Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Aurora kinase A  

UniProtKB / Swiss-Prot ID :  AURKA_HUMAN

Gene Name (Synonyms) : 
AURKASynonyms=AIK, AIRK1, ARK1, AURA, AYK1, BTAK, IAK1, STK15, STK6  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton, centrosome. Cytoplasm, cytoskeleton, spindle pole. 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 t 

Protein Function :  Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for initial activation of CDK1 at centrosomes. Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2. Regulates KIF2A tubulin depolymerase activity. Required for normal axon formation. Plays a role in microtubule remodeling during neurite extension. Important for microtubule formation and/or stabilization. Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and stabilizating p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis. 

Protein Sequence MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRVPLQAQKLVSSHKP...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
11G -> R (in dbSNP:rs6069717). VAR_030840
31F -> I (in dbSNP:rs2273535). VAR_030841
50P -> L (in dbSNP:rs34572020). VAR_041127
57V -> I (in dbSNP:rs1047972). VAR_030842
104S -> L (in dbSNP:rs2230743). VAR_061745
155S -> R (in a colorectal adenocarcinomasample; somatic mutation; reduces
174V -> M (in a metastatic melanoma sample;somatic mutation; constitutively enhanced
373M -> V (in dbSNP:rs33923703). VAR_041130
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
4Phosphoserine-MDRSKENC
-
39.80HPRD
Link-
10PhosphoserineENCISGPVK
38.96Phosphositeplus
Link-
10Phosphoserine (Aurora A)ENCISGPVK
38.96PhosphoELM
Link-
16PhosphothreoninePVKATAPVG
26.27Phosphositeplus
Link-
16Phosphothreonine (Aurora A)PVKATAPVG
26.27PhosphoELM
Link-
41PhosphoserineLPVNSGQAQ
32.30HPRD
Link-
41PhosphoserineLPVNSGQAQ
32.30Phosphositeplus
Link-
41PhosphoserineLPVNSGQAQ
32.30SysPTM
Link-
41Phosphoserine (Aurora A)LPVNSGQAQ
32.30PhosphoELM
Link-
41Phosphoserine.LPVNSGQAQ
32.30UniProtKB
Link-
51PhosphoserineVLCPSNSSQ
48.63HPRD
Link-
51PhosphoserineVLCPSNSSQ
48.63Phosphositeplus
Link-
51PhosphoserineVLCPSNSSQ
48.63SysPTM
Link-
51Phosphoserine.VLCPSNSSQ
48.63UniProtKB
Link-
53PhosphoserineCPSNSSQRV
31.99HPRD
Link-
53Phosphoserine.CPSNSSQRV
31.99UniProtKB
Link-
66PhosphoserineQKLVSSHKP
36.84HPRD
Link-
67PhosphoserineKLVSSHKPV
28.22Phosphositeplus
Link-
67Phosphoserine (Aurora A)KLVSSHKPV
28.22PhosphoELM
Link-
83PhosphoserineLQATSVPHP
36.35HPRD
Link-
83PhosphoserineLQATSVPHP
36.35Phosphositeplus
Link-
83PhosphoserineLQATSVPHP
36.35SysPTM
Link-
83Phosphoserine (Aurora A)LQATSVPHP
36.35PhosphoELM
Link-
83Phosphoserine.LQATSVPHP
36.35UniProtKB
Link-
89PhosphoserinePHPVSRPLN
32.41Phosphositeplus
Link-
98PhosphoserineNTQKSKQPL
27.06Phosphositeplus
Link-
98Phosphoserine (Aurora A)NTQKSKQPL
27.06PhosphoELM
Link-
104PhosphoserineQPLPSAPEN
65.23Phosphositeplus
Link-
104Phosphoserine (Aurora A)QPLPSAPEN
65.23PhosphoELM
Link-
116PhosphoserineEELASKQKN
48.52HPRD
Link-
116PhosphoserineEELASKQKN
48.52Phosphositeplus
Link-
148PhosphotyrosineFGNVYLARE
9.92PhosphoELM
Link
148PhosphotyrosineFGNVYLARE
9.92Phosphositeplus
Link
197PhosphotyrosineILRLYGYFH
11.89Phosphositeplus
Link
199PhosphotyrosineRLYGYFHDA
5.56Phosphositeplus
Link
212PhosphotyrosineLILEYAPLG
15.29Phosphositeplus
Link
226PhosphoserineLQKLSKFDE
38.01Phosphositeplus
Link
226Phosphoserine (Aurora A)LQKLSKFDE
38.01PhosphoELM
Link
266PhosphoserineLLLGSAGEL
32.82Phosphositeplus
Link
266Phosphoserine (Aurora A)LLLGSAGEL
32.82PhosphoELM
Link
278PhosphoserineDFGWSVHAP
12.38Phosphositeplus
Link
278Phosphoserine (Aurora A)DFGWSVHAP
12.38PhosphoELM
Link
284PhosphoserineHAPSSRRTT
25.40Phosphositeplus
Link
287PhosphothreonineSSRRTTLCG
24.02HPRD
Link
287PhosphothreonineSSRRTTLCG
24.02Phosphositeplus
Link
287Phosphothreonine (Aurora A)SSRRTTLCG
24.02PhosphoELM
Link
287Phosphothreonine.SSRRTTLCG
24.02UniProtKB
Link
288PhosphothreonineSRRTTLCGT
20.45Phosphositeplus
Link
288Phosphothreonine (PKA_group;Aurora A)SRRTTLCGT
20.45PhosphoELM
Link
288Phosphothreonine (PRKACA)SRRTTLCGT
20.45HPRD
Link
288Phosphothreonine.SRRTTLCGT
20.45UniProtKB
Link
292PhosphothreonineTLCGTLDYL
18.56Phosphositeplus
Link
342PhosphoserineYKRISRVEF
34.02Phosphositeplus
Link
342Phosphoserine (Aurora A)YKRISRVEF
34.02PhosphoELM
Link
342Phosphoserine; by PKA and PAK.YKRISRVEF
34.02UniProtKB
Link
369PhosphoserineKHNPSQRPM
44.10HPRD
Link
369PhosphoserineKHNPSQRPM
44.10PhosphoELM
Link
369PhosphoserineKHNPSQRPM
44.10Phosphositeplus
Link
369Phosphoserine.KHNPSQRPM
44.10UniProtKB
Link
391PhosphoserineSSKPSNCQN
54.71Phosphositeplus
Link-
391Phosphoserine (Aurora A)SSKPSNCQN
54.71PhosphoELM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The mitotic serine/threonine kinase Aurora2/AIK is regulated byphosphorylation and degradation.";
Walter A.O., Seghezzi W., Korver W., Sheung J., Lees E.;
Oncogene 19:4906-4916(2000).
Cited for: FUNCTION, PHOSPHORYLATION AT THR-288, MUTAGENESIS OF THR-288,UBIQUITINATION, AND ENZYME REGULATION.
"Aurora-A and an interacting activator, the LIM protein Ajuba, arerequired 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).
Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-288.
"BRCA1 phosphorylation by Aurora-A in the regulation of G2 to Mtransition.";
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).
Cited for: FUNCTION, INTERACTION WITH BRCA1, PHOSPHORYLATION AT THR-288, ANDMUTAGENESIS OF LYS-162.
"The GIT-associated kinase PAK targets to the centrosome and regulatesAurora-A.";
Zhao Z.S., Lim J.P., Ng Y.W., Lim L., Manser E.;
Mol. Cell 20:237-249(2005).
Cited for: PHOSPHORYLATION AT THR-288 AND SER-342.
"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).
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PPP2CA, AND PHOSPHORYLATION ATSER-51.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-51 AND SER-83,AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND MASSSPECTROMETRY.
"An essential role of the aPKC-Aurora A-NDEL1 pathway in neuriteelongation 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).
Cited for: FUNCTION, INTERACTION WITH TPX2, PHOSPHORYLATION AT THR-287 ANDTHR-288, AND MUTAGENESIS OF THR287.
"Structural basis of Aurora-A activation by TPX2 at the mitoticspindle.";
Bayliss R., Sardon T., Vernos I., Conti E.;
Mol. Cell 12:851-862(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 122-403 IN COMPLEX WITH TPX2,MUTAGENESIS OF ASP-274, ACTIVE SITE, AND PHOSPHORYLATION AT THR-287AND THR-288.
"Modulation of kinase-inhibitor interactions by auxiliary proteinbinding: crystallography studies on Aurora A interactions with VX-680and 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).
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-391 IN COMPLEX WITHVX-680 AND TPX2, PHOSPHORYLATION AT THR-288, MASS SPECTROMETRY, ANDSUBUNIT.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures