UniProtKB - O14965 (AURKA_HUMAN)
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- BLAST>sp|O14965|AURKA_HUMAN Aurora kinase A OS=Homo sapiens OX=9606 GN=AURKA PE=1 SV=2 MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRVPLQ AQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKN EESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRR EVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITEL ANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEM IEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLI SRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS
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Aurora kinase A
AURKA
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>Select a section on the left to see content.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers."
Bischoff J.R., Anderson L., Zhu Y., Mossie K., Ng L., Souza B., Schryver B., Flanagan P., Clairvoyant F., Ginther C., Chan C.S., Novotny M., Slamon D.J., Plowman G.D.
EMBO J. 17:3052-3065(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION. - Ref.10"The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation."
Walter A.O., Seghezzi W., Korver W., Sheung J., Lees E.
Oncogene 19:4906-4916(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF THR-288, UBIQUITINATION, ENZYME REGULATION. - Ref.11"Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle."
Katayama H., Zhou H., Li Q., Tatsuka M., Sen S.
J. Biol. Chem. 276:46219-46224(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC, MUTAGENESIS OF PHE-165 AND PHE-346, PHOSPHORYLATION. - Ref.13"Roles of aurora-A kinase in mitotic entry and G2 checkpoint in mammalian cells."
Marumoto T., Hirota T., Morisaki T., Kunitoku N., Zhang D., Ichikawa Y., Sasayama T., Kuninaka S., Mimori T., Tamaki N., Kimura M., Okano Y., Saya H.
Genes Cells 7:1173-1182(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION, ENZYME REGULATION. - Ref.15"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 114:585-598(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-288. - Ref.16"Aurora-A kinase maintains the fidelity of early and late mitotic events in HeLa cells."
Marumoto T., Honda S., Hara T., Nitta M., Hirota T., Kohmura E., Saya H.
J. Biol. Chem. 278:51786-51795(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.18"The centrosomal protein Lats2 is a phosphorylation target of Aurora-A kinase."
Toji S., Yabuta N., Hosomi T., Nishihara S., Kobayashi T., Suzuki S., Tamai K., Nojima H.
Genes Cells 9:383-397(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.19"BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M transition."
Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A., Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.
J. Biol. Chem. 279:19643-19648(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF LYS-162. - Ref.20"Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the G2-M transition."
Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V., Dozier C., Mirey G., Bouche J.P., Theis-Febvre N., Schmitt E., Monsarrat B., Prigent C., Ducommun B.
J. Cell Sci. 117:2523-2531(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.21"Phosphorylation by aurora kinase A induces Mdm2-mediated destabilization and inhibition of p53."
Katayama H., Sasai K., Kawai H., Yuan Z.M., Bondaruk J., Suzuki F., Fujii S., Arlinghaus R.B., Czerniak B.A., Sen S.
Nat. Genet. 36:55-62(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF LYS-162, INTERACTION WITH TP53. - Ref.24"Phosphorylation and stabilization of HURP by Aurora-A: implication of HURP as a transforming target of Aurora-A."
Yu C.T., Hsu J.M., Lee Y.C., Tsou A.P., Chou C.K., Huang C.Y.
Mol. Cell. Biol. 25:5789-5800(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION. - Ref.26"Aurora-A kinase regulates breast cancer associated gene 1 inhibition of centrosome-dependent microtubule nucleation."
Sankaran S., Crone D.E., Palazzo R.E., Parvin J.D.
Cancer Res. 67:11186-11194(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.27"HEF1-dependent Aurora A activation induces disassembly of the primary cilium."
Pugacheva E.N., Jablonski S.A., Hartman T.R., Henske E.P., Golemis E.A.
Cell 129:1351-1363(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.31"Antitumor activity of MLN8054, an orally active small-molecule inhibitor of Aurora A kinase."
Manfredi M.G., Ecsedy J.A., Meetze K.A., Balani S.K., Burenkova O., Chen W., Galvin K.M., Hoar K.M., Huck J.J., LeRoy P.J., Ray E.T., Sells T.B., Stringer B., Stroud S.G., Vos T.J., Weatherhead G.S., Wysong D.R., Zhang M., Bolen J.B., Claiborne C.F.
Proc. Natl. Acad. Sci. U.S.A. 104:4106-4111(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION. - Ref.33"Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery."
Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R., Freire R., Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.
Nature 455:119-123(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.34"Phosphorylation of the par polarity complex protein Par3 at serine 962 is mediated by aurora A and regulates its function in neuronal polarity."
Khazaei M.R., Puschel A.W.
J. Biol. Chem. 284:33571-33579(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH PARD3. - Ref.35"Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a."
Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF2A. - Ref.36"An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation by modulation of microtubule dynamics."
Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S., Saya H., Wynshaw-Boris A., Hirotsune S.
Nat. Cell Biol. 11:1057-1068(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 AND THR-288, MUTAGENESIS OF THR-287. - Ref.37"A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function."
Fu J., Bian M., Liu J., Jiang Q., Zhang C.
Proc. Natl. Acad. Sci. U.S.A. 106:6939-6944(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TPX2, MUTAGENESIS OF GLY-198, SUBCELLULAR LOCATION, FUNCTION. - Ref.38"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PIFO, ACTIVATION BY PIFO. - Ref.55"1,4,5,6-tetrahydropyrrolo[3,4-c]pyrazoles: identification of a potent aurora kinase inhibitor with a favorable antitumor kinase inhibition profile."
Fancelli D., Moll J., Varasi M., Bravo R., Artico R., Berta D., Bindi S., Cameron A., Candiani I., Cappella P., Carpinelli P., Croci W., Forte B., Giorgini M.L., Klapwijk J., Marsiglio A., Pesenti E., Rocchetti M. , Roletto F., Severino D., Soncini C., Storici P., Tonani R., Zugnoni P., Vianello P.
J. Med. Chem. 49:7247-7251(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-403 IN COMPLEXES WITH SYNTHETIC INHIBITORS, FUNCTION.
Miscellaneous
Caution
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.3"Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation."
Zhou H., Kuang J., Zhong L., Kuo W.-L., Gray J.W., Sahin A., Brinkley B.R., Sen S.
Nat. Genet. 20:189-193(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-31.
<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. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.51"Crystal structure of aurora-2, an oncogenic serine/threonine kinase."
Cheetham G.M., Knegtel R.M., Coll J.T., Renwick S.B., Swenson L., Weber P., Lippke J.A., Austen D.A.
J. Biol. Chem. 277:42419-42422(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 107-403 IN COMPLEX WITH ADENOSINE, CATALYTIC ACTIVITY. - Ref.54"SAR and inhibitor complex structure determination of a novel class of potent and specific Aurora kinase inhibitors."
Heron N.M., Anderson M., Blowers D.P., Breed J., Eden J.M., Green S., Hill G.B., Johnson T., Jung F.H., McMiken H.H., Mortlock A.A., Pannifer A.D., Pauptit R.A., Pink J., Roberts N.J., Rowsell S.
Bioorg. Med. Chem. Lett. 16:1320-1323(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 123-401 IN COMPLEXES WITH ADPNP AND 5-AMINOPYRIMIDINYL QUINAZOLINE INHIBITOR, CATALYTIC ACTIVITY. - Ref.58"Structure-based drug design of novel Aurora kinase A inhibitors: structural basis for potency and specificity."
Coumar M.S., Leou J.S., Shukla P., Wu J.S., Dixit A.K., Lin W.H., Chang C.Y., Lien T.W., Tan U.K., Chen C.H., Hsu J.T., Chao Y.S., Wu S.Y., Hsieh H.P.
J. Med. Chem. 52:1050-1062(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 123-401 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY. - Ref.59"A class of 2,4-bisanilinopyrimidine Aurora A inhibitors with unusually high selectivity against Aurora B."
Aliagas-Martin I., Burdick D., Corson L., Dotson J., Drummond J., Fields C., Huang O.W., Hunsaker T., Kleinheinz T., Krueger E., Liang J., Moffat J., Phillips G., Pulk R., Rawson T.E., Ultsch M., Walker L., Wiesmann C. , Zhang B., Zhu B.Y., Cochran A.G.
J. Med. Chem. 52:3300-3307(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 125-391 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY. - Ref.60"Structural basis of N-Myc binding by Aurora-A and its destabilization by kinase inhibitors."
Richards M.W., Burgess S.G., Poon E., Carstensen A., Eilers M., Chesler L., Bayliss R.
Proc. Natl. Acad. Sci. U.S.A. 113:13726-13731(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 122-403 OF MUTANTS ALA-290 AND ALA-393 IN COMPLEX WITH ADP, INTERACTION WITH MYCN AND TPX2, MUTAGENESIS OF CYS-290; TYR-334; GLN-335 AND CYS-393, CATALYTIC ACTIVITY.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation."
Walter A.O., Seghezzi W., Korver W., Sheung J., Lees E.
Oncogene 19:4906-4916(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF THR-288, UBIQUITINATION, ENZYME REGULATION. - Ref.13"Roles of aurora-A kinase in mitotic entry and G2 checkpoint in mammalian cells."
Marumoto T., Hirota T., Morisaki T., Kunitoku N., Zhang D., Ichikawa Y., Sasayama T., Kuninaka S., Mimori T., Tamaki N., Kimura M., Okano Y., Saya H.
Genes Cells 7:1173-1182(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION, ENZYME REGULATION. - Ref.31"Antitumor activity of MLN8054, an orally active small-molecule inhibitor of Aurora A kinase."
Manfredi M.G., Ecsedy J.A., Meetze K.A., Balani S.K., Burenkova O., Chen W., Galvin K.M., Hoar K.M., Huck J.J., LeRoy P.J., Ray E.T., Sells T.B., Stringer B., Stroud S.G., Vos T.J., Weatherhead G.S., Wysong D.R., Zhang M., Bolen J.B., Claiborne C.F.
Proc. Natl. Acad. Sci. U.S.A. 104:4106-4111(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ENZYME REGULATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 sitei | 143 | ATP; via amide nitrogenCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 sitei | 162 | ATPCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 sitei | 256 | Proton acceptorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 sitei | 274 | ATPCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
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Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 bindingi | 211 – 213 | ATPCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <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 bindingi | 260 – 261 | ATPCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 |
<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
- ATP binding Source: UniProtKB-KW
- histone serine kinase activity Source: GO_Central
- protein heterodimerization activity Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein kinase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein serine/threonine/tyrosine kinase activity Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- protein serine/threonine kinase activity Source: ReactomeInferred from experimenti
- ubiquitin protein ligase binding Source: Ensembl
<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 - Biological processi
- anaphase-promoting complex-dependent catabolic process Source: Reactome
- anterior/posterior axis specification Source: Ensembl
- cell division Source: UniProtKB-KW
- centrosome localization Source: Ensembl
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
- G2/M transition of mitotic cell cycle Source: Reactome
- liver regeneration Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- mitotic cell cycle Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- mitotic centrosome separation Source: Ensembl
- mitotic spindle organization Source: GO_Central
- negative regulation of apoptotic process Source: Ensembl
- negative regulation of G2/M transition of mitotic cell cycle Source: Reactome
- negative regulation of protein binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- neuron projection extension Source: Ensembl
- positive regulation of mitotic nuclear division Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- positive regulation of oocyte maturation Source: Ensembl
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
- protein autophosphorylation Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- protein localization to centrosome Source: Ensembl
- protein phosphorylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of centrosome cycle Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- regulation of cytokinesis Source: GO_Central
- regulation of G2/M transition of mitotic cell cycle Source: Reactome
- regulation of protein stability Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of signal transduction by p53 class mediator Source: Reactome
- response to wounding Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- spindle assembly involved in female meiosis I Source: Ensembl
- spindle organization Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<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 function | Kinase, Serine/threonine-protein kinase, Transferase |
| Biological process | Cell cycle, Cell division, Cilium biogenesis/degradation, Mitosis |
| Ligand | ATP-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<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
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>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 |
|
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
Cytoskeleton
- centrosome 9 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1."
Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K., Okano Y.
J. Biol. Chem. 272:13766-13771(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION. - Ref.12"Molecular dynamics of Aurora-A kinase in living mitotic cells simultaneously visualized with histone H3 and nuclear membrane protein importinalpha."
Sugimoto K., Urano T., Zushi H., Inoue K., Tasaka H., Tachibana M., Dotsu M.
Cell Struct. Funct. 27:457-467(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.15"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 114:585-598(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-288. - Ref.29"Functional interaction of Aurora-A and PP2A during mitosis."
Horn V., Thelu J., Garcia A., Albiges-Rizo C., Block M.R., Viallet J.
Mol. Biol. Cell 18:1233-1241(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA, PHOSPHORYLATION AT SER-51. - Ref.30"Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis."
North B.J., Verdin E.
PLoS ONE 2:E784-E784(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION. - Ref.37"A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function."
Fu J., Bian M., Liu J., Jiang Q., Zhang C.
Proc. Natl. Acad. Sci. U.S.A. 106:6939-6944(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TPX2, MUTAGENESIS OF GLY-198, SUBCELLULAR LOCATION, FUNCTION. - Ref.42"PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH JTB. - Ref.45"SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity."
Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., Cha Y.I., Gius D., Deng C.X.
Cancer Cell 20:487-499(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION. - Ref.48"CENP-32 is required to maintain centrosomal dominance in bipolar spindle assembly."
Ohta S., Wood L., Toramoto I., Yagyu K., Fukagawa T., Earnshaw W.C.
Mol. Biol. Cell 26:1225-1237(2015) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- spindle pole 7 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1."
Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K., Okano Y.
J. Biol. Chem. 272:13766-13771(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION. - Ref.8"A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers."
Bischoff J.R., Anderson L., Zhu Y., Mossie K., Ng L., Souza B., Schryver B., Flanagan P., Clairvoyant F., Ginther C., Chan C.S., Novotny M., Slamon D.J., Plowman G.D.
EMBO J. 17:3052-3065(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION. - Ref.12"Molecular dynamics of Aurora-A kinase in living mitotic cells simultaneously visualized with histone H3 and nuclear membrane protein importinalpha."
Sugimoto K., Urano T., Zushi H., Inoue K., Tasaka H., Tachibana M., Dotsu M.
Cell Struct. Funct. 27:457-467(2002) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.15"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 114:585-598(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-288. - Ref.30"Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis."
North B.J., Verdin E.
PLoS ONE 2:E784-E784(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION. - Ref.35"Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a."
Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF2A. - Ref.48"CENP-32 is required to maintain centrosomal dominance in bipolar spindle assembly."
Ohta S., Wood L., Toramoto I., Yagyu K., Fukagawa T., Earnshaw W.C.
Mol. Biol. Cell 26:1225-1237(2015) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
- cilium basal body By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- centriole By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
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).By similarity- centrosome 9 Publications
- Ref.8"A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers."
Bischoff J.R., Anderson L., Zhu Y., Mossie K., Ng L., Souza B., Schryver B., Flanagan P., Clairvoyant F., Ginther C., Chan C.S., Novotny M., Slamon D.J., Plowman G.D.
EMBO J. 17:3052-3065(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION. - Ref.29"Functional interaction of Aurora-A and PP2A during mitosis."
Horn V., Thelu J., Garcia A., Albiges-Rizo C., Block M.R., Viallet J.
Mol. Biol. Cell 18:1233-1241(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA, PHOSPHORYLATION AT SER-51. - Ref.30"Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis."
North B.J., Verdin E.
PLoS ONE 2:E784-E784(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION. - Ref.42"PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH JTB. - Ref.45"SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity."
Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., Cha Y.I., Gius D., Deng C.X.
Cancer Cell 20:487-499(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
5 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytoskeleton
- centriole Source: UniProtKB-SubCell
- centrosome Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- chromosome passenger complex Source: GO_Central
- meiotic spindle Source: Ensembl
- microtubule Source: UniProtKB-KW
- microtubule cytoskeleton Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- mitotic spindle pole Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- spindle Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- spindle midzone Source: GO_Central
- spindle pole centrosome Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Cytosol
- cytosol Source: HPA
Nucleus
- condensed nuclear chromosome, centromeric region Source: GO_Central
- germinal vesicle Source: Ensembl
- nucleoplasm Source: Reactome
- nucleus Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- pronucleus Source: Ensembl
Other locations
- axon hillock Source: Ensembl
- cilium Source: UniProtKB-KW
- midbody Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- perinuclear region of cytoplasm Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<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>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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Mutagenesisi | 162 | K → R: Loss of kinase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 165 | F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 198 | G → 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 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 205 | R → A: Reduces ubiquitination and proteasomal degradation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 274 | D → N: Abolishes autophosphorylation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 287 | T → A: No direct effect on catalytic activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 287 | T → E: Enhances interaction with TPX2. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 288 | T → D: Mimics phosphorylation state and increases kinase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 290 | C → A: Enhances stability; when associated with A-393. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 334 | Y → A: Reduces binding to MYCN. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 335 | Q → A: Reduces binding to MYCN. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 346 | F → A: Decreases the interaction with phosphatase type 1 isoforms. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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>Mutagenesisi | 393 | C → A: Enhances stability; when associated with A-290. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<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>Keywords - Diseasei
Proto-oncogeneOrganism-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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_0000086692 | 1 – 403 | Aurora kinase AAdd BLAST | 403 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 residuei | 41 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 51 | Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), 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-linki | 258 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <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 residuei | 287 | Phosphothreonine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 288 | Phosphothreonine7 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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 residuei | 342 | Phosphoserine; by PKA and PAK1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation."
Walter A.O., Seghezzi W., Korver W., Sheung J., Lees E.
Oncogene 19:4906-4916(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF THR-288, UBIQUITINATION, ENZYME REGULATION. - Ref.11"Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle."
Katayama H., Zhou H., Li Q., Tatsuka M., Sen S.
J. Biol. Chem. 276:46219-46224(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC, MUTAGENESIS OF PHE-165 AND PHE-346, PHOSPHORYLATION. - Ref.13"Roles of aurora-A kinase in mitotic entry and G2 checkpoint in mammalian cells."
Marumoto T., Hirota T., Morisaki T., Kunitoku N., Zhang D., Ichikawa Y., Sasayama T., Kuninaka S., Mimori T., Tamaki N., Kimura M., Okano Y., Saya H.
Genes Cells 7:1173-1182(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION, ENZYME REGULATION. - Ref.15"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 114:585-598(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-288. - Ref.19"BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M transition."
Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A., Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.
J. Biol. Chem. 279:19643-19648(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF LYS-162. - Ref.23"The GIT-associated kinase PAK targets to the centrosome and regulates Aurora-A."
Zhao Z.S., Lim J.P., Ng Y.W., Lim L., Manser E.
Mol. Cell 20:237-249(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-288 AND SER-342. - Ref.29"Functional interaction of Aurora-A and PP2A during mitosis."
Horn V., Thelu J., Garcia A., Albiges-Rizo C., Block M.R., Viallet J.
Mol. Biol. Cell 18:1233-1241(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA, PHOSPHORYLATION AT SER-51. - Ref.36"An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation by modulation of microtubule dynamics."
Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S., Saya H., Wynshaw-Boris A., Hirotsune S.
Nat. Cell Biol. 11:1057-1068(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 AND THR-288, MUTAGENESIS OF THR-287. - Ref.53"Structural basis of Aurora-A activation by TPX2 at the mitotic spindle."
Bayliss R., Sardon T., Vernos I., Conti E.
Mol. Cell 12:851-862(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 122-403 IN COMPLEX WITH TPX2, MUTAGENESIS OF ASP-274, ACTIVE SITE, PHOSPHORYLATION AT THR-287 AND THR-288. - Ref.56"Modulation of kinase-inhibitor interactions by auxiliary protein binding: crystallography studies on Aurora A interactions with VX-680 and with TPX2."
Zhao B., Smallwood A., Yang J., Koretke K., Nurse K., Calamari A., Kirkpatrick R.B., Lai Z.
Protein Sci. 17:1791-1797(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-391 IN COMPLEX WITH VX-680 AND TPX2, PHOSPHORYLATION AT THR-288, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"Degradation of human Aurora2 protein kinase by the anaphase-promoting complex-ubiquitin-proteasome pathway."
Honda K., Mihara H., Kato Y., Yamaguchi A., Tanaka H., Yasuda H., Furukawa K., Urano T.
Oncogene 19:2812-2819(2000) [PubMed] [Europe PMC] [Abstract]Cited for: UBIQUITINATION, PROTEASOMAL DEGRADATION, MUTAGENESIS OF ARG-205. - Ref.10"The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation."
Walter A.O., Seghezzi W., Korver W., Sheung J., Lees E.
Oncogene 19:4906-4916(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF THR-288, UBIQUITINATION, ENZYME REGULATION.
<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>Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | 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
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1."
Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K., Okano Y.
J. Biol. Chem. 272:13766-13771(1997) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION. - Ref.8"A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers."
Bischoff J.R., Anderson L., Zhu Y., Mossie K., Ng L., Souza B., Schryver B., Flanagan P., Clairvoyant F., Ginther C., Chan C.S., Novotny M., Slamon D.J., Plowman G.D.
EMBO J. 17:3052-3065(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION. - Ref.13"Roles of aurora-A kinase in mitotic entry and G2 checkpoint in mammalian cells."
Marumoto T., Hirota T., Morisaki T., Kunitoku N., Zhang D., Ichikawa Y., Sasayama T., Kuninaka S., Mimori T., Tamaki N., Kimura M., Okano Y., Saya H.
Genes Cells 7:1173-1182(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION, ENZYME REGULATION. - Ref.14"Cell-cycle-dependent regulation of human aurora A transcription is mediated by periodic repression of E4TF1."
Tanaka M., Ueda A., Kanamori H., Ideguchi H., Yang J., Kitajima S., Ishigatsubo Y.
J. Biol. Chem. 277:10719-10726(2002) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION. - Ref.24"Phosphorylation and stabilization of HURP by Aurora-A: implication of HURP as a transforming target of Aurora-A."
Yu C.T., Hsu J.M., Lee Y.C., Tsou A.P., Chou C.K., Huang C.Y.
Mol. Cell. Biol. 25:5789-5800(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, FUNCTION.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000087586 |
CleanEx database of gene expression profiles More...CleanExi | HS_AURKA |
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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle."
Katayama H., Zhou H., Li Q., Tatsuka M., Sen S.
J. Biol. Chem. 276:46219-46224(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PPP1CA; PPP1CB AND PPP1CC, MUTAGENESIS OF PHE-165 AND PHE-346, PHOSPHORYLATION. - Ref.17"TACC1-chTOG-Aurora A protein complex in breast cancer."
Conte N., Delaval B., Ginestier C., Ferrand A., Isnardon D., Larroque C., Prigent C., Seraphin B., Jacquemier J., Birnbaum D.
Oncogene 22:8102-8116(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TACC1. - Ref.19"BRCA1 phosphorylation by Aurora-A in the regulation of G2 to M transition."
Ouchi M., Fujiuchi N., Sasai K., Katayama H., Minamishima Y.A., Ongusaha P.P., Deng C., Sen S., Lee S.W., Ouchi T.
J. Biol. Chem. 279:19643-19648(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF LYS-162. - Ref.21"Phosphorylation by aurora kinase A induces Mdm2-mediated destabilization and inhibition of p53."
Katayama H., Sasai K., Kawai H., Yuan Z.M., Bondaruk J., Suzuki F., Fujii S., Arlinghaus R.B., Czerniak B.A., Sen S.
Nat. Genet. 36:55-62(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF LYS-162, INTERACTION WITH TP53. - Ref.22"Over-expression of Aurora-A targets cytoplasmic polyadenylation element binding protein and promotes mRNA polyadenylation of Cdk1 and cyclin B1."
Sasayama T., Marumoto T., Kunitoku N., Zhang D., Tamaki N., Kohmura E., Saya H., Hirota T.
Genes Cells 10:627-638(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CPEB1. - Ref.25"Mitotic activation of the kinase Aurora-A requires its binding partner Bora."
Hutterer A., Berdnik D., Wirtz-Peitz F., Zigman M., Schleiffer A., Knoblich J.A.
Dev. Cell 11:147-157(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH BORA. - Ref.28"GEF-H1 modulates localized RhoA activation during cytokinesis under the control of mitotic kinases."
Birkenfeld J., Nalbant P., Bohl B.P., Pertz O., Hahn K.M., Bokoch G.M.
Dev. Cell 12:699-712(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ARHGEF2. - Ref.29"Functional interaction of Aurora-A and PP2A during mitosis."
Horn V., Thelu J., Garcia A., Albiges-Rizo C., Block M.R., Viallet J.
Mol. Biol. Cell 18:1233-1241(2007) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA, PHOSPHORYLATION AT SER-51. - Ref.30"Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis."
North B.J., Verdin E.
PLoS ONE 2:E784-E784(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION. - Ref.34"Phosphorylation of the par polarity complex protein Par3 at serine 962 is mediated by aurora A and regulates its function in neuronal polarity."
Khazaei M.R., Puschel A.W.
J. Biol. Chem. 284:33571-33579(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH PARD3. - Ref.35"Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a."
Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIF2A. - Ref.36"An essential role of the aPKC-Aurora A-NDEL1 pathway in neurite elongation by modulation of microtubule dynamics."
Mori D., Yamada M., Mimori-Kiyosue Y., Shirai Y., Suzuki A., Ohno S., Saya H., Wynshaw-Boris A., Hirotsune S.
Nat. Cell Biol. 11:1057-1068(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 AND THR-288, MUTAGENESIS OF THR-287. - Ref.37"A single amino acid change converts Aurora-A into Aurora-B-like kinase in terms of partner specificity and cellular function."
Fu J., Bian M., Liu J., Jiang Q., Zhang C.
Proc. Natl. Acad. Sci. U.S.A. 106:6939-6944(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TPX2, MUTAGENESIS OF GLY-198, SUBCELLULAR LOCATION, FUNCTION. - Ref.38"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH PIFO, ACTIVATION BY PIFO. - Ref.39"Functional characterization of AIBp, a novel Aurora-A binding protein in centrosome structure and spindle formation."
Lieu A.S., Cheng T.S., Chou C.H., Wu C.H., Hsu C.Y., Huang C.Y., Chang L.K., Loh J.K., Chang C.S., Hsu C.M., Howng S.L., Hong Y.R.
Int. J. Oncol. 37:429-436(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AUNIP. - Ref.40"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase."
Sanchez R., Pantoja-Uceda D., Prieto J., Diercks T., Marcaida M.J., Montoya G., Campos-Olivas R., Blanco F.J.
J. Biol. Chem. 285:22196-22201(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GADD45A. - Ref.42"PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, INTERACTION WITH JTB. - Ref.45"SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity."
Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H., Cha Y.I., Gius D., Deng C.X.
Cancer Cell 20:487-499(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SIRT2, SUBCELLULAR LOCATION. - Ref.46"The nuclear scaffold protein SAF-A is required for kinetochore-microtubule attachment and contributes to the targeting of Aurora-A to mitotic spindles."
Ma N., Matsunaga S., Morimoto A., Sakashita G., Urano T., Uchiyama S., Fukui K.
J. Cell Sci. 124:394-404(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HNRNPU. - Ref.47"Furry protein promotes Aurora A-mediated polo-like kinase 1 activation."
Ikeda M., Chiba S., Ohashi K., Mizuno K.
J. Biol. Chem. 287:27670-27681(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FRY. - Ref.49"Phosphorylation of SAF-A/hnRNP-U serine 59 by polo-like kinase 1 is required for mitosis."
Douglas P., Ye R., Morrice N., Britton S., Trinkle-Mulcahy L., Lees-Miller S.P.
Mol. Cell. Biol. 35:2699-2713(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH HNRNPU. - Ref.51"Crystal structure of aurora-2, an oncogenic serine/threonine kinase."
Cheetham G.M., Knegtel R.M., Coll J.T., Renwick S.B., Swenson L., Weber P., Lippke J.A., Austen D.A.
J. Biol. Chem. 277:42419-42422(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 107-403 IN COMPLEX WITH ADENOSINE, CATALYTIC ACTIVITY. - Ref.52"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
Structure 10:1659-1667(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 125-391 IN COMPLEX WITH ADP. - Ref.53"Structural basis of Aurora-A activation by TPX2 at the mitotic spindle."
Bayliss R., Sardon T., Vernos I., Conti E.
Mol. Cell 12:851-862(2003) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 122-403 IN COMPLEX WITH TPX2, MUTAGENESIS OF ASP-274, ACTIVE SITE, PHOSPHORYLATION AT THR-287 AND THR-288. - Ref.56"Modulation of kinase-inhibitor interactions by auxiliary protein binding: crystallography studies on Aurora A interactions with VX-680 and with TPX2."
Zhao B., Smallwood A., Yang J., Koretke K., Nurse K., Calamari A., Kirkpatrick R.B., Lai Z.
Protein Sci. 17:1791-1797(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-391 IN COMPLEX WITH VX-680 AND TPX2, PHOSPHORYLATION AT THR-288, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT. - Ref.57"A cancer-associated aurora A mutant is mislocalized and misregulated due to loss of interaction with TPX2."
Bibby R.A., Tang C., Faisal A., Drosopoulos K., Lubbe S., Houlston R., Bayliss R., Linardopoulos S.
J. Biol. Chem. 284:33177-33184(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 127-388 IN COMPLEX WITH ADP, CHARACTERIZATION OF VARIANTS ARG-155 AND MET-174, INTERACTION WITH TPX2. - Ref.58"Structure-based drug design of novel Aurora kinase A inhibitors: structural basis for potency and specificity."
Coumar M.S., Leou J.S., Shukla P., Wu J.S., Dixit A.K., Lin W.H., Chang C.Y., Lien T.W., Tan U.K., Chen C.H., Hsu J.T., Chao Y.S., Wu S.Y., Hsieh H.P.
J. Med. Chem. 52:1050-1062(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 123-401 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY. - Ref.59"A class of 2,4-bisanilinopyrimidine Aurora A inhibitors with unusually high selectivity against Aurora B."
Aliagas-Martin I., Burdick D., Corson L., Dotson J., Drummond J., Fields C., Huang O.W., Hunsaker T., Kleinheinz T., Krueger E., Liang J., Moffat J., Phillips G., Pulk R., Rawson T.E., Ultsch M., Walker L., Wiesmann C. , Zhang B., Zhu B.Y., Cochran A.G.
J. Med. Chem. 52:3300-3307(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 125-391 IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY. - Ref.60"Structural basis of N-Myc binding by Aurora-A and its destabilization by kinase inhibitors."
Richards M.W., Burgess S.G., Poon E., Carstensen A., Eilers M., Chesler L., Bayliss R.
Proc. Natl. Acad. Sci. U.S.A. 113:13726-13731(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 122-403 OF MUTANTS ALA-290 AND ALA-393 IN COMPLEX WITH ADP, INTERACTION WITH MYCN AND TPX2, MUTAGENESIS OF CYS-290; TYR-334; GLN-335 AND CYS-393, CATALYTIC ACTIVITY.
<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
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| AURKAIP1 | Q9NWT8 | 2 | EBI-448680,EBI-448665 | |
| BIRC5 | O15392 | 2 | EBI-448680,EBI-518823 | |
| EGFR | P00533 | 4 | EBI-448680,EBI-297353 | |
| HNRNPK | P61978 | 2 | EBI-448680,EBI-304185 | |
| IK | Q13123 | 3 | EBI-448680,EBI-713456 | |
| IKBKB | O14920 | 2 | EBI-448680,EBI-81266 | |
| INCENP | Q9NQS7 | 2 | EBI-448680,EBI-307907 | |
| INCENP | Q9NQS7-1 | 2 | EBI-448680,EBI-15767972 | |
| MYCN | P04198 | 12 | EBI-448680,EBI-878369 | |
| NPM1 | P06748 | 3 | EBI-448680,EBI-78579 | |
| PLK1 | P53350 | 4 | EBI-448680,EBI-476768 | |
| PTPRD | P23468 | 2 | EBI-448680,EBI-2682990 | |
| Sirt2 | Q8VDQ8 | 5 | EBI-448680,EBI-911012 | From Mus musculus. |
| SPAG5 | Q96R06 | 3 | EBI-448680,EBI-413317 | |
| TP73 | O15350 | 11 | EBI-448680,EBI-389606 | |
| TPX2 | Q9ULW0 | 7 | EBI-448680,EBI-1037322 |
<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
- protein heterodimerization activity Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ubiquitin protein ligase binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112666, 329 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, 123 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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 130 – 132 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 133 – 141 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 143 – 152 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 153 – 155 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 158 – 165 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 166 – 171 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 172 – 174 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 175 – 185 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 191 – 193 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 196 – 201 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 203 – 210 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 214 – 217 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 218 – 225 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 230 – 249 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 259 – 261 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 262 – 264 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 266 – 268 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 270 – 272 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 275 – 277 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 280 – 283 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 287 – 289 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 290 – 292 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 293 – 295 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 298 – 302 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 307 – 309 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 310 – 324 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 334 – 342 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 350 – 352 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 354 – 363 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 368 – 370 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 374 – 378 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 381 – 386 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1MQ4 | X-ray | 1.90 | A | 125-391 | [»] | |
| 1MUO | X-ray | 2.90 | A | 107-403 | [»] | |
| 1OL5 | X-ray | 2.50 | A | 122-403 | [»] | |
| 1OL6 | X-ray | 3.00 | A | 122-403 | [»] | |
| 1OL7 | X-ray | 2.75 | A | 122-403 | [»] | |
| 2BMC | X-ray | 2.60 | A/B/C/D/E/F | 100-403 | [»] | |
| 2C6D | X-ray | 2.20 | A | 124-398 | [»] | |
| 2C6E | X-ray | 2.10 | A/B | 123-401 | [»] | |
| 2DWB | X-ray | 2.50 | A | 122-403 | [»] | |
| 2J4Z | X-ray | 2.00 | A/B | 100-403 | [»] | |
| 2J50 | X-ray | 3.00 | A/B | 126-403 | [»] | |
| 2NP8 | X-ray | 2.25 | A | 125-391 | [»] | |
| 2W1C | X-ray | 3.24 | A | 122-389 | [»] | |
| 2W1D | X-ray | 2.97 | A | 122-389 | [»] | |
| 2W1E | X-ray | 2.93 | A | 122-389 | [»] | |
| 2W1F | X-ray | 2.85 | A | 122-389 | [»] | |
| 2W1G | X-ray | 2.71 | A | 122-389 | [»] | |
| 2WQE | X-ray | 2.50 | A | 127-388 | [»] | |
| 2WTV | X-ray | 2.40 | A/B/C/D | 122-403 | [»] | |
| 2WTW | X-ray | 3.30 | A | 122-403 | [»] | |
| 2X6D | X-ray | 2.80 | A | 122-403 | [»] | |
| 2X6E | X-ray | 3.35 | A | 122-403 | [»] | |
| 2X81 | X-ray | 2.91 | A | 126-391 | [»] | |
| 2XNE | X-ray | 2.80 | A | 122-392 | [»] | |
| 2XNG | X-ray | 2.60 | A | 122-403 | [»] | |
| 2XRU | X-ray | 2.90 | A | 126-403 | [»] | |
| 3COH | X-ray | 2.70 | A/B | 124-391 | [»] | |
| 3E5A | X-ray | 2.30 | A | 125-391 | [»] | |
| 3EFW | X-ray | 2.29 | A/B | 125-391 | [»] | |
| 3FDN | X-ray | 1.90 | A | 123-401 | [»] | |
| 3H0Y | X-ray | 2.50 | A | 124-391 | [»] | |
| 3H0Z | X-ray | 2.92 | A/B/C | 124-391 | [»] | |
| 3H10 | X-ray | 2.20 | A/B/D | 124-391 | [»] | |
| 3HA6 | X-ray | 2.36 | A | 125-391 | [»] | |
| 3K5U | X-ray | 2.35 | A | 123-401 | [»] | |
| 3LAU | X-ray | 2.10 | A | 125-399 | [»] | |
| 3M11 | X-ray | 2.75 | A | 123-401 | [»] | |
| 3MYG | X-ray | 2.40 | A | 125-391 | [»] | |
| 3NRM | X-ray | 3.05 | A | 126-403 | [»] | |
| 3O50 | X-ray | 2.00 | A/B | 125-391 | [»] | |
| 3O51 | X-ray | 3.20 | A | 125-391 | [»] | |
| 3P9J | X-ray | 2.80 | A | 125-391 | [»] | |
| 3QBN | X-ray | 3.50 | A | 124-403 | [»] | |
| 3R21 | X-ray | 2.90 | A | 126-391 | [»] | |
| 3R22 | X-ray | 2.90 | A | 126-391 | [»] | |
| 3UNZ | X-ray | 2.80 | A/B | 123-401 | [»] | |
| 3UO4 | X-ray | 2.45 | A | 123-401 | [»] | |
| 3UO5 | X-ray | 2.70 | A | 123-401 | [»] | |
| 3UO6 | X-ray | 2.80 | A/B | 123-401 | [»] | |
| 3UOD | X-ray | 2.50 | A | 123-401 | [»] | |
| 3UOH | X-ray | 2.80 | A/B | 123-401 | [»] | |
| 3UOJ | X-ray | 2.90 | A/B | 123-401 | [»] | |
| 3UOK | X-ray | 2.95 | A/B | 123-401 | [»] | |
| 3UOL | X-ray | 2.40 | A/B | 123-401 | [»] | |
| 3UP2 | X-ray | 2.30 | A | 123-401 | [»] | |
| 3UP7 | X-ray | 3.05 | A | 123-401 | [»] | |
| 3VAP | X-ray | 2.66 | A | 125-391 | [»] | |
| 3W10 | X-ray | 2.70 | A | 126-403 | [»] | |
| 3W16 | X-ray | 2.80 | A | 126-403 | [»] | |
| 3W18 | X-ray | 2.50 | A/B | 126-403 | [»] | |
| 3W2C | X-ray | 2.45 | A/C/E/G | 128-388 | [»] | |
| 4B0G | X-ray | 2.50 | A | 122-403 | [»] | |
| 4BN1 | X-ray | 2.50 | A | 122-403 | [»] | |
| 4BYI | X-ray | 2.60 | A | 122-403 | [»] | |
| 4BYJ | X-ray | 2.75 | A | 122-403 | [»] | |
| 4C3P | X-ray | 2.69 | A/D | 122-403 | [»] | |
| 4C3R | X-ray | 2.79 | A | 122-403 | [»] | |
| 4CEG | X-ray | 2.10 | A | 122-403 | [»] | |
| 4DEA | X-ray | 2.45 | A | 123-401 | [»] | |
| 4DEB | X-ray | 3.05 | A | 123-401 | [»] | |
| 4DED | X-ray | 3.05 | A | 123-401 | [»] | |
| 4DEE | X-ray | 2.30 | A | 123-401 | [»] | |
| 4DHF | X-ray | 2.80 | A/B | 126-391 | [»] | |
| 4J8M | X-ray | 1.85 | A | 123-401 | [»] | |
| 4J8N | X-ray | 3.14 | A/B/C/D | 123-401 | [»] | |
| 4JAI | X-ray | 3.20 | A | 122-396 | [»] | |
| 4JAJ | X-ray | 2.70 | A | 122-396 | [»] | |
| 4JBO | X-ray | 2.49 | A | 123-401 | [»] | |
| 4JBP | X-ray | 2.45 | A | 123-401 | [»] | |
| 4JBQ | X-ray | 2.30 | A | 123-401 | [»] | |
| 4O0S | X-ray | 2.50 | A | 122-403 | [»] | |
| 4O0U | X-ray | 2.60 | A | 122-403 | [»] | |
| 4O0W | X-ray | 2.60 | A | 122-403 | [»] | |
| 4PRJ | X-ray | 2.80 | A | 124-391 | [»] | |
| 4UTD | X-ray | 2.36 | A | 122-403 | [»] | |
| 4UYN | X-ray | 1.90 | A | 125-399 | [»] | |
| 4UZD | X-ray | 3.20 | A/B | 125-399 | [»] | |
| 4UZH | X-ray | 2.00 | A | 125-399 | [»] | |
| 4ZS0 | X-ray | 3.00 | A | 122-403 | [»] | |
| 4ZTQ | X-ray | 2.80 | A | 122-403 | [»] | |
| 4ZTR | X-ray | 2.85 | A | 122-403 | [»] | |
| 4ZTS | X-ray | 2.90 | A | 122-403 | [»] | |
| 5AAD | X-ray | 3.10 | A | 122-403 | [»] | |
| 5AAE | X-ray | 3.11 | A | 122-403 | [»] | |
| 5AAF | X-ray | 2.78 | A | 122-403 | [»] | |
| 5AAG | X-ray | 2.85 | A | 122-403 | [»] | |
| 5DN3 | X-ray | 2.05 | A | 125-391 | [»] | |
| 5DNR | X-ray | 1.95 | A | 125-391 | [»] | |
| 5DOS | X-ray | 2.98 | A | 126-390 | [»] | |
| 5DPV | X-ray | 2.29 | A | 126-390 | [»] | |
| 5DR2 | X-ray | 2.46 | A | 128-390 | [»] | |
| 5DR6 | X-ray | 2.53 | A | 126-390 | [»] | |
| 5DR9 | X-ray | 2.47 | A | 126-390 | [»] | |
| 5DRD | X-ray | 2.13 | A | 126-390 | [»] | |
| 5DT0 | X-ray | 2.15 | A | 126-390 | [»] | |
| 5DT3 | X-ray | 2.33 | A | 126-390 | [»] | |
| 5DT4 | X-ray | 2.86 | A | 126-390 | [»] | |
| 5EW9 | X-ray | 2.18 | A | 123-390 | [»] | |
| 5G15 | X-ray | 2.06 | A | 122-403 | [»] | |
| 5G1X | X-ray | 1.72 | A | 122-403 | [»] | |
| 5L8J | X-ray | 1.68 | A | 122-403 | [»] | |
| 5L8K | X-ray | 1.79 | A | 122-403 | [»] | |
| 5L8L | X-ray | 1.67 | A | 122-403 | [»] | |
| 5LXM | X-ray | 2.08 | A | 122-403 | [»] | |
| 5OBJ | X-ray | 2.90 | A | 125-391 | [»] | |
| 5OBR | X-ray | 2.62 | A | 125-391 | [»] | |
| 5ODT | X-ray | 2.02 | A | 122-403 | [»] | |
| 5ONE | X-ray | 2.60 | A | 122-403 | [»] | |
| 5ORL | X-ray | 1.69 | A | 127-391 | [»] | |
| 5ORN | X-ray | 2.19 | A | 127-391 | [»] | |
| 5ORO | X-ray | 2.12 | A | 127-391 | [»] | |
| 5ORP | X-ray | 2.19 | A | 127-391 | [»] | |
| 5ORR | X-ray | 2.09 | A | 127-391 | [»] | |
| 5ORS | X-ray | 1.98 | A | 127-391 | [»] | |
| 5ORT | X-ray | 2.56 | A | 127-391 | [»] | |
| 5ORV | X-ray | 1.88 | A | 127-391 | [»] | |
| 5ORW | X-ray | 2.00 | A | 127-391 | [»] | |
| 5ORX | X-ray | 1.88 | A | 127-391 | [»] | |
| 5ORY | X-ray | 1.99 | A | 127-391 | [»] | |
| 5ORZ | X-ray | 1.92 | A | 127-391 | [»] | |
| 5OS0 | X-ray | 1.74 | A | 127-391 | [»] | |
| 5OS1 | X-ray | 1.90 | A | 127-391 | [»] | |
| 5OS2 | X-ray | 1.92 | A | 127-391 | [»] | |
| 5OS3 | X-ray | 1.81 | A | 127-391 | [»] | |
| 5OS4 | X-ray | 1.88 | A | 127-391 | [»] | |
| 5OS5 | X-ray | 1.74 | A | 125-392 | [»] | |
| 5OS6 | X-ray | 2.20 | A | 127-391 | [»] | |
| 5OSD | X-ray | 1.99 | A | 125-391 | [»] | |
| 5OSE | X-ray | 1.90 | A | 127-391 | [»] | |
| 5OSF | X-ray | 1.89 | A | 127-391 | [»] | |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Domaini | 133 – 383 | Protein kinasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 251 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 280 – 293 | Activation segmentAdd BLAST | 14 |
<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
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
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 | EOG091G0EU2 |
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>Sequencei
<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.
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
<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
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_030840 | 11 | G → R. Corresponds to variant dbSNP:rs6069717Ensembl. | 1 | |
| <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_030841 | 31 | F → I5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_041127 | 50 | P → L1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_030842 | 57 | V → I4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_061745 | 104 | S → L. Corresponds to variant dbSNP:rs2230743Ensembl. | 1 | |
| <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_041128 | 155 | S → R in a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_041129 | 174 | V → M in a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_041130 | 373 | M → V1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
<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>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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O14965 | AURKA isoform 12 | 403 | |||
| Aurora kinase A | 403 | ||||
| UPI0005F4303E | 412 | ||||
| Aurora kinase A | 408 | ||||
| UPI000C29D12C | 406 | ||||
| +95 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O14965 | AURKA isoform 12 | 403 | |||
| Aurora kinase A | 403 | ||||
| UPI0005F4303E | 412 | ||||
| Aurora kinase A | 408 | ||||
| Uncharacterized protein | 406 | ||||
| +227 | |||||
<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: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1MQ4 | X-ray | 1.90 | A | 125-391 | [»] | |
| 1MUO | X-ray | 2.90 | A | 107-403 | [»] | |
| 1OL5 | X-ray | 2.50 | A | 122-403 | [»] | |
| 1OL6 | X-ray | 3.00 | A | 122-403 | [»] | |
| 1OL7 | X-ray | 2.75 | A | 122-403 | [»] | |
| 2BMC | X-ray | 2.60 | A/B/C/D/E/F | 100-403 | [»] | |
| 2C6D | X-ray | 2.20 | A | 124-398 | [»] | |
| 2C6E | X-ray | 2.10 | A/B | 123-401 | [»] | |
| 2DWB | X-ray | 2.50 | A | 122-403 | [»] | |
| 2J4Z | X-ray | 2.00 | A/B | 100-403 | [»] | |
| 2J50 | X-ray | 3.00 | A/B | 126-403 | [»] | |
| 2NP8 | X-ray | 2.25 | A | 125-391 | [»] | |
| 2W1C | X-ray | 3.24 | A | 122-389 | [»] | |
| 2W1D | X-ray | 2.97 | A | 122-389 | [»] | |
| 2W1E | X-ray | 2.93 | A | 122-389 | [»] | |
| 2W1F | X-ray | 2.85 | A | 122-389 | [»] | |
| 2W1G | X-ray | 2.71 | A | 122-389 | [»] | |
| 2WQE | X-ray | 2.50 | A | 127-388 | [»] | |
| 2WTV | X-ray | 2.40 | A/B/C/D | 122-403 | [»] | |
| 2WTW | X-ray | 3.30 | A | 122-403 | [»] | |
| 2X6D | X-ray | 2.80 | A | 122-403 | [»] | |
| 2X6E | X-ray | 3.35 | A | 122-403 | [»] | |
| 2X81 | X-ray | 2.91 | A | 126-391 | [»] | |
| 2XNE | X-ray | 2.80 | A | 122-392 | [»] | |
| 2XNG | X-ray | 2.60 | A | 122-403 | [»] | |
| 2XRU | X-ray | 2.90 | A | 126-403 | [»] | |
| 3COH | X-ray | 2.70 | A/B | 124-391 | [»] | |
| 3E5A | X-ray | 2.30 | A | 125-391 | [»] | |
| 3EFW | X-ray | 2.29 | A/B | 125-391 | [»] | |
| 3FDN | X-ray | 1.90 | A | 123-401 | [»] | |
| 3H0Y | X-ray | 2.50 | A | 124-391 | [»] | |
| 3H0Z | X-ray | 2.92 | A/B/C | 124-391 | [»] | |
| 3H10 | X-ray | 2.20 | A/B/D | 124-391 | [»] | |
| 3HA6 | X-ray | 2.36 | A | 125-391 | [»] | |
| 3K5U | X-ray | 2.35 | A | 123-401 | [»] | |
| 3LAU | X-ray | 2.10 | A | 125-399 | [»] | |
| 3M11 | X-ray | 2.75 | A | 123-401 | [»] | |
| 3MYG | X-ray | 2.40 | A | 125-391 | [»] | |
| 3NRM | X-ray | 3.05 | A | 126-403 | [»] | |
| 3O50 | X-ray | 2.00 | A/B | 125-391 | [»] | |
| 3O51 | X-ray | 3.20 | A | 125-391 | [»] | |
| 3P9J | X-ray | 2.80 | A | 125-391 | [»] | |
| 3QBN | X-ray | 3.50 | A | 124-403 | [»] | |
| 3R21 | X-ray | 2.90 | A | 126-391 | [»] | |
| 3R22 | X-ray | 2.90 | A | 126-391 | [»] | |
| 3UNZ | X-ray | 2.80 | A/B | 123-401 | [»] | |
| 3UO4 | X-ray | 2.45 | A | 123-401 | [»] | |
| 3UO5 | X-ray | 2.70 | A | 123-401 | [»] | |
| 3UO6 | X-ray | 2.80 | A/B | 123-401 | [»] | |
| 3UOD | X-ray | 2.50 | A | 123-401 | [»] | |
| 3UOH | X-ray | 2.80 | A/B | 123-401 | [»] | |
| 3UOJ | X-ray | 2.90 | A/B | 123-401 | [»] | |
| 3UOK | X-ray | 2.95 | A/B | 123-401 | [»] | |
| 3UOL | X-ray | 2.40 | A/B | 123-401 | [»] | |
| 3UP2 | X-ray | 2.30 | A | 123-401 | [»] | |
| 3UP7 | X-ray | 3.05 | A | 123-401 | [»] | |
| 3VAP | X-ray | 2.66 | A | 125-391 | [»] | |
| 3W10 | X-ray | 2.70 | A | 126-403 | [»] | |
| 3W16 | X-ray | 2.80 | A | 126-403 | [»] | |
| 3W18 | X-ray | 2.50 | A/B | 126-403 | [»] | |
| 3W2C | X-ray | 2.45 | A/C/E/G | 128-388 | [»] | |
| 4B0G | X-ray | 2.50 | A | 122-403 | [»] | |
| 4BN1 | X-ray | 2.50 | A | 122-403 | [»] | |
| 4BYI | X-ray | 2.60 | A | 122-403 | [»] | |
| 4BYJ | X-ray | 2.75 | A | 122-403 | [»] | |
| 4C3P | X-ray | 2.69 | A/D | 122-403 | [»] | |
| 4C3R | X-ray | 2.79 | A | 122-403 | [»] | |
| 4CEG | X-ray | 2.10 | A | 122-403 | [»] | |
| 4DEA | X-ray | 2.45 | A | 123-401 | [»] | |
| 4DEB | X-ray | 3.05 | A | 123-401 | [»] | |
| 4DED | X-ray | 3.05 | A | 123-401 | [»] | |
| 4DEE | X-ray | 2.30 | A | 123-401 | [»] | |
| 4DHF | X-ray | 2.80 | A/B | 126-391 | [»] | |
| 4J8M | X-ray | 1.85 | A | 123-401 | [»] | |
| 4J8N | X-ray | 3.14 | A/B/C/D | 123-401 | [»] | |
| 4JAI | X-ray | 3.20 | A | 122-396 | [»] | |
| 4JAJ | X-ray | 2.70 | A | 122-396 | [»] | |
| 4JBO | X-ray | 2.49 | A | 123-401 | [»] | |
| 4JBP | X-ray | 2.45 | A | 123-401 | [»] | |
| 4JBQ | X-ray | 2.30 | A | 123-401 | [»] | |
| 4O0S | X-ray | 2.50 | A | 122-403 | [»] | |
| 4O0U | X-ray | 2.60 | A | 122-403 | [»] | |
| 4O0W | X-ray | 2.60 | A | 122-403 | [»] | |
| 4PRJ | X-ray | 2.80 | A | 124-391 | [»] | |
| 4UTD | X-ray | 2.36 | A | 122-403 | [»] | |
| 4UYN | X-ray | 1.90 | A | 125-399 | [»] | |
| 4UZD | X-ray | 3.20 | A/B | 125-399 | [»] | |
| 4UZH | X-ray | 2.00 | A | 125-399 | [»] | |
| 4ZS0 | X-ray | 3.00 | A | 122-403 | [»] | |
| 4ZTQ | X-ray | 2.80 | A | 122-403 | [»] | |
| 4ZTR | X-ray | 2.85 | A | 122-403 | [»] | |
| 4ZTS | X-ray | 2.90 | A | 122-403 | [»] | |
| 5AAD | X-ray | 3.10 | A | 122-403 | [»] | |
| 5AAE | X-ray | 3.11 | A | 122-403 | [»] | |
| 5AAF | X-ray | 2.78 | A | 122-403 | [»] | |
| 5AAG | X-ray | 2.85 | A | 122-403 | [»] | |
| 5DN3 | X-ray | 2.05 | A | 125-391 | [»] | |
| 5DNR | X-ray | 1.95 | A | 125-391 | [»] | |
| 5DOS | X-ray | 2.98 | A | 126-390 | [»] | |
| 5DPV | X-ray | 2.29 | A | 126-390 | [»] | |
| 5DR2 | X-ray | 2.46 | A | 128-390 | [»] | |
| 5DR6 | X-ray | 2.53 | A | 126-390 | [»] | |
| 5DR9 | X-ray | 2.47 | A | 126-390 | [»] | |
| 5DRD | X-ray | 2.13 | A | 126-390 | [»] | |
| 5DT0 | X-ray | 2.15 | A | 126-390 | [»] | |
| 5DT3 | X-ray | 2.33 | A | 126-390 | [»] | |
| 5DT4 | X-ray | 2.86 | A | 126-390 | [»] | |
| 5EW9 | X-ray | 2.18 | A | 123-390 | [»] | |
| 5G15 | X-ray | 2.06 | A | 122-403 | [»] | |
| 5G1X | X-ray | 1.72 | A | 122-403 | [»] | |
| 5L8J | X-ray | 1.68 | A | 122-403 | [»] | |
| 5L8K | X-ray | 1.79 | A | 122-403 | [»] | |
| 5L8L | X-ray | 1.67 | A | 122-403 | [»] | |
| 5LXM | X-ray | 2.08 | A | 122-403 | [»] | |
| 5OBJ | X-ray | 2.90 | A | 125-391 | [»] | |
| 5OBR | X-ray | 2.62 | A | 125-391 | [»] | |
| 5ODT | X-ray | 2.02 | A | 122-403 | [»] | |
| 5ONE | X-ray | 2.60 | A | 122-403 | [»] | |
| 5ORL | X-ray | 1.69 | A | 127-391 | [»] | |
| 5ORN | X-ray | 2.19 | A | 127-391 | [»] | |
| 5ORO | X-ray | 2.12 | A | 127-391 | [»] | |
| 5ORP | X-ray | 2.19 | A | 127-391 | [»] | |
| 5ORR | X-ray | 2.09 | A | 127-391 | [»] | |
| 5ORS | X-ray | 1.98 | A | 127-391 | [»] | |
| 5ORT | X-ray | 2.56 | A | 127-391 | [»] | |
| 5ORV | X-ray | 1.88 | A | 127-391 | [»] | |
| 5ORW | X-ray | 2.00 | A | 127-391 | [»] | |
| 5ORX | X-ray | 1.88 | A | 127-391 | [»] | |
| 5ORY | X-ray | 1.99 | A | 127-391 | [»] | |
| 5ORZ | X-ray | 1.92 | A | 127-391 | [»] | |
| 5OS0 | X-ray | 1.74 | A | 127-391 | [»] | |
| 5OS1 | X-ray | 1.90 | A | 127-391 | [»] | |
| 5OS2 | X-ray | 1.92 | A | 127-391 | [»] | |
| 5OS3 | X-ray | 1.81 | A | 127-391 | [»] | |
| 5OS4 | X-ray | 1.88 | A | 127-391 | [»] | |
| 5OS5 | X-ray | 1.74 | A | 125-392 | [»] | |
| 5OS6 | X-ray | 2.20 | A | 127-391 | [»] | |
| 5OSD | X-ray | 1.99 | A | 125-391 | [»] | |
| 5OSE | X-ray | 1.90 | A | 127-391 | [»] | |
| 5OSF | X-ray | 1.89 | A | 127-391 | [»] | |
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... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112666, 329 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, 123 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 |
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 |
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 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | AURKA |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | 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 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 6790 |
| Structural Biology Knowledgebase | Search... |
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 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6790 |
DisGeNET More...DisGeNETi | 6790 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000087586.17 |
GeneCards: human genes, protein and diseases More...GeneCardsi | AURKA |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0015930 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11393 AURKA |
Human Protein Atlas More...HPAi | CAB001454 HPA002636 |
MalaCards human disease database More...MalaCardsi | AURKA |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 603072 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O14965 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36201 |
GenAtlas: human gene database More...GenAtlasi | Search... |
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 | EOG091G0EU2 |
Database for complete collections of gene phylogenies More...PhylomeDBi | O14965 |
TreeFam database of animal gene trees More...TreeFami | TF105331 |
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 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | AURKA human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | O14965 |
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
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000087586 |
CleanEx database of gene expression profiles More...CleanExi | HS_AURKA |
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 |
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 |
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 namei | AURKA_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>Accessioni | O14965Primary (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 historyi | Integrated into UniProtKB/Swiss-Prot: | January 27, 2003 |
| Last sequence update: | January 27, 2003 | |
| Last modified: | June 20, 2018 | |
| This is version 209 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 20
Human chromosome 20: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human and mouse protein kinases
Human and mouse protein kinases: classification and index - SIMILARITY comments
Index of protein domains and families
