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Protein

Baculoviral IAP repeat-containing protein 5

Gene

Birc5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi57Zinc 11
Metal bindingi60Zinc 11
Metal bindingi76Zinc 21
Metal bindingi77Zinc 11
Metal bindingi80Zinc 21
Metal bindingi84Zinc 11

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Repressor, Thiol protease inhibitor

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Chromosome partition, Mitosis, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Protein family/group databases

MEROPSiI32.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Baculoviral IAP repeat-containing protein 5
Alternative name(s):
Apoptosis inhibitor 4
Apoptosis inhibitor survivin
TIAP
Gene namesi
Name:Birc5
Synonyms:Api4, Iap4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1203517. Birc5.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Chromosome
  • Chromosomecentromere By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Chromosomecentromerekinetochore By similarity
  • Midbody By similarity

  • Note: 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001223571 – 140Baculoviral IAP repeat-containing protein 5Add BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23N6-acetyllysineBy similarity1
Modified residuei34Phosphothreonine; by CDK1 and CDK15By similarity1 Publication1
Modified residuei48PhosphothreonineBy similarity1
Modified residuei90N6-acetyllysineBy similarity1
Modified residuei110N6-acetyllysineBy similarity1
Modified residuei112N6-acetyllysineBy similarity1
Modified residuei115N6-acetyllysineBy similarity1
Modified residuei117Phosphothreonine; by AURKBBy similarity1
Modified residuei129N6-acetyllysineBy similarity1

Post-translational modificationi

Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting (By similarity).By similarity
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 (By similarity).By similarity
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.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO70201.
PaxDbiO70201.
PeptideAtlasiO70201.
PRIDEiO70201.

PTM databases

iPTMnetiO70201.
PhosphoSitePlusiO70201.

Expressioni

Gene expression databases

BgeeiENSMUSG00000017716.
CleanExiMM_BIRC5.
ExpressionAtlasiO70201. baseline and differential.
GenevisibleiO70201. MM.

Interactioni

Subunit structurei

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000079124.

Structurei

Secondary structure

1140
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 13Combined sources3
Helixi15 – 20Combined sources6
Beta strandi29 – 31Combined sources3
Helixi35 – 40Combined sources6
Beta strandi43 – 45Combined sources3
Beta strandi55 – 57Combined sources3
Turni58 – 60Combined sources3
Helixi73 – 79Combined sources7
Helixi85 – 88Combined sources4
Helixi93 – 95Combined sources3
Helixi98 – 116Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M4MX-ray2.80A1-140[»]
ProteinModelPortaliO70201.
SMRiO70201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70201.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati18 – 88BIRAdd BLAST71

Domaini

The BIR repeat is necessary and sufficient for LAMTOR5 binding.By similarity

Sequence similaritiesi

Belongs to the IAP family.Curated
Contains 1 BIR repeat.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00510000047537.
HOGENOMiHOG000008032.
HOVERGENiHBG050690.
InParanoidiO70201.
KOiK08731.
OMAiSCTPERM.
OrthoDBiEOG091G0T73.
PhylomeDBiO70201.
TreeFamiTF342652.

Family and domain databases

CDDicd00022. BIR. 1 hit.
Gene3Di1.10.1170.10. 1 hit.
InterProiIPR001370. BIR_rpt.
[Graphical view]
PfamiPF00653. BIR. 1 hit.
[Graphical view]
SMARTiSM00238. BIR. 1 hit.
[Graphical view]
PROSITEiPS50143. BIR_REPEAT_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O70201-1) [UniParc]FASTAAdd to basket
Also known as: Survivin 140

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.

« Hide

        10         20         30         40         50
MGAPALPQIW QLYLKNYRIA TFKNWPFLED CACTPERMAE AGFIHCPTEN
60 70 80 90 100
EPDLAQCFFC FKELEGWEPD DNPIEEHRKH SPGCAFLTVK KQMEELTVSE
110 120 130 140
FLKLDRQRAK NKIAKETNNK QKEFEETAKT TRQSIEQLAA
Length:140
Mass (Da):16,298
Last modified:August 1, 1998 - v1
Checksum:i26F5ABF501A6D83C
GO
Isoform 2 (identifier: O70201-2) [UniParc]FASTAAdd to basket
Also known as: Survivin 121

The sequence of this isoform differs from the canonical sequence as follows:
     114-140: AKETNNKQKEFEETAKTTRQSIEQLAA → VCMIENKD

Show »
Length:121
Mass (Da):14,154
Checksum:i1E0EC7E01BA65585
GO
Isoform 3 (identifier: O70201-3) [UniParc]FASTAAdd to basket
Also known as: Survivin 40

The sequence of this isoform differs from the canonical sequence as follows:
     38-40: MAE → RGA
     41-140: Missing.

Show »
Length:40
Mass (Da):4,670
Checksum:iFAD3C7E34A20518C
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00245538 – 40MAE → RGA in isoform 3. Curated3
Alternative sequenceiVSP_00245641 – 140Missing in isoform 3. CuratedAdd BLAST100
Alternative sequenceiVSP_002457114 – 140AKETN…EQLAA → VCMIENKD in isoform 2. 1 PublicationAdd BLAST27

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077349 mRNA. Translation: AAD34225.1.
AB013819 mRNA. Translation: BAA28266.1.
AF115517 Genomic DNA. Translation: AAD26199.1.
AF115517 Genomic DNA. Translation: AAD26200.1.
AF115517 Genomic DNA. Translation: AAD26201.1.
BC004702 mRNA. Translation: AAH04702.1.
CCDSiCCDS25694.1. [O70201-1]
CCDS25695.1. [O70201-2]
RefSeqiNP_001012273.1. NM_001012273.1. [O70201-2]
NP_033819.1. NM_009689.2. [O70201-1]
UniGeneiMm.8552.

Genome annotation databases

EnsembliENSMUST00000081387; ENSMUSP00000079124; ENSMUSG00000017716. [O70201-1]
ENSMUST00000093906; ENSMUSP00000091433; ENSMUSG00000017716. [O70201-2]
GeneIDi11799.
KEGGimmu:11799.
UCSCiuc007mod.1. mouse. [O70201-1]
uc007moe.1. mouse. [O70201-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077349 mRNA. Translation: AAD34225.1.
AB013819 mRNA. Translation: BAA28266.1.
AF115517 Genomic DNA. Translation: AAD26199.1.
AF115517 Genomic DNA. Translation: AAD26200.1.
AF115517 Genomic DNA. Translation: AAD26201.1.
BC004702 mRNA. Translation: AAH04702.1.
CCDSiCCDS25694.1. [O70201-1]
CCDS25695.1. [O70201-2]
RefSeqiNP_001012273.1. NM_001012273.1. [O70201-2]
NP_033819.1. NM_009689.2. [O70201-1]
UniGeneiMm.8552.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M4MX-ray2.80A1-140[»]
ProteinModelPortaliO70201.
SMRiO70201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000079124.

Protein family/group databases

MEROPSiI32.005.

PTM databases

iPTMnetiO70201.
PhosphoSitePlusiO70201.

Proteomic databases

EPDiO70201.
PaxDbiO70201.
PeptideAtlasiO70201.
PRIDEiO70201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081387; ENSMUSP00000079124; ENSMUSG00000017716. [O70201-1]
ENSMUST00000093906; ENSMUSP00000091433; ENSMUSG00000017716. [O70201-2]
GeneIDi11799.
KEGGimmu:11799.
UCSCiuc007mod.1. mouse. [O70201-1]
uc007moe.1. mouse. [O70201-2]

Organism-specific databases

CTDi332.
MGIiMGI:1203517. Birc5.

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00510000047537.
HOGENOMiHOG000008032.
HOVERGENiHBG050690.
InParanoidiO70201.
KOiK08731.
OMAiSCTPERM.
OrthoDBiEOG091G0T73.
PhylomeDBiO70201.
TreeFamiTF342652.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Miscellaneous databases

EvolutionaryTraceiO70201.
PROiO70201.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000017716.
CleanExiMM_BIRC5.
ExpressionAtlasiO70201. baseline and differential.
GenevisibleiO70201. MM.

Family and domain databases

CDDicd00022. BIR. 1 hit.
Gene3Di1.10.1170.10. 1 hit.
InterProiIPR001370. BIR_rpt.
[Graphical view]
PfamiPF00653. BIR. 1 hit.
[Graphical view]
SMARTiSM00238. BIR. 1 hit.
[Graphical view]
PROSITEiPS50143. BIR_REPEAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBIRC5_MOUSE
AccessioniPrimary (citable) accession number: O70201
Secondary accession number(s): Q923F7, Q9WU53, Q9WU54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 30, 2016
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.