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0IRF3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameIRF3
DescriptionInterferon regulatory factor 3 (irf-3).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0003702 RNA polymerase II transcription factor acti... (TAS)
0003712 transcription cofactor activity (TAS)
0006366 transcription from RNA polymerase II promoter (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:
Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding motif.here the "wings".r loops.re 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 differentiation.eat-shock 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 transposase.here the flexible wing of the enhancer-binding domain is essential for efficient transposition .
  IPR011991:Winged helix repressor DNA-binding
The expression of type I interferon genes (interferons alpha and beta) is induced by many agents.ncluding viral attack . Induction is mediated by the binding of interferon regulatory factor 1 (IRF-1) to a region known as the interferon consensus sequence (ICS).ocated upstream of the interferon genes . Other factors may also bind to the ICS.ncluding IRF-2.hich does not function as an activator.ut rather suppresses the function of IRF-1 under certain circumstances . IRF proteins contain a conserved N-terminal region of about 120 amino acids.hich folds into a structure that binds specifically to the ICS; the remaining parts of thesequences vary depending on the precise function of the protein .
  IPR001346:Interferon regulatory factor
FHA and SMAD (MH2) domains share a common structure consisting of a sandwich of eleven beta strands in two sheets with Greek key topology. Forkhead-associated (FHA) domains were originally identified as a sequence profile of about 75 amino acids.hereas the full-length domain is closer to about 150 amino acids. FHA domains are found in transcription factors.inesin motors.nd in a variety of other signalling molecules in organisms ranging from eubacteria to humans. FHA domains are protein-protein interaction domains that are specific for phosphoproteins. FHA-containing proteins function in maintaining cell-cycle checkpoints.NA repair and transcriptional regulation. FHA domain proteins include the Chk2/Rad53/Cds1 family of proteins that contain one or more FHA domains.s well as a Ser/Thr kinase domain . SMAD domain proteins are found in a range of species from nematodes to humans. These highly conserved proteins contain an N-terminal MH1 domain that contacts DNA.nd is separated by a short linker region from the C-terminal MH2 domain.he later showing a striking similarity to FHA domains. SMAD proteins mediate signalling by the TGF-beta/activin/BMP-2/4 cytokines from receptor Ser/Thr protein kinases at the cell surface to the nucleus. SMAD proteins fall into three functional classes: the receptor-regulated SMADs (R-SMADs).ncluding SMAD1.2.3.5.nd -8.ach of which is involved in a ligand-specific signalling pathway ; the comediator SMADs (co-SMADs).ncluding SMAD4.hich interact with R-SMADs to participate in signalling ; and the inhibitory SMADs (I-SMADs).ncluding SMAD6 and -7.hich block the activation of R-SMADs and Co-SMADs.hereby negatively regulating signalling pathways . The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008984:SMAD/FHA
IPR001346:IRF 
Evalue:-53.8239087409443 
Location:1-112IPR008984:SMAD_FHA 
Evalue:0 
Location:259-389
SequencesProtein: IRF3_HUMAN (427 aa)
mRNA: BC009395 NM_001571
Local Annotation
Synapse Ontology
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentK05411
  Level 3 annotation:
    interferon regulatory factor 3
  Level 2 annotation:
    Toll-like receptor signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 88 residues, 54854641-54854902Exon2: 46 residues, 54855781-54855913Exon3: 129 residues, 54857016-54857397Exon4: 66 residues, 54857493-54857686Exon5: 25 residues, 54858256-54858327Exon6: 59 residues, 54858411-54858583Exon7: 59 residues, 54859742-54859915Exon8: 59 residues, 54860699-54860871Exon9: 2 residues, -Jump to IRF3_HUMANExon1: 88 residues, 54854641-54854902Exon2: 40 residues, 54855781-54855897Exon3: 129 residues, 54857016-54857397Exon4: 66 residues, 54857493-54857686Exon5: 25 residues, 54858256-54858327Exon6: 59 residues, 54858411-54858583Exon7: 59 residues, 54859742-54859915Exon8: 77 residues, 54860699-54860926Exon9: 2 residues, -Jump to IRF3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3124 53589943-53639205 ~-49K 19224(GRIN2D)(+)Loci: 3125 53656317-53661179 ~-5K 19226(KCNJ14)(+)Loci: 3126 53747240-53794495 ~-47K 19229(SULT2B1)(+)Loci: 4406 53833083-53841263 ~-8K 19240(CA11)(-)Loci: 4407 53990131-54006113 ~-16K 19255(BCAT2)(-)Loci: 4408 54262487-54268010 ~-6K 19284(-)Loci: 3127 54309429-54313528 ~-4K 19290(LIN7B)(+)Loci: 3128 54314474-54346090 ~-32K 19292(PPFIA3)(+)Loci: 4409 54484705-54520286 ~-36K 19297(SLC6A16)(-)Loci: 3129 54669297-54681299 ~-12K 19311(FLT3LG)(+)Loci: 4410 54854641-54860926 ~-6K 19323(IRF3)(-)Loci: 3130 54886218-54908800 ~-23K 19334(CPT1C)(+)Loci: 3131 54961991-55002179 ~-40K 19337(AP2A1)(+)Loci: 3132 55124271-55129003 ~-5K 19355(ATF5)(+)Loci: 4411 55510576-55524446 ~-14K 19365(KCNC3)(-)Loci: 4412 55817047-55833114 ~-16K 19382(SYT3)(-)Loci: 4413 55856895-55912007 ~-55K 19383(SHANK1)(-)Loci: 3123 53559468-53571439 ~-12K 19220(SYNGR4)(+)Link out to UCSC