Serine/threonine-protein kinase 12 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q96GD4 (AURKB_HUMAN)

Last modified June 16, 2009. Version 97. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase 12
    EC=2.7.11.1
Alternative name(s):
    Aurora-B
    Aurora- and Ipl1-like midbody-associated protein 1
      Short name=AIM-1
    Aurora/IPL1-related kinase 2
      Short name=Aurora-related kinase 2
    STK-1

Gene names

Name:	AURKB
Synonyms:	AIK2, AIM1, ARK2, STK12

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	May be directly involved in regulating the cleavage of polar spindle microtubules and is a key regulator for the onset of cytokinesis during mitosis. 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. Phosphorylates 'Ser-10' and 'Ser-28' of histone H3 during mitosis. Ref.9 Ref.10 Ref.11 Ref.13
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Subunit structure	Interacts with TACC1. Associates with RACGAP1 during M phase. Component of the CPC at least composed of BIRC5/survivin CDCA8/borealin, INCENP and AURKB/Aurora-B. Interacts with CDCA1 and NDC80. Interacts with EVI5. Ref.11 Ref.13 Ref.12 Ref.14 Ref.15
Subcellular location	Nucleus. Centromere. 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.
Tissue specificity	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. Ref.2 Ref.3
Involvement in disease	Disruptive regulation of expression is a possibile mechanism of the perturbation of chromosomal integrity in cancer cells through its dominant-negative effect on cytokinesis.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. Contains 1 protein kinase domain.

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Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosomal protein Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.11 Ref.14 Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
BIRC5	O15392	1	EBI-624291,EBI-518823
BIRC5	O15392-1	2	EBI-624291,EBI-518838
BIRC5	O15392-2	2	EBI-624291,EBI-518842
CDC2	P06493	1	EBI-624291,EBI-444308
INCENP	Q9NQS7	1	EBI-624291,EBI-307907
PPP1CA	P62136	1	EBI-624291,EBI-357253
SEPT1	Q8WYJ6	3	EBI-624291,EBI-693002
TACC1	O75410	1	EBI-624291,EBI-624237
TACC1	O75410-1	1	EBI-624291,EBI-624252
TACC1	O75410-6	1	EBI-624291,EBI-624278

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 344

344

Serine/threonine-protein kinase 12

PRO_0000085656

Regions

Domain

77 – 327

251

Protein kinase

Nucleotide binding

83 – 91

ATP By similarity

Sites

Active site

200

Proton acceptor By similarity

Binding site

106

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.16 Ref.18

Modified residue

Phosphotyrosine Ref.16

Modified residue

Phosphothreonine Ref.18 Ref.19

Modified residue

Phosphoserine Ref.18

Modified residue

Phosphoserine Ref.18

Modified residue

Phosphothreonine Ref.18

Modified residue

Phosphotyrosine Ref.18

Modified residue

227

Phosphoserine Ref.18

Modified residue

232

Phosphothreonine Ref.16 Ref.18 Ref.17

Modified residue

236

Phosphothreonine Ref.18

Modified residue

313

Phosphoserine Ref.18

Natural variations

Natural variant

A → V Ref.21

VAR_040383

Natural variant

100

H → Q: dbSNP rs3027254.

VAR_027970

Natural variant

179

T → M Ref.21

VAR_040384

Natural variant

298

T → M: dbSNP rs1059476. Ref.7 Ref.20

VAR_027971

Experimental info

Sequence conflict

14 – 15

RQ → DK in AAC98891. Ref.5

Sequence conflict

R → RR in AAH13300. Ref.7

Sequence conflict

161

E → M Ref.4

Sequence conflict

161

E → M Ref.5

Sequence conflict

167 – 169

QKS → HKT in AAB65786. Ref.4

Sequence conflict

179

T → TVRR in AAB65786. Ref.4

Sequence conflict

180

I → VRAV Ref.5

Sequence conflict

226

P → T in BAA82709. Ref.3

Sequence conflict

249 – 250

MH → ID in BAA82709. Ref.3

Sequence conflict

271

Missing in BAA82709. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

Q96GD4-1 [UniParc].

Last modified January 17, 2003. Version 2.
Checksum: 8325E3EF5A1FB170
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FASTA

344

39,280

        10         20         30         40         50         60 
MAQKENSYPW PYGRQTAPSG LSTLPQRVLR KEPVTPSALV LMSRSNVQPT AAPGQKVMEN 

        70         80         90        100        110        120 
SSGTPDILTR HFTIDDFEIG RPLGKGKFGN VYLAREKKSH FIVALKVLFK SQIEKEGVEH 

       130        140        150        160        170        180 
QLRREIEIQA HLHHPNILRL YNYFYDRRRI YLILEYAPRG ELYKELQKSC TFDEQRTATI 

       190        200        210        220        230        240 
MEELADALMY CHGKKVIHRD IKPENLLLGL KGELKIADFG WSVHAPSLRR KTMCGTLDYL 

       250        260        270        280        290        300 
PPEMIEGRMH NEKVDLWCIG VLCYELLVGN PPFESASHNE TYRRIVKVDL KFPASVPTGA 

       310        320        330        340 
QDLISKLLRH NPSERLPLAQ VSAHPWVRAN SRRVLPPSAL QSVA

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9514916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 9809983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[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: 9858806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. 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: 11471245] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[6]	"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].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-298. Tissue: Lung, Lymph and Muscle.
[8]	"Mitotic kinases as regulators of cell division and its checkpoints." Nigg E.A. Nat. Rev. Mol. Cell Biol. 2:21-32(2001) [PubMed: 11413462] [Abstract] Cited for: REVIEW.
[9]	"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: 11856369] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[10]	"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: 11784863] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[11]	"Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during cytokinesis." Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A., Bao Y.C., Deng X., Tatsuka M., Narumiya S., May W.S. Jr., Nosaka T., Semba K., Inoue T., Satoh T., Inagaki M., Kitamura T. Dev. Cell 4:549-560(2003) [PubMed: 12689593] [Abstract] Cited for: FUNCTION, INTERACTION WITH RACGAP1.
[12]	"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: 15249581] [Abstract] Cited for: INTERACTION WITH CDCA8.
[13]	"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: 14602875] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDCA1 AND NDC80.
[14]	"Aurora B -TACC1 protein complex in cytokinesis." Delaval B., Ferrand A., Conte N., Larroque C., Hernandez-Verdun D., Prigent C., Birnbaum D. Oncogene 23:4516-4522(2004) [PubMed: 15064709] [Abstract] Cited for: INTERACTION WITH TACC1.
[15]	"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: 16764853] [Abstract] Cited for: INTERACTION WITH EVI5.
[16]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; TYR-12 AND THR-232, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, MASS SPECTROMETRY.
[18]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-35; SER-45; SER-61; THR-64; TYR-92; SER-227; THR-232; THR-236 AND SER-313, MASS SPECTROMETRY.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, MASS SPECTROMETRY.
[20]	"Aurora kinases A and B and familial breast cancer risk." Tchatchou S., Wirtenberger M., Hemminki K., Sutter C., Meindl A., Wappenschmidt B., Kiechle M., Bugert P., Schmutzler R.K., Bartram C.R., Burwinkel B. Cancer Lett. 247:266-272(2007) [PubMed: 16762494] [Abstract] Cited for: VARIANT MET-298.
[21]	"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. Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-52 AND MET-179.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	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. BT019534 mRNA. Translation: AAV38341.1. BC000442 mRNA. Translation: AAH00442.3. BC009751 mRNA. Translation: AAH09751.1. BC013300 mRNA. Translation: AAH13300.2. Different initiation. BC080581 mRNA. Translation: AAH80581.1.
IPI	IPI00176642.
RefSeq	NP_004208.2.
UniGene	Hs.442658
3D structure databases
HSSP	HSSP built from PDB template 1GZK based on UniProtKB P31751.
SMR	Q96GD4. Positions 70-337.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96GD4. 21 interactions.
PTM databases
PhosphoSite	Q96GD4.
Proteomic databases
PRIDE	Q96GD4.
Genome annotation databases
Ensembl	ENSG00000178999. Homo sapiens. [Contig view]
GeneID	9212.
KEGG	hsa:9212.
Organism-specific databases
GeneCards	GC17M008048.
H-InvDB	HIX0019005.
HGNC	HGNC:11390. AURKB.
HPA	CAB005862.
MIM	604970. gene.
PharmGKB	PA36199.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q96GD4.
HOVERGEN	Q96GD4.
Enzyme and pathway databases
BRENDA	2.7.11.1. 247.
Pathway_Interaction_DB	aurora_a_pathway. Aurora A signaling. aurora_b_pathway. Aurora B signaling. aurora_c_pathway. Aurora C signaling. foxm1pathway. FOXM1 transcription factor network. aurora_kinase_pathway. Signaling by Aurora kinases.
Reactome	REACT_152. Cell Cycle, Mitotic.
Gene expression databases
ArrayExpress	Q96GD4.
Bgee	Q96GD4.
CleanEx	HS_AIM1. HS_AURKB.
GermOnline	ENSG00000178999. Homo sapiens.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	34535.
SOURCE	Search...

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Entry information

Entry name

AURKB_HUMAN

Accession

Primary (citable) accession number: Q96GD4
Secondary accession number(s): O14630

Q9UQ46

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	January 17, 2003
Last modified:	June 16, 2009
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents