AURKB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AURKB_MOUSE
• UniProt AC: O70126
• Protein Name: Aurora kinase B
• Gene Name: Aurkb
• Organism: Mus musculus (Mouse).
• Sequence Length: 345
• 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. AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, HASPIN and histone H3. A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). AURKB is also required for kinetochore localization of BUB1 and SGO1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes..
• Protein Sequence: MAQKENAYPWPYGSKTSQSGLNTLSQRVLRKEPATTSALALVNRFNSQSTAAPGQKLAENKSQGSTASQGSQNKQPFTIDNFEIGRPLGKGKFGNVYLAREKKSRFIVALKILFKSQIEKEGVEHQLRREIEIQAHLKHPNILQLYNYFYDQQRIYLILEYAPRGELYKELQKSRTFDEQRTATIMEELSDALTYCHKKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEMVDLWCIGVLCYELMVGNPPFESPSHSETYRRIVKVDLKFPSSVPSGAQDLISKLLKHNPWQRLPLAEVAAHPWVRANSRRVLPPSAL

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
12	Phosphorylation	ENAYPWPYGSKTSQS CCCCCCCCCCCCCHH	30.11	26745281
14	Phosphorylation	AYPWPYGSKTSQSGL CCCCCCCCCCCHHHH	27.24	29899451
16	Phosphorylation	PWPYGSKTSQSGLNT CCCCCCCCCHHHHHH	33.42	24759943
17	Phosphorylation	WPYGSKTSQSGLNTL CCCCCCCCHHHHHHH	26.53	26745281
19	Phosphorylation	YGSKTSQSGLNTLSQ CCCCCCHHHHHHHHH	45.04	26745281
23	Phosphorylation	TSQSGLNTLSQRVLR CCHHHHHHHHHHHHC	32.59	26745281
25	Phosphorylation	QSGLNTLSQRVLRKE HHHHHHHHHHHHCCC	17.57	22067460
35	Phosphorylation	VLRKEPATTSALALV HHCCCCCHHHHHHHH	31.81	-
47	Phosphorylation	ALVNRFNSQSTAAPG HHHHHHHCCCCCCCC	23.85	29514104
62	Phosphorylation	QKLAENKSQGSTASQ HHHHCCCCCCCCCCC	51.89	-
66	Phosphorylation	ENKSQGSTASQGSQN CCCCCCCCCCCCCCC	36.83	27357545
68	Phosphorylation	KSQGSTASQGSQNKQ CCCCCCCCCCCCCCC	34.85	27357545
71	Phosphorylation	GSTASQGSQNKQPFT CCCCCCCCCCCCCEE	23.96	27357545
78	Phosphorylation	SQNKQPFTIDNFEIG CCCCCCEEEECEEEC	33.82	27357545
102	Ubiquitination	NVYLAREKKSRFIVA CEEEECCCCHHHHHH	50.96	-
103	Ubiquitination	VYLAREKKSRFIVAL EEEECCCCHHHHHHH	41.95	-
207	Sumoylation	KVIHRDIKPENLLLG CEECCCCCHHHHHHH	51.04	-
207	Ubiquitination	KVIHRDIKPENLLLG CEECCCCCHHHHHHH	51.04	-
227	Phosphorylation	KIADFGWSVHAPSLR EEECCCCCCCCCHHC	12.38	26643407
232	Phosphorylation	GWSVHAPSLRRKTMC CCCCCCCHHCCCCCC	34.98	21659605
237	Phosphorylation	APSLRRKTMCGTLDY CCHHCCCCCCCCCCC	18.84	28066266
241	Phosphorylation	RRKTMCGTLDYLPPE CCCCCCCCCCCCCHH	16.13	11879579
299	Phosphorylation	KVDLKFPSSVPSGAQ EEECCCCCCCCCCHH	47.29	22067460

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
-	K	Ubiquitination	E3 ubiquitin ligase	Klhl21	Q3U410	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
237	T	Phosphorylation	The phosphorylation of Thr-237 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism.	-
237	T	Phosphorylation	Thr-237 phosphorylation is indispensable for the AURKB 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 AURKB_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
H33_MOUSE	H3f3a	physical	16179389
AKAP8_HUMAN	AKAP8	physical	20360068
AURKB_HUMAN	AURKB	physical	20360068
BOREA_HUMAN	CDCA8	physical	20360068
EMD_HUMAN	EMD	physical	20360068
AIFM1_HUMAN	AIFM1	physical	20360068
INCE_HUMAN	INCENP	physical	20360068
RCN1_HUMAN	RCN1	physical	20360068
RING2_MOUSE	Rnf2	physical	24034696
BMI1_MOUSE	Bmi1	physical	24034696
CBX7_MOUSE	Cbx7	physical	24034696
UBP16_MOUSE	Usp16	physical	24034696
H2A2C_HUMAN	HIST2H2AC	physical	24034696
UB2D3_HUMAN	UBE2D3	physical	24034696
CO7A1_HUMAN	COL7A1	physical	26496610
INCE_HUMAN	INCENP	physical	26496610
SPTN2_HUMAN	SPTBN2	physical	26496610
LRRF1_HUMAN	LRRFIP1	physical	26496610
KAT7_HUMAN	KAT7	physical	26496610
CE152_HUMAN	CEP152	physical	26496610
ZFY21_HUMAN	ZFYVE21	physical	26496610
OSBL1_HUMAN	OSBPL1A	physical	26496610

Drug and Disease Associations

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