Reviewed, UniProtKB/Swiss-Prot Q96GD4 (AURKB_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase 12
    EC=2.7.11.1
Alternative name(s):
    Aurora kinase B
    Serine/threonine-protein kinase 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
      Short name=ARK-2
    STK-1

Gene names

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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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. Required for kinetochore localization of BUB1 and SGOL1. Ref.9 Ref.10 Ref.11 Ref.15
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. Interacts with SEPT1. Interacts with PSMA3. Ref.11 Ref.15 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20
Subcellular location	Nucleus. Centromere. Cytoplasm › cytoskeleton › spindle. 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. Ref.17
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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosomal protein Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro protein localization to kinetochore Inferred from mutant phenotype. Source: UniProtKB
Cellular component	chromosome passenger complex Ref.20 Inferred from physical interaction. Source: UniProtKB condensed chromosome, centromeric region Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle 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.16 Ref.17 Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 344	343	Serine/threonine-protein kinase 12		PRO_0000085656
Regions
	Domain	77 – 327	251	Protein kinase
	Nucleotide binding	83 – 91	9	ATP By similarity
Sites
	Active site	200	1	Proton acceptor By similarity
	Binding site	106	1	ATP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.22
	Modified residue	7	1	Phosphoserine Ref.22 Ref.21 Ref.24
	Modified residue	12	1	Phosphotyrosine Ref.21
	Modified residue	16	1	Phosphothreonine Ref.22
	Modified residue	35	1	Phosphothreonine Ref.22 Ref.24 Ref.25
	Modified residue	45	1	Phosphoserine Ref.22 Ref.24
	Modified residue	61	1	Phosphoserine Ref.22 Ref.24
	Modified residue	62	1	Phosphoserine Ref.22
	Modified residue	64	1	Phosphothreonine Ref.22 Ref.24
	Modified residue	92	1	Phosphotyrosine Ref.24
	Modified residue	227	1	Phosphoserine Ref.24
	Modified residue	232	1	Phosphothreonine Ref.21 Ref.24 Ref.23
	Modified residue	236	1	Phosphothreonine Ref.24
	Modified residue	313	1	Phosphoserine Ref.24
Natural variations
	Natural variant	52	1	A → V		VAR_040383
	Natural variant	100	1	H → Q: dbSNP rs3027254.		VAR_027970
	Natural variant	179	1	T → M		VAR_040384
	Natural variant	298	1	T → M: dbSNP rs1059476. Ref.7 Ref.27		VAR_027971
Experimental info
	Mutagenesis	106	1	K → R: Loss of kinase activity. Ref.17
	Sequence conflict	14 – 15	2	RQ → DK in AAC98891. Ref.5
	Sequence conflict	70	1	R → RR in AAH13300. Ref.7
	Sequence conflict	161	1	E → M Ref.4
	Sequence conflict	161	1	E → M Ref.5
	Sequence conflict	167 – 169	3	QKS → HKT in AAB65786. Ref.4
	Sequence conflict	179	1	T → TVRR in AAB65786. Ref.4
	Sequence conflict	180	1	I → VRAV Ref.5
	Sequence conflict	226	1	P → T in BAA82709. Ref.3
	Sequence conflict	249 – 250	2	MH → ID in BAA82709. Ref.3
	Sequence conflict	271	1	Missing in BAA82709. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q96GD4-1 [UniParc]. Last modified January 17, 2003. Version 2. Checksum: 8325E3EF5A1FB170	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

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]	"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: 14674694] [Abstract] Cited for: INTERACTION WITH PSMA3.
[13]	"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: 15020684] [Abstract] Cited for: FUNCTION.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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: 16179162] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SEPT1, MUTAGENESIS OF LYS-106.
[18]	"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.
[19]	"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: 17617734] [Abstract] Cited for: FUNCTION.
[20]	"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: 18591255] [Abstract] Cited for: INTERACTION WITH BIRC5.
[21]	"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.
[22]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-16; THR-35; SER-45; SER-61; SER-62 AND THR-64, ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, MASS SPECTROMETRY.
[27]	"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.
[28]	"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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-52 AND MET-179.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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
SMR	Q96GD4. Positions 70-337.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-34530N.
IntAct	Q96GD4. 21 interactions.
STRING	Q96GD4.
PTM databases
PhosphoSite	Q96GD4.
Proteomic databases
PRIDE	Q96GD4.
Genome annotation databases
Ensembl	ENST00000316199; ENSP00000313950; ENSG00000178999; Homo sapiens. [Genome view]
GeneID	9212.
KEGG	hsa:9212.
UCSC	uc002gkm.1. human.
Organism-specific databases
CTD	9212.
GeneCards	GC17M008048.
H-InvDB	HIX0019005.
HGNC	HGNC:11390. AURKB.
HPA	CAB005862.
MIM	604970. gene.
PharmGKB	PA36199.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08834.
HOGENOM	HBG755340.
HOVERGEN	Q96GD4.
InParanoid	Q96GD4.
OrthoDB	EOG9ZW7WT.
PhylomeDB	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.
Genevestigator	Q96GD4.
GermOnline	ENSG00000178999. Homo sapiens.
Family and domain databases
InterPro	IPR020636. Ca/CaM-dep_prot_kinase-like. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. IPR020663. Spindle_assmbl_checkpoint_kin. [Graphical view]
PANTHER	PTHR22982. Ca/CaM-dep_prot_kinase-like. 1 hit. PTHR22982:SF49. Spindle_assmbl_checkpoint_kin. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
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...

Entry information

Entry name

AURKB_HUMAN

Accession

Primary (citable) accession number: Q96GD4
Secondary accession number(s): O14630 , O60446, O95083, Q96DV5, Q9UQ46

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	January 17, 2003
Last modified:	February 9, 2010
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.