dbPTM

AURKA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AURKA_HUMAN
UniProt AC	O14965
Protein Name	Aurora kinase A
Gene Name	AURKA
Organism	Homo sapiens (Human).
Sequence Length	403
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Detected at the
Protein Description	Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Required for 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	MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRVPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MDRSKENCISG ----CCCCCCCCCCC	39.80	18691976
5	Ubiquitination	---MDRSKENCISGP ---CCCCCCCCCCCC	54.57	24816145
10	Phosphorylation	RSKENCISGPVKATA CCCCCCCCCCCEEEC	38.96	16083426
14	Ubiquitination	NCISGPVKATAPVGG CCCCCCCEEECCCCC	43.06	33845483
16	Phosphorylation	ISGPVKATAPVGGPK CCCCCEEECCCCCCC	26.27	16083426
23	Ubiquitination	TAPVGGPKRVLVTQQ ECCCCCCCEEEEEEE	59.41	29967540
39	Ubiquitination	PCQNPLPVNSGQAQR CCCCCCCCCCCCCCE	13.51	24816145
41	Phosphorylation	QNPLPVNSGQAQRVL CCCCCCCCCCCCEEE	32.30	16083426
51	Phosphorylation	AQRVLCPSNSSQRVP CCEEECCCCCCCCCC	48.63	17895985
53	Phosphorylation	RVLCPSNSSQRVPLQ EEECCCCCCCCCCCH	31.99	18691976
54	Phosphorylation	VLCPSNSSQRVPLQA EECCCCCCCCCCCHH	26.68	29214152
63	Acetylation	RVPLQAQKLVSSHKP CCCCHHHHHHHCCCC	54.60	26051181
66	Phosphorylation	LQAQKLVSSHKPVQN CHHHHHHHCCCCCCC	36.84	18691976
67	Phosphorylation	QAQKLVSSHKPVQNQ HHHHHHHCCCCCCCH	28.22	16083426
69	Ubiquitination	QKLVSSHKPVQNQKQ HHHHHCCCCCCCHHH	49.16	-
82	Phosphorylation	KQKQLQATSVPHPVS HHHHHHHCCCCCCCC	19.80	21406692
83	Phosphorylation	QKQLQATSVPHPVSR HHHHHHCCCCCCCCC	36.35	16083426
89	Phosphorylation	TSVPHPVSRPLNNTQ CCCCCCCCCCCCCCC	32.41	22451695
95	Phosphorylation	VSRPLNNTQKSKQPL CCCCCCCCCCCCCCC	35.98	28555341
98	Phosphorylation	PLNNTQKSKQPLPSA CCCCCCCCCCCCCCC	27.06	16083426
99	Ubiquitination	LNNTQKSKQPLPSAP CCCCCCCCCCCCCCC	64.07	29967540
104	Phosphorylation	KSKQPLPSAPENNPE CCCCCCCCCCCCCHH	65.23	16083426
116	Phosphorylation	NPEEELASKQKNEES CHHHHHHHHHCCHHH	48.52	20068231
117	Ubiquitination	PEEELASKQKNEESK HHHHHHHHHCCHHHH	60.73	29967540
141	Ubiquitination	EIGRPLGKGKFGNVY CCCCCCCCCCCCCEE	67.61	32015554
143	Ubiquitination	GRPLGKGKFGNVYLA CCCCCCCCCCCEEEE	54.29	27667366
143	Acetylation	GRPLGKGKFGNVYLA CCCCCCCCCCCEEEE	54.29	25953088
148	Phosphorylation	KGKFGNVYLAREKQS CCCCCCEEEECHHHH	9.92	17192257
171	Ubiquitination	LFKAQLEKAGVEHQL HHHHHHHHCCCCHHH	60.06	33845483
175	Ubiquitination	QLEKAGVEHQLRREV HHHHCCCCHHHHHHH	25.62	22817900
177	Ubiquitination	EKAGVEHQLRREVEI HHCCCCHHHHHHHHH	24.14	27667366
197	Phosphorylation	HPNILRLYGYFHDAT CCCHHHHEEEECCCC	11.89	22817900
199	Phosphorylation	NILRLYGYFHDATRV CHHHHEEEECCCCEE	5.56	22817900
212	Phosphorylation	RVYLILEYAPLGTVY EEEEEEECCCHHHHH	15.29	22817900
226	Phosphorylation	YRELQKLSKFDEQRT HHHHHHHHCCCHHHH	38.01	16083426
227	Ubiquitination	RELQKLSKFDEQRTA HHHHHHHCCCHHHHH	68.24	29967540
250	Ubiquitination	ALSYCHSKRVIHRDI HHHHHHCCCEECCCC	27.33	21963094
258	Acetylation	RVIHRDIKPENLLLG CEECCCCCHHHEECC	51.04	26051181
258	Sumoylation	RVIHRDIKPENLLLG CEECCCCCHHHEECC	51.04	28112733
258	Ubiquitination	RVIHRDIKPENLLLG CEECCCCCHHHEECC	51.04	22817900
266	Phosphorylation	PENLLLGSAGELKIA HHHEECCCCCEEEEE	32.82	16083426
278	Phosphorylation	KIADFGWSVHAPSSR EEEECCEEEECCCCC	12.38	16083426
284	Ubiquitination	WSVHAPSSRRTTLCG EEEECCCCCCCCCCC	25.40	21963094
284	Phosphorylation	WSVHAPSSRRTTLCG EEEECCCCCCCCCCC	25.40	16785988
287	Phosphorylation	HAPSSRRTTLCGTLD ECCCCCCCCCCCCCC	24.02	19668197
288	Phosphorylation	APSSRRTTLCGTLDY CCCCCCCCCCCCCCC	20.45	16785988
292	Ubiquitination	RRTTLCGTLDYLPPE CCCCCCCCCCCCCHH	18.56	22817900
292	Phosphorylation	RRTTLCGTLDYLPPE CCCCCCCCCCCCCHH	18.56	22322096
295	Phosphorylation	TLCGTLDYLPPEMIE CCCCCCCCCCHHHHC	24.99	24732914
342	Phosphorylation	QETYKRISRVEFTFP HHHHHHHHCEEEECC	34.02	16762494
369	Phosphorylation	RLLKHNPSQRPMLRE HHHHCCHHHCHHHHH	44.10	17525332
389	Acetylation	WITANSSKPSNCQNK CCCCCCCCCCCCCCH	52.89	26051181
391	Phosphorylation	TANSSKPSNCQNKES CCCCCCCCCCCCHHH	54.71	16083426

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
10	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
16	T	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
41	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
67	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
83	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
98	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
104	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
148	Y	Phosphorylation	Kinase	AURKA	O14965	GPS
148	Y	Phosphorylation	Kinase	SRC	P12931	PSP
226	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
266	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
278	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
287	T	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
288	T	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
288	T	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
288	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
288	T	Phosphorylation	Kinase	PAK1	Q13153	PSP
288	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
288	T	Phosphorylation	Kinase	CHUK	O15111	GPS
342	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
342	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
342	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
342	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
342	S	Phosphorylation	Kinase	PKA	-	Uniprot
342	S	Phosphorylation	Kinase	PAK	-	Uniprot
391	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL7	Q9UJT9	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:16863506
-	K	Ubiquitination	E3 ubiquitin ligase	CHFR	Q96EP1	PMID:18335050
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:12023018
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL18	O94889	PMID:23213400

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
51	S	Phosphorylation	17229885
PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis.
288	T	Phosphorylation	11039908
Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment.
288	T	Phosphorylation	11039908
Autophosphorylated at Thr-288 upon TPX2 binding.
288	T	Phosphorylation	11039908
Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase.
288	T	Phosphorylation	11039908
Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis.
288	T	Phosphorylation	11039908
Thr-288 can be phosphorylated by several kinases, including PAK and PKA.
342	S	Phosphorylation	16246726
Phosphorylation at Ser-342 decreases the kinase activity.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of AURKA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAB10_HUMAN	RAB10	physical	17353931
CDN2A_HUMAN	CDKN2A	physical	17353931
ARF_HUMAN	CDKN2A	physical	17353931
SODM_HUMAN	SOD2	physical	17353931
UB2L3_HUMAN	UBE2L3	physical	17353931
BRCA1_HUMAN	BRCA1	physical	14990569
NIN_HUMAN	NIN	physical	12927815
UBE2N_HUMAN	UBE2N	physical	12881723
MBD3_HUMAN	MBD3	physical	12354758
NDKA_HUMAN	NME1	physical	12490715
P53_HUMAN	TP53	physical	12198151
P53_HUMAN	TP53	genetic	12198151
TPX2_HUMAN	TPX2	physical	12177045
CHFR_HUMAN	CHFR	physical	18592005
KIF2C_HUMAN	KIF2C	physical	18434591
INCE_HUMAN	INCENP	physical	18773538
TPX2_HUMAN	TPX2	physical	18773538
PLK1_HUMAN	PLK1	physical	18773538
P53_HUMAN	TP53	physical	14702041
TLK1_HUMAN	TLK1	physical	17940067
TLK2_HUMAN	TLK2	physical	17940067
HDAC6_HUMAN	HDAC6	physical	17604723
HDAC2_HUMAN	HDAC2	physical	17604723
RASF1_HUMAN	RASSF1	physical	21874044
MYCN_HUMAN	MYCN	physical	19111882
PUM2_HUMAN	PUM2	physical	21589936
AURKA_HUMAN	AURKA	physical	20360068
CALU_HUMAN	CALU	physical	20360068
TPX2_HUMAN	TPX2	physical	20360068
H31T_HUMAN	HIST3H3	physical	21554500
LATS2_HUMAN	LATS2	physical	21822051
UBP2_HUMAN	USP2	physical	21890637
AP2A_HUMAN	TFAP2A	physical	21829699
CP131_HUMAN	CEP131	physical	17452972
GSK3B_HUMAN	GSK3B	physical	22513362
FBXW7_HUMAN	FBXW7	physical	22513362
HMMR_HUMAN	HMMR	physical	22110403
TPX2_HUMAN	TPX2	physical	22110403
BRCA1_HUMAN	BRCA1	physical	22110403
PML_HUMAN	PML	physical	15749021
MARE1_HUMAN	MAPRE1	physical	19696028
MARE2_HUMAN	MAPRE2	physical	19696028
MARE3_HUMAN	MAPRE3	physical	19696028
LATS2_HUMAN	LATS2	physical	15147269
ARPC2_HUMAN	ARPC2	physical	20603326
ARC1B_HUMAN	ARPC1B	physical	20603326
TBG1_HUMAN	TUBG1	physical	20603326
H31T_HUMAN	HIST3H3	physical	20603326
TPX2A_XENLA	tpx2-a	physical	20603326
PP1A_HUMAN	PPP1CA	physical	11551964
PP1B_HUMAN	PPP1CB	physical	11551964
PP1G_HUMAN	PPP1CC	physical	11551964
CASB_HUMAN	CSN2	physical	11551964
A4_HUMAN	APP	physical	21832049
SYTC_HUMAN	TARS	physical	22939629
P73_HUMAN	TP73	physical	22340593
TACC1_HUMAN	TACC1	physical	14602875
TACC3_HUMAN	TACC3	physical	14602875
NDC80_HUMAN	NDC80	physical	14602875
NUF2_HUMAN	NUF2	physical	14602875
AURKA_HUMAN	AURKA	physical	14602875
IKKB_HUMAN	IKBKB	physical	17939994
IKKA_HUMAN	CHUK	physical	17939994
NEMO_HUMAN	IKBKG	physical	17939994
FBW1A_HUMAN	BTRC	physical	17939994
TPX2_HUMAN	TPX2	physical	19357306
H31T_HUMAN	HIST3H3	physical	19357306
BIRC5_HUMAN	BIRC5	physical	19357306
INCE_HUMAN	INCENP	physical	19357306
GEMI_HUMAN	GMNN	physical	23695679
CBX3_HUMAN	CBX3	physical	23829974
MDM2_HUMAN	MDM2	physical	24240108
GSK3B_HUMAN	GSK3B	physical	23204235
VHL_HUMAN	VHL	physical	23785518
P53_HUMAN	TP53	physical	23201157
PP6R3_HUMAN	PPP6R3	physical	23443559
GRP78_HUMAN	HSPA5	physical	23443559
PPP6_HUMAN	PPP6C	physical	23443559
TCAL4_HUMAN	TCEAL4	physical	23443559
HS90B_HUMAN	HSP90AB1	physical	23443559
SORL_HUMAN	SORL1	physical	23443559
TBB5_HUMAN	TUBB	physical	23443559
RS19_HUMAN	RPS19	physical	23443559
ROA1_HUMAN	HNRNPA1	physical	23443559
RS3_HUMAN	RPS3	physical	23443559
RLA0_HUMAN	RPLP0	physical	23443559
CH60_HUMAN	HSPD1	physical	23443559
PRC2C_HUMAN	PRRC2C	physical	23443559
RS14_HUMAN	RPS14	physical	23443559
NPM_HUMAN	NPM1	physical	23443559
RS16_HUMAN	RPS16	physical	23443559
TBA1C_HUMAN	TUBA1C	physical	23443559
HSP72_HUMAN	HSPA2	physical	23443559
DHX9_HUMAN	DHX9	physical	23443559
TBB4B_HUMAN	TUBB4B	physical	23443559
FRIH_HUMAN	FTH1	physical	23443559
RS4X_HUMAN	RPS4X	physical	23443559
MFAP4_HUMAN	MFAP4	physical	23443559
RL30_HUMAN	RPL30	physical	23443559
DICER_HUMAN	DICER1	physical	23443559
SYEP_HUMAN	EPRS	physical	23443559
EF1A2_HUMAN	EEF1A2	physical	23443559
RS3A_HUMAN	RPS3A	physical	23443559
USP9X_HUMAN	USP9X	physical	23443559
ILF3_HUMAN	ILF3	physical	23443559
RL22_HUMAN	RPL22	physical	23443559
RT22_HUMAN	MRPS22	physical	23443559
RS5_HUMAN	RPS5	physical	23443559
PSA1_HUMAN	PSMA1	physical	23443559
HNRPU_HUMAN	HNRNPU	physical	23443559
RL38_HUMAN	RPL38	physical	23443559
RL23_HUMAN	RPL23	physical	23443559
LYSC_HUMAN	LYZ	physical	23443559
HSP7C_HUMAN	HSPA8	physical	23443559
CEP55_HUMAN	CEP55	physical	23443559
FRIL_HUMAN	FTL	physical	23443559
UBB_HUMAN	UBB	physical	23443559
NUCL_HUMAN	NCL	physical	23443559
CSK21_HUMAN	CSNK2A1	physical	23443559
TIF1B_HUMAN	TRIM28	physical	23443559
GRP75_HUMAN	HSPA9	physical	23443559
LPPRC_HUMAN	LRPPRC	physical	23443559
DGC14_HUMAN	DGCR14	physical	23443559
PSB5_HUMAN	PSMB5	physical	23443559
PP6R2_HUMAN	PPP6R2	physical	23443559
SYIC_HUMAN	IARS	physical	23443559
LARP1_HUMAN	LARP1	physical	23443559
RS10_HUMAN	RPS10	physical	23443559
SRP09_HUMAN	SRP9	physical	23443559
DDX5_HUMAN	DDX5	physical	23443559
ROA2_HUMAN	HNRNPA2B1	physical	23443559
SKP1_HUMAN	SKP1	physical	23443559
RL12_HUMAN	RPL12	physical	23443559
RL27_HUMAN	RPL27	physical	23443559
PSA5_HUMAN	PSMA5	physical	23443559
PSA6_HUMAN	PSMA6	physical	23443559
PYRG1_HUMAN	CTPS1	physical	23443559
IF2B1_HUMAN	IGF2BP1	physical	23443559
IF2B3_HUMAN	IGF2BP3	physical	23443559
YBOX1_HUMAN	YBX1	physical	23443559
MATR3_HUMAN	MATR3	physical	23443559
EF1A1_HUMAN	EEF1A1	physical	23443559
ZSWM8_HUMAN	ZSWIM8	physical	23443559
PDCD6_HUMAN	PDCD6	physical	23443559
IRS4_HUMAN	IRS4	physical	23443559
RS27_HUMAN	RPS27	physical	23443559
DDB1_HUMAN	DDB1	physical	23443559
MK06_HUMAN	MAPK6	physical	23443559
PIMT_HUMAN	PCMT1	physical	23443559
RL11_HUMAN	RPL11	physical	23443559
PSB7_HUMAN	PSMB7	physical	23443559
UQCC2_HUMAN	UQCC2	physical	23443559
CDC37_HUMAN	CDC37	physical	23443559
ILF2_HUMAN	ILF2	physical	23443559
RM24_HUMAN	MRPL24	physical	23443559
HS90A_HUMAN	HSP90AA1	physical	23443559
CTND1_HUMAN	CTNND1	physical	23443559
DCAF7_HUMAN	DCAF7	physical	23443559
ATD3B_HUMAN	ATAD3B	physical	23443559
NCOR2_HUMAN	NCOR2	physical	23443559
TCAL2_HUMAN	TCEAL2	physical	23443559
RS11_HUMAN	RPS11	physical	23443559
SC61G_HUMAN	SEC61G	physical	23443559
RLA2_HUMAN	RPLP2	physical	23443559
DHX9_HUMAN	DHX9	physical	25852190
PP6R2_HUMAN	PPP6R2	physical	26186194
AMER1_HUMAN	AMER1	physical	26186194
REL_HUMAN	REL	physical	26186194
DICER_HUMAN	DICER1	physical	26186194
SNX9_HUMAN	SNX9	physical	26186194
TPX2_HUMAN	TPX2	physical	26186194
TNR6C_HUMAN	TNRC6C	physical	26186194
TACC3_HUMAN	TACC3	physical	26186194
SORL_HUMAN	SORL1	physical	26186194
SCYL1_HUMAN	SCYL1	physical	26186194
CACO1_HUMAN	CALCOCO1	physical	26186194
HTR5B_HUMAN	HEATR5B	physical	26186194
TTC4_HUMAN	TTC4	physical	26186194
SH3G1_HUMAN	SH3GL1	physical	26186194
WDR62_HUMAN	WDR62	physical	26186194
SETD2_HUMAN	SETD2	physical	26186194
TB182_HUMAN	TNKS1BP1	physical	26186194
PP6R3_HUMAN	PPP6R3	physical	26186194
PASK_HUMAN	PASK	physical	26186194
WAPL_HUMAN	WAPAL	physical	26186194
NFKB1_HUMAN	NFKB1	physical	26186194
LIMD1_HUMAN	LIMD1	physical	26186194
MTMR4_HUMAN	MTMR4	physical	26186194
MTMR3_HUMAN	MTMR3	physical	26186194
RPIA_HUMAN	RPIA	physical	26186194
SNX18_HUMAN	SNX18	physical	26186194
CNOT8_HUMAN	CNOT8	physical	26186194
CNOT7_HUMAN	CNOT7	physical	26186194
CNOT2_HUMAN	CNOT2	physical	26186194
OSBL3_HUMAN	OSBPL3	physical	26186194
IP3KC_HUMAN	ITPKC	physical	26186194
PEAK1_HUMAN	PEAK1	physical	26186194
CNOT9_HUMAN	RQCD1	physical	26186194
P53_HUMAN	TP53	physical	26186194
FBN2_HUMAN	FBN2	physical	26186194
TRBP2_HUMAN	TARBP2	physical	26186194
OSBL6_HUMAN	OSBPL6	physical	26186194
AUNIP_HUMAN	AUNIP	physical	26186194
SDCG3_HUMAN	SDCCAG3	physical	26186194
EPS15_HUMAN	EPS15	physical	26186194
UBP47_HUMAN	USP47	physical	26186194
ARFG1_HUMAN	ARFGAP1	physical	26186194
GAPD1_HUMAN	GAPVD1	physical	26186194
FBX30_HUMAN	FBXO30	physical	26186194
SYNRG_HUMAN	SYNRG	physical	26186194
EF2_HUMAN	EEF2	physical	26344197
EZRI_HUMAN	EZR	physical	26344197
FUS_HUMAN	FUS	physical	26344197
HNRPD_HUMAN	HNRNPD	physical	26344197
PFKAM_HUMAN	PFKM	physical	26344197
SMC2_HUMAN	SMC2	physical	26344197
SYTC_HUMAN	TARS	physical	26344197
UBA1_HUMAN	UBA1	physical	26344197
ANGL4_HUMAN	ANGPTL4	physical	25640309
BEX2_HUMAN	BEX2	physical	25640309
BLID_HUMAN	BLID	physical	25640309
CAD13_HUMAN	CDH13	physical	25640309
DKK3_HUMAN	DKK3	physical	25640309
ESIP1_HUMAN	EPSTI1	physical	25640309
ERRFI_HUMAN	ERRFI1	physical	25640309
KLK5_HUMAN	KLK5	physical	25640309
LYPD3_HUMAN	LYPD3	physical	25640309
MTA3_HUMAN	MTA3	physical	25640309
ARY2_HUMAN	NAT2	physical	25640309
PDLI2_HUMAN	PDLIM2	physical	25640309
HOP2_HUMAN	PSMC3IP	physical	25640309
S10AE_HUMAN	S100A14	physical	25640309
SG3A1_HUMAN	SCGB3A1	physical	25640309
THRSP_HUMAN	THRSP	physical	25640309
WIF1_HUMAN	WIF1	physical	25640309
CTNB1_HUMAN	CTNNB1	physical	26496610
TF3C2_HUMAN	GTF3C2	physical	26496610
DNLI1_HUMAN	LIG1	physical	26496610
TAF9_HUMAN	TAF9	physical	26496610
KLF4_HUMAN	KLF4	physical	26496610
MED16_HUMAN	MED16	physical	26496610
RM28_HUMAN	MRPL28	physical	26496610
SYHM_HUMAN	HARS2	physical	26496610
ASCC1_HUMAN	ASCC1	physical	26496610
MECR_HUMAN	MECR	physical	26496610
CHMP5_HUMAN	CHMP5	physical	26496610
SIR7_HUMAN	SIRT7	physical	26496610
LARP7_HUMAN	LARP7	physical	26496610
RM16_HUMAN	MRPL16	physical	26496610
KI16B_HUMAN	KIF16B	physical	26496610
WDR35_HUMAN	WDR35	physical	26496610
RT35_HUMAN	MRPS35	physical	26496610
ZMYM1_HUMAN	ZMYM1	physical	26496610
ELOF1_HUMAN	ELOF1	physical	26496610
FOXP1_HUMAN	FOXP1	physical	28218735
TCAL2_HUMAN	TCEAL2	physical	28218735
MYT1_HUMAN	MYT1	physical	28218735
SOX30_HUMAN	SOX30	physical	28218735
SP20H_HUMAN	SUPT20H	physical	28218735
UBF1_HUMAN	UBTF	physical	28218735
CTCFL_HUMAN	CTCFL	physical	28218735
BTK_HUMAN	BTK	physical	28218735
SSRP1_HUMAN	SSRP1	physical	28218735
STAT2_HUMAN	STAT2	physical	28218735
PAX4_HUMAN	PAX4	physical	28218735
SOX18_HUMAN	SOX18	physical	28218735
TYY1_HUMAN	YY1	physical	28218735
TBX10_HUMAN	TBX10	physical	28218735
AATF_HUMAN	AATF	physical	28218735
SWT1_HUMAN	SWT1	physical	28218735
IF16_HUMAN	IFI16	physical	28218735
ZFHX3_HUMAN	ZFHX3	physical	28218735
REST_HUMAN	REST	physical	28218735
ATRX_HUMAN	ATRX	physical	28218735
MYT1L_HUMAN	MYT1L	physical	28218735
TCRG1_HUMAN	TCERG1	physical	28218735
SRBP2_HUMAN	SREBF2	physical	28218735
PO4F3_HUMAN	POU4F3	physical	28218735
HNRPK_HUMAN	HNRNPK	physical	28218735
TRRAP_HUMAN	TRRAP	physical	28218735
MED26_HUMAN	MED26	physical	28218735
SIN3B_HUMAN	SIN3B	physical	28218735
TF3C4_HUMAN	GTF3C4	physical	28218735
NFXL1_HUMAN	NFXL1	physical	28218735
FOXF1_HUMAN	FOXF1	physical	28218735
AP2B_HUMAN	TFAP2B	physical	28218735
ZKSC2_HUMAN	ZKSCAN2	physical	28218735
HNRPF_HUMAN	HNRNPF	physical	28218735
KLH18_HUMAN	KLHL18	physical	23213400
IP3KC_HUMAN	ITPKC	physical	28514442
SNX18_HUMAN	SNX18	physical	28514442
TPX2_HUMAN	TPX2	physical	28514442
SDCG3_HUMAN	SDCCAG3	physical	28514442
MTMR4_HUMAN	MTMR4	physical	28514442
SETD2_HUMAN	SETD2	physical	28514442
OSBL3_HUMAN	OSBPL3	physical	28514442
SCYL1_HUMAN	SCYL1	physical	28514442
CACO1_HUMAN	CALCOCO1	physical	28514442
SYNRG_HUMAN	SYNRG	physical	28514442
MTMR3_HUMAN	MTMR3	physical	28514442
SH3G1_HUMAN	SH3GL1	physical	28514442
HTR5B_HUMAN	HEATR5B	physical	28514442
AMER1_HUMAN	AMER1	physical	28514442
AUNIP_HUMAN	AUNIP	physical	28514442
EPS15_HUMAN	EPS15	physical	28514442
OSBL6_HUMAN	OSBPL6	physical	28514442
TACC3_HUMAN	TACC3	physical	28514442
WDR62_HUMAN	WDR62	physical	28514442
TB182_HUMAN	TNKS1BP1	physical	28514442
SORL_HUMAN	SORL1	physical	28514442
UBP47_HUMAN	USP47	physical	28514442
REL_HUMAN	REL	physical	28514442
LIMD1_HUMAN	LIMD1	physical	28514442
DICER_HUMAN	DICER1	physical	28514442
TRBP2_HUMAN	TARBP2	physical	28514442
WAPL_HUMAN	WAPAL	physical	28514442
TNR6C_HUMAN	TNRC6C	physical	28514442
NFKB1_HUMAN	NFKB1	physical	28514442
COPRS_HUMAN	COPRS	physical	28514442
PEAK1_HUMAN	PEAK1	physical	28514442
SNX9_HUMAN	SNX9	physical	28514442
RPGF6_HUMAN	RAPGEF6	physical	28514442
EP15R_HUMAN	EPS15L1	physical	28514442
PP6R3_HUMAN	PPP6R3	physical	28514442
P53_HUMAN	TP53	physical	28514442
PASK_HUMAN	PASK	physical	28514442
CNOT8_HUMAN	CNOT8	physical	28514442
RPIA_HUMAN	RPIA	physical	28514442
FANCA_HUMAN	FANCA	physical	27398318
VHL_HUMAN	VHL	physical	28114281
B2CL1_HUMAN	BCL2L1	physical	22617334

Drug and Disease Associations

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

Regulatory Network of AURKA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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.	19369195 [Abstract]
"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.	18691976 [Abstract]
"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.	19007248 [Abstract]
"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.	17525332 [Abstract]
"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.	17229885 [Abstract]
"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.	16246726 [Abstract]
"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.	18662907 [Abstract]
"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.	14580337 [Abstract]
"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.	19668197 [Abstract]
"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.	14990569 [Abstract]
"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.	13678582 [Abstract]
"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.	11039908 [Abstract]

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