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O70201 (BIRC5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Baculoviral IAP repeat-containing protein 5
Alternative name(s):
Apoptosis inhibitor 4
Apoptosis inhibitor survivin
TIAP
Gene names
Name:Birc5
Synonyms:Api4, Iap4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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.

Subunit structure

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 and AURKC. Interacts with JTB. Interacts with CDCA8 and INCENP; interaction is direct. 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.

Subcellular location

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.

Domain

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

Post-translational modification

Ubiquitination is required for centrosomal targeting By similarity.

In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes 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.

Sequence similarities

Belongs to the IAP family.

Contains 1 BIR repeat.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Cell division
Chromosome partition
Mitosis
Transcription
Transcription regulation
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
Zinc
   Molecular functionProtease inhibitor
Repressor
Thiol protease inhibitor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

cell division

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of chromosome localization

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from mutant phenotype PubMed 11084331. Source: MGI

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 16049172. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of exit from mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex localization

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype PubMed 19644667. Source: MGI

regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 19644667. Source: MGI

regulation of type B pancreatic cell proliferation

Inferred from mutant phenotype PubMed 19644667. Source: MGI

spindle checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentriole

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome passenger complex

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome, centromeric region

Inferred from sequence or structural similarity. Source: UniProtKB

condensed chromosome kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

interphase microtubule organizing center

Inferred from sequence or structural similarity. Source: UniProtKB

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

spindle microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncofactor binding

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17881355. Source: MGI

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O70201-1)

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.
Isoform 2 (identifier: O70201-2)

Also known as: Survivin 121;

The sequence of this isoform differs from the canonical sequence as follows:
     114-140: AKETNNKQKEFEETAKTTRQSIEQLAA → VCMIENKD
Isoform 3 (identifier: O70201-3)

Also known as: Survivin 40;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 140140Baculoviral IAP repeat-containing protein 5
PRO_0000122357

Regions

Repeat18 – 8871BIR

Sites

Metal binding571Zinc 1
Metal binding601Zinc 1
Metal binding761Zinc 2
Metal binding771Zinc 1
Metal binding801Zinc 2
Metal binding841Zinc 1

Amino acid modifications

Modified residue231N6-acetyllysine By similarity
Modified residue341Phosphothreonine; by CDK1 Ref.5
Modified residue481Phosphothreonine By similarity
Modified residue901N6-acetyllysine By similarity
Modified residue1101N6-acetyllysine By similarity
Modified residue1121N6-acetyllysine By similarity
Modified residue1151N6-acetyllysine By similarity
Modified residue1171Phosphothreonine; by AURKB By similarity
Modified residue1291N6-acetyllysine By similarity

Natural variations

Alternative sequence38 – 403MAE → RGA in isoform 3.
VSP_002455
Alternative sequence41 – 140100Missing in isoform 3.
VSP_002456
Alternative sequence114 – 14027AKETN…EQLAA → VCMIENKD in isoform 2.
VSP_002457

Secondary structure

...................... 140
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Survivin 140) [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 26F5ABF501A6D83C

FASTA14016,298
        10         20         30         40         50         60 
MGAPALPQIW QLYLKNYRIA TFKNWPFLED CACTPERMAE AGFIHCPTEN EPDLAQCFFC 

        70         80         90        100        110        120 
FKELEGWEPD DNPIEEHRKH SPGCAFLTVK KQMEELTVSE FLKLDRQRAK NKIAKETNNK 

       130        140 
QKEFEETAKT TRQSIEQLAA 

« Hide

Isoform 2 (Survivin 121) [UniParc].

Checksum: 1E0EC7E01BA65585
Show »

FASTA12114,154
Isoform 3 (Survivin 40) [UniParc].

Checksum: FAD3C7E34A20518C
Show »

FASTA404,670

References

« Hide 'large scale' references
[1]"Mammalian inhibitor of apoptosis (IAP) homolog."
Uren A.G., Vaux D.L.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Kobayashi K., Otaki M., Ogasawara T., Tokuhisa T.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Embryo.
[3]"Three differentially expressed survivin cDNA variants encode proteins with distinct antiapoptotic functions."
Conway E.M., Pollefeyt S., Cornelissen J., DeBaere I., Steiner-Mosonyi M., Ong K., Baens M., Collen D., Schuh A.C.
Blood 95:1435-1442(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 7-118, PHOSPHORYLATION AT THR-34.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS25694.1. [O70201-1]
CCDS25695.1. [O70201-2]
RefSeqNP_001012273.1. NM_001012273.1. [O70201-2]
NP_033819.1. NM_009689.2. [O70201-1]
UniGeneMm.8552.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M4MX-ray2.80A1-140[»]
ProteinModelPortalO70201.
SMRO70201. Positions 7-118.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI32.005.

PTM databases

PhosphoSiteO70201.

Proteomic databases

MaxQBO70201.
PRIDEO70201.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081387; ENSMUSP00000079124; ENSMUSG00000017716. [O70201-1]
ENSMUST00000093906; ENSMUSP00000091433; ENSMUSG00000017716. [O70201-2]
GeneID11799.
KEGGmmu:11799.
UCSCuc007mod.1. mouse. [O70201-1]

Organism-specific databases

CTD332.
MGIMGI:1203517. Birc5.

Phylogenomic databases

eggNOGNOG271140.
GeneTreeENSGT00510000047537.
HOGENOMHOG000008032.
HOVERGENHBG050690.
InParanoidO70201.
KOK08731.
OMANSPDIAM.
OrthoDBEOG7SFJ01.
PhylomeDBO70201.
TreeFamTF342652.

Gene expression databases

ArrayExpressO70201.
BgeeO70201.
CleanExMM_BIRC5.
GenevestigatorO70201.

Family and domain databases

Gene3D1.10.1170.10. 1 hit.
InterProIPR001370. BIR.
[Graphical view]
PfamPF00653. BIR. 1 hit.
[Graphical view]
SMARTSM00238. BIR. 1 hit.
[Graphical view]
PROSITEPS50143. BIR_REPEAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO70201.
NextBio279641.
PROO70201.
SOURCESearch...

Entry information

Entry nameBIRC5_MOUSE
AccessionPrimary (citable) accession number: O70201
Secondary accession number(s): Q923F7, Q9WU53, Q9WU54
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot