O70201 · BIRC5_MOUSE
- ProteinBaculoviral IAP repeat-containing protein 5
- GeneBirc5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids140 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:25778398).
Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (By similarity).
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 (By similarity).
Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity).
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 (By similarity).
May counteract a default induction of apoptosis in G2/M phase (By similarity).
The acetylated form represses STAT3 transactivation of target gene promoters (By similarity).
May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity).
Essential for the maintenance of mitochondrial integrity and function (PubMed:25778398).
Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (By similarity).
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 (By similarity).
Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity).
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 (By similarity).
May counteract a default induction of apoptosis in G2/M phase (By similarity).
The acetylated form represses STAT3 transactivation of target gene promoters (By similarity).
May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity).
Essential for the maintenance of mitochondrial integrity and function (PubMed:25778398).
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 57 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 60 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 76 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 77 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 80 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 84 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 126 | Interaction with FBXL7 | ||||
Sequence: E |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBaculoviral IAP repeat-containing protein 5
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionO70201
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes at the centromeres from prophase to metaphase, at the spindle midzone during anaphase and a the midbody during telophase and cytokinesis. Accumulates in the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor (By similarity).
Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes. Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear export (By similarity).
Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes. Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear export (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000122357 | 1-140 | Baculoviral IAP repeat-containing protein 5 | |||
Sequence: MGAPALPQIWQLYLKNYRIATFKNWPFLEDCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLTVKKQMEELTVSEFLKLDRQRAKNKIAKETNNKQKEFEETAKTTRQSIEQLAA | ||||||
Modified residue | 23 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 34 | Phosphothreonine; by CDK1 and CDK15 | ||||
Sequence: T | ||||||
Modified residue | 48 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 90 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 110 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 112 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 115 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 117 | Phosphothreonine; by AURKB | ||||
Sequence: T | ||||||
Modified residue | 129 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting. Deubiquitinated by USP35 or USP38; leading to stabilization.
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. The acetylated form represses STAT3 transactivation. 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.
In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes. Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities. Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Monomer or homodimer. Exists as a homodimer in the apo state and as a monomer in the CPC-bound state. The monomer protects cells against apoptosis more efficiently than the dimer. Only the dimeric form is capable of enhancing tubulin stability in cells. When phosphorylated, interacts with LAMTOR5/HBXIP; the resulting complex binds pro-CASP9, as well as active CASP9, but much less efficiently. Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex forms a triple-helix bundle-based subcomplex with INCENP and CDCA8. Interacts with JTB. Interacts (via BIR domain) with histone H3 phosphorylated at 'Thr-3' (H3pT3). Interacts with EVI5. Interacts with GTP-bound RAN in both the S and M phases of the cell cycle. Interacts with USP9X. Interacts with tubulin. Interacts with BIRC2/c-IAP1. The acetylated form at Lys-129 interacts with STAT3. The monomeric form deacetylated at Lys-129 interacts with XPO1/CRM1. The monomeric form interacts with XIAP/BIRC4. Both the dimeric and monomeric form can interact with DIABLO/SMAC. Interacts with BIRC6/bruce. Interacts with FBXL7; this interaction facilitates the polyubiquitination and subsequent proteasomal degradation of BIRC5 by the SCF(FBXL7) E3 ubiquitin-protein ligase complex (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 18-88 | BIR | ||||
Sequence: RIATFKNWPFLEDCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLT | ||||||
Compositional bias | 113-130 | Basic and acidic residues | ||||
Sequence: IAKETNNKQKEFEETAKT | ||||||
Region | 113-140 | Disordered | ||||
Sequence: IAKETNNKQKEFEETAKTTRQSIEQLAA |
Domain
The BIR repeat is necessary and sufficient for LAMTOR5 binding.
Sequence similarities
Belongs to the IAP family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O70201-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsSurvivin 140
- Length140
- Mass (Da)16,298
- Last updated1998-08-01 v1
- Checksum26F5ABF501A6D83C
O70201-2
- Name2
- SynonymsSurvivin 121
- Differences from canonical
- 114-140: AKETNNKQKEFEETAKTTRQSIEQLAA → VCMIENKD
O70201-3
- Name3
- SynonymsSurvivin 40
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002455 | 38-40 | in isoform 3 | |||
Sequence: MAE → RGA | ||||||
Alternative sequence | VSP_002456 | 41-140 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 113-130 | Basic and acidic residues | ||||
Sequence: IAKETNNKQKEFEETAKT | ||||||
Alternative sequence | VSP_002457 | 114-140 | in isoform 2 | |||
Sequence: AKETNNKQKEFEETAKTTRQSIEQLAA → VCMIENKD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF077349 EMBL· GenBank· DDBJ | AAD34225.1 EMBL· GenBank· DDBJ | mRNA | ||
AB013819 EMBL· GenBank· DDBJ | BAA28266.1 EMBL· GenBank· DDBJ | mRNA | ||
AF115517 EMBL· GenBank· DDBJ | AAD26199.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF115517 EMBL· GenBank· DDBJ | AAD26200.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF115517 EMBL· GenBank· DDBJ | AAD26201.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004702 EMBL· GenBank· DDBJ | AAH04702.1 EMBL· GenBank· DDBJ | mRNA |