dbPTM

AURKB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AURKB_HUMAN
UniProt AC	Q96GD4
Protein Name	Aurora kinase B
Gene Name	AURKB
Organism	Homo sapiens (Human).
Sequence Length	344
Subcellular Localization	Nucleus. Chromosome. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle. Midbody. Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through
Protein Description	Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. [PubMed: 22422861]
Protein Sequence	MAQKENSYPWPYGRQTAPSGLSTLPQRVLRKEPVTPSALVLMSRSNVQPTAAPGQKVMENSSGTPDILTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQKENSYP ------CCCCCCCCC	29.20	-
4	Ubiquitination	----MAQKENSYPWP ----CCCCCCCCCCC	49.69	29967540
4 (in isoform 4)	Phosphorylation	-	49.69	25849741
7	Phosphorylation	-MAQKENSYPWPYGR -CCCCCCCCCCCCCC	33.39	25159151
8	Phosphorylation	MAQKENSYPWPYGRQ CCCCCCCCCCCCCCC	22.39	21951684
12	Phosphorylation	ENSYPWPYGRQTAPS CCCCCCCCCCCCCCC	22.52	22817900
15	Ubiquitination	YPWPYGRQTAPSGLS CCCCCCCCCCCCCCC	37.34	23000965
16	Phosphorylation	PWPYGRQTAPSGLST CCCCCCCCCCCCCCC	38.89	20860994
19	Phosphorylation	YGRQTAPSGLSTLPQ CCCCCCCCCCCCCCH	50.32	20860994
22	Phosphorylation	QTAPSGLSTLPQRVL CCCCCCCCCCCHHHH	31.27	28555341
26	Ubiquitination	SGLSTLPQRVLRKEP CCCCCCCHHHHHCCC	51.75	22817900
27	Ubiquitination	GLSTLPQRVLRKEPV CCCCCCHHHHHCCCC	27.74	22817900
31	Ubiquitination	LPQRVLRKEPVTPSA CCHHHHHCCCCCHHH	63.31	-
34	Ubiquitination	RVLRKEPVTPSALVL HHHHCCCCCHHHEEE	14.95	21963094
35	Phosphorylation	VLRKEPVTPSALVLM HHHCCCCCHHHEEEE	23.42	21712546
37	Phosphorylation	RKEPVTPSALVLMSR HCCCCCHHHEEEEEC	25.52	21815630
42	Ubiquitination	TPSALVLMSRSNVQP CHHHEEEEECCCCCC	2.14	22817900
43	Ubiquitination	PSALVLMSRSNVQPT HHHEEEEECCCCCCC	28.53	21963094
43	Phosphorylation	PSALVLMSRSNVQPT HHHEEEEECCCCCCC	28.53	22210691
44	Ubiquitination	SALVLMSRSNVQPTA HHEEEEECCCCCCCC	20.48	22817900
45	Phosphorylation	ALVLMSRSNVQPTAA HEEEEECCCCCCCCC	33.76	30266825
45	Ubiquitination	ALVLMSRSNVQPTAA HEEEEECCCCCCCCC	33.76	22817900
46	Ubiquitination	LVLMSRSNVQPTAAP EEEEECCCCCCCCCC	35.02	27667366
47	Ubiquitination	VLMSRSNVQPTAAPG EEEECCCCCCCCCCC	8.32	27667366
50	Ubiquitination	SRSNVQPTAAPGQKV ECCCCCCCCCCCCCC	20.54	21963094
56	Ubiquitination	PTAAPGQKVMENSSG CCCCCCCCCCCCCCC	49.84	23000965
56	Ubiquitination	PTAAPGQKVMENSSG CCCCCCCCCCCCCCC	49.84	21890473
56	Ubiquitination	PTAAPGQKVMENSSG CCCCCCCCCCCCCCC	49.84	21890473
56	Ubiquitination	PTAAPGQKVMENSSG CCCCCCCCCCCCCCC	49.84	21890473
56	Ubiquitination	PTAAPGQKVMENSSG CCCCCCCCCCCCCCC	49.84	21890473
56	Acetylation	PTAAPGQKVMENSSG CCCCCCCCCCCCCCC	49.84	26051181
57	Ubiquitination	TAAPGQKVMENSSGT CCCCCCCCCCCCCCC	4.46	33845483
58	Sulfoxidation	AAPGQKVMENSSGTP CCCCCCCCCCCCCCC	5.34	21406390
58	Ubiquitination	AAPGQKVMENSSGTP CCCCCCCCCCCCCCC	5.34	33845483
59	Ubiquitination	APGQKVMENSSGTPD CCCCCCCCCCCCCCC	57.88	21963094
61	Phosphorylation	GQKVMENSSGTPDIL CCCCCCCCCCCCCCC	19.48	25159151
62	Phosphorylation	QKVMENSSGTPDILT CCCCCCCCCCCCCCE	59.26	25159151
63	Ubiquitination	KVMENSSGTPDILTR CCCCCCCCCCCCCEE	40.88	21963094
64	Phosphorylation	VMENSSGTPDILTRH CCCCCCCCCCCCEEC	21.53	25159151
69	Ubiquitination	SGTPDILTRHFTIDD CCCCCCCEECEEECC	23.56	22817900
69	Phosphorylation	SGTPDILTRHFTIDD CCCCCCCEECEEECC	23.56	24732914
69 (in isoform 3)	Phosphorylation	-	23.56	23879269
69 (in isoform 5)	Phosphorylation	-	23.56	23879269
70	Ubiquitination	GTPDILTRHFTIDDF CCCCCCEECEEECCE	21.34	22817900
73	Phosphorylation	DILTRHFTIDDFEIG CCCEECEEECCEECC	19.85	21712546
74	Ubiquitination	ILTRHFTIDDFEIGR CCEECEEECCEECCC	4.71	33845483
75	Ubiquitination	LTRHFTIDDFEIGRP CEECEEECCEECCCC	52.03	33845483
79	Ubiquitination	FTIDDFEIGRPLGKG EEECCEECCCCCCCC	5.99	22505724
85	Sumoylation	EIGRPLGKGKFGNVY ECCCCCCCCCCCCEE	67.61	-
85	Ubiquitination	EIGRPLGKGKFGNVY ECCCCCCCCCCCCEE	67.61	21906983
85	Sumoylation	EIGRPLGKGKFGNVY ECCCCCCCCCCCCEE	67.61	-
85	Ubiquitination	EIGRPLGKGKFGNVY ECCCCCCCCCCCCEE	67.61	21890473
85	Ubiquitination	EIGRPLGKGKFGNVY ECCCCCCCCCCCCEE	67.61	21890473
86	Ubiquitination	IGRPLGKGKFGNVYL CCCCCCCCCCCCEEE	28.82	22817900
86	Ubiquitination	IGRPLGKGKFGNVYL CCCCCCCCCCCCEEE	28.82	21890473
87	Sumoylation	GRPLGKGKFGNVYLA CCCCCCCCCCCEEEE	54.29	-
87	Ubiquitination	GRPLGKGKFGNVYLA CCCCCCCCCCCEEEE	54.29	21906983
87	Sumoylation	GRPLGKGKFGNVYLA CCCCCCCCCCCEEEE	54.29	-
87	Ubiquitination	GRPLGKGKFGNVYLA CCCCCCCCCCCEEEE	54.29	21890473
87	Ubiquitination	GRPLGKGKFGNVYLA CCCCCCCCCCCEEEE	54.29	21890473
88	Ubiquitination	RPLGKGKFGNVYLAR CCCCCCCCCCEEEEC	13.51	27667366
88	Ubiquitination	RPLGKGKFGNVYLAR CCCCCCCCCCEEEEC	13.51	21890473
91	Ubiquitination	GKGKFGNVYLAREKK CCCCCCCEEEECCCC	4.19	21890473
92	Phosphorylation	KGKFGNVYLAREKKS CCCCCCEEEECCCCC	9.92	17192257
95	Ubiquitination	FGNVYLAREKKSHFI CCCEEEECCCCCHHE	54.39	21963094
98	Ubiquitination	VYLAREKKSHFIVAL EEEECCCCCHHEEEE	44.39	33845483
99	Ubiquitination	YLAREKKSHFIVALK EEECCCCCHHEEEEH	34.40	33845483
110	Ubiquitination	VALKVLFKSQIEKEG EEEHHHHHHHHHHCC	36.97	22817900
111	Ubiquitination	ALKVLFKSQIEKEGV EEHHHHHHHHHHCCH	29.11	22817900
115	Ubiquitination	LFKSQIEKEGVEHQL HHHHHHHHCCHHHHH	62.49	21906983
116	Ubiquitination	FKSQIEKEGVEHQLR HHHHHHHCCHHHHHH	56.53	33845483
119	Ubiquitination	QIEKEGVEHQLRREI HHHHCCHHHHHHHHE	36.45	21890473
121	Ubiquitination	EKEGVEHQLRREIEI HHCCHHHHHHHHEHH	24.14	21963094
122	Ubiquitination	KEGVEHQLRREIEIQ HCCHHHHHHHHEHHH	6.34	22817900
123	Ubiquitination	EGVEHQLRREIEIQA CCHHHHHHHHEHHHH	27.84	27667366
124	Ubiquitination	GVEHQLRREIEIQAH CHHHHHHHHEHHHHH	58.81	27667366
127	Ubiquitination	HQLRREIEIQAHLHH HHHHHHEHHHHHCCC	25.05	21963094
128	Ubiquitination	QLRREIEIQAHLHHP HHHHHEHHHHHCCCC	5.57	21963094
129	Ubiquitination	LRREIEIQAHLHHPN HHHHEHHHHHCCCCC	15.22	21963094
132	Ubiquitination	EIEIQAHLHHPNILR HEHHHHHCCCCCHHH	4.44	27667366
132	Ubiquitination	EIEIQAHLHHPNILR HEHHHHHCCCCCHHH	4.44	21890473
135	Ubiquitination	IQAHLHHPNILRLYN HHHHCCCCCHHHHHH	20.86	21890473
136	Ubiquitination	QAHLHHPNILRLYNY HHHCCCCCHHHHHHH	41.38	21963094
138	Ubiquitination	HLHHPNILRLYNYFY HCCCCCHHHHHHHHH	3.82	21963094
139	Ubiquitination	LHHPNILRLYNYFYD CCCCCHHHHHHHHHH	31.18	22817900
141	Phosphorylation	HPNILRLYNYFYDRR CCCHHHHHHHHHHHC	11.03	29496907
142	Ubiquitination	PNILRLYNYFYDRRR CCHHHHHHHHHHHCE	25.65	21890473
147	Methylation	LYNYFYDRRRIYLIL HHHHHHHHCEEEEEE	20.56	-
151	Phosphorylation	FYDRRRIYLILEYAP HHHHCEEEEEEECCC	5.96	26074081
153	Ubiquitination	DRRRIYLILEYAPRG HHCEEEEEEECCCCC	1.22	21963094
154	Ubiquitination	RRRIYLILEYAPRGE HCEEEEEEECCCCCH	3.67	21963094
155	Ubiquitination	RRIYLILEYAPRGEL CEEEEEEECCCCCHH	32.43	22817900
156	Phosphorylation	RIYLILEYAPRGELY EEEEEEECCCCCHHH	20.61	26074081
158	Ubiquitination	YLILEYAPRGELYKE EEEEECCCCCHHHHH	43.86	22505724
161	Ubiquitination	LEYAPRGELYKELQK EECCCCCHHHHHHHH	50.64	21963094
162	Ubiquitination	EYAPRGELYKELQKS ECCCCCHHHHHHHHH	9.13	21963094
163	Phosphorylation	YAPRGELYKELQKSC CCCCCHHHHHHHHHC	9.71	26074081
163	Ubiquitination	YAPRGELYKELQKSC CCCCCHHHHHHHHHC	9.71	22817900
164	Ubiquitination	APRGELYKELQKSCT CCCCHHHHHHHHHCC	65.65	21906983
164	Ubiquitination	APRGELYKELQKSCT CCCCHHHHHHHHHCC	65.65	21890473
164	Ubiquitination	APRGELYKELQKSCT CCCCHHHHHHHHHCC	65.65	21890473
165	Ubiquitination	PRGELYKELQKSCTF CCCHHHHHHHHHCCC	42.76	27667366
168	Ubiquitination	ELYKELQKSCTFDEQ HHHHHHHHHCCCCHH	61.19	21963094
169	Ubiquitination	LYKELQKSCTFDEQR HHHHHHHHCCCCHHH	12.87	21963094
170	Ubiquitination	YKELQKSCTFDEQRT HHHHHHHCCCCHHHH	5.91	21963094
171	Ubiquitination	KELQKSCTFDEQRTA HHHHHHCCCCHHHHH	41.01	21963094
174	Ubiquitination	QKSCTFDEQRTATIM HHHCCCCHHHHHHHH	37.46	21890473
175	Ubiquitination	KSCTFDEQRTATIME HHCCCCHHHHHHHHH	50.28	21890473
179	Ubiquitination	FDEQRTATIMEELAD CCHHHHHHHHHHHHH	21.90	21963094
179	Ubiquitination	FDEQRTATIMEELAD CCHHHHHHHHHHHHH	21.90	21890473
183	Ubiquitination	RTATIMEELADALMY HHHHHHHHHHHHHHH	31.70	21890473
183	Ubiquitination	RTATIMEELADALMY HHHHHHHHHHHHHHH	31.70	21890473
190	Ubiquitination	ELADALMYCHGKKVI HHHHHHHHHCCCEEE	5.11	22505724
191	Ubiquitination	LADALMYCHGKKVIH HHHHHHHHCCCEEEC	1.81	22505724
194	Ubiquitination	ALMYCHGKKVIHRDI HHHHHCCCEEECCCC	21.87	21963094
195	Ubiquitination	LMYCHGKKVIHRDIK HHHHCCCEEECCCCC	51.52	21963094
196	Ubiquitination	MYCHGKKVIHRDIKP HHHCCCEEECCCCCH	5.19	22817900
199	Ubiquitination	HGKKVIHRDIKPENL CCCEEECCCCCHHHE	35.90	22505724
202	Sumoylation	KVIHRDIKPENLLLG EEECCCCCHHHEEHH	51.04	-
202	Ubiquitination	KVIHRDIKPENLLLG EEECCCCCHHHEEHH	51.04	21906983
202	Sumoylation	KVIHRDIKPENLLLG EEECCCCCHHHEEHH	51.04	-
203	Ubiquitination	VIHRDIKPENLLLGL EECCCCCHHHEEHHH	35.72	21963094
211	Ubiquitination	ENLLLGLKGELKIAD HHEEHHHCCEEEEEC	48.84	21906983
211	Ubiquitination	ENLLLGLKGELKIAD HHEEHHHCCEEEEEC	48.84	21890473
211	Ubiquitination	ENLLLGLKGELKIAD HHEEHHHCCEEEEEC	48.84	21890473
211	Acetylation	ENLLLGLKGELKIAD HHEEHHHCCEEEEEC	48.84	26051181
212	Ubiquitination	NLLLGLKGELKIADF HEEHHHCCEEEEECC	50.98	21963094
214	Ubiquitination	LLGLKGELKIADFGW EHHHCCEEEEECCCC	7.10	21890473
215	Acetylation	LGLKGELKIADFGWS HHHCCEEEEECCCCC	31.39	108937001
215	Ubiquitination	LGLKGELKIADFGWS HHHCCEEEEECCCCC	31.39	21963094
215	Ubiquitination	LGLKGELKIADFGWS HHHCCEEEEECCCCC	31.39	21890473
215	Ubiquitination	LGLKGELKIADFGWS HHHCCEEEEECCCCC	31.39	21890473
216	Ubiquitination	GLKGELKIADFGWSV HHCCEEEEECCCCCC	7.51	21890473
218	Ubiquitination	KGELKIADFGWSVHA CCEEEEECCCCCCCC	46.17	22817900
227	Phosphorylation	GWSVHAPSLRRKTMC CCCCCCHHHCCCCCC	34.98	21082442
231	Ubiquitination	HAPSLRRKTMCGTLD CCHHHCCCCCCCCCC	33.89	22505724
232	Phosphorylation	APSLRRKTMCGTLDY CHHHCCCCCCCCCCC	18.84	16762494
232	Ubiquitination	APSLRRKTMCGTLDY CHHHCCCCCCCCCCC	18.84	22505724
233	Ubiquitination	PSLRRKTMCGTLDYL HHHCCCCCCCCCCCC	1.91	22817900
236	Phosphorylation	RRKTMCGTLDYLPPE CCCCCCCCCCCCCHH	16.13	22322096
239	Phosphorylation	TMCGTLDYLPPEMIE CCCCCCCCCCHHHHC	24.99	20068231
246	Ubiquitination	YLPPEMIEGRMHNEK CCCHHHHCCCCCCCC	39.16	21890473
247	Ubiquitination	LPPEMIEGRMHNEKV CCHHHHCCCCCCCCC	22.68	21890473
250	Ubiquitination	EMIEGRMHNEKVDLW HHHCCCCCCCCCCHH	37.63	22817900
251	Ubiquitination	MIEGRMHNEKVDLWC HHCCCCCCCCCCHHH	41.25	22817900
255	Ubiquitination	RMHNEKVDLWCIGVL CCCCCCCCHHHHHHH	45.58	21890473
255	Ubiquitination	RMHNEKVDLWCIGVL CCCCCCCCHHHHHHH	45.58	21890473
259	Ubiquitination	EKVDLWCIGVLCYEL CCCCHHHHHHHHHHH	2.64	22817900
265	Ubiquitination	CIGVLCYELLVGNPP HHHHHHHHHHHCCCC	34.33	22817900
266	Ubiquitination	IGVLCYELLVGNPPF HHHHHHHHHHCCCCC	1.57	22817900
274	Ubiquitination	LVGNPPFESASHNET HHCCCCCCCCCCCCH	51.69	22817900
287	Ubiquitination	ETYRRIVKVDLKFPA CHHEEEEEEECCCCC	27.88	22817900
287	Ubiquitination	ETYRRIVKVDLKFPA CHHEEEEEEECCCCC	27.88	21890473
287	Ubiquitination	ETYRRIVKVDLKFPA CHHEEEEEEECCCCC	27.88	21890473
288	Ubiquitination	TYRRIVKVDLKFPAS HHEEEEEEECCCCCC	7.84	21890473
288	Ubiquitination	TYRRIVKVDLKFPAS HHEEEEEEECCCCCC	7.84	-
291	Ubiquitination	RIVKVDLKFPASVPM EEEEEECCCCCCCCC	44.85	21906983
292	Ubiquitination	IVKVDLKFPASVPMG EEEEECCCCCCCCCC	8.75	22817900
306	Ubiquitination	GAQDLISKLLRHNPS CHHHHHHHHHHCCHH	44.54	21906983
307	Ubiquitination	AQDLISKLLRHNPSE HHHHHHHHHHCCHHH	3.97	22817900
313	Phosphorylation	KLLRHNPSERLPLAQ HHHHCCHHHCCCHHH	40.44	17192257
331	Phosphorylation	HPWVRANSRRVLPPS CHHHCCCCCCCCCHH	22.07	22024163

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
7	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
16	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
227	S	Phosphorylation	Kinase	PRKCE	Q02156	GPS
232	T	Phosphorylation	Kinase	AURKB	Q96GD4	PhosphoELM
232	T	Phosphorylation	Kinase	STK4	Q13043	GPS
331	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
331	S	Phosphorylation	Kinase	CHK2	O96017	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL9	Q9P2J3	PMID:19995937
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL13	Q9P2N7	PMID:19995937
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL2	Q9UKC9	PMID:23370391
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	KLHL21	Q9UJP4	PMID:19995937
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:16204042

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
232	T	Phosphorylation	14722118
The phosphorylation of Thr-232 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism.
232	T	Phosphorylation	14722118
Thr-232 phosphorylation is indispensable for the AURKB 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 AURKB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RCC2_HUMAN	RCC2	physical	15249581
AURKB_HUMAN	AURKB	physical	15249581
INCE_HUMAN	INCENP	physical	15249581
BOREA_HUMAN	CDCA8	physical	15249581
TACC1_HUMAN	TACC1	physical	15064709
RGAP1_HUMAN	RACGAP1	physical	12689593
BARD1_HUMAN	BARD1	physical	19176389
KI20A_HUMAN	KIF20A	physical	15263015
RB_HUMAN	RB1	physical	19225156
NSUN2_HUMAN	NSUN2	physical	17215513
H31_HUMAN	HIST1H3A	physical	21397507
RASF1_HUMAN	RASSF1	physical	21874044
BIRC5_HUMAN	BIRC5	physical	19995937
INCE_HUMAN	INCENP	physical	19995937
KLHL9_HUMAN	KLHL9	physical	19995937
KLH21_HUMAN	KLHL21	physical	19995937
CND2_HUMAN	NCAPH	physical	21633354
CENPA_HUMAN	CENPA	physical	20663916
H31T_HUMAN	HIST3H3	physical	20663916
H31T_HUMAN	HIST3H3	physical	21554500
INCE_HUMAN	INCENP	physical	21554500
BOREA_HUMAN	CDCA8	physical	21554500
BIRC5_HUMAN	BIRC5	physical	21554500
NSL1_HUMAN	NSL1	physical	20231385
PSA3_HUMAN	PSMA3	physical	14674694
AURKB_HUMAN	AURKB	physical	22371557
SKA1_HUMAN	SKA1	physical	22371557
SKA3_HUMAN	SKA3	physical	22371557
AURKB_HUMAN	AURKB	physical	21658950
HASP_HUMAN	GSG2	physical	21658950
H32_HUMAN	HIST2H3C	physical	21658950
LATS2_HUMAN	LATS2	physical	21822051
CDC20_HUMAN	CDC20	physical	15923616
FZR1_HUMAN	FZR1	physical	15923616
CDC27_HUMAN	CDC27	physical	15923616
H31T_HUMAN	HIST3H3	physical	20593489
CENPA_HUMAN	CENPA	physical	20593489
BUB1B_HUMAN	BUB1B	physical	18710370
AURKB_HUMAN	AURKB	physical	18710370
AJUBA_HUMAN	AJUBA	physical	18710370
MARE1_HUMAN	MAPRE1	physical	19696028
MARE2_HUMAN	MAPRE2	physical	19696028
MARE3_HUMAN	MAPRE3	physical	19696028
RGAP1_HUMAN	RACGAP1	physical	18201571
A4_HUMAN	APP	physical	21832049
MARE1_HUMAN	MAPRE1	physical	18477699
H31_HUMAN	HIST1H3A	physical	18477699
PP2AA_HUMAN	PPP2CA	physical	18477699
INCE_HUMAN	INCENP	physical	18477699
BIRC5_HUMAN	BIRC5	physical	18477699
GFAP_HUMAN	GFAP	physical	12686604
DESM_HUMAN	DES	physical	12686604
H31_HUMAN	HIST1H3A	physical	11756469
CENPA_HUMAN	CENPA	physical	11756469
FBXW7_HUMAN	FBXW7	physical	23095493
INCE_HUMAN	INCENP	physical	16571674
FBXL2_HUMAN	FBXL2	physical	23370391
SEPT1_HUMAN	SEPT1	physical	16179162
BIRC5_HUMAN	BIRC5	physical	16291752
HS90A_HUMAN	HSP90AA1	physical	22939624
NDC80_HUMAN	NDC80	physical	14602875
NUF2_HUMAN	NUF2	physical	14602875
TPX2_HUMAN	TPX2	physical	19357306
INCE_HUMAN	INCENP	physical	19357306
BIRC5_HUMAN	BIRC5	physical	19357306
AURKC_HUMAN	AURKC	physical	15316025
CBX3_HUMAN	CBX3	physical	23829974
RACK1_HUMAN	GNB2L1	physical	21988832
SEPT1_HUMAN	SEPT1	physical	21988832
PSA3_HUMAN	PSMA3	physical	21988832
B2L11_HUMAN	BCL2L11	physical	21988832
CIB1_HUMAN	CIB1	physical	21988832
INCE_HUMAN	INCENP	physical	20430883
FLOT1_HUMAN	FLOT1	physical	20430883
BOREA_HUMAN	CDCA8	physical	20430883
BIRC5_HUMAN	BIRC5	physical	20430883
H2A2C_HUMAN	HIST2H2AC	physical	17914355
H2A2A_HUMAN	HIST2H2AA3	physical	17914355
H2B2E_HUMAN	HIST2H2BE	physical	17914355
LPPRC_HUMAN	LRPPRC	physical	23443559
GGYF2_HUMAN	GIGYF2	physical	23443559
IRS4_HUMAN	IRS4	physical	23443559
DDB1_HUMAN	DDB1	physical	23443559
RAVR1_HUMAN	RAVER1	physical	23443559
GRP78_HUMAN	HSPA5	physical	23443559
MOGS_HUMAN	MOGS	physical	23443559
HNRPU_HUMAN	HNRNPU	physical	23443559
PRC2C_HUMAN	PRRC2C	physical	23443559
TBB5_HUMAN	TUBB	physical	23443559
KPBB_HUMAN	PHKB	physical	23443559
IASPP_HUMAN	PPP1R13L	physical	23443559
TBA1A_HUMAN	TUBA1A	physical	23443559
TBCD4_HUMAN	TBC1D4	physical	23443559
UBR4_HUMAN	UBR4	physical	23443559
GRP75_HUMAN	HSPA9	physical	23443559
ABR_HUMAN	ABR	physical	23443559
AURKA_HUMAN	AURKA	physical	23443559
DDX5_HUMAN	DDX5	physical	23443559
TCAL4_HUMAN	TCEAL4	physical	23443559
PKHA5_HUMAN	PLEKHA5	physical	23443559
CH60_HUMAN	HSPD1	physical	23443559
4ET_HUMAN	EIF4ENIF1	physical	23443559
PUM1_HUMAN	PUM1	physical	23443559
RS16_HUMAN	RPS16	physical	23443559
UBR5_HUMAN	UBR5	physical	23443559
CE170_HUMAN	CEP170	physical	23443559
MARK2_HUMAN	MARK2	physical	23443559
PRPF3_HUMAN	PRPF3	physical	23443559
CDC73_HUMAN	CDC73	physical	23443559
RS4X_HUMAN	RPS4X	physical	23443559
SNW1_HUMAN	SNW1	physical	23443559
4EBP3_HUMAN	EIF4EBP3	physical	23443559
ZCCHV_HUMAN	ZC3HAV1	physical	23443559
UBB_HUMAN	UBB	physical	23443559
ROA1_HUMAN	HNRNPA1	physical	23443559
KINH_HUMAN	KIF5B	physical	23443559
DOCK7_HUMAN	DOCK7	physical	23443559
AMOT_HUMAN	AMOT	physical	23443559
RT27_HUMAN	MRPS27	physical	23443559
PPP6_HUMAN	PPP6C	physical	23443559
EP300_HUMAN	EP300	physical	23443559
TBA1C_HUMAN	TUBA1C	physical	23443559
ANR17_HUMAN	ANKRD17	physical	23443559
HS90A_HUMAN	HSP90AA1	physical	23443559
HDAC5_HUMAN	HDAC5	physical	23443559
HS90B_HUMAN	HSP90AB1	physical	23443559
MAP9_HUMAN	MAP9	physical	23443559
SMRC1_HUMAN	SMARCC1	physical	23443559
MTMR1_HUMAN	MTMR1	physical	23443559
FRIH_HUMAN	FTH1	physical	23443559
RL10_HUMAN	RPL10	physical	23443559
SHRPN_HUMAN	SHARPIN	physical	23443559
LIPA1_HUMAN	PPFIA1	physical	23443559
PPM1B_HUMAN	PPM1B	physical	23443559
RS27_HUMAN	RPS27	physical	23443559
EPN4_HUMAN	CLINT1	physical	23443559
RS25_HUMAN	RPS25	physical	23443559
NUCG_HUMAN	ENDOG	physical	26186194
HS90A_HUMAN	HSP90AA1	physical	26186194
HS90B_HUMAN	HSP90AB1	physical	26186194
CDC37_HUMAN	CDC37	physical	26186194
RB12B_HUMAN	RBM12B	physical	26186194
TTK_HUMAN	TTK	physical	26186194
UBS3B_HUMAN	UBASH3B	physical	26766443
CUL3_HUMAN	CUL3	physical	26766443
KI20A_HUMAN	KIF20A	physical	26766443
RB12B_HUMAN	RBM12B	physical	28514442
SGT1_HUMAN	SUGT1	physical	28514442
HS90A_HUMAN	HSP90AA1	physical	28514442
HS90B_HUMAN	HSP90AB1	physical	28514442
KPYM_HUMAN	PKM	physical	25412762
SYAC_HUMAN	AARS	physical	27173435
MICU1_HUMAN	MICU1	physical	27173435
RAD52_YEAST	RAD52	physical	29078282
RAD52_HUMAN	RAD52	physical	29078282

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 AURKB_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-7; THR-16; THR-35;SER-45; SER-61; SER-62 AND THR-64, ACETYLATION [LARGE SCALE ANALYSIS]AT ALA-2, AND MASS SPECTROMETRY.	19007248 [Abstract]
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-61, 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-7; THR-35; SER-45;SER-61; THR-64; TYR-92; SER-227; THR-232; THR-236 AND SER-313, ANDMASS 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-7; THR-16; THR-35;SER-45; SER-61; SER-62 AND THR-64, ACETYLATION [LARGE SCALE ANALYSIS]AT ALA-2, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; TYR-12 AND THR-232,AND MASS SPECTROMETRY.	16565220 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-232, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Autophosphorylation of a newly identified site of Aurora-B isindispensable for cytokinesis."; Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H.,Furukawa K., Takahashi T., Izawa I., Inagaki M.; J. Biol. Chem. 279:12997-13003(2004). Cited for: AUTOPHOSPHORYLATION AT THR-232, FUNCTION, INTERACTION WITH INCENP,ENZYME REGULATION, AND MUTAGENESIS OF LYS-106.	14722118 [Abstract]

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