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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi57Zinc 11
Metal bindingi60Zinc 11
Metal bindingi76Zinc 21
Metal bindingi77Zinc 11
Metal bindingi80Zinc 21
Metal bindingi84Zinc 11

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionProtease inhibitor, Repressor, Thiol protease inhibitor
Biological processApoptosis, Cell cycle, Cell division, Chromosome partition, Mitosis, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-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
R-MMU-8951664 Neddylation

Protein family/group databases

MEROPS protease database

More...
MEROPSi
I32.005

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Baculoviral IAP repeat-containing protein 5
Alternative name(s):
Apoptosis inhibitor 4
Apoptosis inhibitor survivin
TIAP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Birc5
Synonyms:Api4, Iap4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1203517 Birc5

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001223571 – 140Baculoviral IAP repeat-containing protein 5Add BLAST140

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei23N6-acetyllysineBy similarity1
Modified residuei34Phosphothreonine; by CDK1 and CDK151 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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Encyclopedia of Proteome Dynamics

More...
EPDi
O70201

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O70201

PeptideAtlas

More...
PeptideAtlasi
O70201

PRoteomics IDEntifications database

More...
PRIDEi
O70201

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O70201

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O70201

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000017716 Expressed in 259 organ(s), highest expression level in primary oocyte

CleanEx database of gene expression profiles

More...
CleanExi
MM_BIRC5

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O70201 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O70201 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
198150, 2 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-113 Survivin homodimer complex
CPX-119 Chromosomal passenger complex

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000079124

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1140
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M4MX-ray2.80A1-140[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
O70201

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O70201

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O70201

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati18 – 88BIRAdd BLAST71

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the IAP family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1101 Eukaryota
ENOG410YPNM LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00510000047537

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000008032

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG050690

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O70201

KEGG Orthology (KO)

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KOi
K08731

Identification of Orthologs from Complete Genome Data

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OMAi
APQCEFV

Database of Orthologous Groups

More...
OrthoDBi
1404665at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O70201

TreeFam database of animal gene trees

More...
TreeFami
TF342652

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00022 BIR, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001370 BIR_rpt

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00653 BIR, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00238 BIR, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50143 BIR_REPEAT_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS25694.1 [O70201-1]
CCDS25695.1 [O70201-2]

NCBI Reference Sequences

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RefSeqi
NP_001012273.1, NM_001012273.1 [O70201-2]
NP_033819.1, NM_009689.2 [O70201-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.8552

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000081387; ENSMUSP00000079124; ENSMUSG00000017716 [O70201-1]
ENSMUST00000093906; ENSMUSP00000091433; ENSMUSG00000017716 [O70201-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
11799

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:11799

UCSC genome browser

More...
UCSCi
uc007mod.1 mouse [O70201-1]
uc007moe.1 mouse [O70201-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

BioGridi198150, 2 interactors
ComplexPortaliCPX-113 Survivin homodimer complex
CPX-119 Chromosomal passenger complex
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

Comparative Toxicogenomics Database

More...
CTDi
332
MGIiMGI:1203517 Birc5

Phylogenomic databases

eggNOGiKOG1101 Eukaryota
ENOG410YPNM LUCA
GeneTreeiENSGT00510000047537
HOGENOMiHOG000008032
HOVERGENiHBG050690
InParanoidiO70201
KOiK08731
OMAiAPQCEFV
OrthoDBi1404665at2759
PhylomeDBiO70201
TreeFamiTF342652

Enzyme and pathway databases

ReactomeiR-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-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
R-MMU-8951664 Neddylation

Miscellaneous databases

EvolutionaryTraceiO70201

Protein Ontology

More...
PROi
PR:O70201

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000017716 Expressed in 259 organ(s), highest expression level in primary oocyte
CleanExiMM_BIRC5
ExpressionAtlasiO70201 baseline and differential
GenevisibleiO70201 MM

Family and domain databases

CDDicd00022 BIR, 1 hit
InterProiView protein in InterPro
IPR001370 BIR_rpt
PfamiView protein in Pfam
PF00653 BIR, 1 hit
SMARTiView protein in SMART
SM00238 BIR, 1 hit
PROSITEiView protein in PROSITE
PS50143 BIR_REPEAT_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBIRC5_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O70201
Secondary accession number(s): Q923F7, Q9WU53, Q9WU54
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 16, 2019
This is version 174 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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