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0BIRC5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameBIRC5
DescriptionBaculoviral iap repeat-containing protein 5 (apoptosis inhibitor survivin) (apoptosis inhibitor 4).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005876 spindle microtubule (TAS)
0043027 caspase inhibitor activity (IMP)
0008017 microtubule binding (IDA)
0030414 protease inhibitor activity (NAS)
0005515 protein binding (IPI)
0008270 zinc ion binding (NAS)
0006916 anti-apoptosis (IDA)
0000086 G2/M transition of mitotic cell cycle (IDA)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors.espectively. In many cases they are synthesised as part of a larger precursor protein.ither as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. The baculovirus inhibitor of apoptosis protein repeat (BIR) is a domain of tandem repeats separated by a variable length linker that seems to confer cell death-preventing activity . The BIR domains characterise the Inhibitor of Apoptosis (IAP) family of proteins (MEROPS proteinase inhibitor family I32.lan IV) that suppress apoptosis by interacting with and inhibiting the enzymatic activity of both initiator and effector caspases (MEROPS peptidase family C14.. Several distinct mammalian IAPs including XIAP.-IAP1.-IAP2.nd ML-IAP.ave been identified.nd they all exhibit antiapoptotic activity in cell culture. The functional unit in each IAP protein is the baculoviral IAP repeat (BIR).hich contains approximately 80 amino acids folded around a zinc atom. Most mammalian IAPs have more than one BIR domain.ith the different BIR domains performing distinct functions. For example.n XIAP.he third BIR domain (BIR3) potently inhibits the catalytic activity of caspase-9.hereas the linker sequences immediately preceding the second BIR domain (BIR2) selectively targets caspase-3 or 7. Homologs of most components in the mammalian apoptotic pathway have been identified in fruit flies. The Drosophila Apaf-1.nown as Dapaf-1.AC-1 or Dark.hares significant sequence similarity with its mammalian counterpart.nd is critically important for the activation of the Drosophila initiator caspase Dronc. Dronc.n turn.leaves and activates the effector caspase DrICE. The Drosophila IAP.IAP1.inds to and in-activates both DrICE and Dronc through its BIR1 and BIR2 domains. During apoptosis.he anti-death function of DIAP1 is countered by at least four pro-apoptotic proteins.eaper.id.rim.nd sickle.hrough direct physical interactions. These four proteins represent the functional homologs of the mammalian protein Smac.nd they all share a conserved IAP-binding motif at their N termini. The three proteins Reaper.id.nd Grim are collectively referred to as the RHG proteins . Both XIAP and DIAP1 contain a RING domain at their C termini.nd can act as an E3 ubiquitin ligase. Indeed.oth XIAP and DIAP1 have been shown to promote self-ubiquitination and degradation as well as to negatively regulate the target caspases. Nonetheless.mportant differences exist between XIAP and DIAP1. The primary function of XIAP is thought to inhibit the catalytic activities of caspases; to what extent the ubiquitinating activity of XIAP contributes to its function remains unclear. For DIAP1.owever.he ubiquitinating activity appears to be essential for its function. Recently a Drosophila p53 protein has been identified that mediates apoptosis via a novel pathway involving the activation of the Reaper gene and subsequent inhibition of the inhibitors of apoptosis (IAPs). CIAP1. major mammalian homolog of Drosophila IAPs.s irreversibly inhibited (cleaved) during p53-dependent apoptosis and this cleavage is mediated by a serine protease. Serine protease inhibitors that block CIAP1 cleavage inhibit p53-dependent apoptosis. Furthermore.ctivation of the p53 protein increases the transcription of the HTRA2 gene.hich encodes a serine protease that interacts with CIAP1 and potentiates apoptosis. Therefore mammalian p53 protein activates apoptosis through a novel pathway functionally similar to that in Drosophila.hich involves HTRA2 and subsequent inhibition of CIAP1 by cleavage .
  IPR001370:Proteinase inhibitor I32, inhibitor of apoptosis
IPR001370:BIR 
Evalue:-35.7695510786217 
Location:13-89IPR001370:BIR_REPEAT_1 
Evalue:0 
Location:0-0
SequencesProtein: BIRC5_HUMAN (142 aa)
mRNA: NM_001012271 NM_001168
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 78 residues, 73721871-73722103Exon2: 38 residues, 73722355-73722465Exon3: 25 residues, 73723641-73723710Exon4: 41 residues, 73724339-73724457Exon5: 725 residues, 73731140-73733310Exon6: 2 residues, -Jump to BIRC5_HUMANExon1: 78 residues, 73721871-73722103Exon2: 38 residues, 73722355-73722465Exon3: 41 residues, 73724339-73724457Exon4: 725 residues, 73731140-73733310Exon5: 2 residues, -Jump to BIRC5_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3043 73721871-73733310 ~-11K 16728(BIRC5)(+)Loci: 4320 73931373-73980451 ~-49K 16737(-)Loci: 3042 73676265-73680604 ~-4K 16723(SYNGR2)(+)Link out to UCSC