelli P., Earnshaw W.C.
    Curr. Biol. 11:886-890(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CPC COMPLEX, SUBCELLULAR LOCATION, FUNCTION.
  13. "CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis."
    Zeitlin S.G., Shelby R.D., Sullivan K.F.
    J. Cell Biol. 155:1147-1157(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "Mitotic kinases as regulators of cell division and its checkpoints."
    Nigg E.A.
    Nat. Rev. Mol. Cell Biol. 2:21-32(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  15. "Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation."
    Goto H., Yasui Y., Nigg E.A., Inagaki M.
    Genes Cells 7:11-17(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
  16. "Mitotic phosphorylation of histone H3: spatio-temporal regulation by mammalian Aurora kinases."
    Crosio C., Fimia G.M., Loury R., Kimura M., Okano Y., Zhou H., Sen S., Allis C.D., Sassone-Corsi P.
    Mol. Cell. Biol. 22:874-885(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
  17. Cited for: FUNCTION, INTERACTION WITH RACGAP1.
  18. "Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process."
    Goto H., Yasui Y., Kawajiri A., Nigg E.A., Terada Y., Tatsuka M., Nagata K., Inagaki M.
    J. Biol. Chem. 278:8526-8530(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  19. "Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinatedly with Rho-kinase."
    Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K., Inagaki M.
    Mol. Biol. Cell 14:1489-1500(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-106.
  20. "Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis."
    Honda R., Korner R., Nigg E.A.
    Mol. Biol. Cell 14:3325-3341(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CPC COMPLEX, FUNCTION OF THE CPC COMPLEX, INDUCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF LYS-106.
  21. "Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner."
    Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C., Zhao S., Yu L.
    Mol. Cell. Biochem. 254:157-162(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSMA3.
  22. "Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo."
    Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.
    J. Biol. Chem. 279:5655-5660(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Autophosphorylation of a newly identified site of Aurora-B is indispensable 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION AT THR-232, FUNCTION, INTERACTION WITH INCENP, ENZYME REGULATION, MUTAGENESIS OF LYS-106.
  24. "Bub1 is required for kinetochore localization of BubR1, Cenp-E, Cenp-F and Mad2, and chromosome congression."
    Johnson V.L., Scott M.I., Holt S.V., Hussein D., Taylor S.S.
    J. Cell Sci. 117:1577-1589(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Borealin: a novel chromosomal passenger required for stability of the bipolar 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDCA8, ENZYME REGULATION, FUNCTION.
  26. "Identification of the substrates and interaction proteins of aurora kinases from a protein-protein interaction model."
    Tien A.-C., Lin M.-H., Su L.-J., Hong Y.-R., Cheng T.-S., Lee Y.-C.G., Lin W.-J., Still I.H., Huang C.-Y.F.
    Mol. Cell. Proteomics 3:93-104(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDCA1 AND NDC80.
  27. Cited for: INTERACTION WITH TACC1.
  28. "Septin1, a new interaction partner for human serine/threonine kinase aurora-B."
    Qi M., Yu W., Liu S., Jia H., Tang L., Shen M., Yan X., Saiyin H., Lang Q., Wan B., Zhao S., Yu L.
    Biochem. Biophys. Res. Commun. 336:994-1000(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SEPT1, MUTAGENESIS OF LYS-106.
  29. "An ECT2-centralspindlin complex regulates the localization and function of RhoA."
    Yuce O., Piekny A., Glotzer M.
    J. Cell Biol. 170:571-582(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "EVI5 protein associates with the INCENP-aurora B kinase-survivin chromosomal passenger complex and is involved in the completion of cytokinesis."
    Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.
    Exp. Cell Res. 312:2325-2335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EVI5.
  31. "Shugoshin 1 plays a central role in kinetochore assembly and is required for kinetochore targeting of Plk1."
    Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J., Stukenberg T., Kallio M.J.
    Cell Cycle 6:1579-1585(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  32. "A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells."
    Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., Peter M.
    Dev. Cell 12:887-900(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  33. "Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis."
    North B.J., Verdin E.
    PLoS ONE 2:E784-E784(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION.
  34. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  35. "A survivin-ran complex regulates spindle formation in tumor cells."
    Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.
    Mol. Cell. Biol. 28:5299-5311(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BIRC5.
  36. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  37. "The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis."
    Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W., Quadroni M., Sumara I., Peter M.
    J. Cell Biol. 187:791-800(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. Cited for: INTERACTION WITH SPDYC, SUBCELLULAR LOCATION.
  40. "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms through Aurora B activation."
    Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N., Kimura H., Obuse C.
    Nat. Cell Biol. 12:719-727(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INCENP.
  41. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND THR-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  42. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  43. "A positive feedback loop involving Haspin and Aurora B promotes CPC accumulation at centromeres in mitosis."
    Wang F., Ulyanova N.P., van der Waal M.S., Patnaik D., Lens S.M., Higgins J.M.
    Curr. Biol. 21:1061-1069(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GSG2.
  44. "Aurora B interacts with NIR-p53, leading to p53 phosphorylation in its DNA-binding domain and subsequent functional suppression."
    Wu L., Ma C.A., Zhao Y., Jain A.
    J. Biol. Chem. 286:2236-2244(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TP53, INTERACTION WITH NOC2L AND TP53, SUBCELLULAR LOCATION.
  45. "PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
    Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
    Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JTB.
  46. "A novel big protein TPRBK possessing 25 units of TPR motif is essential for the progress of mitosis and cytokinesis."
    Izumiyama T., Minoshima S., Yoshida T., Shimizu N.
    Gene 511:202-217(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TTC28, SUBCELLULAR LOCATION.
  47. "ESCRT-III governs the Aurora B-mediated abscission checkpoint through CHMP4C."
    Carlton J.G., Caballe A., Agromayor M., Kloc M., Martin-Serrano J.
    Science 336:220-225(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHMP4C.
  48. "ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4."
    Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K., Andersen J.S., Raiborg C., Stenmark H.
    Nat. Cell Biol. 16:550-560(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  49. Cited for: VARIANT THR-298.
  50. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-52 AND MET-179.

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 historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 159 of the entry and version 3 of the sequence. [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

External Data

Dasty 3

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