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1O60519_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
NameN/A
DescriptionCre binding protein-like 2 (crebl2 protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005634 nucleus (TAS)
0003700 transcription factor activity (TAS)
0007165 signal transduction (TAS)
0006350 transcription (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 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
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
IPR011700:bZIP_2 
Evalue:-6.36653137207031 
Location:24-75
SequencesProtein: O60519_HUMAN (120 aa)
mRNA: NM_001310
Local Annotation
Synapse Ontology
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 98 residues, 12656097-12656388Exon2: 68 residues, 12679977-12680175Exon3: 50 residues, 12681770-12681915Exon4: 1040 residues, 12686194-12689308Exon5: 2 residues, -Jump to O60519_HUMAN  
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Loci Cluster (Details)Loci: 2739 12935222-12957865 ~-23K 8455(GPRC5A)(+)Loci: 2738 12656097-12689308 ~-33K 8446(+)Link out to UCSC