Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0000204
UniProt IDO14965
Primary gene name(s)AURKA
Synonym gene name(s)AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6
Protein nameAurora kinase A
Protein functionMitotic serine/threonine kinase that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1, PP1 isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. {ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14523000, ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:14990569, ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15147269, ECO:0000269|PubMed:15987997, ECO:0000269|PubMed:17125279, ECO:0000269|PubMed:17360485, ECO:0000269|PubMed:17604723, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19357306, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:19812038, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:9606188}.
Subcellular locationCytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12576638, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19357306, ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:9153231}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:9153231, ECO:0000269|PubMed:9606188}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P97477}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P97477}. Note=Detected at the neurite hillock in developing neurons, By similarity. Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase, PubMed:9606188, PubMed:17229885, PubMed:21225229. Colocalized with SIRT2 at centrosome, PubMed:22014574. Moves to the midbody during both telophase and cytokinesis, PubMed:17726514. Associates with both the pericentriolar material, PCM and centrioles, PubMed:22014574. {ECO:0000250|UniProtKB:P97477, ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:9606188}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: O14965
Gene Ontology
(Biological Process)
Complete annatation
anaphase-promoting complex-dependent catabolic process [GO:0031145];
anterior/posterior axis specification [GO:0009948];
cell division [GO:0051301];
centrosome localization [GO:0051642];
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977];
G2/M transition of mitotic cell cycle [GO:0000086];
liver regeneration [GO:0097421];
meiotic spindle organization [GO:0000212];
mitotic centrosome separation [GO:0007100];
mitotic nuclear division [GO:0007067];
mitotic spindle organization [GO:0007052];
negative regulation of apoptotic process [GO:0043066];
negative regulation of protein binding [GO:0032091];
neuron projection extension [GO:1990138];
positive regulation of mitotic nuclear division [GO:0045840];
positive regulation of oocyte maturation [GO:1900195];
positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436];
protein autophosphorylation [GO:0046777];
protein localization to centrosome [GO:0071539];
protein phosphorylation [GO:0006468];
protein ubiquitination involved in ubiquitin-dependent protein catabolic process [GO:0042787];
regulation of centrosome cycle [GO:0046605];
regulation of cytokinesis [GO:0032465];
regulation of protein stability [GO:0031647];
regulation of signal transduction by p53 class mediator [GO:1901796];
response to wounding [GO:0009611];
spindle assembly involved in female meiosis I [GO:0007057];
spindle organization [GO:0007051]
Gene Ontology
(Molecular Function)
Complete annatation
ATP binding [GO:0005524];
histone serine kinase activity [GO:0035174];
protein kinase activity [GO:0004672];
protein kinase binding [GO:0019901];
protein serine/threonine/tyrosine kinase activity [GO:0004712];
protein serine/threonine kinase activity [GO:0004674]
Gene Ontology
(Cellular Component)
Complete annatation
axon hillock [GO:0043203];
centriole [GO:0005814];
centrosome [GO:0005813];
chromosome passenger complex [GO:0032133];
cilium [GO:0005929];
condensed nuclear chromosome, centromeric region [GO:0000780];
cytosol [GO:0005829];
germinal vesicle [GO:0042585];
meiotic spindle [GO:0072687];
microtubule [GO:0005874];
microtubule cytoskeleton [GO:0015630];
midbody [GO:0030496];
mitotic spindle [GO:0072686];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
perinuclear region of cytoplasm [GO:0048471];
pronucleus [GO:0045120];
spindle [GO:0005819];
spindle midzone [GO:0051233];
spindle pole centrosome [GO:0031616]
Protein-protein interaction112666
Phylogenetic treeO14965
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
      unknown
Brass et al., Science, 2008
      unknown
Smith et al., J. Immunol, 2010
      unknown
Interferon-stimulated
gene status
Lu et al., J. Virol., 2011
      Folds changes 8h: unknown; Folds changes 16h: unknown; Tested: unknown;
Schoggins JW and Rice CM, Curr. Opin. Virol., 2011
      Targeted viruses: unknown
      Viral life cycle: unknown
      Mechanism related to antiviral activity: unknown
Anti-viral restriction factor Liu et al., Retrovirology, 2011
      unknown (Triplicates)

Gene Expression Profile       top

            Up-regulated;            Down-regulated

For brief introduction to each study, please go to the help page.

Gene expression during HIV latency

(1). Mohammadi et al., PLoS Pathog., 2014

Differentially expressed transcripts (Pairwise) during latency and subsequent viral reactivation using several agents - Primary CD4+ T-cell based model


DMSO: Dimethyl suloxyde (negative control) - 0.0033% final
SAHA: Vorinostat (Histone deacetylase inhibitor) - 0.5 μM
CD3: TCR Stimulation by IL-2+ antiCD3/anti-CD28 antibodies
IL7: Interleukin-7 based stimulation
DISU: Disulfiram (alcohol dehydrogenase inhibitor) - 0.5 μM
AZA: 5-azacytidine (AZA; DNA methylation inhibitor) - 1 μM
Experimental Condition Log2 Fold Change P value Adjusted P value
AZA vs. CD31.22053109823710.04947855773789740.0990096683783312
AZA vs. DISU0.2368175981417670.6284637200112120.960057478314726
AZA vs. IL7-0.09554647607146150.8508774474337240.999311006273513
AZA vs. SAHA-0.4661701926005310.2623224044567550.634527912638371
DISU vs. CD3-0.9956165210033860.08317495921445170.161465464932214
DISU vs. IL7-0.342199939193090.4471959715534210.794517297721605
DISU vs. SAHA-0.700771669475710.0352609201587960.228370145128154
DMSO vs. AZA-0.09281171357715250.8604583316275111
DMSO vs. CD3-1.326143741970680.02926081512210650.0615476504038117
DMSO vs. DISU-0.3325691522548230.4783503732323060.900624300571113
DMSO vs. IL70.005168831925046910.9915766057439640.998922198828488
DMSO vs. SAHA-0.3790815217853860.3289362827450850.682743247107998
HIV vs. Mock in Activation0.1368939257336350.9033331658846470.999983755607037
HIV vs. Mock in Latency0.138683583060960.682336595767420.999834320637052
IL7 vs. CD3-1.309122921261190.0292469896857510.0712641247224903
SAHA vs. CD3-1.709905225381210.001481137404158890.00501702420334334
SAHA vs. IL7-0.3716807364102050.3105381577638610.559532893871915
(2). Iglesias-Ussel et al., J. Virol., 2013

Up and Downregulated transcripts during Latency (Latently infected CD4+ T cells vs Uninfected)- Primary CD4+Tcell based model
Log2 Fold Change P Value
unknown unknown

Gene expression during HIV infection and replication

(1). Imbeault et al., PloS Pathog., 2012

Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells
Experiment type Log2 Fold Change P Value Adjusted P Value
Infected vs. Mock unknown unknown unknown
Infected vs. Bystander unknown unknown unknown
(2). Lefebvre et al., J. Virol., 2011

Transcriptome analysis of T-cell line (Sup T1)
Log2 Fold Change unknown
(3). Li et al., J. Immunol., 2013

Lymphatic tissue
Acute Fold Change Acute P Value Asymt Fold Change Asypt P Value AIDS Fold Change AIDS P Value
1.9 0.000823814 1.3 0.073864404 1.5 0.131982827
(4). Chang et al., MBio., 2011

Transcriptome analysis of T-cell line (Sup T1)

Derived from Sherrill-Mix et al., BMC Retrovirol., 2015 cross validation
Up-regulated (True) FALSE
(5). Sherrill-Mix et al., BMC Retrovirol., 2015

Deep RNA-seq analysis of primary human T cell infected with low passage HIV isolate HIV89.6 - Primary CD4+ T cell based
Test Status Log2 Fold Change P Value
OK 0.344926 0.00639837
(6). Rotger et al., PLoS Pathog., 2010

Genome-wide mRNA expression of CD4+ T cells from HIV-infected patient
(Genes differentially expressed (at adjusted p<0.01) according to the empirical Bayes approach)
Log2 Fold Change P Value
0.025 0.004

Proteomic/Transcriptomics studies indicating differentially expressed genes mediated by HIV

(1). Greenwood et al., Elife, 2016

Activated (CD3/CD28) Primary human CD4+ T cells infected with pNL4-3-dE-EGFP. The table shows the complete (unfiltered) TMT (tandem mass tag)-based proteomic time course dataset
6 h 24 h 48 h 72 h RTi
1.121 1.727 2.304 2.303 1.349
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
unknown unknown unknown unknown unknown unknown unknown
(3). Hyrcza et al., J. Virolo., 2007

Primary human CD4+ and CD8+ T Cells
Affymetrix Prob ID Fold Change In CD8? Category
208079_s_at 4.92 No upregulated in CD8+ cells

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

Drugbank ID Drug Name Drug Status Pharmacological Action Drug Action
DB02482 Phosphonothreonine experimental unknown unknown
DB05220 MLN8237 investigational unknown unknown
DB05198 CYC116 investigational unknown unknown
DB05169 AT9283 investigational unknown unknown
DB07186 4-(4-METHYLPIPERAZIN-1-YL)-N-[5-(2-THIENYLACETYL)-1,5-DIHYDROPYRROLO[3,4-C]PYRAZOL-3-YL]BENZAMIDE experimental unknown unknown
DB07266 8-ethyl-3,10,10-trimethyl-4,5,6,8,10,12-hexahydropyrazolo[4&,39;,3&,39;:6,7]cyclohepta[1,2-b]pyrrolo[2,3-f]indol-9(1H)-one experimental unknown unknown
DB07360 1-{5-[2-(thieno[3,2-d]pyrimidin-4-ylamino)ethyl]-1,3-thiazol-2-yl}-3-[3-(trifluoromethyl)phenyl]urea experimental unknown unknown
DB07361 1-(3-chlorophenyl)-3-{5-[2-(thieno[3,2-d]pyrimidin-4-ylamino)ethyl]-1,3-thiazol-2-yl}urea experimental unknown unknown
DB07362 1-(5-{2-[(1-methyl-1H-pyrazolo[4,3-d]pyrimidin-7-yl)amino]ethyl}-1,3-thiazol-2-yl)-3-[3-(trifluoromethyl)phenyl]urea experimental unknown unknown
DB07545 N-{3-[(4-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-2-YL)AMINO]PHENYL}CYCLOPROPANECARBOXAMIDE experimental unknown unknown
DB07801 N-butyl-3-{[6-(9H-purin-6-ylamino)hexanoyl]amino}benzamide experimental unknown unknown
DB08065 2-(1H-pyrazol-3-yl)-1H-benzimidazole experimental unknown unknown
DB08066 N-[3-(1H-BENZIMIDAZOL-2-YL)-1H-PYRAZOL-4-YL]BENZAMIDE experimental unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1MQ4 X-ray 1.9Å A=125-391.
1MUO X-ray 2.9Å A=107-403.
1OL5 X-ray 2.5Å A=122-403.
1OL6 X-ray 3.0Å A=122-403.
1OL7 X-ray 2.7Å A=122-403.
2BMC X-ray 2.6Å A/B/C/D/E/F=100-403.
2C6D X-ray 2.2Å A=124-398.
2C6E X-ray 2.1Å A/B=123-401.
2DWB X-ray 2.5Å A=122-403.
2J4Z X-ray 2.0Å A/B=100-403.
2J50 X-ray 3.0Å A/B=126-403.
2NP8 X-ray 2.2Å A=125-391.
2W1C X-ray 3.2Å A=122-389.
2W1D X-ray 2.9Å A=122-389.
2W1E X-ray 2.9Å A=122-389.
2W1F X-ray 2.8Å A=122-389.
2W1G X-ray 2.7Å A=122-389.
2WQE X-ray 2.5Å A=127-388.
2WTV X-ray 2.4Å A/B/C/D=122-403.
2WTW X-ray 3.3Å A=122-403.
2X6D X-ray 2.8Å A=122-403.
2X6E X-ray 3.3Å A=122-403.
2X81 X-ray 2.9Å A=126-391.
2XNE X-ray 2.8Å A=122-392.
2XNG X-ray 2.6Å A=122-403.
2XRU X-ray 2.9Å A=126-403.
3COH X-ray 2.7Å A/B=124-391.
3E5A X-ray 2.3Å A=125-391.
3EFW X-ray 2.2Å A/B=125-391.
3FDN X-ray 1.9Å A=123-401.
3H0Y X-ray 2.5Å A=124-391.
3H0Z X-ray 2.9Å A/B/C=124-391.
3H10 X-ray 2.2Å A/B/D=124-391.
3HA6 X-ray 2.3Å A=125-391.
3K5U X-ray 2.3Å A=123-401.
3LAU X-ray 2.1Å A=125-399.
3M11 X-ray 2.7Å A=123-401.
3MYG X-ray 2.4Å A=125-391.
3NRM X-ray 3.0Å A=126-403.
3O50 X-ray 2.0Å A/B=125-391.
3O51 X-ray 3.2Å A=125-391.
3P9J X-ray 2.8Å A=125-391.
3QBN X-ray 3.5Å A=124-403.
3R21 X-ray 2.9Å A=126-391.
3R22 X-ray 2.9Å A=126-391.
3UNZ X-ray 2.8Å A/B=123-401.
3UO4 X-ray 2.4Å A=123-401.
3UO5 X-ray 2.7Å A=123-401.
3UO6 X-ray 2.8Å A/B=123-401.
3UOD X-ray 2.5Å A=123-401.
3UOH X-ray 2.8Å A/B=123-401.
3UOJ X-ray 2.9Å A/B=123-401.
3UOK X-ray 2.9Å A/B=123-401.
3UOL X-ray 2.4Å A/B=123-401.
3UP2 X-ray 2.3Å A=123-401.
3UP7 X-ray 3.0Å A=123-401.
3VAP X-ray 2.6Å A=125-391.
3W10 X-ray 2.7Å A=126-403.
3W16 X-ray 2.8Å A=126-403.
3W18 X-ray 2.5Å A/B=126-403.
3W2C X-ray 2.4Å A/C/E/G=128-388.
4B0G X-ray 2.5Å A=122-403.
4BN1 X-ray 2.5Å A=122-403.
4BYI X-ray 2.6Å A=122-403.
4BYJ X-ray 2.7Å A=122-403.
4C3P X-ray 2.6Å A/D=122-403.
4C3R X-ray 2.7Å A=122-403.
4CEG X-ray 2.1Å A=122-403.
4DEA X-ray 2.4Å A=123-401.
4DEB X-ray 3.0Å A=123-401.
4DED X-ray 3.0Å A=123-401.
4DEE X-ray 2.3Å A=123-401.
4DHF X-ray 2.8Å A/B=126-391.
4J8M X-ray 1.8Å A=123-401.
4J8N X-ray 3.1Å A/B/C/D=123-401.
4JAI X-ray 3.2Å A=122-396.
4JAJ X-ray 2.7Å A=122-396.
4JBO X-ray 2.4Å A=123-401.
4JBP X-ray 2.4Å A=123-401.
4JBQ X-ray 2.3Å A=123-401.
4O0S X-ray 2.5Å A=122-403.
4O0U X-ray 2.6Å A=122-403.
4O0W X-ray 2.6Å A=122-403.
4PRJ X-ray 2.8Å A=124-391.
4UTD X-ray 2.3Å A=122-403.
4UYN X-ray 1.9Å A=125-399.
4UZD X-ray 3.2Å A/B=125-399.
4UZH X-ray 2.0Å A=125-399.
4ZS0 X-ray 3.0Å A=122-403.
4ZTQ X-ray 2.8Å A=122-403.
4ZTR X-ray 2.8Å A=122-403.
4ZTS X-ray 2.9Å A=122-403.
5AAD X-ray 3.1Å A=122-403.
5AAE X-ray 3.1Å A=122-403.
5AAF X-ray 2.7Å A=122-403.
5AAG X-ray 2.8Å A=122-403.
5DN3 X-ray 2.0Å A=125-391.
5DNR X-ray 1.9Å A=125-391.
5DOS X-ray 2.9Å A=126-390.
5DPV X-ray 2.2Å A=126-390.
5DR2 X-ray 2.4Å A=128-390.
5DR6 X-ray 2.5Å A=126-390.
5DR9 X-ray 2.4Å A=126-390.
5DRD X-ray 2.1Å A=126-390.
5DT0 X-ray 2.1Å A=126-390.
5DT3 X-ray 2.3Å A=126-390.
5DT4 X-ray 2.8Å A=126-390.
5EW9 X-ray 2.1Å A=123-390.
5L8J X-ray 1.6Å A=122-403.
5L8K X-ray 1.7Å A=122-403.
5L8L X-ray 1.6Å A=122-403.

HIV-1 Interaction       (annotations from NCBI HIV-1 Interaction Database)      top

HIV Partner Interaction Type PubMed
Vpu binds 23047923

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04114 Oocyte meiosis - Homo sapiens (human)
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