BIRC5_BOVIN
ID BIRC5_BOVIN Reviewed; 142 AA.
AC Q6J1J1; Q32LI0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Baculoviral IAP repeat-containing protein 5;
DE AltName: Full=Apoptosis inhibitor survivin;
GN Name=BIRC5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gutierrez-Adan A.;
RT "mRNA expression in sheep and cattle blastocysts.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multitasking protein that has dual roles in promoting cell
CC proliferation and preventing apoptosis (By similarity). Component of a
CC chromosome passage protein complex (CPC) which is essential for
CC chromosome alignment and segregation during mitosis and cytokinesis (By
CC similarity). Acts as an important regulator of the localization of this
CC complex; directs CPC movement to different locations from the inner
CC centromere during prometaphase to midbody during cytokinesis and
CC participates in the organization of the center spindle by associating
CC with polymerized microtubules (By similarity). Involved in the
CC recruitment of CPC to centromeres during early mitosis via association
CC with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By
CC similarity). The complex with RAN plays a role in mitotic spindle
CC formation by serving as a physical scaffold to help deliver the RAN
CC effector molecule TPX2 to microtubules (By similarity). May counteract
CC a default induction of apoptosis in G2/M phase (By similarity). The
CC acetylated form represses STAT3 transactivation of target gene
CC promoters (By similarity). May play a role in neoplasia. Inhibitor of
CC CASP3 and CASP7 (By similarity). Essential for the maintenance of
CC mitochondrial integrity and function (By similarity).
CC {ECO:0000250|UniProtKB:O15392}.
CC -!- SUBUNIT: Monomer or homodimer. Exists as a homodimer in the apo state
CC and as a monomer in the CPC-bound state. The monomer protects cells
CC against apoptosis more efficiently than the dimer. Only the dimeric
CC form is capable of enhancing tubulin stability in cells. When
CC phosphorylated, interacts with LAMTOR5/HBXIP; the resulting complex
CC binds pro-CASP9, as well as active CASP9, but much less efficiently.
CC Component of the chromosomal passenger complex (CPC) composed of at
CC least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the
CC complex forms a triple-helix bundle-based subcomplex with INCENP and
CC CDCA8. Interacts with JTB. Interacts (via BIR domain) with histone H3
CC phosphorylated at 'Thr-3' (H3pT3). Interacts with EVI5. Interacts with
CC GTP-bound RAN in both the S and M phases of the cell cycle. Interacts
CC with USP9X. Interacts with tubulin. Interacts with BIRC2/c-IAP1. The
CC acetylated form at Lys-129 interacts with STAT3. The monomeric form
CC deacetylated at Lys-129 interacts with XPO1/CRM1. The monomeric form
CC interacts with XIAP/BIRC4. Both the dimeric and monomeric form can
CC interact with DIABLO/SMAC. Interacts with BIRC6/bruce. Interacts with
CC FBXL7; this interaction facilitates the polyubiquitination and
CC subsequent proteasomal degradation of BIRC5 by the SCF(FBXL7) E3
CC ubiquitin-protein ligase complex (By similarity).
CC {ECO:0000250|UniProtKB:O15392}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus
CC {ECO:0000250|UniProtKB:O15392}. Chromosome
CC {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O15392}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:O15392}. Midbody {ECO:0000250|UniProtKB:O15392}.
CC Note=Localizes at the centromeres from prophase to metaphase, at the
CC spindle midzone during anaphase and a the midbody during telophase and
CC cytokinesis. Accumulates in the nucleus upon treatment with leptomycin
CC B (LMB), a XPO1/CRM1 nuclear export inhibitor (By similarity).
CC Localizes on chromosome arms and inner centromeres from prophase
CC through metaphase. Localizes to kinetochores in metaphase, distributes
CC to the midzone microtubules in anaphase and at telophase, localizes
CC exclusively to the midbody. Colocalizes with AURKB at mitotic
CC chromosomes. Acetylation at Lys-129 directs its localization to the
CC nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-
CC mediated nuclear export (By similarity). {ECO:0000250|UniProtKB:E3SCZ8,
CC ECO:0000250|UniProtKB:O15392}.
CC -!- DOMAIN: The BIR repeat is necessary and sufficient for LAMTOR5 binding.
CC {ECO:0000250|UniProtKB:O15392}.
CC -!- PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex,
CC leading to its degradation. Ubiquitination is required for centrosomal
CC targeting. {ECO:0000250|UniProtKB:O15392}.
CC -!- PTM: Acetylation at Lys-129 results in its homodimerization, while
CC deacetylation promotes the formation of monomers which heterodimerize
CC with XPO1/CRM1 which facilitates its nuclear export. The acetylated
CC form represses STAT3 transactivation. The dynamic equilibrium between
CC its acetylation and deacetylation at Lys-129 determines its interaction
CC with XPO1/CRM1, its subsequent subcellular localization, and its
CC ability to inhibit STAT3 transactivation.
CC {ECO:0000250|UniProtKB:O15392}.
CC -!- PTM: In vitro phosphorylation at Thr-117 by AURKB prevents interaction
CC with INCENP and localization to mitotic chromosomes. Phosphorylation at
CC Thr-48 by CK2 is critical for its mitotic and anti-apoptotic
CC activities. Phosphorylation at Thr-34 by CDK15 is critical for its
CC anti-apoptotic activity. Phosphorylation at Ser-20 by AURKC is critical
CC for regulation of proper chromosome alignment and segregation, and
CC possibly cytokinesis. {ECO:0000250|UniProtKB:O15392}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR EMBL; AY606044; AAT37504.1; -; mRNA.
DR EMBL; BC109566; AAI09567.1; -; mRNA.
DR RefSeq; NP_001001855.2; NM_001001855.3.
DR AlphaFoldDB; Q6J1J1; -.
DR SMR; Q6J1J1; -.
DR STRING; 9913.ENSBTAP00000018046; -.
DR MEROPS; I32.005; -.
DR PaxDb; Q6J1J1; -.
DR PRIDE; Q6J1J1; -.
DR Ensembl; ENSBTAT00000018046; ENSBTAP00000018046; ENSBTAG00000013573.
DR GeneID; 414925; -.
DR KEGG; bta:414925; -.
DR CTD; 332; -.
DR VEuPathDB; HostDB:ENSBTAG00000013573; -.
DR VGNC; VGNC:26501; BIRC5.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00510000047537; -.
DR HOGENOM; CLU_016347_0_1_1; -.
DR InParanoid; Q6J1J1; -.
DR OMA; FEGWPFD; -.
DR OrthoDB; 1404665at2759; -.
DR TreeFam; TF342652; -.
DR Reactome; R-BTA-8951664; Neddylation.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000013573; Expressed in spermatid and 105 other tissues.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0032133; C:chromosome passenger complex; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031021; C:interphase microtubule organizing center; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0051303; P:establishment of chromosome localization; ISS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0007127; P:meiosis I; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0031536; P:positive regulation of exit from mitosis; ISS:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0031503; P:protein-containing complex localization; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; IEA:Ensembl.
DR CDD; cd00022; BIR; 1.
DR InterPro; IPR001370; BIR_rpt.
DR Pfam; PF00653; BIR; 1.
DR SMART; SM00238; BIR; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Kinetochore; Metal-binding;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Protease inhibitor;
KW Reference proteome; Repressor; Thiol protease inhibitor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..142
FT /note="Baculoviral IAP repeat-containing protein 5"
FT /id="PRO_0000226729"
FT REPEAT 18..88
FT /note="BIR"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT SITE 126
FT /note="Interaction with FBXL7"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 20
FT /note="Phosphoserine; by AURKC"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 34
FT /note="Phosphothreonine; by CDK1 and CDK15"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 117
FT /note="Phosphothreonine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT MOD_RES 129
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15392"
FT CONFLICT 2..4
FT /note="GAQ -> SAP (in Ref. 1; AAT37504)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="V -> I (in Ref. 1; AAT37504)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="A -> E (in Ref. 1; AAT37504)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="F -> L (in Ref. 1; AAT37504)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="T -> A (in Ref. 1; AAT37504)"
FT /evidence="ECO:0000305"
FT CONFLICT 139..142
FT /note="AALE -> VAMD (in Ref. 1; AAT37504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 16341 MW; 577CA9AC3FDB9E68 CRC64;
MGAQSLPPAW QLYLKDHRVS TFKNWPFLEG CACTPERMAA AGFIHCPTEN EPDLAQCFFC
FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLSE FLKLDKERTK NKIAKETNNK
QKEFEETAKK VRCAIEQLAA LE
