dbPTM

BIRC5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BIRC5_HUMAN
UniProt AC	O15392
Protein Name	Baculoviral IAP repeat-containing protein 5
Gene Name	BIRC5
Organism	Homo sapiens (Human).
Sequence Length	142
Subcellular Localization	Cytoplasm . Nucleus . Chromosome . Chromosome, centromere . Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . Midbody . Localizes at the centromeres from prophase to metaphase, at the spindle midzone during anaphase and a the m
Protein Description	Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. [PubMed: 9859993]
Protein Sequence	MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Ubiquitination	PAWQPFLKDHRISTF CCCHHHHCCCCCCCC	52.44	-
20	Phosphorylation	FLKDHRISTFKNWPF HHCCCCCCCCCCCCC	27.96	20427271
21	Phosphorylation	LKDHRISTFKNWPFL HCCCCCCCCCCCCCC	35.94	20427271
23	Acetylation	DHRISTFKNWPFLEG CCCCCCCCCCCCCCC	59.18	20826784
23	Ubiquitination	DHRISTFKNWPFLEG CCCCCCCCCCCCCCC	59.18	PubMed
34	Phosphorylation	FLEGCACTPERMAEA CCCCCCCCHHHHHHC	15.06	25159151
48	Phosphorylation	AGFIHCPTENEPDLA CCCEECCCCCCCCHH	57.76	21252625
62	Ubiquitination	AQCFFCFKELEGWEP HHHHHHHHHHCCCCC	63.67	PubMed
78 (in isoform 5)	Ubiquitination	-	56.30	21906983
78 (in isoform 4)	Ubiquitination	-	56.30	21906983
78 (in isoform 1)	Ubiquitination	-	56.30	21906983
78	Ubiquitination	DDPIEEHKKHSSGCA CCHHHHHHHHCCCCE	56.30	PubMed
78	Acetylation	DDPIEEHKKHSSGCA CCHHHHHHHHCCCCE	56.30	26051181
79	Ubiquitination	DPIEEHKKHSSGCAF CHHHHHHHHCCCCEE	51.10	PubMed
82	Phosphorylation	EEHKKHSSGCAFLSV HHHHHHCCCCEEHHH	37.30	29214152
90	Ubiquitination	GCAFLSVKKQFEELT CCEEHHHHHHHHHCC	37.16	-
90	Acetylation	GCAFLSVKKQFEELT CCEEHHHHHHHHHCC	37.16	20826784
91	Ubiquitination	CAFLSVKKQFEELTL CEEHHHHHHHHHCCH	59.05	-
103	Ubiquitination	LTLGEFLKLDRERAK CCHHHHHHHHHHHHH	54.37	-
110	Acetylation	KLDRERAKNKIAKET HHHHHHHHHHHHHHH	66.06	20826784
112	Acetylation	DRERAKNKIAKETNN HHHHHHHHHHHHHHH	43.25	20826784
113	Acetylation	RERAKNKIAKETNNK HHHHHHHHHHHHHHH	10.40	20826784
113	Ubiquitination	RERAKNKIAKETNNK HHHHHHHHHHHHHHH	10.40	20826784
114	Ubiquitination	ERAKNKIAKETNNKK HHHHHHHHHHHHHHH	12.77	-
115	Acetylation	RAKNKIAKETNNKKK HHHHHHHHHHHHHHH	69.42	20826784
117	Phosphorylation	KNKIAKETNNKKKEF HHHHHHHHHHHHHHH	43.30	14610074
120	Acetylation	IAKETNNKKKEFEET HHHHHHHHHHHHHHH	68.26	20826784
121	Acetylation	AKETNNKKKEFEETA HHHHHHHHHHHHHHH	60.71	20826784
122	Acetylation	KETNNKKKEFEETAK HHHHHHHHHHHHHHH	70.06	20826784
126	Ubiquitination	NKKKEFEETAKKVRR HHHHHHHHHHHHHHH	60.43	-
129	Acetylation	KEFEETAKKVRRAIE HHHHHHHHHHHHHHH	60.26	20826784
130	Acetylation	EFEETAKKVRRAIEQ HHHHHHHHHHHHHHH	38.21	20826784
133	Acetylation	ETAKKVRRAIEQLAA HHHHHHHHHHHHHHC	42.79	20826784
135	Acetylation	AKKVRRAIEQLAAMD HHHHHHHHHHHHCCC	3.08	20826784
138	Acetylation	VRRAIEQLAAMD--- HHHHHHHHHCCC---	1.81	20826784
140	Phosphorylation	RAIEQLAAMD----- HHHHHHHCCC-----	15.98	14610074
143	Acetylation	EQLAAMD-------- HHHHCCC--------		-
144	Acetylation	QLAAMD--------- HHHCCC---------		20826784

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
20	S	Phosphorylation	Kinase	AURC	Q9UQB9	PSP
20	S	Phosphorylation	Kinase	PKACA	P17612	PSP
20	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
20	S	Phosphorylation	Kinase	PLK1	P53350	PSP
21	T	Phosphorylation	Kinase	PLK1	P53350	PSP
34	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
34	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
34	T	Phosphorylation	Kinase	CDK15	Q96Q40	Uniprot
48	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
48	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
48	T	Phosphorylation	Kinase	CK2	-	Uniprot
117	T	Phosphorylation	Kinase	AURB	Q96GD4	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FBXL7	Q9UJT9	PMID:25778398
-	K	Ubiquitination	E3 ubiquitin ligase	XIAP	P98170	PMID:17613533

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
20	S	Phosphorylation	27332895
Phosphorylation at Ser-20 by AURKC is critical for regulation of proper chromosome alignment and segregation, and possibly cytokinesis.
34	T	Phosphorylation	11069302
Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity.
48	T	Phosphorylation	21252625
Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities.
117	T	Phosphorylation	14610074
In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes.
129	K	Acetylation	20826784
Acetylation at Lys-129 by CBP results in its homodimerization, while deacetylation promotes the formation of monomers which heterodimerize with XPO1/CRM1 which facilitates its nuclear export.
129	K	Acetylation	20826784
The dynamic equilibrium between its acetylation and deacetylation at Lys-129 determines its interaction with XPO1/CRM1, its subsequent subcellular localization, and its ability to inhibit STAT3 transactivation.

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
120	Acetylation	129 (9)	E ⇒ K	rs2071214	Behavioural disinhibition (generation interaction)	23942779
121	Acetylation	129 (8)	E ⇒ K	rs2071214	Behavioural disinhibition (generation interaction)	23942779
122	Acetylation	129 (7)	E ⇒ K	rs2071214	Behavioural disinhibition (generation interaction)	23942779
129	Acetylation	129 (0)	E ⇒ K	rs2071214	Behavioural disinhibition (generation interaction)	23942779
130	Acetylation	129 (1)	E ⇒ K	rs2071214	Behavioural disinhibition (generation interaction)	23942779

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AURKB_HUMAN	AURKB	physical	11516652
AURKB_HUMAN	AURKB	physical	12419797
AURKB_HUMAN	AURKB	genetic	12419797
INCE_CHICK	INCENP	physical	11516652
INCE_HUMAN	INCENP	physical	11516652
BIRC5_HUMAN	BIRC5	physical	10876248
BIRC5_HUMAN	BIRC5	physical	10949039
CASP7_HUMAN	CASP7	physical	9850056
CASP3_HUMAN	CASP3	physical	9850056
CDK2_HUMAN	CDK2	physical	11069302
CASP9_HUMAN	CASP9	physical	11069302
BIRC5_HUMAN	BIRC5	physical	11170436
CASP7_HUMAN	CASP7	physical	11170436
CASP3_HUMAN	CASP3	physical	11170436
CDK4_HUMAN	CDK4	physical	10713676
AURKB_HUMAN	AURKB	physical	19951914
XIAP_HUMAN	XIAP	physical	15218035
USP9X_HUMAN	USP9X	physical	16322459
UFD1_HUMAN	UFD1L	physical	16322459
PRKDC_HUMAN	PRKDC	physical	20394854
MDC1_HUMAN	MDC1	physical	20394854
XRCC6_HUMAN	XRCC6	physical	20394854
H2AX_HUMAN	H2AFX	physical	20394854
XPO1_HUMAN	XPO1	physical	17099693
AURKB_HUMAN	AURKB	physical	17099693
INCE_HUMAN	INCENP	physical	17099693
BOREA_HUMAN	CDCA8	physical	17099693
BIRC5_HUMAN	BIRC5	physical	17099693
BIRC2_HUMAN	BIRC2	physical	15665297
H32_HUMAN	HIST2H3C	physical	20929775
INCE_HUMAN	INCENP	physical	16571674
BOREA_HUMAN	CDCA8	physical	16571674
BIRC5_HUMAN	BIRC5	physical	16571674
BIRC5_HUMAN	BIRC5	physical	16291752
BOREA_HUMAN	CDCA8	physical	16291752
AURKB_HUMAN	AURKB	physical	16291752
PAR2_HUMAN	F2RL1	physical	20826780
BOREA_HUMAN	CDCA8	physical	20430883
AIP_HUMAN	AIP	physical	19366855
BIRC5_HUMAN	BIRC5	physical	21536684
DBLOH_HUMAN	DIABLO	physical	21536684
BIRC5_HUMAN	BIRC5	physical	23251006
RAN_HUMAN	RAN	physical	23251006
CASP9_HUMAN	CASP9	physical	25241761
BIRC2_HUMAN	BIRC2	physical	25635055
FBXL7_HUMAN	FBXL7	physical	28218735
BOREA_HUMAN	CDCA8	physical	28514442
C102A_HUMAN	CCDC102A	physical	28514442
INCE_HUMAN	INCENP	physical	28514442
HBAZ_HUMAN	HBZ	physical	28514442
SRCRL_HUMAN	SSC5D	physical	28514442
LTOR4_HUMAN	LAMTOR4	physical	28514442
ASC_HUMAN	PYCARD	physical	28514442
MED6_HUMAN	MED6	physical	28514442
MED14_HUMAN	MED14	physical	28514442
MED10_HUMAN	MED10	physical	28514442
MED30_HUMAN	MED30	physical	28514442
MED18_HUMAN	MED18	physical	28514442
MED8_HUMAN	MED8	physical	28514442
MED17_HUMAN	MED17	physical	28514442
MED22_HUMAN	MED22	physical	28514442
MED21_HUMAN	MED21	physical	28514442
MED31_HUMAN	MED31	physical	28514442
MED29_HUMAN	MED29	physical	28514442
MED20_HUMAN	MED20	physical	28514442
MED1_HUMAN	MED1	physical	28514442
MED4_HUMAN	MED4	physical	28514442
BIRC5_HUMAN	BIRC5	physical	14699067
DBLOH_HUMAN	DIABLO	physical	14699067

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 BIRC5_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Acetylation directs survivin nuclear localization to repress STAT3oncogenic activity."; Wang H., Holloway M.P., Ma L., Cooper Z.A., Riolo M., Samkari A.,Elenitoba-Johnson K.S., Chin Y.E., Altura R.A.; J. Biol. Chem. 285:36129-36137(2010). Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAT3 AND XPO1/CRM1,ACETYLATION AT LYS-23; LYS-90; LYS-110; LYS-112; LYS-115; LYS-121 ANDLYS-129, MUTAGENESIS OF LYS-129, AND CHARACTERIZATION OF VARIANTGLU-129.	20826784 [Abstract]
Phosphorylation
Reference	PubMed
"Threonine 48 in the BIR domain of survivin is critical to its mitoticand anti-apoptotic activities and can be phosphorylated by CK2 invitro."; Barrett R.M., Colnaghi R., Wheatley S.P.; Cell Cycle 10:538-548(2011). Cited for: PHOSPHORYLATION AT THR-48, AND MUTAGENESIS OF THR-48.	21252625 [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 THR-34, AND MASSSPECTROMETRY.	18691976 [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 THR-34, AND MASSSPECTROMETRY.	16565220 [Abstract]
"Aurora-B phosphorylation in vitro identifies a residue of survivinthat is essential for its localization and binding to inner centromereprotein (INCENP) in vivo."; Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.; J. Biol. Chem. 279:5655-5660(2004). Cited for: INTERACTION WITH INCENP, SUBCELLULAR LOCATION, PHOSPHORYLATION ATTHR-117, AND MUTAGENESIS OF THR-117.	14610074 [Abstract]
"Regulation of apoptosis at cell division by p34cdc2 phosphorylationof survivin."; O'Connor D.S., Grossman D., Plescia J., Li F., Zhang H., Villa A.,Tognin S., Marchisio P.C., Altieri D.C.; Proc. Natl. Acad. Sci. U.S.A. 97:13103-13107(2000). Cited for: PHOSPHORYLATION AT THR-34.	11069302 [Abstract]

show

show

show

show

show

show