AURKC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AURKC_HUMAN
• UniProt AC: Q9UQB9
• Protein Name: Aurora kinase C
• Gene Name: AURKC
• Organism: Homo sapiens (Human).
• Sequence Length: 309
• Subcellular Localization: Nucleus. Chromosome. Chromosome, centromere . Cytoplasm, cytoskeleton, spindle . Distributes in the condensed chromosomes during prophase to metaphase. After entering anaphase, there is a dissociation from separated chromosomes and a redistribution t
• 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. Plays also a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin and INCENP leading to increased AURKC activity. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'..
• Protein Sequence: MSSPRAVVQLGKAQPAGEELATANQTAQQPSSPAMRRLTVDDFEIGRPLGKGKFGNVYLARLKESHFIVALKVLFKSQIEKEGLEHQLRREIEIQAHLQHPNILRLYNYFHDARRVYLILEYAPRGELYKELQKSEKLDEQRTATIIEELADALTYCHDKKVIHRDIKPENLLLGFRGEVKIADFGWSVHTPSLRRKTMCGTLDYLPPEMIEGRTYDEKVDLWCIGVLCYELLVGYPPFESASHSETYRRILKVDVRFPLSMPLGARDLISRLLRYQPLERLPLAQILKHPWVQAHSRRVLPPCAQMAS

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
17	Ubiquitination	LGKAQPAGEELATAN CCCCCCCCHHHHHHH	35.28	22817900
19 (in isoform 2)	Ubiquitination	-	42.67	21890473
19	Ubiquitination	KAQPAGEELATANQT CCCCCCHHHHHHHHC	42.67	27667366
22	Phosphorylation	PAGEELATANQTAQQ CCCHHHHHHHHCCCC	38.47	24043423
26	Phosphorylation	ELATANQTAQQPSSP HHHHHHHCCCCCCCH	26.66	24043423
31	Phosphorylation	NQTAQQPSSPAMRRL HHCCCCCCCHHHHHC	44.61	24043423
32	Ubiquitination	QTAQQPSSPAMRRLT HCCCCCCCHHHHHCE	24.30	22817900
32	Phosphorylation	QTAQQPSSPAMRRLT HCCCCCCCHHHHHCE	24.30	24043423
34	Ubiquitination	AQQPSSPAMRRLTVD CCCCCCHHHHHCEEC	13.18	21890473
34	Ubiquitination	AQQPSSPAMRRLTVD CCCCCCHHHHHCEEC	13.18	27667366
51	Ubiquitination	EIGRPLGKGKFGNVY ECCCCCCCCCCCCEE	67.61	22817900
53 (in isoform 1)	Ubiquitination	-	54.29	21890473
53	Ubiquitination	GRPLGKGKFGNVYLA CCCCCCCCCCCEEEE	54.29	27667366
58	Phosphorylation	KGKFGNVYLARLKES CCCCCCEEEECCCCH	9.92	17192257
76	Ubiquitination	VALKVLFKSQIEKEG HEEHHHHHHHHHHCC	36.97	-
77	Phosphorylation	ALKVLFKSQIEKEGL EEHHHHHHHHHHCCH	29.11	-
96	Ubiquitination	RREIEIQAHLQHPNI HHHHHHHHHCCCCCH	15.83	21890473
96 (in isoform 2)	Ubiquitination	-	15.83	21890473
100	Ubiquitination	EIQAHLQHPNILRLY HHHHHCCCCCHHHHH	24.59	22817900
111	Ubiquitination	LRLYNYFHDARRVYL HHHHHHHHHHHHEEE	19.91	21890473
115	Ubiquitination	NYFHDARRVYLILEY HHHHHHHHEEEEEEC	24.13	22817900
129	Phosphorylation	YAPRGELYKELQKSE CCCCCHHHHHHHHHH	9.71	29496907
130	Ubiquitination	APRGELYKELQKSEK CCCCHHHHHHHHHHC	65.65	21890473
130 (in isoform 1)	Ubiquitination	-	65.65	21890473
134	Ubiquitination	ELYKELQKSEKLDEQ HHHHHHHHHHCCCHH	73.53	22817900
143	Phosphorylation	EKLDEQRTATIIEEL HCCCHHHHHHHHHHH	28.04	24719451
149	Ubiquitination	RTATIIEELADALTY HHHHHHHHHHHHHHH	38.56	22817900
156	Phosphorylation	ELADALTYCHDKKVI HHHHHHHHHCCCCEE	6.66	24719451
163	Ubiquitination	YCHDKKVIHRDIKPE HHCCCCEECCCCCHH	2.79	22505724
168	Ubiquitination	KVIHRDIKPENLLLG CEECCCCCHHHEEEE	51.04	22817900
178	Ubiquitination	NLLLGFRGEVKIADF HEEEEEEEEEEEECC	41.61	22505724
193	Phosphorylation	GWSVHTPSLRRKTMC CCCCCCHHHCCCCCC	35.35	24719451
197	Ubiquitination	HTPSLRRKTMCGTLD CCHHHCCCCCCCCCC	33.89	22505724
197	Acetylation	HTPSLRRKTMCGTLD CCHHHCCCCCCCCCC	33.89	28735677
198	Phosphorylation	TPSLRRKTMCGTLDY CHHHCCCCCCCCCCC	18.84	22322096
202	Phosphorylation	RRKTMCGTLDYLPPE CCCCCCCCCCCCCHH	16.13	22322096
205	Phosphorylation	TMCGTLDYLPPEMIE CCCCCCCCCCHHHHC	24.99	20068231
271	Phosphorylation	LGARDLISRLLRYQP CCHHHHHHHHHHCCC	24.95	22210691

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
198	T	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AURKC_HUMAN !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CENPA_HUMAN	CENPA	physical	20663916
TACC2_HUMAN	TACC2	physical	14602875
H31_HUMAN	HIST1H3A	physical	15316025
BIRC5_HUMAN	BIRC5	physical	21988832
HS90A_HUMAN	HSP90AA1	physical	26186194
HS90B_HUMAN	HSP90AB1	physical	26186194
FKBP5_HUMAN	FKBP5	physical	26186194
CDC37_HUMAN	CDC37	physical	26186194
MYH1_HUMAN	MYH1	physical	26186194
MYH8_HUMAN	MYH8	physical	26186194
MYH4_HUMAN	MYH4	physical	26186194
UBP19_HUMAN	USP19	physical	26186194
TBB8_HUMAN	TUBB8	physical	26186194
INCE_HUMAN	INCENP	physical	26186194
CL043_HUMAN	C12orf43	physical	26186194
PRP16_HUMAN	DHX38	physical	26186194
MYH8_HUMAN	MYH8	physical	28514442
INCE_HUMAN	INCENP	physical	28514442
MYH1_HUMAN	MYH1	physical	28514442
MYH4_HUMAN	MYH4	physical	28514442
CL043_HUMAN	C12orf43	physical	28514442
UBP19_HUMAN	USP19	physical	28514442
PRP16_HUMAN	DHX38	physical	28514442
HS90A_HUMAN	HSP90AA1	physical	28514442
FKBP5_HUMAN	FKBP5	physical	28514442
CDK5_HUMAN	CDK5	physical	28514442
HS90B_HUMAN	HSP90AB1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 243060: Spermatogenic failure 5 (SPGF5)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.