Q9VKN7 (AURKB_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aurora kinase B
EC=2.7.11.1

Alternative name(s):
IPL1/Aurora-like protein kinase
Serine/threonine-protein kinase Ial
Serine/threonine-protein kinase aurora-B

Gene names

Name:	ial
ORF Names:	CG6620

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase which mediates both meiotic and mitotic chromosome segregation. Required for histone H3 'Ser-10' phosphorylation. Phosphorylates mei-S332 within residues 124-126 and stabilizes its association with centromeres during meiosis. Ref.6 Ref.7 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Subunit structure	Interacts with Incenp and Cdc37. Ref.7 Ref.8
Subcellular location	Chromosome. Cytoplasm › cytoskeleton. Midbody. Note: Meiotic and mitotic chromosomes. During each division, relocates to the midbody microtubules. Ref.6 Ref.7
Developmental stage	Ubiquitously expressed at very high levels in embryo. Expressed at low levels during larval stages, and at higher levels in female adults (at protein level). Ref.1 Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAD34349.1 differs from that shown. Reason: Frameshift at positions 285 and 289. The sequence AAD37504.1 differs from that shown. Reason: Frameshift at positions 285 and 289.

Ontologies

Keywords
Biological process	Cell cycle Cell division Chromosome partition Meiosis Mitosis
Cellular component	Chromosome Cytoplasm Cytoskeleton
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	attachment of spindle microtubules to kinetochore Traceable author statement. Source: FlyBase cytokinesis Inferred from mutant phenotype Ref.6. Source: FlyBase histone phosphorylation Inferred from mutant phenotype Ref.6. Source: FlyBase meiosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic chromosome condensation Inferred from mutant phenotype Ref.6. Source: FlyBase mitotic spindle organization Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW kinetochore Traceable author statement. Source: FlyBase midbody Inferred from direct assay Ref.6. Source: FlyBase spindle midzone Inferred from direct assay. Source: FlyBase
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 – 329	329	Aurora kinase B		PRO_0000280545
Regions
	Domain	53 – 305	253	Protein kinase
	Nucleotide binding	59 – 67	9	ATP By similarity
Sites
	Active site	178	1	Proton acceptor By similarity
	Binding site	82	1	ATP By similarity
Experimental info
	Sequence conflict	320	1	E → D in AAD34349. Ref.1
	Sequence conflict	320	1	E → D in AAD37504. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9VKN7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B489A0A33A4F2128	FASTA	329	38,301
	10 20 30 40 50 60 MTLSRAKHAN RNHLPHLLAK VPEEHQEPIK NMCLKMMSHD AYGQPYDWSP RDFEMGAHLG 70 80 90 100 110 120 RGKFGRVYLA RERHSHYLVA MKVMFKEELR KGCVQRQVLR EIEIQSRLKH PHILRLLTWF 130 140 150 160 170 180 HDESRIYLAL EIASEGELFK HLRGAPNHRF DEPRSAKYTY QVANALNYCH LNNVIHRDLK 190 200 210 220 230 240 PENILLTSTD DLKLADFGWS AHTPNNKRRT LCGTLDYLPP EMVDGNSYDD SVDQWCLGIL 250 260 270 280 290 300 CYEFVVGCPP FESNSTESTY SKIRRMEISY PSHLSKGCKE LIGGLLRKES KGRITLVDVM 310 320 THYWVKAGMA ERELQLQKRE RGKENTARN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, mapping, and expression of ial, a novel Drosophila member of the Ipl1/aurora mitotic control kinase family." Reich A., Yanai A., Mesilaty-Gross S., Chen-Moses A., Wides R., Motro B. DNA Cell Biol. 18:593-603(1999) [PubMed: 10433558] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE. Strain: Canton-S.
[2]	"The Drosophila STAM gene homolog is in a tight gene cluster, and its expression correlates to that of the adjacent gene ial." Mesilaty-Gross S., Reich A., Motro B., Wides R. Gene 231:173-186(1999) [PubMed: 10231582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE. Strain: Canton-S.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis." Giet R., Glover D.M. J. Cell Biol. 152:669-682(2001) [PubMed: 11266459] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Essential roles of Drosophila inner centromere protein (INCENP) and aurora B in histone H3 phosphorylation, metaphase chromosome alignment, kinetochore disjunction, and chromosome segregation." Adams R.R., Maiato H., Earnshaw W.C., Carmena M. J. Cell Biol. 153:865-880(2001) [PubMed: 11352945] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH INCENP.
[8]	"Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes." Lange B.M.H., Rebollo E., Herold A., Gonzalez C. EMBO J. 21:5364-5374(2002) [PubMed: 12374737] [Abstract] Cited for: INTERACTION WITH CDC37.
[9]	"INCENP and Aurora B promote meiotic sister chromatid cohesion through localization of the Shugoshin MEI-S332 in Drosophila." Resnick T.D., Satinover D.L., MacIsaac F., Stukenberg P.T., Earnshaw W.C., Orr-Weaver T.L., Carmena M. Dev. Cell 11:57-68(2006) [PubMed: 16824953] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF121358 mRNA. Translation: AAD34349.1. Frameshift. AF121361 Genomic DNA. Translation: AAD37504.1. Frameshift. AE014134 Genomic DNA. Translation: AAF53026.1. AY118562 mRNA. Translation: AAM49931.1.
RefSeq	NP_477336.1. NM_057988.3.
UniGene	Dm.3103.
3D structure databases
HSSP	HSSP built from PDB template 1OL6 based on UniProtKB O14965.
ProteinModelPortal	Q9VKN7.
SMR	Q9VKN7. Positions 47-311.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VKN7. 1 interaction.
MINT	MINT-802090.
STRING	Q9VKN7.
Proteomic databases
PRIDE	Q9VKN7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0080180; FBpp0079769; FBgn0024227.
GeneID	34504.
KEGG	dme:Dmel_CG6620.
NMPDR	fig|7227.3.peg.1919.
Organism-specific databases
CTD	34504.
FlyBase	FBgn0024227. ial.
Phylogenomic databases
eggNOG	inNOG04316.
GeneTree	EMGT00050000001100.
InParanoid	Q9VKN7.
OMA	ANALNYC.
OrthoDB	EOG4JDFPN.
PhylomeDB	Q9VKN7.
Gene expression databases
ArrayExpress	Q9VKN7.
Bgee	Q9VKN7.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08850.
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
NextBio	788823.

Entry information

Entry name

AURKB_DROME

Accession

Primary (citable) accession number: Q9VKN7
Secondary accession number(s): Q9XTQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project