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UniProtKB - O14965 (AURKA_HUMAN)

Entry version 216 (10 Apr 2019)
Sequence version 2 (27 Jan 2003)
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Protein

Aurora kinase A

Gene

AURKA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Mitotic 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 normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426). 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.22 Publications

Miscellaneous

Centrosome amplification can occur when the cycles are uncoupled, and this amplification is associated with cancer and with an increase in the levels of chromosomal instability.

Caution

Authors initially considered AURKA/STK6 and STK15 as 2 different proteins (PubMed:9771714). It is clear that they are the same protein.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activation of CDK1, appears to be an upstream event of AURKA activation. Phosphatase inhibitor-2 (PPP1R2) and TPX2 act also as activators. Inactivated by the G2 checkpoint. Inhibited by GADD45A and p53/TP53, and through dephosphorylation by protein phosphatase type 1 (PP1). MLN8054 is also a potent and selective inhibitor. Activated during the early phase of cilia disassembly in the presence of PIFO.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei143ATP; via amide nitrogenCombined sources1 Publication1
Binding sitei162ATPCombined sources1 Publication1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei256Proton acceptorPROSITE-ProRule annotation1 Publication1
Binding sitei274ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi211 – 213ATPCombined sources1 Publication3
Nucleotide bindingi260 – 261ATPCombined sources1 Publication2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Cilium biogenesis/degradation, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-6804114 TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8854518 AURKA Activation by TPX2
R-HSA-8854521 Interaction between PHLDA1 and AURKA

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		O14965

SIGNOR Signaling Network Open Resource

More...SIGNORi		O14965

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Aurora kinase A (EC:2.7.11.11 Publication)
Alternative name(s):
Aurora 2
Aurora/IPL1-related kinase 1
Short name:
ARK-1
Short name:
Aurora-related kinase 1
Short name:
hARK1
Breast tumor-amplified kinase
Serine/threonine-protein kinase 15
Serine/threonine-protein kinase 6
Serine/threonine-protein kinase aurora-A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AURKA
Synonyms:AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000087586.17

Human Gene Nomenclature Database

More...HGNCi		HGNC:11393 AURKA

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603072 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O14965

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Microtubule

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi162K → R: Loss of kinase activity. 2 Publications1
Mutagenesisi165F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication1
Mutagenesisi198G → N: Reduces interaction with TPX2. Reduces kinase activity tenfold. Promotes interaction with the AURKB binding partners INCENP and BIRC5 that are normally not bound by AURKA. 1 Publication1
Mutagenesisi205R → A: Reduces ubiquitination and proteasomal degradation. 1 Publication1
Mutagenesisi274D → N: Abolishes autophosphorylation. 1 Publication1
Mutagenesisi287T → A: No direct effect on catalytic activity. 1 Publication1
Mutagenesisi287T → E: Enhances interaction with TPX2. 1 Publication1
Mutagenesisi288T → D: Mimics phosphorylation state and increases kinase activity. 1 Publication1
Mutagenesisi290C → A: Enhances stability; when associated with A-393. 1 Publication1
Mutagenesisi334Y → A: Reduces binding to MYCN. 1 Publication1
Mutagenesisi335Q → A: Reduces binding to MYCN. 1 Publication1
Mutagenesisi346F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication1
Mutagenesisi393C → A: Enhances stability; when associated with A-290. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		6790

MalaCards human disease database

More...MalaCardsi		AURKA

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA36201

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4722

Drug and drug target database

More...DrugBanki		DB08065 2-(1H-pyrazol-3-yl)-1H-benzimidazole
DB05169 AT9283
DB05198 CYC116
DB05220 MLN8237
DB08066 N-[3-(1H-BENZIMIDAZOL-2-YL)-1H-PYRAZOL-4-YL]BENZAMIDE
DB07801 N-butyl-3-{[6-(9H-purin-6-ylamino)hexanoyl]amino}benzamide
DB07545 N-{3-[(4-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-2-YL)AMINO]PHENYL}CYCLOPROPANECARBOXAMIDE
DB02482 Phosphonothreonine

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1936

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		AURKA

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000866921 – 403Aurora kinase AAdd BLAST403

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei41PhosphoserineCombined sources1
Modified residuei51Phosphoserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei287Phosphothreonine2 Publications1
Modified residuei288Phosphothreonine7 Publications1
Modified residuei342Phosphoserine; by PKA and PAK1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-288 upon TPX2 binding. Thr-288 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis. Phosphorylation at Ser-342 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis.10 Publications
Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome. Ubiquitinated by CHFR, leading to its degradation by the proteasome (By similarity). Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome.By similarity2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O14965

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O14965

MaxQB - The MaxQuant DataBase

More...MaxQBi		O14965

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		O14965

PeptideAtlas

More...PeptideAtlasi		O14965

PRoteomics IDEntifications database

More...PRIDEi		O14965

ProteomicsDB human proteome resource

More...ProteomicsDBi		48339

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O14965

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		O14965

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in testis and weakly in skeletal muscle, thymus and spleen. Also highly expressed in colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is cell-cycle regulated, low in G1/S, accumulates during G2/M, and decreases rapidly after.5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000087586 Expressed in 175 organ(s), highest expression level in oocyte

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O14965 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O14965 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB001454
HPA002636

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with FBXL7 (By similarity). Interacts with CPEB1, JTB, TACC1, TPX2, PPP2CA, as well as with the protein phosphatase type 1 (PP1) isoforms PPP1CA, PPP1CB and PPP1CC. Interacts also with its substrates ARHGEF2, BORA, BRCA1, KIF2A, PARD3, and p53/TP53. Interaction with BORA promotes phosphorylation of PLK1. Interacts with PIFO. Interacts with GADD45A, competing with its oligomerization. Interacts (via C-terminus) with AUNIP (via C-terminus). Identified in a complex with AUNIP and NIN. Interacts with FRY; this interaction facilitates AURKA-mediated PLK1 phosphorylation. Interacts with SIRT2 (PubMed:17726514, PubMed:22014574). Interacts with MYCN; interaction is phospho-independent and triggers AURKA activation; AURKA competes with FBXW7 for binding to unphosphorylated MYCN but not for binding to phosphorylated MYCN (PubMed:27837025). Interacts with HNRNPU (PubMed:21242313, PubMed:25986610).By similarity29 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		112666, 374 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O14965

Database of interacting proteins

More...DIPi		DIP-33068N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		O14965

Protein interaction database and analysis system

More...IntActi		O14965, 122 interactors

Molecular INTeraction database

More...MINTi		O14965

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000216911

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O14965

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1403
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MQ4X-ray1.90A125-391[»]
1MUOX-ray2.90A107-403[»]
1OL5X-ray2.50A122-403[»]
1OL6X-ray3.00A122-403[»]
1OL7X-ray2.75A122-403[»]
2BMCX-ray2.60A/B/C/D/E/F100-403[»]
2C6DX-ray2.20A124-398[»]
2C6EX-ray2.10A/B123-401[»]
2DWBX-ray2.50A122-403[»]
2J4ZX-ray2.00A/B100-403[»]
2J50X-ray3.00A/B126-403[»]
2NP8X-ray2.25A125-391[»]
2W1CX-ray3.24A122-389[»]
2W1DX-ray2.97A122-389[»]
2W1EX-ray2.93A122-389[»]
2W1FX-ray2.85A122-389[»]
2W1GX-ray2.71A122-389[»]
2WQEX-ray2.50A127-388[»]
2WTVX-ray2.40A/B/C/D122-403[»]
2WTWX-ray3.30A122-403[»]
2X6DX-ray2.80A122-403[»]
2X6EX-ray3.35A122-403[»]
2X81X-ray2.91A126-391[»]
2XNEX-ray2.80A122-392[»]
2XNGX-ray2.60A122-403[»]
2XRUX-ray2.90A126-403[»]
3COHX-ray2.70A/B124-391[»]
3E5AX-ray2.30A125-391[»]
3EFWX-ray2.29A/B125-391[»]
3FDNX-ray1.90A123-401[»]
3H0YX-ray2.50A124-391[»]
3H0ZX-ray2.92A/B/C124-391[»]
3H10X-ray2.20A/B/D124-391[»]
3HA6X-ray2.36A125-391[»]
3K5UX-ray2.35A123-401[»]
3LAUX-ray2.10A125-399[»]
3M11X-ray2.75A123-401[»]
3MYGX-ray2.40A125-391[»]
3NRMX-ray3.05A126-403[»]
3O50X-ray2.00A/B125-391[»]
3O51X-ray3.20A125-391[»]
3P9JX-ray2.80A125-391[»]
3QBNX-ray3.50A124-403[»]
3R21X-ray2.90A126-391[»]
3R22X-ray2.90A126-391[»]
3UNZX-ray2.80A/B123-401[»]
3UO4X-ray2.45A123-401[»]
3UO5X-ray2.70A123-401[»]
3UO6X-ray2.80A/B123-401[»]
3UODX-ray2.50A123-401[»]
3UOHX-ray2.80A/B123-401[»]
3UOJX-ray2.90A/B123-401[»]
3UOKX-ray2.95A/B123-401[»]
3UOLX-ray2.40A/B123-401[»]
3UP2X-ray2.30A123-401[»]
3UP7X-ray3.05A123-401[»]
3VAPX-ray2.66A125-391[»]
3W10X-ray2.70A126-403[»]
3W16X-ray2.80A126-403[»]
3W18X-ray2.50A/B126-403[»]
3W2CX-ray2.45A/C/E/G128-388[»]
4B0GX-ray2.50A122-403[»]
4BN1X-ray2.50A122-403[»]
4BYIX-ray2.60A122-403[»]
4BYJX-ray2.75A122-403[»]
4C3PX-ray2.69A/D122-403[»]
4C3RX-ray2.79A122-403[»]
4CEGX-ray2.10A122-403[»]
4DEAX-ray2.45A123-401[»]
4DEBX-ray3.05A123-401[»]
4DEDX-ray3.05A123-401[»]
4DEEX-ray2.30A123-401[»]
4DHFX-ray2.80A/B126-391[»]
4J8MX-ray1.85A123-401[»]
4J8NX-ray3.14A/B/C/D123-401[»]
4JAIX-ray3.20A122-396[»]
4JAJX-ray2.70A122-396[»]
4JBOX-ray2.49A123-401[»]
4JBPX-ray2.45A123-401[»]
4JBQX-ray2.30A123-401[»]
4O0SX-ray2.50A122-403[»]
4O0UX-ray2.60A122-403[»]
4O0WX-ray2.60A122-403[»]
4PRJX-ray2.80A124-391[»]
4UYNX-ray1.90A125-399[»]
4UZDX-ray3.20A/B125-399[»]
4UZHX-ray2.00A125-399[»]
4ZS0X-ray3.00A122-403[»]
4ZTQX-ray2.80A122-403[»]
4ZTRX-ray2.85A122-403[»]
4ZTSX-ray2.90A122-403[»]
5AADX-ray3.10A122-403[»]
5AAEX-ray3.11A122-403[»]
5AAFX-ray2.78A122-403[»]
5AAGX-ray2.85A122-403[»]
5DN3X-ray2.05A125-391[»]
5DNRX-ray1.95A125-391[»]
5DOSX-ray2.98A126-390[»]
5DPVX-ray2.29A126-390[»]
5DR2X-ray2.46A128-390[»]
5DR6X-ray2.53A126-390[»]
5DR9X-ray2.47A126-390[»]
5DRDX-ray2.13A126-390[»]
5DT0X-ray2.15A126-390[»]
5DT3X-ray2.33A126-390[»]
5DT4X-ray2.86A126-390[»]
5EW9X-ray2.18A123-390[»]
5G15X-ray2.06A122-403[»]
5G1XX-ray1.72A122-403[»]
5L8JX-ray1.68A122-403[»]
5L8KX-ray1.79A122-403[»]
5L8LX-ray1.67A122-403[»]
5LXMX-ray2.08A122-403[»]
5OBJX-ray2.90A125-391[»]
5OBRX-ray2.62A125-391[»]
5ODTX-ray2.02A122-403[»]
5ONEX-ray2.60A122-403[»]
5ORLX-ray1.69A127-391[»]
5ORNX-ray2.19A127-391[»]
5OROX-ray2.12A127-391[»]
5ORPX-ray2.19A127-391[»]
5ORRX-ray2.09A127-391[»]
5ORSX-ray1.98A127-391[»]
5ORTX-ray2.56A127-391[»]
5ORVX-ray1.88A127-391[»]
5ORWX-ray2.00A127-391[»]
5ORXX-ray1.88A127-391[»]
5ORYX-ray1.99A127-391[»]
5ORZX-ray1.92A127-391[»]
5OS0X-ray1.74A127-391[»]
5OS1X-ray1.90A127-391[»]
5OS2X-ray1.92A127-391[»]
5OS3X-ray1.81A127-391[»]
5OS4X-ray1.88A127-391[»]
5OS5X-ray1.74A125-392[»]
5OS6X-ray2.20A127-391[»]
5OSDX-ray1.99A125-391[»]
5OSEX-ray1.90A127-391[»]
5OSFX-ray1.89A127-391[»]
6C2RX-ray1.96A125-391[»]
6C2TX-ray1.73A125-391[»]
6CPEX-ray2.45A122-403[»]
6CPFX-ray2.30A122-403[»]
6CPGX-ray2.80A/D122-403[»]
6HJJX-ray2.13A122-403[»]
6HJKX-ray2.40A122-403[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		O14965

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		O14965

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O14965

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini133 – 383Protein kinasePROSITE-ProRule annotationAdd BLAST251

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni280 – 293Activation segmentAdd BLAST14

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.PROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0580 Eukaryota
ENOG410XNRB LUCA

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG108519

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O14965

KEGG Orthology (KO)

More...KOi		K11481

Database of Orthologous Groups

More...OrthoDBi		1464823at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O14965

TreeFam database of animal gene trees

More...TreeFami		TF105331

Family and domain databases

Conserved Domains Database

More...CDDi		cd14116 STKc_Aurora-A, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR030616 Aur
IPR030611 AURKA
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

The PANTHER Classification System

More...PANTHERi		PTHR24350 PTHR24350, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

O14965-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDRSKENCIS GPVKATAPVG GPKRVLVTQQ FPCQNPLPVN SGQAQRVLCP 
        60         70         80         90        100
SNSSQRVPLQ AQKLVSSHKP VQNQKQKQLQ ATSVPHPVSR PLNNTQKSKQ 
       110        120        130        140        150
PLPSAPENNP EEELASKQKN EESKKRQWAL EDFEIGRPLG KGKFGNVYLA 
       160        170        180        190        200
REKQSKFILA LKVLFKAQLE KAGVEHQLRR EVEIQSHLRH PNILRLYGYF 
       210        220        230        240        250
HDATRVYLIL EYAPLGTVYR ELQKLSKFDE QRTATYITEL ANALSYCHSK 
       260        270        280        290        300
RVIHRDIKPE NLLLGSAGEL KIADFGWSVH APSSRRTTLC GTLDYLPPEM 
       310        320        330        340        350
IEGRMHDEKV DLWSLGVLCY EFLVGKPPFE ANTYQETYKR ISRVEFTFPD 
       360        370        380        390        400
FVTEGARDLI SRLLKHNPSQ RPMLREVLEH PWITANSSKP SNCQNKESAS 

KQS
Length:403
Mass (Da):45,809
Last modified:January 27, 2003 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i125F3594834CD157
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A3KFJ0A3KFJ0_HUMAN
Aurora kinase A
AURKA
347Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5QPD4Q5QPD4_HUMAN
Aurora kinase A
AURKA
271Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A3KFJ1A3KFJ1_HUMAN
Aurora kinase A
AURKA
188Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5QPD2Q5QPD2_HUMAN
Aurora kinase A
AURKA
146Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5QPD1Q5QPD1_HUMAN
Aurora kinase A
AURKA
106Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A3KFJ2A3KFJ2_HUMAN
Aurora kinase A
AURKA
79Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA23592 differs from that shown. Reason: Frameshift at positions 105, 125, 129, 235 and 241.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03084011G → R. Corresponds to variant dbSNP:rs6069717Ensembl.1
Natural variantiVAR_03084131F → I5 PublicationsCorresponds to variant dbSNP:rs2273535EnsemblClinVar.1
Natural variantiVAR_04112750P → L1 PublicationCorresponds to variant dbSNP:rs34572020Ensembl.1
Natural variantiVAR_03084257V → I4 PublicationsCorresponds to variant dbSNP:rs1047972Ensembl.1
Natural variantiVAR_061745104S → L. Corresponds to variant dbSNP:rs2230743Ensembl.1
Natural variantiVAR_041128155S → R in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2. 2 Publications1
Natural variantiVAR_041129174V → M in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity. 2 Publications1
Natural variantiVAR_041130373M → V1 PublicationCorresponds to variant dbSNP:rs33923703Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
D84212 mRNA Translation: BAA23592.1 Frameshift.
AF008551 mRNA Translation: AAC12708.1
AF011467 Genomic DNA Translation: AAC23448.1
AF011468 mRNA Translation: AAC63902.1
AF195947
, AF195942, AF195943, AF195944, AF195945, AF195946 Genomic DNA Translation: AAF29508.1
AL121914 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75550.1
CH471077 Genomic DNA Translation: EAW75551.1
CH471077 Genomic DNA Translation: EAW75552.1
CH471077 Genomic DNA Translation: EAW75553.1
CH471077 Genomic DNA Translation: EAW75554.1
CH471077 Genomic DNA Translation: EAW75555.1
CH471077 Genomic DNA Translation: EAW75556.1
CH471077 Genomic DNA Translation: EAW75557.1
CH471077 Genomic DNA Translation: EAW75558.1
CH471077 Genomic DNA Translation: EAW75559.1
CH471077 Genomic DNA Translation: EAW75561.1
CH471077 Genomic DNA Translation: EAW75562.1
BC001280 mRNA Translation: AAH01280.1
BC002499 mRNA Translation: AAH02499.1
BC006423 mRNA Translation: AAH06423.1
BC027464 mRNA Translation: AAH27464.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13451.1

Protein sequence database of the Protein Information Resource

More...PIRi		JC5974

NCBI Reference Sequences

More...RefSeqi		NP_001310232.1, NM_001323303.1
NP_001310233.1, NM_001323304.1
NP_001310234.1, NM_001323305.1
NP_003591.2, NM_003600.3
NP_940835.1, NM_198433.2
NP_940836.1, NM_198434.2
NP_940837.1, NM_198435.2
NP_940838.1, NM_198436.2
NP_940839.1, NM_198437.2
XP_016883524.1, XM_017028035.1

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.250822

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000312783; ENSP00000321591; ENSG00000087586
ENST00000347343; ENSP00000216911; ENSG00000087586
ENST00000371356; ENSP00000360407; ENSG00000087586
ENST00000395911; ENSP00000379247; ENSG00000087586
ENST00000395913; ENSP00000379249; ENSG00000087586
ENST00000395914; ENSP00000379250; ENSG00000087586
ENST00000395915; ENSP00000379251; ENSG00000087586

Database of genes from NCBI RefSeq genomes

More...GeneIDi		6790

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:6790

UCSC genome browser

More...UCSCi		uc002xxe.1 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84212 mRNA Translation: BAA23592.1 Frameshift.
AF008551 mRNA Translation: AAC12708.1
AF011467 Genomic DNA Translation: AAC23448.1
AF011468 mRNA Translation: AAC63902.1
AF195947
, AF195942, AF195943, AF195944, AF195945, AF195946 Genomic DNA Translation: AAF29508.1
AL121914 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW75550.1
CH471077 Genomic DNA Translation: EAW75551.1
CH471077 Genomic DNA Translation: EAW75552.1
CH471077 Genomic DNA Translation: EAW75553.1
CH471077 Genomic DNA Translation: EAW75554.1
CH471077 Genomic DNA Translation: EAW75555.1
CH471077 Genomic DNA Translation: EAW75556.1
CH471077 Genomic DNA Translation: EAW75557.1
CH471077 Genomic DNA Translation: EAW75558.1
CH471077 Genomic DNA Translation: EAW75559.1
CH471077 Genomic DNA Translation: EAW75561.1
CH471077 Genomic DNA Translation: EAW75562.1
BC001280 mRNA Translation: AAH01280.1
BC002499 mRNA Translation: AAH02499.1
BC006423 mRNA Translation: AAH06423.1
BC027464 mRNA Translation: AAH27464.1
CCDSiCCDS13451.1
PIRiJC5974
RefSeqiNP_001310232.1, NM_001323303.1
NP_001310233.1, NM_001323304.1
NP_001310234.1, NM_001323305.1
NP_003591.2, NM_003600.3
NP_940835.1, NM_198433.2
NP_940836.1, NM_198434.2
NP_940837.1, NM_198435.2
NP_940838.1, NM_198436.2
NP_940839.1, NM_198437.2
XP_016883524.1, XM_017028035.1
UniGeneiHs.250822

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MQ4X-ray1.90A125-391[»]
1MUOX-ray2.90A107-403[»]
1OL5X-ray2.50A122-403[»]
1OL6X-ray3.00A122-403[»]
1OL7X-ray2.75A122-403[»]
2BMCX-ray2.60A/B/C/D/E/F100-403[»]
2C6DX-ray2.20A124-398[»]
2C6EX-ray2.10A/B123-401[»]
2DWBX-ray2.50A122-403[»]
2J4ZX-ray2.00A/B100-403[»]
2J50X-ray3.00A/B126-403[»]
2NP8X-ray2.25A125-391[»]
2W1CX-ray3.24A122-389[»]
2W1DX-ray2.97A122-389[»]
2W1EX-ray2.93A122-389[»]
2W1FX-ray2.85A122-389[»]
2W1GX-ray2.71A122-389[»]
2WQEX-ray2.50A127-388[»]
2WTVX-ray2.40A/B/C/D122-403[»]
2WTWX-ray3.30A122-403[»]
2X6DX-ray2.80A122-403[»]
2X6EX-ray3.35A122-403[»]
2X81X-ray2.91A126-391[»]
2XNEX-ray2.80A122-392[»]
2XNGX-ray2.60A122-403[»]
2XRUX-ray2.90A126-403[»]
3COHX-ray2.70A/B124-391[»]
3E5AX-ray2.30A125-391[»]
3EFWX-ray2.29A/B125-391[»]
3FDNX-ray1.90A123-401[»]
3H0YX-ray2.50A124-391[»]
3H0ZX-ray2.92A/B/C124-391[»]
3H10X-ray2.20A/B/D124-391[»]
3HA6X-ray2.36A125-391[»]
3K5UX-ray2.35A123-401[»]
3LAUX-ray2.10A125-399[»]
3M11X-ray2.75A123-401[»]
3MYGX-ray2.40A125-391[»]
3NRMX-ray3.05A126-403[»]
3O50X-ray2.00A/B125-391[»]
3O51X-ray3.20A125-391[»]
3P9JX-ray2.80A125-391[»]
3QBNX-ray3.50A124-403[»]
3R21X-ray2.90A126-391[»]
3R22X-ray2.90A126-391[»]
3UNZX-ray2.80A/B123-401[»]
3UO4X-ray2.45A123-401[»]
3UO5X-ray2.70A123-401[»]
3UO6X-ray2.80A/B123-401[»]
3UODX-ray2.50A123-401[»]
3UOHX-ray2.80A/B123-401[»]
3UOJX-ray2.90A/B123-401[»]
3UOKX-ray2.95A/B123-401[»]
3UOLX-ray2.40A/B123-401[»]
3UP2X-ray2.30A123-401[»]
3UP7X-ray3.05A123-401[»]
3VAPX-ray2.66A125-391[»]
3W10X-ray2.70A126-403[»]
3W16X-ray2.80A126-403[»]
3W18X-ray2.50A/B126-403[»]
3W2CX-ray2.45A/C/E/G128-388[»]
4B0GX-ray2.50A122-403[»]
4BN1X-ray2.50A122-403[»]
4BYIX-ray2.60A122-403[»]
4BYJX-ray2.75A122-403[»]
4C3PX-ray2.69A/D122-403[»]
4C3RX-ray2.79A122-403[»]
4CEGX-ray2.10A122-403[»]
4DEAX-ray2.45A123-401[»]
4DEBX-ray3.05A123-401[»]
4DEDX-ray3.05A123-401[»]
4DEEX-ray2.30A123-401[»]
4DHFX-ray2.80A/B126-391[»]
4J8MX-ray1.85A123-401[»]
4J8NX-ray3.14A/B/C/D123-401[»]
4JAIX-ray3.20A122-396[»]
4JAJX-ray2.70A122-396[»]
4JBOX-ray2.49A123-401[»]
4JBPX-ray2.45A123-401[»]
4JBQX-ray2.30A123-401[»]
4O0SX-ray2.50A122-403[»]
4O0UX-ray2.60A122-403[»]
4O0WX-ray2.60A122-403[»]
4PRJX-ray2.80A124-391[»]
4UYNX-ray1.90A125-399[»]
4UZDX-ray3.20A/B125-399[»]
4UZHX-ray2.00A125-399[»]
4ZS0X-ray3.00A122-403[»]
4ZTQX-ray2.80A122-403[»]
4ZTRX-ray2.85A122-403[»]
4ZTSX-ray2.90A122-403[»]
5AADX-ray3.10A122-403[»]
5AAEX-ray3.11A122-403[»]
5AAFX-ray2.78A122-403[»]
5AAGX-ray2.85A122-403[»]
5DN3X-ray2.05A125-391[»]
5DNRX-ray1.95A125-391[»]
5DOSX-ray2.98A126-390[»]
5DPVX-ray2.29A126-390[»]
5DR2X-ray2.46A128-390[»]
5DR6X-ray2.53A126-390[»]
5DR9X-ray2.47A126-390[»]
5DRDX-ray2.13A126-390[»]
5DT0X-ray2.15A126-390[»]
5DT3X-ray2.33A126-390[»]
5DT4X-ray2.86A126-390[»]
5EW9X-ray2.18A123-390[»]
5G15X-ray2.06A122-403[»]
5G1XX-ray1.72A122-403[»]
5L8JX-ray1.68A122-403[»]
5L8KX-ray1.79A122-403[»]
5L8LX-ray1.67A122-403[»]
5LXMX-ray2.08A122-403[»]
5OBJX-ray2.90A125-391[»]
5OBRX-ray2.62A125-391[»]
5ODTX-ray2.02A122-403[»]
5ONEX-ray2.60A122-403[»]
5ORLX-ray1.69A127-391[»]
5ORNX-ray2.19A127-391[»]
5OROX-ray2.12A127-391[»]
5ORPX-ray2.19A127-391[»]
5ORRX-ray2.09A127-391[»]
5ORSX-ray1.98A127-391[»]
5ORTX-ray2.56A127-391[»]
5ORVX-ray1.88A127-391[»]
5ORWX-ray2.00A127-391[»]
5ORXX-ray1.88A127-391[»]
5ORYX-ray1.99A127-391[»]
5ORZX-ray1.92A127-391[»]
5OS0X-ray1.74A127-391[»]
5OS1X-ray1.90A127-391[»]
5OS2X-ray1.92A127-391[»]
5OS3X-ray1.81A127-391[»]
5OS4X-ray1.88A127-391[»]
5OS5X-ray1.74A125-392[»]
5OS6X-ray2.20A127-391[»]
5OSDX-ray1.99A125-391[»]
5OSEX-ray1.90A127-391[»]
5OSFX-ray1.89A127-391[»]
6C2RX-ray1.96A125-391[»]
6C2TX-ray1.73A125-391[»]
6CPEX-ray2.45A122-403[»]
6CPFX-ray2.30A122-403[»]
6CPGX-ray2.80A/D122-403[»]
6HJJX-ray2.13A122-403[»]
6HJKX-ray2.40A122-403[»]
ProteinModelPortaliO14965
SMRiO14965
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112666, 374 interactors
CORUMiO14965
DIPiDIP-33068N
ELMiO14965
IntActiO14965, 122 interactors
MINTiO14965
STRINGi9606.ENSP00000216911

Chemistry databases

BindingDBiO14965
ChEMBLiCHEMBL4722
DrugBankiDB08065 2-(1H-pyrazol-3-yl)-1H-benzimidazole
DB05169 AT9283
DB05198 CYC116
DB05220 MLN8237
DB08066 N-[3-(1H-BENZIMIDAZOL-2-YL)-1H-PYRAZOL-4-YL]BENZAMIDE
DB07801 N-butyl-3-{[6-(9H-purin-6-ylamino)hexanoyl]amino}benzamide
DB07545 N-{3-[(4-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-2-YL)AMINO]PHENYL}CYCLOPROPANECARBOXAMIDE
DB02482 Phosphonothreonine
GuidetoPHARMACOLOGYi1936

PTM databases

iPTMnetiO14965
PhosphoSitePlusiO14965

Polymorphism and mutation databases

BioMutaiAURKA

Proteomic databases

EPDiO14965
jPOSTiO14965
MaxQBiO14965
PaxDbiO14965
PeptideAtlasiO14965
PRIDEiO14965
ProteomicsDBi48339

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		6790
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312783; ENSP00000321591; ENSG00000087586
ENST00000347343; ENSP00000216911; ENSG00000087586
ENST00000371356; ENSP00000360407; ENSG00000087586
ENST00000395911; ENSP00000379247; ENSG00000087586
ENST00000395913; ENSP00000379249; ENSG00000087586
ENST00000395914; ENSP00000379250; ENSG00000087586
ENST00000395915; ENSP00000379251; ENSG00000087586
GeneIDi6790
KEGGihsa:6790
UCSCiuc002xxe.1 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6790
DisGeNETi6790
EuPathDBiHostDB:ENSG00000087586.17

GeneCards: human genes, protein and diseases

More...GeneCardsi		AURKA

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0015930
HGNCiHGNC:11393 AURKA
HPAiCAB001454
HPA002636
MalaCardsiAURKA
MIMi603072 gene
neXtProtiNX_O14965
PharmGKBiPA36201

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0580 Eukaryota
ENOG410XNRB LUCA
HOVERGENiHBG108519
InParanoidiO14965
KOiK11481
OrthoDBi1464823at2759
PhylomeDBiO14965
TreeFamiTF105331

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-2565942 Regulation of PLK1 Activity at G2/M Transition
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-6804114 TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8854518 AURKA Activation by TPX2
R-HSA-8854521 Interaction between PHLDA1 and AURKA
SignaLinkiO14965
SIGNORiO14965

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		AURKA human
EvolutionaryTraceiO14965

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Aurora_A_kinase

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		6790

Protein Ontology

More...PROi		PR:O14965

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000087586 Expressed in 175 organ(s), highest expression level in oocyte
ExpressionAtlasiO14965 baseline and differential
GenevisibleiO14965 HS

Family and domain databases

CDDicd14116 STKc_Aurora-A, 1 hit
InterProiView protein in InterPro
IPR030616 Aur
IPR030611 AURKA
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR24350 PTHR24350, 1 hit
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAURKA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O14965
Secondary accession number(s): E1P5F9
, O60445, O75873, Q9BQD6, Q9UPG5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: January 27, 2003
Last modified: April 10, 2019
This is version 216 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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