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Baculoviral IAP repeat-containing protein 5 (Apoptosis inhibitor survivin)

 BIRC5_CAVPO             Reviewed;         142 AA.
E3SCZ8;
07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 1.
25-OCT-2017, entry version 44.
RecName: Full=Baculoviral IAP repeat-containing protein 5 {ECO:0000305};
AltName: Full=Apoptosis inhibitor survivin {ECO:0000303|PubMed:20727954, ECO:0000303|PubMed:21364656};
Name=BIRC5 {ECO:0000303|PubMed:20627126, ECO:0000312|EMBL:ACZ18223.1};
Cavia porcellus (Guinea pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
Hystricomorpha; Caviidae; Cavia.
NCBI_TaxID=10141;
[1] {ECO:0000312|EMBL:ACZ18223.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, MUTAGENESIS OF PHE-93; LEU-96 AND LEU-98, AND
PHYLOGENETIC ANALYSIS.
TISSUE=Spleen {ECO:0000303|PubMed:20727954};
PubMed=20727954; DOI=10.1016/j.gene.2010.08.007;
Habtemichael N., Wunsch D., Bier C., Tillmann S., Unruhe B.,
Frauenknecht K., Heinrich U.R., Mann W.J., Stauber R.H., Knauer S.K.;
"Cloning and functional characterization of the guinea pig apoptosis
inhibitor protein Survivin.";
Gene 469:9-17(2010).
[2] {ECO:0000312|Proteomes:UP000005447}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=2N {ECO:0000312|Proteomes:UP000005447};
PubMed=21993624; DOI=10.1038/nature10530;
Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
Pedersen J.S., Lander E.S., Kellis M.;
"A high-resolution map of human evolutionary constraint using 29
mammals.";
Nature 478:476-482(2011).
[3]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=21364656; DOI=10.1038/cddis.2010.25;
Knauer S.K., Heinrich U.R., Bier C., Habtemichael N., Docter D.,
Helling K., Mann W.J., Stauber R.H.;
"An otoprotective role for the apoptosis inhibitor protein survivin.";
Cell Death Dis. 1:E51-E51(2010).
[4]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=20627126; DOI=10.1016/j.mcn.2010.07.003;
Habtemichael N., Heinrich U.R., Knauer S.K., Schmidtmann I., Bier C.,
Docter D., Brochhausen C., Helling K., Brieger J., Stauber R.H.,
Mann W.J.;
"Expression analysis suggests a potential cytoprotective role of Birc5
in the inner ear.";
Mol. Cell. Neurosci. 45:297-305(2010).
-!- FUNCTION: Multitasking protein that has dual roles in promoting
cell proliferation and preventing apoptosis (PubMed:20727954,
PubMed:21364656, PubMed:20627126). Component of a chromosome
passage protein complex (CPC) which is essential for chromosome
alignment and segregation during mitosis and cytokinesis
(PubMed:20727954). 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. May
play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By
similarity). {ECO:0000250|UniProtKB:O15392,
ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954,
ECO:0000269|PubMed:21364656}.
-!- SUBUNIT: 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 monomeric
form interacts with XIAP/BIRC4. Both the dimeric and monomeric
form can interact with DIABLO/SMAC. Interacts with BIRC6/bruce.
{ECO:0000250|UniProtKB:O15392}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20627126,
ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. Nucleus
{ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954,
ECO:0000269|PubMed:21364656}. Chromosome
{ECO:0000250|UniProtKB:O15392}. Chromosome, centromere
{ECO:0000269|PubMed:20727954}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:20727954}. Chromosome, centromere, kinetochore
{ECO:0000250|UniProtKB:O15392}. Midbody
{ECO:0000269|PubMed:20727954}. Note=Localizes at the centromeres
from prophase to metaphase, at the spindle midzone during anaphase
and a the midbody during telophase and cytokinesis. Accumulates in
the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1
nuclear export inhibitor (PubMed:20727954). 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 (By similarity). {ECO:0000250|UniProtKB:O15392,
ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954,
ECO:0000269|PubMed:21364656}.
-!- TISSUE SPECIFICITY: Expressed in spleen, lung, brain, heart,
kidney and intestine (at protein level) (PubMed:20727954).
Expressed in cochlea including the organ of Corti, the lateral
wall, the interdental cells of the Limbus as well as in cells of
the cochlear nerve and the spiral ganglions (at protein level)
(PubMed:20727954, PubMed:21364656, PubMed:20627126). Also
expressed in Schwann cells (at protein level) (PubMed:21364656,
PubMed:20627126). Not expressed in cells of the inner and outer
sulcus or the Reissner's membrane (at protein level)
(PubMed:20727954, PubMed:21364656, PubMed:20627126).
{ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954,
ECO:0000269|PubMed:21364656}.
-!- INDUCTION: Expression is up-regulated in the spiral ligament and
nerve fibers of the cochlea upon moderate noise exposure causing
only a temporary hearing impairment. Expression is down-regulated
in the organ of Corti, the spiral ganglion, the stria vascularis
and the spiral ligament of the cochlea upon intratympanic
injection of aminoglycoside antibiotic gentamicin inducing cell
damage and permanent hearing loss. {ECO:0000269|PubMed:20627126,
ECO:0000269|PubMed:21364656}.
-!- DOMAIN: The BIR repeat is necessary and sufficient for LAMTOR5
binding. {ECO:0000250|UniProtKB:O15392}.
-!- PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase
complex, leading to its degradation. Ubiquitination is required
for centrosomal targeting. {ECO:0000250|UniProtKB:O15392}.
-!- PTM: 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. Phosphorylation at Ser-
20 by AURKC is critical for regulation of proper chromosome
alignment and segregation, and possibly cytokinesis.
{ECO:0000250|UniProtKB:O15392}.
-!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; GQ496319; ACZ18223.1; -; mRNA.
EMBL; AAKN02047321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001186646.1; NM_001199717.1.
SMR; E3SCZ8; -.
STRING; 10141.ENSCPOP00000016661; -.
MEROPS; I32.005; -.
GeneID; 100527953; -.
CTD; 332; -.
eggNOG; KOG1101; Eukaryota.
eggNOG; ENOG410YPNM; LUCA.
OMA; APQCEFV; -.
OrthoDB; EOG091G0T73; -.
TreeFam; TF342652; -.
Proteomes; UP000005447; Unassembled WGS sequence.
Bgee; ENSCPOG00000027390; -.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00022; BIR; 1.
InterPro; IPR001370; BIR_rpt.
Pfam; PF00653; BIR; 1.
SMART; SM00238; BIR; 1.
PROSITE; PS50143; BIR_REPEAT_2; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Cell cycle; Cell division; Centromere;
Chromosome; Chromosome partition; Complete proteome; Cytoplasm;
Cytoskeleton; Kinetochore; Metal-binding; Microtubule; Mitosis;
Nucleus; Phosphoprotein; Protease inhibitor; Reference proteome;
Repressor; Stress response; Thiol protease inhibitor; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 142 Baculoviral IAP repeat-containing protein
5.
/FTId=PRO_0000440217.
REPEAT 18 88 BIR. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 57 57 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 60 60 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 77 77 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 84 84 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
MOD_RES 20 20 Phosphoserine; by AURKC.
{ECO:0000250|UniProtKB:O15392}.
MOD_RES 23 23 N6-acetyllysine.
{ECO:0000250|UniProtKB:O15392}.
MOD_RES 34 34 Phosphothreonine; by CDK1 and CDK15.
{ECO:0000250|UniProtKB:O15392}.
MOD_RES 48 48 Phosphothreonine; by CK2; in vitro.
{ECO:0000250|UniProtKB:O15392}.
MOD_RES 90 90 N6-acetyllysine.
{ECO:0000250|UniProtKB:O15392}.
MOD_RES 110 110 N6-acetyllysine.
{ECO:0000250|UniProtKB:O15392}.
MOD_RES 112 112 N6-acetyllysine.
{ECO:0000250|UniProtKB:O15392}.
MOD_RES 115 115 N6-acetyllysine.
{ECO:0000250|UniProtKB:O15392}.
MOD_RES 117 117 Phosphothreonine; by AURKB.
{ECO:0000250|UniProtKB:O15392}.
MUTAGEN 93 93 F->P: Disrupts nuclear export and loss of
cytoprotection; when associated with A-96
and A-98. {ECO:0000269|PubMed:20727954}.
MUTAGEN 96 96 L->A: Disrupts nuclear export and loss of
cytoprotection; when associated with P-93
and A-98. {ECO:0000269|PubMed:20727954}.
MUTAGEN 98 98 L->A: Disrupts nuclear export and loss of
cytoprotection; when associated with P-93
and A-96. {ECO:0000269|PubMed:20727954}.
SEQUENCE 142 AA; 16356 MW; 791171160207C2C8 CRC64;
MGAPSLPRAW QLYLKEHRVS TFKNWPFVNG CSCTPERMAE AGFIHCPTEN EPDLAQCFFC
FKELEGWEPD DNPIEEHKKH SSGCAFLSVK KQFEELTLSE FLKLDKERAK NKIAKETNSK
QKEFEETAAK VRQAMEQLAA LE


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