AURKA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AURKA_MOUSE
• UniProt AC: P97477
• Protein Name: Aurora kinase A
• Gene Name: Aurka
• Organism: Mus musculus (Mouse).
• Sequence Length: 395
• Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Localizes on cen
• Protein Description: 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 stabilizing p53/TP53. Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity. Necessary for proper cilia disassembly prior to mitosis..
• Protein Sequence: MDRCKENCVSRPVKTTVPFGPKRVLVTEQIPSQNLGSASSGQAQRVLCPSNSQRVPSQAQKLGAGQKPAPKQLPAASVPRPVSRLNNPQKNEQPAASGNDSEKEQASLQKTEDTKKRQWTLEDFDIGRPLGKGKFGNVYLARERQSKFILALKVLFKTQLEKANVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSNGELKIADFGWSVHAPSSRRTTMCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGMPPFEAHTYQETYRRISRVEFTFPDFVTEGARDLISRLLKHNASQRLTLAEVLEHPWIKANSSKPPTGHTSKEPTSKSS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
40	Phosphorylation	QNLGSASSGQAQRVL CCCCCCCCCCCCEEE	34.34	-
50	Phosphorylation	AQRVLCPSNSQRVPS CCEEECCCCCCCCCH	48.38	-
274	Phosphorylation	GWSVHAPSSRRTTMC CEEEECCCCCCCCCC	36.94	20531401
275	Phosphorylation	WSVHAPSSRRTTMCG EEEECCCCCCCCCCC	25.40	20531401
278	Phosphorylation	HAPSSRRTTMCGTLD ECCCCCCCCCCCCCC	20.12	-
279	Phosphorylation	APSSRRTTMCGTLDY CCCCCCCCCCCCCCC	14.51	25266776
283	Phosphorylation	RRTTMCGTLDYLPPE CCCCCCCCCCCCCHH	16.13	28066266
333	Phosphorylation	QETYRRISRVEFTFP HHHHHHHCCEEECCC	28.58	-
356	Acetylation	DLISRLLKHNASQRL HHHHHHHHCCHHHCC	39.13	22902405

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
333	S	Phosphorylation	Kinase	PKA	-	Uniprot
333	S	Phosphorylation	Kinase	PAK	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Chfr	Q810L3	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	Fbxl7	Q5BJ29	PMID:22306998

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
52	S	Phosphorylation	PPP2CA controls degradation by dephosphorylating Ser-52 at the end of mitosis (By similarity).	-
279	T	Phosphorylation	Activated by phosphorylation at Thr-279; this brings about a change in the conformation of the activation segment (By similarity).	-
279	T	Phosphorylation	Autophosphorylated at Thr-279 upon TPX2 binding (By similarity).	-
279	T	Phosphorylation	Phosphorylation at Thr-279 varies during the cell cycle and is highest during M phase (By similarity).	-
279	T	Phosphorylation	Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-279 during mitosis (By similarity).	-
279	T	Phosphorylation	Thr-279 can be phosphorylated by several kinases, including PAK and PKA (By similarity).	-
333	S	Phosphorylation	Phosphorylation at Ser-333 decreases the kinase activity (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of AURKA_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIR2_MOUSE	Sirt2	physical	22014574
SRC8_MOUSE	Cttn	physical	24574519
CASL_MOUSE	Nedd9	physical	24574519

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.