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0BIRC1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameBIRC1
DescriptionBaculoviral iap repeat-containing protein 1 (neuronal apoptosis inhibitory protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0006916 anti-apoptosis (TAS)
0007399 neurogenesis (TAS)

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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:
The NACHT domain is a 300 to 400 residue predicted nucleoside triphosphatase (NTPase) domain.hich is found in animal.ungal and bacterial proteins. The NACHT domain has been named after NAIP.IITA.ET-E and TP1. It is found inassociation with other domains.uch as the CARD domain ().heDAPIN domain ().he HEAT repeat ().he WDrepeat ().he leucine-rich repeat (LRR) or the BIR repeat () .The NACHT domain consists of seven distinct conserved motifs.ncluding the ATP/GTPase specific P-loop.he Mg(2+)-binding site (WalkerA and B motifs.espectively) and five more specific motifs. The unique features of the NACHT domain include the prevalence of tiny residues(glycine.lanine or serine) directly C-terminal of the Mg(2+)-coordinating aspartate in the Walker B motif.n place of a second acidic residue prevalentin other NTPases. A second acidic residue is typically found in the NACHT-containing proteins two positions downstream. Furthermore.he distal motif VII contains a conserved pattern of polar.romatic and hydrophobic residues that is not seen in any other NTPase family .
  IPR007111:NACHT nucleoside triphosphatase
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
AAA ATPases form a large.unctionally diverse protein family belonging to the AAA+ superfamily of ring-shaped P-loop NTPases.hich exert their activity through the energy-dependent unfolding of macromolecules. AAA ATPases contain a P-loop NTPase domain.hich is the most abundant class of NTP-binding protein fold.nd is found throughout all kingdoms of life . P-loop NTPase domains act to hydrolyse the beta-gamma phosphate bond of bound nucleoside triphosphate. There are two classes of P-loop domains: the KG (kinase-GTPase) division.nd the ASCE division.he latter including the AAA+ group as well as several other ATPases.There are at least six major clades of AAA domains (metalloproteases.eiotic proteins.1 and D2 domains of ATPases with two AAA domains.roteasome subunits.nd BSC1).s well as several minor clades.ome of which consist of hypothetical proteins . The domain organisation of AAA ATPases consists of a non-ATPase N-terminal domain that acts in substrate recognition.ollowed by one or two AAA domains (D1 and D2).ne of which may be degenerate.
  IPR003593:AAA ATPase
IPR007111:NACHT 
Evalue:-55.9208183288574 
Location:464-618IPR001370:BIR 
Evalue:-39.4948500216801 
Location:157-229IPR001370:BIR 
Evalue:-36.6777807052661 
Location:276-347IPR001370:BIR 
Evalue:-26.2006594505464 
Location:58-129
SequencesProtein: BIRC1_HUMAN (1403 aa)
mRNA: NM_004536
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 663 residues, 70300065-70302051Exon2: 57 residues, 70305711-70305876Exon3: 31 residues, 70307742-70307829Exon4: 53 residues, 70308488-70308641Exon5: 58 residues, 70311451-70311619Exon6: 706 residues, 70315357-70317469Exon7: 21 residues, 70318327-70318385Exon8: 29 residues, 70319375-70319457Exon9: 35 residues, 70330306-70330406Exon10: 42 residues, 70333280-70333400Exon11: 19 residues, 70333674-70333726Exon12: 29 residues, 70335358-70335440Exon13: 35 residues, 70342857-70342957Exon14: 192 residues, 70343930-70344501Exon15: 44 residues, 70352241-70352367Exon16: 31 residues, 70355900-70355989Exon17: 29 residues, 70356197-70356279Exon18: 2 residues, -Jump to BIRC1_HUMANLoci index, Chromosomal location, Length, Possible relational loci clusterExon1: 28 residues, 393545-393627Exon2: 31 residues, 393835-393924Exon3: 44 residues, 397456-397582Exon4: 192 residues, 405321-405892Exon5: 35 residues, 406865-406965Exon6: 29 residues, 414383-414465Exon7: 19 residues, 416078-416130Exon8: 42 residues, 416404-416524Exon9: 35 residues, 419396-419496Exon10: 29 residues, 430350-430432Exon11: 21 residues, 431422-431480Exon12: 706 residues, 432338-434450Exon13: 58 residues, 438190-438358Exon14: 53 residues, 441158-441311Exon15: 31 residues, 441970-442057Exon16: 57 residues, 443923-444088Exon17: 664 residues, 447751-449737Exon18: 2 residues, -Jump to BIRC1_HUMAN  
Loci Cluster (Details)Loci: 4716 70300065-70356279 ~-56K 28969(BIRC1)(-)Loci: 3462 70051445-70327856 ~-276K 28960(SMA3)(+)Link out to UCSC  
Loci: 3515 393545-449737 ~-56K 30164(BIRC1)(+)Loci: 4764 465177-493242 ~-28K 30167(SMN1)(-)Loci: 4765 499652-517517 ~-18K 30169(SERF1A)(-)Loci: 4766 621245-720436 ~-99K 30171(SMA3)(-)Loci: 3514 160403-205618 ~-45K 30155(RAD17)(+)Link out to UCSC