BIRC5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BIRC5_MOUSE
• UniProt AC: O70201
• Protein Name: Baculoviral IAP repeat-containing protein 5
• Gene Name: Birc5
• Organism: Mus musculus (Mouse).
• Sequence Length: 140
• 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. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7..
• Protein Sequence: MGAPALPQIWQLYLKNYRIATFKNWPFLEDCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLTVKKQMEELTVSEFLKLDRQRAKNKIAKETNNKQKEFEETAKTTRQSIEQLAA

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
23	Acetylation	NYRIATFKNWPFLED HCEEEEECCCCCHHC	54.47	-
23	Ubiquitination	NYRIATFKNWPFLED HCEEEEECCCCCHHC	54.47	-
34	Phosphorylation	FLEDCACTPERMAEA CHHCCCCCHHHHHHC	15.06	10949038
48	Phosphorylation	AGFIHCPTENEPDLA CCCEECCCCCCCCHH	57.76	-
90	Acetylation	GCAFLTVKKQMEELT CCEEEEHHHHHHHCC	31.86	-
99	Phosphorylation	QMEELTVSEFLKLDR HHHHCCHHHHHHHHH	19.86	22807455
110	Acetylation	KLDRQRAKNKIAKET HHHHHHHHHHHHHHH	62.05	-
112	Acetylation	DRQRAKNKIAKETNN HHHHHHHHHHHHHHH	43.25	-
115	Acetylation	RAKNKIAKETNNKQK HHHHHHHHHHHHHHH	69.42	-
117	Phosphorylation	KNKIAKETNNKQKEF HHHHHHHHHHHHHHH	43.30	-
129	Acetylation	KEFEETAKTTRQSIE HHHHHHHHHHHHHHH	58.82	-
134	Phosphorylation	TAKTTRQSIEQLAA- HHHHHHHHHHHHHC-	25.46	29514104

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
34	T	Phosphorylation	Kinase	CDK1	P11440	Uniprot
34	T	Phosphorylation	Kinase	CDK15	Q3V3A1	Uniprot
117	T	Phosphorylation	Kinase	AURKB	O70126	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
34	T	Phosphorylation	Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity.	10949038
48	T	Phosphorylation	Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities.	-
117	T	Phosphorylation	In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes.	-
129	K	Acetylation	Acetylation at Lys-129 results in its homodimerization, while deacetylation promotes the formation of monomers which heterodimerize with XPO1/CRM1 which facilitates its nuclear export.	-
129	K	Acetylation	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.

Oops, there are no SNP-PTM records of BIRC5_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of BIRC5_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Crystal structure and mutagenic analysis of the inhibitor-of-apoptosis protein survivin.";
Muchmore S.W., Chen J., Jakob C., Zakula D., Matayoshi E.D., Wu W.,Zhang H., Li F., Ng S.C., Altieri D.C.;
Mol. Cell 6:173-182(2000).
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 7-118, AND PHOSPHORYLATION ATTHR-34.
PubMed: 10949038