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0FOS_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameFOS
DescriptionProto-oncogene protein c-fos (cellular oncogene fos) (g0/g1 switch regulatory protein 7).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (TAS)
0003704 specific RNA polymerase II transcription fa... (TAS)
0006306 DNA methylation (TAS)
0006954 inflammatory response (TAS)
0006357 regulation of transcription from RNA polyme... (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 basic-leucine zipper (bZIP) transcription factors .f eukaryotic are proteins that contain a basic region mediating sequence-specific DNA-binding followed by a leucine zipper region (see ) required for dimerization.
  IPR004827:Basic-leucine zipper (bZIP) transcription factor
The basic-leucine zipper (bZIP) transcription factors .f eukaryotes are proteins that contain a basic region mediating sequence-specific DNA-binding.ollowed by a leucine zipper region (see ).hich is required for dimerization.
  IPR011700:Basic leucine zipper
Both the cellular and viral forms of the fos oncogene encode a phosphoprotein that is located in the nucleus of cells.nd forms a noncovalent complex with several other proteins. A leucine zipper holds the dimer together. The dimer is associated with chromatin and demonstrates specific and non-specific DNA-binding properties .he DNA being bound by a highly basic area in the protein sequence immediately preceding the zipper domain. Expression of the fos gene is stimulated by mitogens.uggesting that the gene product is involved in cell growth .nd may act as a nuclear signal in a more general sense. The leucine zipper is a structure that is believed to mediate the function of several eukaryotic gene regulatory proteins. The zipper consists of a periodic repetition of leucine residues at every seventh position.nd regions containing them appear to span 8 turns of alpha-helix. The leucine side chains that extend from one helix interact with those from a similar helix.ence facilitating dimerisation in the form of a coiled-coil. Leucine zippers are present in many gene regulatory proteins.ncluding the CREB proteins.un/AP1 transcription factors.os oncogene and fos-related proteins.-myc.-myc and N-myc oncogenes.nd so on.
  IPR000837:Fos transforming protein
The DNA-binding domain of certain eukaryotic transcription factors displays a distinctive helix-turn-helix (HTH) motif. The MafG basic region-leucine zipper (bZIP) protein and the C. elegans Skn-1 transcription factor share this HTH motif. MafG is a member of the Maf family of proteins.hich are a subgroup of bZIP proteins that function as transcriptional regulators of cellular differentiation. Mafs can form either homodimers.r heterodimers with other bZIP proteins through their leucine zipper domains. MafG proteins are small Mafs that lack a putative transactivation domain. The DNA-binding domain of MafG contains the conserved Maf extended homology region (EHR).hich is not present in other bZIP proteins. The EHR together with the basic region are responsible for the DNA-binding specificity of Mafs. Skn-1 is a transcription factor that specifies mesodermal development in C. elegans. Skn-1 and MafG share a conserved DNA-binding motif.owever Skn-1 lacks the leucine zipper dimerisation domain that is found in all bZIP proteins. Skn-1 acts as a monomer. The DNA-binding domains in MafG and Skn-1 share structural similarity.espite a sequence identity of only 25%. The domain fold consists of three (MafG) to four (Skn-1) helices.here the long C-terminal helix protrudes from the domain and binds to DNA. MafG lacks the N-terminal helix of Skn-1. A basic cluster of residues is present on the surface of the domain.hich together with the amino acid sequence motif.XXYAXXCR.orms a DNA-binding surface. MafG and Skn-1 may use a common DNA-binding mode. However.he involvement of helix 2 (H2) in DNA recognition differs between MafG and Skn-1.ith two residues at the beginning of H2 in MafG contributing to the unique DNA-binding specificity of Mafs. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008917:Eukaryotic transcription factor, DNA-binding
IPR004827:BRLZ 
Evalue:-14.7695510786217 
Location:135-199IPR000837:LEUZIPPRFOS 
Evalue:0 
Location:62-79
SequencesProtein: FOS_HUMAN (380 aa)
mRNA: NM_005252
Local Annotation
Synapse Ontology
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords)
KO assignmentK04379
  Level 3 annotation:
    v-fos FBJ murine osteosarcoma viral oncogene homolog
  Level 2 annotation:
    MAPK signaling pathway
    Toll-like receptor signaling pathway
    T cell receptor signaling pathway
    B cell receptor signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 99 residues, 74815283-74815579Exon2: 86 residues, 74816332-74816584Exon3: 38 residues, 74817015-74817123Exon4: 477 residues, 74817238-74818663Exon5: 2 residues, -Jump to FOS_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2854 74815283-74818663 ~-3K 11490(FOS)(+)Loci: 2853 74418371-74440196 ~-22K 11476(DLST)(+)Link out to UCSC