SynDB Home Page
SynDB Home Page

blue bulletSynDB protein details  

Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0DSRAD_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionDouble-stranded rna-specific adenosine deaminase (ec 3.5.4.-) (drada) (136 kda double-stranded rna binding protein) (p136) (k88dsrbp) (interferon-inducible protein 4) (ifi-4 protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005737 cytoplasm (TAS)
0005634 nucleus (TAS)
0003726 double-stranded RNA adenosine deaminase act... (NAS)
0019735 antimicrobial humoral response (sensu Verte... (TAS)
0016547 RNA editing (NAS)

Warning: fopen(/home/kongl/syndb/www/temp/ [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:
Editase () are enzymes that alter mRNA by catalyzing thesite-selective deamination of adenosine residue into inosine residue.The editase domain contains the active site and binds three Zn atoms . Several editases share a common global arrangement of domains.rom N to C terminus: twodouble-stranded RNA-specific adenosine deaminase (DRADA) repeat domains ().ollowed bythree double-stranded RNA binding (DsRBD) domains ().ollowed bythe editase domain. Other editases have a simplified domains structure with noDRADA_REP and possibly fewer DSRBD domains. Editase that deaminate cytidine are not detected by this signature.
  IPR002466:Adenosine deaminase/editase
Double-stranded RNA-specific adenosine deaminase (.-) converts multiple adenosines to inosinesand creates I/U mismatched base pairs in double-helical RNA substrates without apparent sequencespecificity. DRADA has been found to modify adenosines in AU-rich regions more frequently.robablydue to the relative ease of melting A/U base pairs compared to G/C base pairs. The protein functions tomodify viral RNA genomes.nd may be responsible for hypermutation of certain negative-stranded viruses.DRADA edits the mRNAs for the glutamate receptor subunits by site-selective adenosine deamination. TheDRADA repeat is also found in viral E3 proteins.hich contain a double-stranded RNA-binding domain.
  IPR000607:Double-stranded RNA-specific adenosine deaminase (DRADA)
Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding the "wings".r small beta-sheets. The winged helix motif consists of two wings (W1.2).hree alpha helices (H1.2.3) and three beta-sheets (S1.2.3) arranged in the order H1-S1-H2-H3-S2-W1-S3-W2 . The DNA-recognition helix makes sequence-specific DNA contacts with the major groove of DNA.hile the wings make different DNA contacts.ften with the minor groove or the backbone of DNA. Several winged-helix proteins display an exposed patch of hydrophobic residues thought to mediate protein-protein interactions.Many different proteins with diverse biological functions contain a winged helix DNA-binding domain.ncluding transcriptional repressors such as biotin repressor.exA repressor and the arginine repressor ; transcription factors such as the hepatocyte nuclear factor-3 proteins involved in cell transcription factor.nd the general transcription factors TFIIE and TFIIF . helicases such as RuvB that promotes branch migration at the Holliday junction.nd CDC6 in the pre-replication complex . endonucleases such as FokI and TnsA ; histones; and Mu the flexible wing of the enhancer-binding domain is essential for efficient transposition .
  IPR011991:Winged helix repressor DNA-binding
The DsRBD domain is found in a variety of RNA-binding proteins with differentstructures and exhibiting a diversity of functions .It is involved in localization of at least five different mRNAs in the early Drosophila embryo and by interferon-induced protein kinase in humans.hich is part of the cellular response to dsRNA.
  IPR001159:Double-stranded RNA binding
SequencesProtein: DSRAD_HUMAN (1226 aa)
mRNA: NM_001111
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK01500
  Level 3 annotation:
  Level 2 annotation:
    Atrazine degradation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 996 residues, 152821158-152824143Exon2: 44 residues, 152824316-152824444Exon3: 39 residues, 152824852-152824965Exon4: 63 residues, 152825280-152825463Exon5: 46 residues, 152827224-152827358Exon6: 43 residues, 152827650-152827773Exon7: 33 residues, 152828468-152828562Exon8: 59 residues, 152828856-152829028Exon9: 77 residues, 152829283-152829509Exon10: 65 residues, 152835904-152836095Exon11: 50 residues, 152836222-152836367Exon12: 51 residues, 152836927-152837076Exon13: 63 residues, 152837501-152837685Exon14: 530 residues, 152840140-152841726Exon15: 73 residues, 152847091-152847306Exon16: 2 residues, -Jump to DSRAD_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3833 152220753-152225430 ~-5K 2681(RAB13)(-)Loci: 2551 152511662-152514973 ~-3K 2706(HAX1)(+)Loci: 2552 152806880-152815707 ~-9K 2720(CHRNB2)(+)Loci: 3834 152821158-152847306 ~-26K 2722(ADAR)(-)Loci: 3835 153201398-153209847 ~-8K 2739(SHC1)(-)Loci: 2553 153412983-153424069 ~-11K 2783(TRIM46)(+)Loci: 2554 153513997-153526262 ~-12K 2831(HCN3)(+)Loci: 3836 153526253-153537835 ~-12K 2833(PKLR)(-)Loci: 2555 153669594-153670676 ~-1K 2846(POU5FLC1)(+)Loci: 2556 154095923-154121459 ~-26K 2875(SYT11)(+)Loci: 3837 154183269-154214942 ~-32K 2882(ARHGEF2)(-)Loci: 2557 154297589-154306917 ~-9K 2890(RAB25)(+)Loci: 2558 154362603-154374280 ~-12K 2897(+)Loci: 2559 154855709-154862142 ~-6K 2944(HAPLN2)(+)Loci: 2560 154878363-154895942 ~-18K 2945(BCAN)(+)Loci: 3838 154905181-154913813 ~-9K 2947(NES)(-)Loci: 2561 155097294-155118266 ~-21K 2961(NTRK1)(+)Loci: 3839 155171256-155281786 ~-111K 2965(ARHGEF11)(-)Loci: 2550 151897823-151900928 ~-3K 2658(SNAPAP)(+)Link out to UCSC