BIRC5
entrez
332
canonical
uniprot
O15392
canonical
ensembl
ENSG00000089685
resolver
ensp
ENSP00000301633
resolver
ensp
ENSP00000324180
resolver
ensp
ENSP00000364086
resolver
enst
ENST00000301633
resolver
enst
ENST00000350051
resolver
genesymbol
BIRC5
resolver
genesymbol_syn
API4
resolver
genesymbol_syn
IAP4
resolver
hgnc
HGNC:593
resolver
uniprot
A0A0B4J1S3
resolver
uniprot
A2SUH6
resolver
uniprot
B2R4R1
resolver
uniprot
H3BLT4
resolver
uniprot
Q2I3N8
resolver
uniprot
Q4VGX0
resolver
uniprot
Q53F61
resolver
uniprot
Q5MGC6
resolver
uniprot
Q6FHL2
resolver
uniprot
Q75SP2
resolver
uniprot
Q9P2W8
resolver
uniprot_entry
A0A0B4J1S3_HUMAN
resolver
uniprot_entry
BIRC5_HUMAN
resolver
uniprot_entry
H3BLT4_HUMAN
resolver
uniprot_sec
A2SUH6
resolver
uniprot_sec
B2R4R1
resolver
uniprot_sec
Q2I3N8
resolver
uniprot_sec
Q4VGX0
resolver
uniprot_sec
Q53F61
resolver
uniprot_sec
Q5MGC6
resolver
uniprot_sec
Q6FHL2
resolver
uniprot_sec
Q75SP2
resolver
uniprot_sec
Q9P2W8
resolver
amino_acid_sequence
MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD
uniprot
proteins
function
FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:20627126, PubMed:21364656, PubMed:25778398, PubMed:28218735, PubMed:9859993). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (PubMed:16322459). 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 (PubMed:20826784). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (PubMed:20929775). 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 (PubMed:18591255). May counteract a default induction of apoptosis in G2/M phase (PubMed:9859993). The acetylated form represses STAT3 transactivation of target gene promoters (PubMed:20826784). May play a role in neoplasia (PubMed:10626797). Inhibitor of CASP3 and CASP7 (PubMed:21536684). Essential for the maintenance of mitochondrial integrity and function (PubMed:25778398). Isoform 2 and isoform 3 do not appear to play vital roles in mitosis (PubMed:12773388, PubMed:16291752). Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform (PubMed:10626797). {ECO:0000269|PubMed:10626797, ECO:0000269|PubMed:12773388, ECO:0000269|PubMed:16291752, ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:20929775, ECO:0000269|PubMed:21364656, ECO:0000269|PubMed:21536684, ECO:0000269|PubMed:25778398, ECO:0000269|PubMed:28218735, ECO:0000269|PubMed:9859993}.
uniprot
proteins
mass_dalton
16389
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="R->A: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP."; /evidence="ECO:0000269|PubMed:20929775"; MUTAGEN 23; /note="K->R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-62; R-78 and R-79."; /evidence="ECO:0000269|PubMed:16322459"; MUTAGEN 25; /note="W->A: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP."; /evidence="ECO:0000269|PubMed:20929775"; MUTAGEN 33; /note="C->R: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP."; /evidence="ECO:0000269|PubMed:20929775"; MUTAGEN 34; /note="T->A: Loss of LAMTOR5 binding."; /evidence="ECO:0000269|PubMed:12773388"; MUTAGEN 34; /note="T->E: Higher affinity for LAMTOR5 binding."; /evidence="ECO:0000269|PubMed:12773388"; MUTAGEN 48; /note="T->A,E: Localizes normally during mitosis but cannot support cell proliferation. Increased affinity for CDCA8/borealin."; /evidence="ECO:0000269|PubMed:21252625"; MUTAGEN 57; /note="C->A: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP."; /evidence="ECO:0000269|PubMed:20929775"; MUTAGEN 62; /note="K->R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-78 and R-79."; /evidence="ECO:0000269|PubMed:16322459"; MUTAGEN 65; /note="E->A: Almost abolishes RAN-binding. Does not disrupt binding to AURKB or CDCA8. Disrupts mitotic spindle assembly. Does not disrupt nuclear export."; /evidence="ECO:0000269|PubMed:18591255"; MUTAGEN 67; /note="W->A: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP."; /evidence="ECO:0000269|PubMed:20929775"; MUTAGEN 70; /note="D->A: No change. Loss of interaction with AURKB; when associated with A-71."; /evidence="ECO:0000269|PubMed:16762323"; MUTAGEN 71; /note="D->A: No change. Loss of interaction with AURKB; when associated with A-70."; /evidence="ECO:0000269|PubMed:16762323"; MUTAGEN 78; /note="K->R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-79."; /evidence="ECO:0000269|PubMed:16322459"; MUTAGEN 79; /note="K->R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-78."; /evidence="ECO:0000269|PubMed:16322459"; MUTAGEN 84; /note="C->A: Loss of cytoprotection."; MUTAGEN 90..91; /note="KK->RR: Loss of FBXL7 mediated polyubiquitination."; /evidence="ECO:0000269|PubMed:25778398"; MUTAGEN 117; /note="T->A: Prevents phosphorylation by AURKB. Still able to localize correctly but prevents interaction with INCENP."; /evidence="ECO:0000269|PubMed:14610074"; MUTAGEN 117; /note="T->E: Mimics phosphorylation. Disrupts subcellular localization during mitosis and prevents interaction with INCENP."; /evidence="ECO:0000269|PubMed:14610074"; MUTAGEN 126; /note="E->A: Loss of FBXL7 binding."; /evidence="ECO:0000269|PubMed:25778398"; MUTAGEN 129; /note="K->A,Q: Mimics acetylation. Localization primarily within the nucleus."; /evidence="ECO:0000269|PubMed:20826784"; MUTAGEN 129; /note="K->R: Loss of acetylation. Localization primarily within the cytoplasm."; /evidence="ECO:0000269|PubMed:20826784
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting. Deubiquitinated by USP35 or USP38; leading to stabilization (PubMed:34438346). {ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:24793696, ECO:0000269|PubMed:34438346}.; PTM: In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes (PubMed:14610074). Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities (PubMed:21252625). Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity (PubMed:24866247). Phosphorylation at Ser-20 by AURKC is critical for regulation of proper chromosome alignment and segregation, and possibly cytokinesis. {ECO:0000269|PubMed:11069302, ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:21252625, ECO:0000269|PubMed:24866247, ECO:0000269|PubMed:27332895}.; PTM: Acetylation at Lys-129 by CBP 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. {ECO:0000269|PubMed:20826784}.
uniprot
proteins
protein_family
IAP family
uniprot
proteins
pubmed
10626797
uniprot
proteins
pubmed
10876248
uniprot
proteins
pubmed
10949039
uniprot
proteins
pubmed
11069302
uniprot
proteins
pubmed
11084331
uniprot
proteins
pubmed
12773388
uniprot
proteins
pubmed
14610074
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14741722
uniprot
proteins
pubmed
15249581
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15665297
uniprot
proteins
pubmed
16239925
uniprot
proteins
pubmed
16291752
uniprot
proteins
pubmed
16322459
uniprot
proteins
pubmed
16329164
uniprot
proteins
pubmed
16344111
uniprot
proteins
pubmed
16427043
uniprot
proteins
pubmed
16436504
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16762323
uniprot
proteins
pubmed
16764853
uniprot
proteins
pubmed
17956729
uniprot
proteins
pubmed
17993464
uniprot
proteins
pubmed
18329369
uniprot
proteins
pubmed
18591255
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19530738
uniprot
proteins
pubmed
20627126
uniprot
proteins
pubmed
20826784
uniprot
proteins
pubmed
20929775
uniprot
proteins
pubmed
21225229
uniprot
proteins
pubmed
21252625
uniprot
proteins
pubmed
21364656
uniprot
proteins
pubmed
21536684
uniprot
proteins
pubmed
24793696
uniprot
proteins
pubmed
24866247
uniprot
proteins
pubmed
25778398
uniprot
proteins
pubmed
27332895
uniprot
proteins
pubmed
28077791
uniprot
proteins
pubmed
28218735
uniprot
proteins
pubmed
34438346
uniprot
proteins
pubmed
9256286
uniprot
proteins
pubmed
9859993
uniprot
proteins
sequence_length
142
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:21364656}. Nucleus {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:21364656}. Chromosome {ECO:0000269|PubMed:14610074}. Chromosome, centromere {ECO:0000269|PubMed:11084331, ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:16322459}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11084331}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11084331}. Midbody {ECO:0000269|PubMed:15665297}. 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 (By similarity). 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 (PubMed:11084331). Colocalizes with AURKB at mitotic chromosomes (PubMed:14610074). Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear export (PubMed:20826784). {ECO:0000250|UniProtKB:E3SCZ8, ECO:0000269|PubMed:11084331, ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:20826784}.
uniprot
proteins