| IED ID | IndEnz0002005139 |
| Enzyme Type ID | protease005139 |
| Protein Name |
Baculoviral IAP repeat-containing protein 5 Apoptosis inhibitor survivin |
| Gene Name | BIRC5 |
| Organism | Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Ponginae Pongo Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
| Enzyme Sequence | MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD |
| Enzyme Length | 142 |
| Uniprot Accession Number | Q5RAH9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (By similarity). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (By similarity). 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 (By similarity). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity). 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 (By similarity). May counteract a default induction of apoptosis in G2/M phase (By similarity). The acetylated form represses STAT3 transactivation of target gene promoters (By similarity). May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). Essential for the maintenance of mitochondrial integrity and function (By similarity). {ECO:0000250|UniProtKB:O15392}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (4); Modified residue (10); Repeat (1); Site (1) |
| Keywords | Acetylation;Apoptosis;Cell cycle;Cell division;Centromere;Chromosome;Chromosome partition;Cytoplasm;Cytoskeleton;Kinetochore;Metal-binding;Microtubule;Mitosis;Nucleus;Phosphoprotein;Protease inhibitor;Reference proteome;Repressor;Thiol protease inhibitor;Transcription;Transcription regulation;Ubl conjugation;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus {ECO:0000250|UniProtKB:O15392}. Chromosome {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere {ECO:0000250|UniProtKB:O15392}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O15392}. Midbody {ECO:0000250|UniProtKB:O15392}. Note=ocalizes 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. 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). {ECO:0000250|UniProtKB:E3SCZ8, ECO:0000250|UniProtKB:O15392}. |
| Modified Residue | MOD_RES 20; /note=Phosphoserine; by AURKC; /evidence=ECO:0000250|UniProtKB:O15392; MOD_RES 23; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O15392; MOD_RES 34; /note=Phosphothreonine; by CDK1 and CDK15; /evidence=ECO:0000250|UniProtKB:O15392; MOD_RES 48; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:O15392; MOD_RES 90; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O15392; MOD_RES 110; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O15392; MOD_RES 112; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O15392; MOD_RES 115; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O15392; MOD_RES 117; /note=Phosphothreonine; by AURKB; /evidence=ECO:0000250|UniProtKB:O15392; MOD_RES 129; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O15392 |
| Post Translational Modification | 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: 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. {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}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 16,389 |
| Kinetics | |
| Metal Binding | METAL 57; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00029; METAL 60; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00029; METAL 77; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00029; METAL 84; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00029 |
| Rhea ID | |
| Cross Reference Brenda |