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
0PEA15_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePEA15
DescriptionAstrocytic phosphoprotein pea-15 (phosphoprotein enriched in diabetes) (ped).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005875 microtubule associated complex (NAS)
0005515 protein binding (IPI)
0006916 anti-apoptosis (IDA)
0046325 negative regulation of glucose import (IDA)
0042981 regulation of apoptosis (IDA)
0006810 transport (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/1327471840.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:
The death effector domain (DED) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DED is related in sequence and structure to the death domain (DD.ee ) and the caspase recruitment domain (CARD.ee ).hich work in similar pathways and show similar interaction properties . The dimerisation of DED domains is mediated primarily by electrostatic interactions. DED domains can be found in isolation.r in combination with other domains. Domains associated with DED include: caspase catalytic domains (in caspase-8.10).eath domains (in FADD).uclear localisation sequences (in DEDD).ransmembrane domains (in Bap31 and Bar).ucleotide-binding domains (in Dap3).oiled-coil domains (in Hip and Hippi).AM domains (in Bar).nd E2-binding RING domains (in Bar) .Several DED-containing proteins are involved in the regulation of apoptosis through their interactions with DED-containing caspases ().uch as caspases 8 and 10 in humans.oth of which contain tandem pairs of DEDs. There are many DED-containing modulators of apoptosis.hich can either enhance or inhibit caspase activation .
  IPR001875:Death effector
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
IPR001875:DED 
Evalue:-29.5528411865234 
Location:4-87
SequencesProtein: PEA15_HUMAN (130 aa)
mRNA: NM_003768
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
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)
activation of protein kinase C
sdb:0206 activation of protein kinase C  (Evidence:keywords)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 63 residues, 158441750-158441936Exon2: 60 residues, 158447956-158448130Exon3: 54 residues, 158449523-158449679Exon4: 651 residues, 158449835-158451784Exon5: 2 residues, -Jump to PEA15_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2563 158352171-158379996 ~-28K 3053(ATP1A2)(+)Loci: 2564 158441750-158451784 ~-10K 3060(PEA15)(+)Loci: 3841 158721443-158759666 ~-38K 3073(SLAMF6)(-)Loci: 3842 158846513-158883493 ~-37K 3083(SLAMF1)(-)Loci: 2562 158317983-158325836 ~-8K 3047(KCNJ9)(+)Link out to UCSC