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0BIRC7_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionBaculoviral iap repeat-containing protein 7 (kidney inhibitor of apoptosis protein) (kiap) (melanoma inhibitor of apoptosis protein) (ml-iap) (livin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005622 intracellular (IC)
0019899 enzyme binding (NAS)
0007257 activation of JNK activity (NAS)
0006309 DNA fragmentation during apoptosis (NAS)
0001719 inhibition of caspase activation (IEP)

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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 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 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
Quality control of intracellular proteins is essential for cellular homeostasis. Molecular chaperones recognise and contribute to the refolding of misfolded or unfolded proteins.hereas the ubiquitin-proteasome system mediates the degradation of such abnormal proteins. Ubiquitin-protein ligases (E3s) determine the substrate specificity for ubiquitylation and have been classified into HECT and RING-finger families. More recently.owever.-box proteins.hich contain a domain (the U box) of about 70 amino acids that is conserved from yeast to humans.ave been identified as a new type of E3 .The RING-finger is a specialised type of Zn-finger of 40 to 60 residues that binds two atoms of zinc.nd is probably involved in mediating protein-protein interactions. . There are two different variants.he C3HC4-type and a C3H2C3-type.hich is clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as RING-H2 finger. The RING domain is a protein interaction domain which has been implicated in a range of diverse biological processes.E3 ubiquitin-protein ligase activity is intrinsic to the RING domain ofc-Cbl and is likely to be a general function of this domain; Various RINGfingers exhibit binding to E2 ubiquitin-conjugating enzymes (Ubcs) .Several 3D-structures for RING-fingers are known . The 3D structure of the zinc ligation system is unique to the RING domain and is referred to as the cross-brace motif. The spacing of the cysteines in such a domain is C-x(2)-C-x(9 to 39)-C-x(1 to 3)-H-x(2 to 3)-C-x(2)-C-x(4 to 48)-C-x(2)-C. Metal ligand pairs one and three co-ordinate to bind one zinc ion.hilst pairs two and four bind the second.s illustrated in the following schematic representation:Note that in the older literature.ome RING-fingers are denoted as LIM-domains. The LIM-domain Zn-finger is a fundamentally different family.lbeit with similar Cys-spacing (see ).
  IPR001841:Zinc finger, RING-type
SequencesProtein: BIRC7_HUMAN (298 aa)
mRNA: NM_139317
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 175 residues, 61337720-61338242Exon2: 35 residues, 61339699-61339799Exon3: 29 residues, 61340192-61340274Exon4: 17 residues, 61340365-61340411Exon5: 26 residues, 61340958-61341030Exon6: 86 residues, 61341154-61341407Exon7: 84 residues, 61342052-61342298Exon8: 2 residues, -Jump to BIRC7_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3279 60906621-60915796 ~-9K 23505(OGFR)(+)Loci: 3280 61337720-61342298 ~-5K 23526(BIRC7)(+)Loci: 4537 61448389-61463100 ~-15K 23536(CHRNA4)(-)Loci: 4538 61507985-61574437 ~-66K 23542(KCNQ2)(-)Loci: 4539 61630221-61639151 ~-9K 23549(PTK6)(-)Loci: 4540 61642606-61649301 ~-7K 23550(SRMS)(-)Loci: 4541 61659883-61676033 ~-16K 23552(PRIC285)(-)Loci: 4542 61689398-61721673 ~-32K 23556(GMEB2)(-)Loci: 3281 61996961-62035838 ~-39K 23585(DNAJC5)(+)Loci: 3282 62082900-62134895 ~-52K 23593(C20orf14)(+)Loci: 3283 62181931-62202435 ~-21K 23600(OPRL1)(+)Loci: 3278 60810633-60864567 ~-54K 23503(NTSR1)(+)Link out to UCSC