Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Baculoviral IAP repeat-containing protein 5

Gene

BIRC5

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571ZincPROSITE-ProRule annotation
Metal bindingi60 – 601ZincPROSITE-ProRule annotation
Metal bindingi77 – 771ZincPROSITE-ProRule annotation
Metal bindingi84 – 841ZincPROSITE-ProRule annotation

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

Protein family/group databases

MEROPSiI32.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Baculoviral IAP repeat-containing protein 5
Alternative name(s):
Apoptosis inhibitor survivin
Gene namesi
Name:BIRC5
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
Proteomesi
  • UP000011712 Componenti: Chromosome E1

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 142142Baculoviral IAP repeat-containing protein 5PRO_0000226730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231N6-acetyllysineBy similarity
Modified residuei34 – 341Phosphothreonine; by CDK1 and CDK15By similarity
Modified residuei48 – 481PhosphothreonineBy similarity
Modified residuei90 – 901N6-acetyllysineBy similarity
Modified residuei110 – 1101N6-acetyllysineBy similarity
Modified residuei112 – 1121N6-acetyllysineBy similarity
Modified residuei115 – 1151N6-acetyllysineBy similarity
Modified residuei117 – 1171Phosphothreonine; by AURKBBy similarity
Modified residuei129 – 1291N6-acetyllysineBy similarity

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

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 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).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000016716.

Structurei

3D structure databases

ProteinModelPortaliQ6I6F4.
SMRiQ6I6F4. Positions 5-142.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 8871BIRAdd
BLAST

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.
InParanoidiQ6I6F4.
KOiK08731.
OMAiSCTPERM.
TreeFamiTF342652.

Family and domain databases

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]

Sequencei

Sequence statusi: Complete.

Q6I6F4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGASSLPPAW QLYLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN
60 70 80 90 100
EPDLAQCFFC FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLSE
110 120 130 140
FLKLDKERAK NKIAKETNHK QKEFEETAKR VRCAIEQLAA LE
Length:142
Mass (Da):16,393
Last modified:July 19, 2004 - v1
Checksum:i45E67A17622798C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB182320 mRNA. Translation: BAD23994.1.
RefSeqiNP_001009280.1. NM_001009280.1.

Genome annotation databases

EnsembliENSFCAT00000029978; ENSFCAP00000016716; ENSFCAG00000023080.
GeneIDi493835.
KEGGifca:493835.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB182320 mRNA. Translation: BAD23994.1.
RefSeqiNP_001009280.1. NM_001009280.1.

3D structure databases

ProteinModelPortaliQ6I6F4.
SMRiQ6I6F4. Positions 5-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000016716.

Protein family/group databases

MEROPSiI32.005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSFCAT00000029978; ENSFCAP00000016716; ENSFCAG00000023080.
GeneIDi493835.
KEGGifca:493835.

Organism-specific databases

CTDi332.

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00510000047537.
HOGENOMiHOG000008032.
HOVERGENiHBG050690.
InParanoidiQ6I6F4.
KOiK08731.
OMAiSCTPERM.
TreeFamiTF342652.

Family and domain databases

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...

Publicationsi

  1. "Felis catus mRNA for survivin."
    Inoue C., Kano R.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiBIRC5_FELCA
AccessioniPrimary (citable) accession number: Q6I6F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 19, 2004
Last modified: March 16, 2016
This is version 86 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

Complete proteome, Reference proteome

Documents

  1. 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.