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0ATF2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameATF2
DescriptionCyclic-amp-dependent transcription factor atf-2 (activating transcription factor 2) (camp response element binding protein cre- bp1) (hb16).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
0003702 RNA polymerase II transcription factor acti... (TAS)
0003713 transcription coactivator activity (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 eukaryotic are proteins that contain a basic region mediating sequence-specific DNA-binding followed by a leucine zipper region (see ) required for dimerization.
  IPR011616:bZIP transcription factor, bZIP_1
Zinc finger domains .re nucleic acid-binding protein structures first identified in the Xenopus laevis transcription factor TFIIIA. These domains have since been found in numerous nucleic acid-binding proteins. A zinc finger domain is composed of 25 to 30 amino-acid residues including 2 conserved Cys and 2 conserved His residues in a C-2-C-12-H-3-H type motif. The 12 residues separating the second Cys and the first His are mainly polar and basic.mplicating this region in particular in nucleic acid binding. The zinc finger motif is an unusually small.elf-folding domain in which Zn is a crucial component of its tertiary structure. All bind 1 atom of Zn in a tetrahedral array to yield a finger-like projection.hich interacts with nucleotides in the major groove of the nucleic acid. The Zn binds to the conserved Cys and His residues. Fingers have been found to bind to about 5 base pairs of nucleic acid containing short runs of guanine residues. They have the ability to bind to both RNA and DNA.nd it has been suggested that the zinc finger may thus represent the original nucleic acid binding protein. It has also been suggested that a Zn-centred domain could be used in a protein interaction..g. in protein kinase C. Many classes of zinc fingers are characterized according to the number and positions of the histidine and cysteine residues involved in the zinc atom coordination. In the first class to be characterized.alled C2H2.he first pair of zinc coordinating residues are cysteines.hile the second pair are histidines.
  IPR007087:Zinc finger, C2H2-type
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:-20.4948500216801 
Location:332-396IPR007087:zf-C2H2 
Evalue:-3.02227640151978 
Location:7-31
SequencesProtein: ATF2_HUMAN (487 aa)
mRNA: DQ003036 DQ003041 NM_001880
Local Annotation
Synapse Ontology
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentK04450
  Level 3 annotation:
    activating transcription factor 2
  Level 2 annotation:
    MAPK signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 186 residues, 175647253-175647809Exon2: 37 residues, 175653633-175653739Exon3: 71 residues, 175666034-175666241Exon4: 52 residues, 175670417-175670567Exon5: 31 residues, 175684541-175684628Exon6: 40 residues, 175686967-175687082Exon7: 61 residues, 175687663-175687842Exon8: 45 residues, 175690963-175691092Exon9: 41 residues, 175691224-175691343Exon10: 34 residues, 175694417-175694514Exon11: 25 residues, 175703111-175703181Exon12: 27 residues, 175709385-175709460Exon13: 35 residues, 175724033-175724132Exon14: 42 residues, 175741023-175741143Exon15: 2 residues, -Jump to ATF2_HUMANExon1: 111 residues, 175647478-175647809Exon2: 37 residues, 175653633-175653739Exon3: 71 residues, 175666034-175666241Exon4: 52 residues, 175670417-175670567Exon5: 31 residues, 175684541-175684628Exon6: 40 residues, 175686967-175687082Exon7: 61 residues, 175687663-175687842Exon8: 45 residues, 175690963-175691092Exon9: 41 residues, 175691224-175691343Exon10: 34 residues, 175694417-175694514Exon11: 25 residues, 175703111-175703181Exon12: 27 residues, 175709385-175709460Exon13: 13 residues, 175720919-175720954Exon14: 35 residues, 175724033-175724132Exon15: 42 residues, 175741023-175741143Exon16: 2 residues, -Jump to ATF2_HUMANExon1: 122 residues, 175647478-175647841Exon2: 31 residues, 175647973-175648061Exon3: 37 residues, 175653633-175653739Exon4: 26 residues, 175665516-175665590Exon5: 71 residues, 175666034-175666241Exon6: 52 residues, 175670417-175670567Exon7: 31 residues, 175684541-175684628Exon8: 40 residues, 175686967-175687082Exon9: 61 residues, 175687663-175687842Exon10: 45 residues, 175690963-175691092Exon11: 41 residues, 175691224-175691343Exon12: 34 residues, 175694417-175694514Exon13: 25 residues, 175703111-175703181Exon14: 27 residues, 175709385-175709460Exon15: 13 residues, 175720919-175720954Exon16: 35 residues, 175724033-175724132Exon17: 42 residues, 175741023-175741143Exon18: 2 residues, -Jump to ATF2_HUMAN  
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Loci Cluster (Details)Loci: 4480 175320852-175337416 ~-17K 21613(CHRNA1)(-)Loci: 4481 175372337-175578361 ~-206K 21615(CHN1)(-)Loci: 4482 175647253-175741143 ~-94K 21619(ATF2)(-)Loci: 4479 175132548-175255873 ~-123K 21610(WASPIP)(-)Link out to UCSC