SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0CASP1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCASP1
DescriptionCaspase-1 precursor (ec 3.4.22.36) (casp-1) (interleukin-1 beta convertase) (il-1bc) (il-1 beta-converting enzyme) (ice) (interleukin- 1 beta-converting enzyme) (p45) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008656 caspase activator activity (TAS)
0030693 caspase activity (TAS)
0004871 signal transducer activity (IEP)
0006915 apoptosis (TAS)
0043123 positive regulation of I-kappaB kinase/NF-k... (IEP)
0006508 proteolysis and peptidolysis (TAS)
0007165 signal transduction (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/1363331896.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
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:
Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. Cysteine peptidases have characteristic molecular topologies.hich can be seen not only in their three-dimensional structures.ut commonly also in the two-dimensional structures. The peptidase domain is responsible for peptide bond hydrolysis; in Merops this is termed the peptidase unit. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related).nd further sub-divided into families.n the basis of the architecture of their catalytic dyad or triad : Clan CA contains the families of papain (C1).alpain (C2).treptopain (C10) and the ubiquitin-specific peptidases (C12.19).s well as many families of viral cysteine endopeptidases. Clan CD contains the families of clostripain (C11).ingipain R (C25).egumain (C13).aspase-1 (C14) and separin (C50). These enzymes have specificities dominated by the interactions of the S1 subsite. Clan CE contains the families of adenain (C5) from adenoviruses.he eukaryotic Ulp1 protease (C48) and the bacterial YopJ proteases (C55). Clan CF contains only pyroglutamyl peptidase I (C15). Clan PA contains the picornains (C3).hich have probably evolved from serine peptidases and which form the majority of enzymes in this clan. Clans PB and CH contain the autolytic cysteine peptidases. This group of sequences represent the p20 (20kDa) and p10 (10kDa) subunits of caspases.hich together form the catalytic domain of the caspase and are derived from the p45 (45 kDa) precursor () .Caspases (Cysteine-dependent ASPartyl-specific proteASE) are cysteine peptidases that belong to the MEROPS peptidase family C14 (caspase family.lan CD) based on the architecture of their catalytic dyad or triad . Caspases are tightly regulated proteins that require zymogen activation to become active.nd once active can be regulated by caspase inhibitors. Activated caspases act as cysteine proteases.sing the sulphydryl group of a cysteine side chain for catalysing peptide bond cleavage at aspartyl residues in their substrates. The catalytic cysteine and histidine residues are on the p20 subunit after cleavage of the p45 precursor.Caspases are mainly involved in mediating cell death (apoptosis) . They have two main roles within the apoptosis cascade: as initiators that trigger the cell death process.nd as effectors of the process itself. Caspase-mediated apoptosis follows two main pathways.ne extrinsic and the other intrinsic or mitochondrial-mediated. The extrinsic pathway involves the stimulation of various TNF (tumour necrosis factor) cell surface receptors on cells targeted to die by various TNF cytokines that are produced by cells such as cytotoxic T cells. The activated receptor transmits the signal to the cytoplasm by recruiting FADD.hich forms a death-inducing signalling complex (DISC) with caspase-8. The subsequent activation of caspase-8 initiates the apoptosis cascade involving caspases 3.... and 10. The intrinsic pathway arises from signals that originate within the cell as a consequence of cellular stress or DNA damage. The stimulation or inhibition of different Bcl-2 family receptors results in the leakage of cytochrome c from the mitochondria.nd the formation of an apoptosome composed of cytochrome c.paf1 and caspase-9. The subsequent activation of caspase-9 initiates the apoptosis cascade involving caspases 3 and 7.mong others. At the end of the cascade.aspases act on a variety of signal transduction proteins.ytoskeletal and nuclear proteins.hromatin-modifying proteins.NA repair proteins and endonucleases that destroy the cell by disintegrating its contents.ncluding its DNA. The different caspases have different domain architectures depending upon where they fit into the apoptosis cascades.owever they all carry the catalytic p10 and p20 subunits.Caspases can have roles other than in apoptosis.uch as caspase-1 (interleukin-1 beta convertase) ().hich is involved in the inflammatory process. The activation of apoptosis can sometimes lead to caspase-1 activation.roviding a link between apoptosis and inflammation.uch as during the targeting of infected cells. Caspases may also be involved in cell differentiation .
  IPR011600:Peptidase C14, caspase catalytic
The caspase recruitment domain domain (CARD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. CARD is related in sequence and structure to the death domain (DD.ee ) and the death effector domain (DED.ee ).hich work in similar pathways and show similar interaction properties . The CARD domain typically associates with other CARD-containing proteins.orming either dimers or trimers. CARD domains can be found in isolation.r in combination with other domains. Domains associated with CARD include: NACHT () (in Nal1 and Bir1).B-ARC () (in Apaf-1).yrin/dapin domains () (in Nal1).eucine-rich repeats () (in Nal1).D repeats () (in Apaf1).rc homology domains ().DZ ().ING.inase and DD domains .CARD-containing proteins are involved in apoptosis through their regulation of caspases that contain CARDs in their N-terminal pro-domains.ncluding human caspases 1...1 and 12 . CARD-containing proteins are also involved in inflammation through their regulation of NF-kappaB . The mechanisms by which CARDs activate caspases and NF-kappaB involve the assembly of multi-protein complexes.hich can facilitate dimerisation or serve as scaffolds on which proteases and kinases are assembled and activated.
  IPR001315:Caspase Recruitment
The death domain (DD) is a conserved region of about 80 residues found on death receptors.nd which is required for death signalling.s well as a variety of non-apoptotic functions . Proteins containing this domain include the low affinity neurotrophin receptor p73.as.ADD (Fas-associated death domain protein).NF-1 (tumour necrosis factor receptor-1).elle protein kinase.nd the Tube adaptor protein .The induction of apoptosis also relies on the presence of a second domain.alled the death effector domain. The death effector domain (DED) occurs in proteins that regulate programmed cell death.ncluding both pro- and anti-apoptotic proteins; many of these proteins are also involved in controlling cellular activation and proliferation pathways . Proteins containing this domain include FADD (DED N-terminal.D C-terminal).EA-15 (phosphoproteins enriched in astrocytes 15kDa).aspases and FLIP.The induction of apoptosis results in the activation of caspases. family of aspartyl-specific cysteine proteases that are the main executioners of apoptosis. For example.he DED of FADD recruits two DED-containing caspases.aspase-8 and caspase-10.o form the death-inducing signal complex.hich initiates apoptosis. Proteins containing the caspase recruitment domain (CARD) are involved in the recruitment and activation of caspases during apoptosis . Other CARD proteins participate in NF-kappaB signalling pathways associated with innate or adaptive immune responses. Proteins containing CARD include Raidd.PAF-1 (apoptotic protease activating factor 1).rocaspase 9 and iceberg (inhibitor of interleukin-1-beta generation).The DD shows strong structural similarity to both DED and CARD. They all display a 6-helical closed bundle fold.ith greek key topology and an internal psuedo two-fold symmetry. However.espite their overall similarity in topology.ach domain forms specialised interactions.ypically only with members of its own subfamily.or example DED with DED.Please be aware that some of the proteins hit by the SSF signature may be false positives.
  IPR011029:DEATH-like
Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. Cysteine peptidases have characteristic molecular topologies.hich can be seen not only in their three-dimensional structures.ut commonly also in the two-dimensional structures. The peptidase domain is responsible for peptide bond hydrolysis; in Merops this is termed the peptidase unit. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related).nd further sub-divided into families.n the basis of the architecture of their catalytic dyad or triad : Clan CA contains the families of papain (C1).alpain (C2).treptopain (C10) and the ubiquitin-specific peptidases (C12.19).s well as many families of viral cysteine endopeptidases. Clan CD contains the families of clostripain (C11).ingipain R (C25).egumain (C13).aspase-1 (C14) and separin (C50). These enzymes have specificities dominated by the interactions of the S1 subsite. Clan CE contains the families of adenain (C5) from adenoviruses.he eukaryotic Ulp1 protease (C48) and the bacterial YopJ proteases (C55). Clan CF contains only pyroglutamyl peptidase I (C15). Clan PA contains the picornains (C3).hich have probably evolved from serine peptidases and which form the majority of enzymes in this clan. Clans PB and CH contain the autolytic cysteine peptidases. This group of sequences represent the p45 (45 kDa) precursor of caspases.hich can be processed to produce the active p20 (20 kDa) and p10 (10 kDa) subunits. Caspases (Cysteine-dependent ASPartyl-specific proteASE) are cysteine peptidases that belong to the MEROPS peptidase family C14 (caspase family.lan CD) based on the architecture of their catalytic dyad or triad . Caspases are tightly regulated proteins that require zymogen activation to become active.nd once active can be regulated by caspase inhibitors. Activated caspases act as cysteine proteases.sing the sulphydryl group of a cysteine side chain for catalysing peptide bond cleavage at aspartyl residues in their substrates. The catalytic cysteine and histidine residues are on the p20 subunit after cleavage of the p45 precursor.Caspases are mainly involved in mediating cell death (apoptosis) . They have two main roles within the apoptosis cascade: as initiators that trigger the cell death process.nd as effectors of the process itself. Caspase-mediated apoptosis follows two main pathways.ne extrinsic and the other intrinsic or mitochondrial-mediated. The extrinsic pathway involves the stimulation of various TNF (tumour necrosis factor) cell surface receptors on cells targeted to die by various TNF cytokines that are produced by cells such as cytotoxic T cells. The activated receptor transmits the signal to the cytoplasm by recruiting FADD.hich forms a death-inducing signalling complex (DISC) with caspase-8. The subsequent activation of caspase-8 initiates the apoptosis cascade involving caspases 3.... and 10. The intrinsic pathway arises from signals that originate within the cell as a consequence of cellular stress or DNA damage. The stimulation or inhibition of different Bcl-2 family receptors results in the leakage of cytochrome c from the mitochondria.nd the formation of an apoptosome composed of cytochrome c.paf1 and caspase-9. The subsequent activation of caspase-9 initiates the apoptosis cascade involving caspases 3 and 7.mong others. At the end of the cascade.aspases act on a variety of signal transduction proteins.ytoskeletal and nuclear proteins.hromatin-modifying proteins.NA repair proteins and endonucleases that destroy the cell by disintegrating its contents.ncluding its DNA. The different caspases have different domain architectures depending upon where they fit into the apoptosis cascades.owever they all carry the catalytic p10 and p20 subunits.Caspases can have roles other than in apoptosis.uch as caspase-1 (interleukin-1 beta convertase) ().hich is involved in the inflammatory process. The activation of apoptosis can sometimes lead to caspase-1 activation.roviding a link between apoptosis and inflammation.uch as during the targeting of infected cells. Caspases may also be involved in cell differentiation .
  IPR002398:Peptidase C14, caspase precursor p45
IPR002398:CASc 
Evalue:-136.52287874528 
Location:152-402IPR001315:CARD 
Evalue:-31.6382713317871 
Location:3-90IPR000873:AMP_BINDING 
Evalue:0 
Location:123-134
SequencesProtein: CASP1_HUMAN (404 aa)
mRNA: NM_033292 X65019
Local Annotation
Synapse Ontology
A process that increases short-term neuronal synaptic plasticity, the ability of neuronal synapses to change in the short-term as circumstances require. Short-term neuronal synaptic plasticity generally involves increasing or decreasing synaptic sensitivity.
sdb:0043 positive regulation of short-term neuronal synaptic plasticity  (Evidence:keywords)
KO assignmentK01370
  Level 3 annotation:
    caspase 1, apoptosis-related cysteine protease (interleukin 1, beta, convertase)
  Level 2 annotation:
    MAPK signaling pathway
    Huntington's disease
    Dentatorubropallidoluysian atrophy (DRPLA)
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 29 residues, 104401451-104401537Exon2: 45 residues, 104402162-104402293Exon3: 38 residues, 104402778-104402888Exon4: 50 residues, 104405060-104405204Exon5: 80 residues, 104405601-104405836Exon6: 60 residues, 104406266-104406440Exon7: 40 residues, 104407101-104407217Exon8: 23 residues, 104409000-104409063Exon9: 91 residues, 104410144-104410411Exon10: 10 residues, 104411043-104411067Exon11: 2 residues, -Jump to CASP1_HUMANExon1: 28 residues, 104401451-104401534Exon2: 46 residues, 104402161-104402293Exon3: 38 residues, 104402778-104402888Exon4: 50 residues, 104405060-104405204Exon5: 80 residues, 104405601-104405836Exon6: 60 residues, 104406266-104406440Exon7: 40 residues, 104407101-104407217Exon8: 23 residues, 104409000-104409063Exon9: 91 residues, 104410144-104410411Exon10: 6 residues, 104421227-104421241Exon11: 2 residues, -Jump to CASP1_HUMAN  
Tune and view alternative isoforms