AURKA (aurora kinase A)

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Home Genes Leukemias Solid Tumors Cancer-Prone Deep Insight Case Reports Journals Portal Teaching

X Y 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NA

AURKA (aurora kinase A)

Written	2008-05	Laura Lentini, Aldo Di Leonardo
		Department of Cellular, Developmental Biology A, Monroy, University of Palermo, viale delle Scienze, Palermo, Italy

(Note : for Links provided by Atlas : click)

Identity

Alias (NCBI)	Aurora A
	ARK1
	AURA
	Aurora2
	BTAK
	MGC34538
	STK15
	STK6
	STK7
HGNC (Hugo)	AURKA
HGNC Alias symb	BTAK
	AurA
	STK7
	ARK1
	PPP1R47
	AIK
HGNC Alias name	protein phosphatase 1, regulatory subunit 47
	Aurora-A kinase
HGNC Previous name	STK15
	STK6
HGNC Previous name	serine/threonine kinase 15
	serine/threonine kinase 6
LocusID (NCBI)	6790
Atlas_Id	730
Location	20q13.2 [Link to chromosome band 20q13]
Location_base_pair	Starts at 56369390 and ends at 56392215 bp from pter ( according to GRCh38/hg38-Dec_2013) [Mapping AURKA.png]

Fusion genes
(updated 2017)

Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)

AURKA (20q13.2) / PCK1 (20q13.31)

BCAS4 (20q13.13) / AURKA (20q13.2)

DNA/RNA

Description	The gene encompasses 22,8 kb of DNA; 9 Exons.
Transcription	2253 bp mRNA.

Protein



Description	403 amino acids, 46kDa protein. At the amino terminal domain, three putative conserved Aurora boxes (A-boxI, A-boxII and A-boxIII) can be identified. The functional significance of these boxes are not yet clearly known and there is suggestive evidence in the literature that these may be involved in subcellular localization or substrate recognition for the proteins. One of the serine residues in the A-boxII of Aurora-A kinase has recently been shown to be involved in the degradation of the protein. One activation motif and a destruction box in C-terminal. AURKA is regulated by phosphorylation in a cell cycle dependent manner. This phosphorylation occurs on a conserved residue, threonine 288, within the activation loop of the catalytic domain of the kinase and results in a significant increase in the enzymatic activity. AURKA protein is able to physically associate with multiple important cellular proteins such as p53, BRCA1, and TACC1. The interactions of AURKA with those critical molecules have been shown to disrupt/alter their physiological functions and may play roles in tumorigenesis.
Expression	Widely expressed, AURKA mRNA and protein expression levels are low during G1 and S phase and peak during the G2/M phase of the cell cycle. Kinase activity of the protein is also cell cycle regulated and the highest activity coincides with the most elevated expression level of the protein during mitosis.
Localisation	AURKA localizes next to the centrosome late in the G1 phase and early in the S phase. As the cell cycle progresses, concentration of AURKA increases and the kinase associates with the mitotic poles and the adjacent spindle microtubules. AURKA remains associated with the spindles through telophase.
Function	Serine/threonine kinase identified as key regulator of the mitotic cell division process. Known to be involved in the regulation of centrosome function, bipolar spindle assembly and chromosome segregation processes. AURKA is critical for proper formation of mitotic spindle. It is required for the recruitment of several different proteins important to the spindle formation. Among these target proteins are TACC, a microtubule-associated protein that stabilizes centrosomal microtubules and Kinesin 5, a motor protein involved in the formation of the bipolar mitotic spindle. Two upstream regulators of AURKA, Ajuba and targeting protein for Xklp2 ( TPX2 ) are known. TPX2 is a MT-binding protein involved in spindle pole formation and is the best characterized RanGTP-dependent spindle activator. TPX2 is required for AURKA binding to spindle MTs and its binding to AURKA holds the latter in an active conformation. Ajuba and AURKA interact in mitotic cells and become phosphorylated. In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of AURKA. Depletion of Ajuba prevented activation of AURKA at centrosomes in late G2 phase and inhibited mitotic entry. AURKA induces p53 degradation by phosphorylation of Ser-315. It was demonstrated that DNA binding and transactivation activity of p53 was abrogated by AURKA. AURKA phosphorylates p53 at Ser-215 in vitro and in vivo. The inhibition of p53 DNA binding and transactivation activity by AURKA depends on phosphorylation of Ser-215 but not Ser-315. Further, AURKA phosphorylation of Ser-215 of p53 is associated with AURKA -regulated cell cycle progression, cell survival, and transformation. The p53 is a physiological substrate of AURKA and that AURKA exerts its function through phosphorylation of Ser-215 of p53.
Homology	Aurora related kinases, AURKA and AURKB are present in Drosophila,C.elegans and X. laevis. Among mammals, three members of the family, AURKA, -B and -C have so far been identified. The three members of the mammalian kinases of varying peptide lengths share similar catalytic domains located in the carboxyl terminus but their amino terminal extensions are of variable length and display little or no similarity. By examination of the AURKA cDNA sequence the threonine at residue 288 in the catalytic domain was found to be highly conserved in all Aurora family members as well as in various other serine/threonine kinases.

Mutations

Germinal

No germline mutations have been reported.

Somatic

Recent studies have demonstrated the overexpression and amplification of AURKA in many malignant human cancers and cell lines including breast, ovarian, colon, prostate, and neuroblastoma cancer cell lines. AURKA overexpression induces supernumerary centrosomes aneuploidy and cells transformation. It has been also reported that ectopic overexpression of AURKA in NIH3T3 and immortalized Rat1 induces cells transformation that generates tumor when implanted in nude mice. Elevated AURKA expression amplification overrides the checkpoint mechanism that monitors mitotic spindle assembly, inducing resistance to the chemotherapeutic agent paclitaxel. Cells overexpressing Aurora-A inappropriately enter anaphase despite defective spindle formation, and the persistence of MAD2 at the kinetochores, marking continued activation of the spindle assembly checkpoint. These findings suggest that enhanced AURKA expression causes resistence to apoptosis induced by mitotic inhibitors in human cancer cells.

Implicated in

Note

Entity	Breast cancer
Disease	Breast cancer is the most common cause of cancer in women and the second most common cause of cancer death in women. Some of the patients are hereditary, with a large proportion characterized by mutation in BRCA1 and/or BRCA2 genes.
Oncogenesis	The protein level of AURKA is increased at the G2 to M phase transition in normal cells, where AURKA is specifically localised at centrosomes and mitotic spindles. By contrast, analysis of tumour cells of the breast for AURKA expression patterns shows that overexpression of AURKA was present in 94% of the cases, regardless of their cell-cycle phases, and is diffusely detected in the cytoplasm. Amplification of AURKA has been detected at higher frequency in tumors from BRCA1 and BRCA2 mutation carriers than in sporadic breast tumors, suggesting that overexpression of AURKA and inactivation of BRCA1 and BRCA2 cooperate during tumor development and progression. The F31I polymorphism in AURKA has been associated with breast cancer risk in the homozygous state in prior studies. Studies have demonstrated that AURKA overexpression contributes to genetic instability and tumourigenesis by disrupting the proper assembly of the mitotic checkpoint complex and occurs in a high proportion of breast cancers.


Entity	Pancreatic cancer
Disease	Pancreatic ductal adenocarcinoma is one of the most fatal malignancies. Intensive investigation of molecular pathogenesis might lead to identifying useful molecules for diagnosis and treatment of the disease.
Oncogenesis	Pancreatic ductal adenocarcinoma harbors complicated aberrations of alleles including losses of 1p, 6q, 9p, 12q, 17p, 18q, and 21q, and gains of 8q and 20q. Pancreatic cancer is usually initiated by mutation of KRAS and aberrant expression of SHH. Overexpression of AURKA mapping on 20q13.2 may significantly enhance overt tumorigenesity. AURKA was a direct downstream target of MAPK1, suggesting that the overexpression of AURKA without gene amplification may be induced by constitutive activation of MAPK1 in cancer cells. The constitutive activation of MAPK1 is frequently observed in pancreatic cancer.


Entity	Ovarian cancer
Disease	Ovarian cancer is the most lethal gynecologic malignancy in developed countries. The exact cause is usually unknown. The risk of developing ovarian cancer appears to be affected by several factors.
Oncogenesis	Recent studies have shown that DNA gains of the chromosomal region 20q13 and overexpression of the centrosomal kinase AURKA, the gene of which is found within the 20q13 region, are hallmarks of ovarian cancer. Amplification of AURKA has been reported in ovarian tumors, suggesting a role in ovarian cancer pathology. AURKA is polymorphic with two single nucleotide substitutions (449t/a and 527g/a) in evolutionarily conserved regions causing amino acid changes (F31I and V57I). Two other nucleotide substitutions (287c/g and 1891g/c) of unknown significance are in 5' and 3' untranslated regions (UTR), respectively. AURKA overexpression represented a survival factor for tumor cells and a negative prognostic molecular marker.


Entity	Human esophageal squamous cell carcinoma
Disease	Human esophageal squamous cell carcinoma (ESCC) is one of the most frequent malignancies worldwide and occurs at a very high frequency in the People's Republic of China, South Africa, France, and Italy. A number of epidemiological investigations have shown that esophageal carcinogenesis and the malignant development of esophageal cancers are complex and associated with multiple etiologic factors, including genetic backgrounds, environmental stimuli, nutritional conditions, and cultural habits.
Oncogenesis	Despite some epidemiological observations, the biological mechanism(s) that is involved in ESCC occurrence and progression remains to be elucidated. It has been shown that point mutations of the tumor suppressor gene p53 are detected in 40% of human esophageal cancers. The Rb gene is also frequently mutated in ESCC. Amplification of the cellular protooncogenes Myc, EGFR, HST1, INT2, and cyclin D1 are often found in this malignant disease. A recent demonstration indicates that AURKA polymorphisms are associated with advanced disease status of ESCC, and there are strong evidence that AURKA is overexpressed in human ESCC and may play a role in carcinogenesis and malignancy development of ESCC.


Entity	Human Bladder Cancer
Disease	Bladder tumors are among the most common human cancers, with approximately 55 000 new cases detected each year in the United States. Bladder cancers, which represent a group of tumors with diverse morphologic and clinical behavior, exhibit one of the strongest relationships seen in any cancer between clinical aggressiveness and degree of aneuploidy.
Oncogenesis	Bladder cancers arise from at least two distinct, albeit sometimes overlapping, pathways that lead to the development of papillary and solid or nonpapillary tumors. Most superficially growing, low-grade papillary lesions are diploid or near-diploid. Although they often recur, they are unlikely to invade the bladder wall and metastasize. By contrast, virtually all nonpapillary tumors are highly aneuploid and have a strong propensity to invade the stroma and metastasize. Superficial bladder tumors that are aneuploid are also likely to progress to invasive clinically aggressive carcinomas, which may metastasize. AURKA amplification is frequently overexpressed in bladder tumors tested by FISH and the strong association of the gene amplification and overexpression levels with the degree of aneuploidy suggests that AURKA may play an important role in bladder carcinogenesis by contributing to the development of aneuploid cell populations with aggressive phenotypes.


Entity	Human colon cancer
Disease	It is the third most common form of cancer and the second leading cause of cancer-related death in the Western world. Colorectal cancer causes 655,000 deaths worldwide per year, including about 16,000 in the UK, where it is the second most common site (after lung) to cause cancer death. The most common colon cancer cell type is adenocarcinoma which accounts for 95% of cases. Other, rarer types include lymphoma and squamous cell carcinoma. Adenocarcinoma is a malignant epithelial tumor, originating from glandular epithelium of the colorectal mucosa. It invades the wall, infiltrating the muscularis mucosae, the submucosa and thence the muscularis propria.
Oncogenesis	Colorectal cancer is a disease originating from the epithelial cells lining the gastrointestinal tract. Hereditary or somatic mutations in specific DNA sequences, among which are included DNA replication or DNA repair genes and also the APC, K-Ras, NOD2 and p53 genes, lead to unrestricted cell division. Furthermore, genetic instability is expressed in colon cancer by an increased rate of a number of different genetic alterations. These different manifestations of genetic instability are classified into two major categories. The first one involves subtle changes in DNA sequences typically represented by microsatellite instability (MIN). The second one is characterized by gains and losses of whole or parts of chromosomes, named chromosomal instability (CIN), and it is considered a driving force for tumourigenesis. MIN occurs in approximately 15% of colon cancers and results from inactivation of the mismatch repair (MMR) system by either MMR gene mutations or hypermethylation of the MLH1 promoter. The mechanisms inducing CIN in cancer and more specifically in colon cancer are only partly understood. At least two possible causes, not mutually exclusive, could be responsible for CIN: mutations in genes encoding mitotic regulators, such as spindle checkpoint proteins, and defects in genes controlling centrosome homeostasis. The presence of mutations of the mitotic checkpoint regulators BUB1 and BUBR1 and amplification of AURKA in a subset of human colon cancers have suggested that CIN results primarily from deregulation of DNA replication and mitotic-spindle checkpoints.


Entity	Human Multiple myeloma
Disease	Multiple myeloma (also known as MM, myeloma, plasma cell myeloma, or as Kahler's disease after Otto Kahler) is a type of cancer of plasma cells which are immune system cells in bone marrow that produce antibodies. Myeloma is regarded as incurable, but remissions may be induced with steroids, chemotherapy, thalidomide and stem cell transplants. Myeloma is part of the broad group of diseases called hematological malignancies. Multiple myeloma (MM) is a malignancy characterized by genetic instability, suggesting a disruption of checkpoints that arrest cells at G2M when injury to the mitotic machinery occurs.
Oncogenesis	The expression of RHAMM and other centrosome-associated genes are known to correlate with the extent of centrosome amplification in multiple myeloma, and with poor prognosis. RHAMM has a significant interaction with TPX2, a protein which regulates the localization and action of AURKA at the spindle poles. AURKA is expressed ubiquitously in myeloma, to varying degrees. Aurora kinase inhibitor VE-465 also induces apoptosis and death in myeloma cell lines and primary myeloma plasma cells. The combination of VE-465 and dexamethasone improves cell killing compared with the use of either agent alone, even in cells resistant to the single agents.


Entity	Human hepatocellular carcinoma
Disease	Hepatocellular carcinoma (HCC, also called hepatoma) is a primary malignancy (cancer) of the liver. Most cases of HCC are secondary to either a viral hepatitide infection (hepatitis B or C) or cirrhosis (alcoholism being the most common cause of hepatic cirrhosis). In countries where hepatitis is not endemic, most malignant cancers in the liver are not primary HCC but metastasis (spread) of cancer from elsewhere in the body, e.g. the colon. Treatment options of HCC and prognosis are dependent on many factors but especially on tumor size and staging.
Oncogenesis	AURKA is overexpressed frequently in HCC, and correlated with high grade and high stage, indicating that overexpression of AURKA plays a role in the development and progression of HCC. Furthermore in HCC is frequently associated the homozygous deletion of p15E2 ( MTS2/INK4b/CDKN2B ) and p16E2 ( MTS1/INK4a/CDKN2A ) with overexpression of AURKA gene, this association may play a role in the oncogenesis and malignant progression of HCC.


Entity	Human Upper gastrointestinal adenocarcinomas
Disease	Upper gastrointestinal adenocarcinomas are the second most common cause of cancer-related death in the world. and are characterized by complex molecular changes. Several epidemiological studies have indicated that the incidence of proximal adenocarcinomas of the gastroesophageal junction and lower esophagus is rising faster than ever before in the Western world. The incidence of adenocarcinoma of the cardia, gastroesophageal junction, and lower esophagus has been rapidly rising, 5-fold to 6-fold in the past few decades, especially in patients younger than 50 years of age.
Oncogenesis	Overexpression of AURKA is frequent in upper gastrointestinal adenocarcinomas and in recently works it was identified the AURKA/AKT axis as an important mechanism that provides cancer cells with potent antiapoptotic properties through regulating p53-dependent apoptosis. Frequent overexpression of AURKA at the mRNA and protein levels in upper gastrointestinal adenocarcinomas, and interestingly, this overexpression was more prevalent in gastroesophageal junction adenocarcinomas andlower esophageal, Barrett-related adenocarcinomas (BAs) than in antrum and body gastric adenocarcinomas. There are not an association between AURKA overexpression and histopathological paramters such as tumor grade, TNM classification, and lymph-node metastasis.

Bibliography

A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers.

Bischoff JR, Anderson L, Zhu Y, Mossie K, Ng L, Souza B, Schryver B, Flanagan P, Clairvoyant F, Ginther C, Chan CS, Novotny M, Slamon DJ, Plowman GD.

EMBO J. 1998 Jun 1;17(11):3052-65.

PMID 9606188

Aurora-A and p16 polymorphisms contribute to an earlier age at diagnosis of pancreatic cancer in Caucasians.

Chen J, Li D, Wei C, Sen S, Killary AM, Amos CI, Evans DB, Abbruzzese JL, Frazier ML.

Clin Cancer Res. 2007 May 15;13(10):3100-4.

PMID 17505013

Consortium analysis of 7 candidate SNPs for ovarian cancer.

Couch FJ, Sinilnikova O, Vierkant RA, Pankratz VS, Fredericksen ZS, Stoppa-Lyonnet D, Coupier I, Hughes D, Hardouin A, Berthet P, Peock S, Cook M, Baynes C, Hodgson S, Morrison PJ, Porteous ME, Jakubowska A, Lubinski J, Gronwald J, Spurdle AB; kConFab, Schmutzler R, Versmold B, Engel C, Meindl A, Sutter C, Horst J, Schaefer D, Offit K, Kirchhoff T, Andrulis IL, Ilyushik E, Glendon G, Devilee P, Vreeswijk MP, Vasen HF, Borg A, Backenhorn K, Struewing JP, Greene MH, Neuhausen SL, Rebbeck TR, Nathanson K, Domchek S, Wagner T, Garber JE, Szabo C, Zikan M, Foretova L, Olson JE, Sellers TA, Lindor N, Nevanlinna H, Tommiska J, Aittomaki K, Hamann U, Rashid MU, Torres D, Simard J, Durocher F, Guenard F, Lynch HT, Isaacs C, Weitzel J, Olopade OI, Narod S, Daly MB, Godwin AK, Tomlinson G, Easton DF, Chenevix-Trench G, Antoniou AC; Consortium of Investigators of Modifiers of BRCA1/2.

Cancer Epidemiol Biomarkers Prev. 2007 Jul;16(7):1416-21.

PMID 17627006

A functional interplay between Aurora-A, Plk1 and TPX2 at spindle poles: Plk1 controls centrosomal localization of Aurora-A and TPX2 spindle association.

De Luca M, Lavia P, Guarguaglini G.

Cell Cycle. 2006 Feb;5(3):296-303. Epub 2006 Feb 7.

PMID 16418575

STK15 polymorphisms and association with risk of invasive ovarian cancer.

Dicioccio RA, Song H, Waterfall C, Kimura MT, Nagase H, McGuire V, Hogdall E, Shah MN, Luben RN, Easton DF, Jacobs IJ, Ponder BA, Whittemore AS, Gayther SA, Pharoah PD, Kruger-Kjaer S.

Cancer Epidemiol Biomarkers Prev. 2004 Oct;13(10):1589-94.

PMID 15466974

Aurora A kinase RNAi and small molecule inhibition of Aurora kinases with VE-465 induce apoptotic death in multiple myeloma cells.

Evans R, Naber C, Steffler T, Checkland T, Keats J, Maxwell C, Perry T, Chau H, Belch A, Pilarski L, Reiman T.

Leuk Lymphoma. 2008 Mar;49(3):559-69.

PMID 18297535

AURKA is one of the downstream targets of MAPK1/ERK2 in pancreatic cancer.

Furukawa T, Kanai N, Shiwaku HO, Soga N, Uehara A, Horii A.

Oncogene. 2006 Aug 10;25(35):4831-9.

PMID 16532023

Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells.

Hirota T, Kunitoku N, Sasayama T, Marumoto T, Zhang D, Nitta M, Hatakeyama K, Saya H.

Cell. 2003 Sep 5;114(5):585-98.

PMID 13678582

Overexpression and amplification of Aurora-A in hepatocellular carcinoma.

Jeng YM, Peng SY, Lin CY, Hsu HC.

Clin Cancer Res. 2004 Mar 15;10(6):2065-71.

PMID 15041727

The Aurora kinases: role in cell transformation and tumorigenesis.

Katayama H, Brinkley WR, Sen S.

Cancer Metastasis Rev. 2003 Dec; 22(4): 451-64. (Review).

PMID 12884918

Two functional coding single nucleotide polymorphisms in STK15 (Aurora-A) coordinately increase esophageal cancer risk.

Kimura MT, Mori T, Conroy J, Nowak NJ, Satomi S, Tamai K, Nagase H.

Cancer Res. 2005 May 1;65(9):3548-54.

PMID 15867347

Simultaneous Aurora-A/STK15 overexpression and centrosome amplification induce chromosomal instability in tumour cells with a MIN phenotype.

Lentini L, Amato A, Schillaci T, Di Leonardo A.

BMC Cancer. 2007 Nov 13;7:212.

PMID 17999753

Identification of phosphorylated residues that affect the activity of the mitotic kinase Aurora-A.

Littlepage LE, Wu H, Andresson T, Deanehan JK, Amundadottir LT, Ruderman JV.

Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15440-5.

PMID 12422018

Aurora-A abrogation of p53 DNA binding and transactivation activity by phosphorylation of serine 215.

Liu Q, Kaneko S, Yang L, Feldman RI, Nicosia SV, Chen J, Cheng JQ.

J Biol Chem. 2004 Dec 10;279(50):52175-82. Epub 2004 Oct 6.

PMID 15469940

Amplification/Overexpression of a Mitotic Kinase Gene in Human Bladder Cancer.

Sen S, Zhou H, Zhang RD, Yoon DS, Vakar-Lopez F, Ito S, Jiang F, Johnston D, Grossman HB, Ruifrok AC, Katz RL, Brinkley W, Czerniak B.

J Natl Cancer Inst. 2002 Sep 4;94(17):1320-9.

PMID 12208897

Overexpression of Aurora-A Contributes to Malignant Development of Human Esophageal Squamous Cell Carcinoma.

Tong T, Zhong Y, Kong J, Dong L, Song Y, Fu M, Liu Z, Wang M, Guo L, Lu S, Wu M, Zhan Q.

Clin Cancer Res. 2004 Nov 1;10(21):7304-10.

PMID 15534106

Citation

This paper should be referenced as such :

Lentini, L ; Di, Leonardo A

AURKA (aurora kinase A)

Atlas Genet Cytogenet Oncol Haematol. 2009;13(4):253-257.

Free journal version : [ pdf ] [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]

inv(16)(p13q24) CBFA2T3/GLIS2

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 4 ]

Thyroid: Anaplastic (undifferentiated) carcinoma
Male breast cancer
AURKA/PCK1 (20q13)
BCAS4/AURKA (20q13)

External links

	Nomenclature
HGNC (Hugo)	AURKA 11393
	Cards
Atlas	AURKAID730ch20q13
Entrez_Gene (NCBI)	AURKA aurora kinase A
Aliases	AIK; ARK1; AURA; BTAK;
	PPP1R47; STK15; STK6; STK7
GeneCards (Weizmann)	AURKA
Ensembl hg19 (Hinxton)	ENSG00000087586 [Gene_View]
Ensembl hg38 (Hinxton)	ENSG00000087586 [Gene_View] ENSG00000087586 [Sequence] chr20:56369390-56392215 [Contig_View] AURKA [Vega]
ICGC DataPortal	ENSG00000087586
TCGA cBioPortal	AURKA
AceView (NCBI)	AURKA
Genatlas (Paris)	AURKA
SOURCE (Princeton)	AURKA
Genetics Home Reference (NIH)	AURKA
	Genomic and cartography
GoldenPath hg38 (UCSC)	AURKA - chr20:56369390-56392215 - 20q13.2 [Description] (hg38-Dec_2013)
GoldenPath hg19 (UCSC)	AURKA - 20q13.2 [Description] (hg19-Feb_2009)
GoldenPath	AURKA - 20q13.2 [CytoView hg19] AURKA - 20q13.2 [CytoView hg38]
ImmunoBase	ENSG00000087586
genome Data Viewer NCBI	AURKA [Mapview hg19]
OMIM	114500 603072
	Gene and transcription
Genbank (Entrez)	AF008551 AF011468 AK301769 AK312776 AL711075
RefSeq transcript (Entrez)	NM_001323303 NM_001323304 NM_001323305 NM_003600 NM_198433 NM_198434 NM_198435 NM_198436 NM_198437
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)	AURKA
Alternative Splicing Gallery	ENSG00000087586
Gene Expression	AURKA [ NCBI-GEO ] AURKA [ EBI - ARRAY_EXPRESS ] AURKA [ SEEK ] AURKA [ MEM ]
Gene Expression Viewer (FireBrowse)	AURKA [ Firebrowse - Broad ]
Genevisible	Expression of AURKA in : [tissues] [cell-lines] [cancer] [perturbations]
BioGPS (Tissue expression)	6790
GTEX Portal (Tissue expression)	AURKA
Human Protein Atlas	ENSG00000087586-AURKA [pathology] [cell] [tissue]
	Protein : pattern, domain, 3D structure
UniProt/SwissProt	O14965 [function] [subcellular_location] [family_and_domains] [pathology_and_biotech] [ptm_processing] [expression] [interaction]
NextProt	O14965 [Sequence] [Exons] [Medical] [Publications]
With graphics : InterPro	O14965
Splice isoforms : SwissVar	O14965
PhosPhoSitePlus	O14965
Domaine pattern : Prosite (Expaxy)	PROTEIN_KINASE_ATP (PS00107) PROTEIN_KINASE_DOM (PS50011) PROTEIN_KINASE_ST (PS00108)
Domains : Interpro (EBI)	Aur AURKA Kinase-like_dom_sf Prot_kinase_dom Protein_kinase_ATP_BS Ser/Thr_kinase_AS
Domain families : Pfam (Sanger)	Pkinase (PF00069)
Domain families : Pfam (NCBI)	pfam00069
Domain families : Smart (EMBL)	S_TKc (SM00220)
Conserved Domain (NCBI)	AURKA
Blocks (Seattle)	AURKA
PDB (RSDB)	1MQ4 1MUO 1OL5 1OL6 1OL7 2BMC 2C6D 2C6E 2DWB 2J4Z 2J50 2NP8 2W1C 2W1D 2W1E 2W1F 2W1G 2WQE 2WTV 2WTW 2X6D 2X6E 2X81 2XNE 2XNG 2XRU 3COH 3E5A 3EFW 3FDN 3H0Y 3H0Z 3H10 3HA6 3K5U 3LAU 3M11 3MYG 3NRM 3O50 3O51 3P9J 3QBN 3R21 3R22 3UNZ 3UO4 3UO5 3UO6 3UOD 3UOH 3UOJ 3UOK 3UOL 3UP2 3UP7 3VAP 3W10 3W16 3W18 3W2C 4B0G 4BN1 4BYI 4BYJ 4C3P 4C3R 4CEG 4DEA 4DEB 4DED 4DEE 4DHF 4J8M 4J8N 4JAI 4JAJ 4JBO 4JBP 4JBQ 4O0S 4O0U 4O0W 4PRJ 4UYN 4UZD 4UZH 4ZS0 4ZTQ 4ZTR 4ZTS 5AAD 5AAE 5AAF 5AAG 5DN3 5DNR 5DOS 5DPV 5DR2 5DR6 5DR9 5DRD 5DT0 5DT3 5DT4 5EW9 5G15 5G1X 5L8J 5L8K 5L8L 5LXM 5OBJ 5OBR 5ODT 5ONE 5ORL 5ORN 5ORO 5ORP 5ORR 5ORS 5ORT 5ORV 5ORW 5ORX 5ORY 5ORZ 5OS0 5OS1 5OS2 5OS3 5OS4 5OS5 5OS6 5OSD 5OSE 5OSF 5ZAN 6C2R 6C2T 6C83 6CPE 6CPF 6CPG 6GRA 6HJJ 6HJK 6I2U 6R49 6R4A 6R4B 6R4C 6R4D
PDB Europe	1MQ4 1MUO 1OL5 1OL6 1OL7 2BMC 2C6D 2C6E 2DWB 2J4Z 2J50 2NP8 2W1C 2W1D 2W1E 2W1F 2W1G 2WQE 2WTV 2WTW 2X6D 2X6E 2X81 2XNE 2XNG 2XRU 3COH 3E5A 3EFW 3FDN 3H0Y 3H0Z 3H10 3HA6 3K5U 3LAU 3M11 3MYG 3NRM 3O50 3O51 3P9J 3QBN 3R21 3R22 3UNZ 3UO4 3UO5 3UO6 3UOD 3UOH 3UOJ 3UOK 3UOL 3UP2 3UP7 3VAP 3W10 3W16 3W18 3W2C 4B0G 4BN1 4BYI 4BYJ 4C3P 4C3R 4CEG 4DEA 4DEB 4DED 4DEE 4DHF 4J8M 4J8N 4JAI 4JAJ 4JBO 4JBP 4JBQ 4O0S 4O0U 4O0W 4PRJ 4UYN 4UZD 4UZH 4ZS0 4ZTQ 4ZTR 4ZTS 5AAD 5AAE 5AAF 5AAG 5DN3 5DNR 5DOS 5DPV 5DR2 5DR6 5DR9 5DRD 5DT0 5DT3 5DT4 5EW9 5G15 5G1X 5L8J 5L8K 5L8L 5LXM 5OBJ 5OBR 5ODT 5ONE 5ORL 5ORN 5ORO 5ORP 5ORR 5ORS 5ORT 5ORV 5ORW 5ORX 5ORY 5ORZ 5OS0 5OS1 5OS2 5OS3 5OS4 5OS5 5OS6 5OSD 5OSE 5OSF 5ZAN 6C2R 6C2T 6C83 6CPE 6CPF 6CPG 6GRA 6HJJ 6HJK 6I2U 6R49 6R4A 6R4B 6R4C 6R4D
PDB (PDBSum)	1MQ4 1MUO 1OL5 1OL6 1OL7 2BMC 2C6D 2C6E 2DWB 2J4Z 2J50 2NP8 2W1C 2W1D 2W1E 2W1F 2W1G 2WQE 2WTV 2WTW 2X6D 2X6E 2X81 2XNE 2XNG 2XRU 3COH 3E5A 3EFW 3FDN 3H0Y 3H0Z 3H10 3HA6 3K5U 3LAU 3M11 3MYG 3NRM 3O50 3O51 3P9J 3QBN 3R21 3R22 3UNZ 3UO4 3UO5 3UO6 3UOD 3UOH 3UOJ 3UOK 3UOL 3UP2 3UP7 3VAP 3W10 3W16 3W18 3W2C 4B0G 4BN1 4BYI 4BYJ 4C3P 4C3R 4CEG 4DEA 4DEB 4DED 4DEE 4DHF 4J8M 4J8N 4JAI 4JAJ 4JBO 4JBP 4JBQ 4O0S 4O0U 4O0W 4PRJ 4UYN 4UZD 4UZH 4ZS0 4ZTQ 4ZTR 4ZTS 5AAD 5AAE 5AAF 5AAG 5DN3 5DNR 5DOS 5DPV 5DR2 5DR6 5DR9 5DRD 5DT0 5DT3 5DT4 5EW9 5G15 5G1X 5L8J 5L8K 5L8L 5LXM 5OBJ 5OBR 5ODT 5ONE 5ORL 5ORN 5ORO 5ORP 5ORR 5ORS 5ORT 5ORV 5ORW 5ORX 5ORY 5ORZ 5OS0 5OS1 5OS2 5OS3 5OS4 5OS5 5OS6 5OSD 5OSE 5OSF 5ZAN 6C2R 6C2T 6C83 6CPE 6CPF 6CPG 6GRA 6HJJ 6HJK 6I2U 6R49 6R4A 6R4B 6R4C 6R4D
PDB (IMB)	1MQ4 1MUO 1OL5 1OL6 1OL7 2BMC 2C6D 2C6E 2DWB 2J4Z 2J50 2NP8 2W1C 2W1D 2W1E 2W1F 2W1G 2WQE 2WTV 2WTW 2X6D 2X6E 2X81 2XNE 2XNG 2XRU 3COH 3E5A 3EFW 3FDN 3H0Y 3H0Z 3H10 3HA6 3K5U 3LAU 3M11 3MYG 3NRM 3O50 3O51 3P9J 3QBN 3R21 3R22 3UNZ 3UO4 3UO5 3UO6 3UOD 3UOH 3UOJ 3UOK 3UOL 3UP2 3UP7 3VAP 3W10 3W16 3W18 3W2C 4B0G 4BN1 4BYI 4BYJ 4C3P 4C3R 4CEG 4DEA 4DEB 4DED 4DEE 4DHF 4J8M 4J8N 4JAI 4JAJ 4JBO 4JBP 4JBQ 4O0S 4O0U 4O0W 4PRJ 4UYN 4UZD 4UZH 4ZS0 4ZTQ 4ZTR 4ZTS 5AAD 5AAE 5AAF 5AAG 5DN3 5DNR 5DOS 5DPV 5DR2 5DR6 5DR9 5DRD 5DT0 5DT3 5DT4 5EW9 5G15 5G1X 5L8J 5L8K 5L8L 5LXM 5OBJ 5OBR 5ODT 5ONE 5ORL 5ORN 5ORO 5ORP 5ORR 5ORS 5ORT 5ORV 5ORW 5ORX 5ORY 5ORZ 5OS0 5OS1 5OS2 5OS3 5OS4 5OS5 5OS6 5OSD 5OSE 5OSF 5ZAN 6C2R 6C2T 6C83 6CPE 6CPF 6CPG 6GRA 6HJJ 6HJK 6I2U 6R49 6R4A 6R4B 6R4C 6R4D
Structural Biology KnowledgeBase	1MQ4 1MUO 1OL5 1OL6 1OL7 2BMC 2C6D 2C6E 2DWB 2J4Z 2J50 2NP8 2W1C 2W1D 2W1E 2W1F 2W1G 2WQE 2WTV 2WTW 2X6D 2X6E 2X81 2XNE 2XNG 2XRU 3COH 3E5A 3EFW 3FDN 3H0Y 3H0Z 3H10 3HA6 3K5U 3LAU 3M11 3MYG 3NRM 3O50 3O51 3P9J 3QBN 3R21 3R22 3UNZ 3UO4 3UO5 3UO6 3UOD 3UOH 3UOJ 3UOK 3UOL 3UP2 3UP7 3VAP 3W10 3W16 3W18 3W2C 4B0G 4BN1 4BYI 4BYJ 4C3P 4C3R 4CEG 4DEA 4DEB 4DED 4DEE 4DHF 4J8M 4J8N 4JAI 4JAJ 4JBO 4JBP 4JBQ 4O0S 4O0U 4O0W 4PRJ 4UYN 4UZD 4UZH 4ZS0 4ZTQ 4ZTR 4ZTS 5AAD 5AAE 5AAF 5AAG 5DN3 5DNR 5DOS 5DPV 5DR2 5DR6 5DR9 5DRD 5DT0 5DT3 5DT4 5EW9 5G15 5G1X 5L8J 5L8K 5L8L 5LXM 5OBJ 5OBR 5ODT 5ONE 5ORL 5ORN 5ORO 5ORP 5ORR 5ORS 5ORT 5ORV 5ORW 5ORX 5ORY 5ORZ 5OS0 5OS1 5OS2 5OS3 5OS4 5OS5 5OS6 5OSD 5OSE 5OSF 5ZAN 6C2R 6C2T 6C83 6CPE 6CPF 6CPG 6GRA 6HJJ 6HJK 6I2U 6R49 6R4A 6R4B 6R4C 6R4D
SCOP (Structural Classification of Proteins)	1MQ4 1MUO 1OL5 1OL6 1OL7 2BMC 2C6D 2C6E 2DWB 2J4Z 2J50 2NP8 2W1C 2W1D 2W1E 2W1F 2W1G 2WQE 2WTV 2WTW 2X6D 2X6E 2X81 2XNE 2XNG 2XRU 3COH 3E5A 3EFW 3FDN 3H0Y 3H0Z 3H10 3HA6 3K5U 3LAU 3M11 3MYG 3NRM 3O50 3O51 3P9J 3QBN 3R21 3R22 3UNZ 3UO4 3UO5 3UO6 3UOD 3UOH 3UOJ 3UOK 3UOL 3UP2 3UP7 3VAP 3W10 3W16 3W18 3W2C 4B0G 4BN1 4BYI 4BYJ 4C3P 4C3R 4CEG 4DEA 4DEB 4DED 4DEE 4DHF 4J8M 4J8N 4JAI 4JAJ 4JBO 4JBP 4JBQ 4O0S 4O0U 4O0W 4PRJ 4UYN 4UZD 4UZH 4ZS0 4ZTQ 4ZTR 4ZTS 5AAD 5AAE 5AAF 5AAG 5DN3 5DNR 5DOS 5DPV 5DR2 5DR6 5DR9 5DRD 5DT0 5DT3 5DT4 5EW9 5G15 5G1X 5L8J 5L8K 5L8L 5LXM 5OBJ 5OBR 5ODT 5ONE 5ORL 5ORN 5ORO 5ORP 5ORR 5ORS 5ORT 5ORV 5ORW 5ORX 5ORY 5ORZ 5OS0 5OS1 5OS2 5OS3 5OS4 5OS5 5OS6 5OSD 5OSE 5OSF 5ZAN 6C2R 6C2T 6C83 6CPE 6CPF 6CPG 6GRA 6HJJ 6HJK 6I2U 6R49 6R4A 6R4B 6R4C 6R4D
CATH (Classification of proteins structures)	1MQ4 1MUO 1OL5 1OL6 1OL7 2BMC 2C6D 2C6E 2DWB 2J4Z 2J50 2NP8 2W1C 2W1D 2W1E 2W1F 2W1G 2WQE 2WTV 2WTW 2X6D 2X6E 2X81 2XNE 2XNG 2XRU 3COH 3E5A 3EFW 3FDN 3H0Y 3H0Z 3H10 3HA6 3K5U 3LAU 3M11 3MYG 3NRM 3O50 3O51 3P9J 3QBN 3R21 3R22 3UNZ 3UO4 3UO5 3UO6 3UOD 3UOH 3UOJ 3UOK 3UOL 3UP2 3UP7 3VAP 3W10 3W16 3W18 3W2C 4B0G 4BN1 4BYI 4BYJ 4C3P 4C3R 4CEG 4DEA 4DEB 4DED 4DEE 4DHF 4J8M 4J8N 4JAI 4JAJ 4JBO 4JBP 4JBQ 4O0S 4O0U 4O0W 4PRJ 4UYN 4UZD 4UZH 4ZS0 4ZTQ 4ZTR 4ZTS 5AAD 5AAE 5AAF 5AAG 5DN3 5DNR 5DOS 5DPV 5DR2 5DR6 5DR9 5DRD 5DT0 5DT3 5DT4 5EW9 5G15 5G1X 5L8J 5L8K 5L8L 5LXM 5OBJ 5OBR 5ODT 5ONE 5ORL 5ORN 5ORO 5ORP 5ORR 5ORS 5ORT 5ORV 5ORW 5ORX 5ORY 5ORZ 5OS0 5OS1 5OS2 5OS3 5OS4 5OS5 5OS6 5OSD 5OSE 5OSF 5ZAN 6C2R 6C2T 6C83 6CPE 6CPF 6CPG 6GRA 6HJJ 6HJK 6I2U 6R49 6R4A 6R4B 6R4C 6R4D
Superfamily	O14965
Human Protein Atlas [tissue]	ENSG00000087586-AURKA [tissue]
Peptide Atlas	O14965
HPRD	04066
IPI	IPI00298940 IPI00790518 IPI00646206 IPI00640695 IPI00641685 IPI00646759 IPI00796387
	Protein Interaction databases
DIP (DOE-UCLA)	O14965
IntAct (EBI)	O14965
BioGRID	AURKA
STRING (EMBL)	AURKA
ZODIAC	AURKA
	Ontologies - Pathways
QuickGO	O14965
Ontology : AmiGO	G2/M transition of mitotic cell cycle mitotic cell cycle condensed nuclear chromosome, centromeric region protein kinase activity protein serine/threonine kinase activity protein serine/threonine kinase activity protein serine/threonine kinase activity protein serine/threonine/tyrosine kinase activity protein binding ATP binding nucleus nucleoplasm nucleoplasm centrosome centrosome centriole spindle cytosol cytosol spindle microtubule cilium protein phosphorylation ubiquitin-dependent protein catabolic process DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest spindle organization mitotic spindle organization spindle assembly involved in female meiosis I mitotic centrosome separation response to wounding anterior/posterior axis specification regulation of G2/M transition of mitotic cell cycle negative regulation of gene expression negative regulation of G2/M transition of mitotic cell cycle microtubule cytoskeleton peptidyl-serine phosphorylation protein kinase binding midbody anaphase-promoting complex-dependent catabolic process spindle pole centrosome spindle pole centrosome ubiquitin protein ligase binding regulation of protein stability negative regulation of protein binding chromosome passenger complex positive regulation of proteasomal ubiquitin-dependent protein catabolic process regulation of cytokinesis histone serine kinase activity histone-serine phosphorylation germinal vesicle negative regulation of apoptotic process axon hillock pronucleus positive regulation of mitotic nuclear division regulation of centrosome cycle protein autophosphorylation protein heterodimerization activity perinuclear region of cytoplasm spindle midzone cell division centrosome localization protein localization to centrosome meiotic spindle liver regeneration mitotic spindle pole positive regulation of oocyte maturation regulation of signal transduction by p53 class mediator neuron projection extension
Ontology : EGO-EBI	G2/M transition of mitotic cell cycle mitotic cell cycle condensed nuclear chromosome, centromeric region protein kinase activity protein serine/threonine kinase activity protein serine/threonine kinase activity protein serine/threonine kinase activity protein serine/threonine/tyrosine kinase activity protein binding ATP binding nucleus nucleoplasm nucleoplasm centrosome centrosome centriole spindle cytosol cytosol spindle microtubule cilium protein phosphorylation ubiquitin-dependent protein catabolic process DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest spindle organization mitotic spindle organization spindle assembly involved in female meiosis I mitotic centrosome separation response to wounding anterior/posterior axis specification regulation of G2/M transition of mitotic cell cycle negative regulation of gene expression negative regulation of G2/M transition of mitotic cell cycle microtubule cytoskeleton peptidyl-serine phosphorylation protein kinase binding midbody anaphase-promoting complex-dependent catabolic process spindle pole centrosome spindle pole centrosome ubiquitin protein ligase binding regulation of protein stability negative regulation of protein binding chromosome passenger complex positive regulation of proteasomal ubiquitin-dependent protein catabolic process regulation of cytokinesis histone serine kinase activity histone-serine phosphorylation germinal vesicle negative regulation of apoptotic process axon hillock pronucleus positive regulation of mitotic nuclear division regulation of centrosome cycle protein autophosphorylation protein heterodimerization activity perinuclear region of cytoplasm spindle midzone cell division centrosome localization protein localization to centrosome meiotic spindle liver regeneration mitotic spindle pole positive regulation of oocyte maturation regulation of signal transduction by p53 class mediator neuron projection extension
Pathways : KEGG	Oocyte meiosis
NDEx Network	AURKA
Atlas of Cancer Signalling Network	AURKA
Wikipedia pathways	AURKA
	Orthology - Evolution
OrthoDB	6790
GeneTree (enSembl)	ENSG00000087586
Phylogenetic Trees/Animal Genes : TreeFam	AURKA
HOGENOM	O14965
Homologs : HomoloGene	AURKA
Homology/Alignments : Family Browser (UCSC)	AURKA
	Gene fusions - Rearrangements
Fusion : Mitelman	AURKA/PCK1 [20q13.2/20q13.31]
Fusion : Mitelman	BCAS4/AURKA [20q13.13/20q13.2]
Fusion Portal	AURKA 20q13.2 PCK1 20q13.31 BRCA
Fusion : Fusion_Hub	AURKA--AL034429.1 AURKA--ARHGEF7 AURKA--BACH2 AURKA--BCAS4 AURKA--FLI1 AURKA--LOC401588 AURKA--PCK1 AURKA--RAB3GAP2 AURKA--SAR1B AURKA--SOGA1 AURKA--SP1 BCAS4--AURKA SARS--AURKA
Fusion : Quiver	AURKA
	Polymorphisms : SNP and Copy number variants
NCBI Variation Viewer	AURKA [hg38]
dbVar	AURKA
ClinVar	AURKA
Monarch	AURKA
1000_Genomes	AURKA
Exome Variant Server	AURKA
GNOMAD Browser	ENSG00000087586
Varsome Browser	AURKA
Genomic Variants (DGV)	AURKA [DGVbeta]
DECIPHER	AURKA [patients] [syndromes] [variants] [genes]
CONAN: Copy Number Analysis	AURKA
	Mutations
ICGC Data Portal	AURKA
TCGA Data Portal	AURKA
Broad Tumor Portal	AURKA
OASIS Portal	AURKA [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMIC	AURKA [overview] [genome browser] [tissue] [distribution]
Somatic Mutations in Cancer : COSMIC3D	AURKA
Mutations and Diseases : HGMD	AURKA
LOVD (Leiden Open Variation Database)	Whole genome datasets
LOVD (Leiden Open Variation Database)	LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)	LOVD 3.0 shared installation
BioMuta	search AURKA
DgiDB (Drug Gene Interaction Database)	AURKA
DoCM (Curated mutations)	AURKA (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)	AURKA (select a term)
intoGen	AURKA
OncoKB	AURKA
NCG6 (London)	select AURKA
Cancer3D	AURKA(select the gene name)
Impact of mutations	[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
	Diseases
OMIM	114500 603072
Orphanet
DisGeNET	AURKA
Medgen	AURKA
Genetic Testing Registry	AURKA
NextProt	O14965 [Medical]
GENETests	AURKA
Target Validation	AURKA
Huge Navigator	AURKA [HugePedia]
ClinGen	AURKA
	Clinical trials, drugs, therapy
MyCancerGenome	AURKA
Protein Interactions : CTD
Pharm GKB Gene	PA36201
Pharos	O14965
Clinical trial	AURKA
	Miscellaneous
canSAR (ICR)	AURKA (select the gene name)
Harmonizome	AURKA
DataMed Index	AURKA
	Probes
	Litterature
PubMed	499 Pubmed reference(s) in Entrez
GeneRIFs	Gene References Into Functions (Entrez)
EVEX	AURKA

REVIEW articles	automatic search in PubMed
Last year publications	automatic search in PubMed

Search in all EBI NCBI

indexed on : Fri Jan 1 18:47:00 CET 2021

Home Genes Leukemias Solid Tumors Cancer-Prone Deep Insight Case Reports Journals Portal Teaching

For comments and suggestions or contributions, please contact us

jlhuret@AtlasGeneticsOncology.org.