O70126 (AURKB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aurora kinase B
EC=2.7.11.1

Alternative name(s):
Aurora 1
Aurora- and IPL1-like midbody-associated protein 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 names

Name:	Aurkb
Synonyms:	Aik2, Aim1, Airk2, Ark2, Stk1, Stk12, Stk5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity By similarity. Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activity is greatly increased when AURKB is within the CPC complex. In particular, AURKA-phosphorylated INCENP acts as an activator of AURKB By similarity.
Subunit structure	Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC By similarity. Associates with RACGAP1 during M phase. Interacts with CDCA1, EVI5, JTB, NDC80, PSMA3, SEPT1 and TACC1 By similarity. Interacts with SPDYC; this interaction may be required for proper localization of active, Thr-237-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) By similarity. Interacts with TTC28 By similarity.
Subcellular location	Nucleus By similarity. Chromosome By similarity. Chromosome › centromere By similarity. Cytoplasm › cytoskeleton › spindle By similarity. 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 By similarity. Proper localization of the active, Thr-237-phosphorylated form during metaphase may be dependent upon interaction with SPDYC By similarity.
Tissue specificity	Expressed in testis, intestine and spleen. All of them are tissues that contain a large number of proliferating cells. Expressed during S phase, in a cell-cycle-dependent fashion.
Developmental stage	Strongly expressed in 8.5 and 12.5 dpc.
Post-translational modification	The phosphorylation of Thr-237 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-237 phosphorylation is indispensable for the AURKB kinase activity By similarity. 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 By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Nucleus
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara cell proliferation Inferred from electronic annotation. Source: Compara cellular response to UV Inferred from sequence or structural similarity. Source: UniProtKB cleavage furrow formation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of B cell apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell cycle cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB protein localization to kinetochore Inferred from sequence or structural similarity. Source: UniProtKB spindle midzone assembly involved in mitosis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	chromocenter Inferred from direct assay PubMed 19283064. Source: MGI chromosome passenger complex Inferred from direct assay PubMed 20562830. Source: MGI condensed nuclear chromosome, centromeric region Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW kinetochore Inferred from sequence orthology PubMed 23036704. Source: MGI midbody Inferred from electronic annotation. Source: Compara mitotic spindle pole Inferred from sequence orthology PubMed 23036704. Source: MGI nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 345	345	Aurora kinase B		PRO_0000085657
Regions
	Domain	82 – 332	251	Protein kinase
	Nucleotide binding	88 – 96	9	ATP By similarity
Sites
	Active site	205	1	Proton acceptor By similarity
	Binding site	111	1	ATP By similarity
Amino acid modifications
	Modified residue	35	1	Phosphothreonine By similarity
	Modified residue	237	1	Phosphothreonine; by autocatalysis By similarity
Experimental info
	Sequence conflict	44	1	R → W in BAA04658. Ref.1
	Sequence conflict	45	1	F → S in BAA04658. Ref.1
	Sequence conflict	45	1	F → S in AAC12683. Ref.2
	Sequence conflict	45	1	F → S in AAH03261. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	O70126 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: D204D8B91CFF00A4	FASTA	345	39,384
	10 20 30 40 50 60 MAQKENAYPW PYGSKTSQSG LNTLSQRVLR KEPATTSALA LVNRFNSQST AAPGQKLAEN 70 80 90 100 110 120 KSQGSTASQG SQNKQPFTID NFEIGRPLGK GKFGNVYLAR EKKSRFIVAL KILFKSQIEK 130 140 150 160 170 180 EGVEHQLRRE IEIQAHLKHP NILQLYNYFY DQQRIYLILE YAPRGELYKE LQKSRTFDEQ 190 200 210 220 230 240 RTATIMEELS DALTYCHKKK VIHRDIKPEN LLLGLQGELK IADFGWSVHA PSLRRKTMCG 250 260 270 280 290 300 TLDYLPPEMI EGRMHNEMVD LWCIGVLCYE LMVGNPPFES PSHSETYRRI VKVDLKFPSS 310 320 330 340 VPSGAQDLIS KLLKHNPWQR LPLAEVAAHP WVRANSRRVL PPSAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cell-cycle-dependent expression of the STK-1 gene encoding a novel murine putative protein kinase." Niwa H., Abe K., Kunisada T., Yamamura K. Gene 169:197-201(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Testis.
[2]	"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]. Strain: BALB/c.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo and Embryonic stem cell.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Mammary gland.
[7]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D21099 mRNA. Translation: BAA04658.1. U69107 mRNA. Translation: AAC12683.1. AK075951 mRNA. Translation: BAC36078.1. AK132006 mRNA. Translation: BAE20935.1. AL645902 Genomic DNA. Translation: CAI24442.1. CH466601 Genomic DNA. Translation: EDL10472.1. BC003261 mRNA. Translation: AAH03261.1.
IPI	IPI00268655.
PIR	JC4665.
RefSeq	NP_035626.1. NM_011496.1.
UniGene	Mm.3488.
3D structure databases
ProteinModelPortal	O70126.
SMR	O70126. Positions 41-343.
ModBase	Search...
Protein-protein interaction databases
IntAct	O70126. 8 interactions.
MINT	MINT-1341009.
PTM databases
PhosphoSite	O70126.
Proteomic databases
PaxDb	O70126.
PRIDE	O70126.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021277; ENSMUSP00000021277; ENSMUSG00000020897. ENSMUST00000108666; ENSMUSP00000104306; ENSMUSG00000020897.
GeneID	20877.
KEGG	mmu:20877.
Organism-specific databases
CTD	9212.
MGI	MGI:107168. Aurkb.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00550000074590.
HOGENOM	HOG000233016.
HOVERGEN	HBG108519.
InParanoid	Q8C6C1.
KO	K11479.
OMA	VPTGAQD.
OrthoDB	EOG4TTGJG.
Gene expression databases
Bgee	O70126.
CleanEx	MM_AURKB.
Genevestigator	O70126.
GermOnline	ENSMUSG00000020897. Mus musculus.
Family and domain databases
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. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1075275.
ChiTaRS	AURKB. mouse.
NextBio	299727.
SOURCE	Search...

Entry information

Entry name

AURKB_MOUSE

Accession

Primary (citable) accession number: O70126
Secondary accession number(s): Q61882, Q8C6C1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program