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0PO2F1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePOU2F1
DescriptionPou domain, class 2, transcription factor 1 (octamer-binding transcription factor 1) (oct-1) (otf-1) (nf-a1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005515 protein binding (IPI)
0003700 transcription factor 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 assigned to SynO:
POU proteins are eukaryotic transcription factors containing a bipartite DNA binding domain referred to as the POU domain. The acronym POU (pronounced pow) is derived from the names of three mammalian transcription factors.he pituitary-specific Pit-1.he octamer-binding proteins Oct-1 and Oct-2.nd the neural Unc-86 from Caenorhabditis elegans. POU domain genes have been described in organisms as divergent as Caenorhabditis elegans.rosophila.enopus.ebrafish and human but have not been yet identified in plants and fungi. The various members of the POU family have a wide variety of functions.ll of which are related to the function of the neuroendocrine system and the development of an organism . Some other genes are also regulated.ncluding those for immunoglobulin light and heavy chains (Oct-2) and trophic hormone genes.uch as those for prolactin and growth hormone (Pit-1). The POU domain is a bipartite domain composed of two subunits separated by a non-conserved region of 15-55 aa. The N-terminal subunit is known as the POU-specific (POUs) domain ().hile the C-terminal subunit is a homeobox domain (). 3D structures of complexes including both POU subdomains bound to DNA are available. Both subdomains contain the structural motif helix-turn-helix.hich directly associates with the two components of bipartite DNA binding sites.nd both are required for high affinity sequence-specific DNA-binding. The domain may also be involved in protein-protein interactions . The subdomains are connected by a flexible linker . In proteins a POU-specific domain is always accompanied by a homeodomain. Despite of the lack of sequence homology.D structure of POUs is similar to 3D structure of bacteriophage lambda repressor and other members of HTH_3 family .This entry represents the POU-specific subunit of the POU domain.
  IPR000327:POU-specific
InterPro domains unassigned to SynO:
The octamer-binding protein is a transcription factor that binds specifically to the octamer motif (ATTTGCAT) of immunoglobulin promoters and activates these genes. There are two Ig octamer-binding proteins.esignated NF-A1 and NF-A2. NF-A1 is found in all cell types.hile NF-A2 is found only in lymphoid cells. The sequences of these proteins contain a region that correponds closely to the DNA-binding homeobox domains and POU transcription factors.
  IPR000972:Octamer-binding transcription factor
The homeobox domain was first identified in a number of drosophila homeotic and segmentation proteins.ut is now known to be well-conserved in many other animals.ncluding vertebrates . Hox genes encode homeodomain-containing transcriptional regulators that operate differential genetic programs along the anterior-posterior axis of animal bodies . The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA . The first helix helps to stabilise the structure. The motif is very similar in sequence and structure in a wide range of DNA-binding proteins (e.g..ro and repressor proteins.omeotic proteins.tc.). One of the principal differences between HTH motifs in these different proteins arises from the stereo-chemical requirement for glycine in the turn which is needed to avoid steric interference of the beta-carbon with the main chain: for cro and repressor proteins the glycine appears to be mandatory.hile for many of the homeotic and other DNA-binding proteins the requirement is relaxed.
  IPR001356:Homeobox
Homeodomain proteins are transcription factors that share a related DNA binding homeodomain . The homeodomain was first identified in a number of Drosophila homeotic and segmentation proteins.ut is now known to be well conserved in many other animals.ncluding vertebrates. The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA. The first helix helps to stabilise the structure. Many proteins contain homeodomains.ncluding Drosophila Engrailed.east mating type proteins.epatocyte nuclear factor 1a and HOX proteins.The homeodomain motif is very similar in sequence and structure to domains in a wide range of DNA-binding proteins.ncluding recombinases.yb proteins.ARP response regulators.uman telomeric proteins (hTRF1).aired domain proteins (PAX).east RAP1.entromere-binding proteins CENP-B and ABP-1.ranscriptional regulators (TyrR).raC-type transcriptional activators.nd tetracycline repressor-like proteins (TetR.acR.cdC) .
  IPR009057:Homeodomain-like
Bacteriophage lambda C1 repressor controls the expression of viral genes as part of the lysogeny/lytic growth switch. C1 is essential for maintaining lysogeny.here the phage replicates non-disruptively along with the host. If the host cell is threatened.hen lytic growth is induced. The Lambda C1 repressor consists of two domains connected by a linker: an N-terminal DNA-binding domain that also mediates interactions with RNA polymerase.nd a C-terminal dimerisation domain . The DNA-binding domain consists of four helices in a closed folded leaf motif. Several different phage repressors from different helix-turn-helix families contain DNA-binding domains that adopt a similar topology. These include the Lambda Cro repressor.acteriophage 434 C1 and Cro repressors.22 C2 repressor.nd bacteriophage Mu Ner protein.The DNA-binding domain of Bacillus subtilis spore inhibition repressor SinR is identical to that of phage repressors . SinR represses sporulation.hich only occurs in response to adverse conditions. This provides a possible evolutionary link between the two adaptive responses of bacterial sporulation and prophage induction.Other DNA-binding domains also display similar structural folds to that of Lambda C1. These include bacterial regulators such as the purine repressor (PurR).he lactose repressor (Lacr) and the fructose repressor (FruR).ach of which has an N-terminal DNA-binding domain that exhibits a fold similar to that of lambda C1.xcept that they lack the first helix . POU-specific domains found in transcription factors such as in Oct-1.it-1 and Hepatocyte nuclear factor 1a (LFB1/HNF1) display four-helical fold DNA-binding domains similar to that of Lambda C1 . The N-terminal domain of cyanase has an alpha-helix bundle motif similar to Lambda C1.ut it probably does not bind DNA. Cyanase is an enzyme found in bacteria and plants that catalyses the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide in response to extracellular cyanate .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR010982:Lambda repressor-like, DNA-binding
Homeodomain proteins are transcription factors that share a related DNA binding homeodomain . The homeodomain was first identified in a number of Drosophila homeotic and segmentation proteins.ut is now known to be well conserved in many other animals.ncluding vertebrates. The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA. The first helix helps to stabilise the structure. Many proteins contain homeodomains.ncluding Drosophila Engrailed.east mating type proteins.epatocyte nuclear factor 1a and HOX proteins.The homeodomain motif is very similar in sequence and structure to domains in a wide range of DNA-binding proteins.ncluding recombinases.yb proteins.ARP response regulators.uman telomeric proteins (hTRF1).aired domain proteins (PAX).east RAP1.entromere-binding proteins CENP-B and ABP-1.ranscriptional regulators (TyrR).raC-type transcriptional activators.nd tetracycline repressor-like proteins (TetR.acR.cdC) .
  IPR012287:Homeodomain-related
POU proteins are eukaryotic transcription factors containing a bipartite DNA binding domain referred to as the POU domain. The acronym POU (pronounced pow) is derived from the names of three mammalian transcription factors.he pituitary-specific Pit-1.he octamer-binding proteins Oct-1 and Oct-2.nd the neural Unc-86 from Caenorhabditis elegans. POU domain genes have been described in organisms as divergent as Caenorhabditis elegans.rosophila.enopus.ebrafish and human but have not been yet identified in plants and fungi. The various members of the POU family have a wide variety of functions.ll of which are related to the development of an organism . The POU domain is a bipartite domain composed of two subunits separated by a non-conserved region of 15-55 aa. The N-terminal subunit is known as the POU-specific (POUs) domain ().hile the C-terminal subunit is a homeobox domain (). 3D structures of complexes including both POU subdomains bound to DNA are available. Both subdomains contain the structural motif helix-turn-helix.hich directly associates with the two components of bipartite DNA binding sites.nd both are required for high affinity sequence-specific DNA-binding. The subdomains are connected by a flexible linker . In proteins a POU-specific domain is always accompanied by a homeodomain. Despite of the lack of sequence homology.D structure of POUs is similar to 3D structure of bacteriophage lambda repressor and other members of HTH_3 family .This entry represents the complete POU domain.
  IPR013847:POU
IPR000327:Pou 
Evalue:-53.4317970275879 
Location:280-354IPR001356:Homeobox 
Evalue:-22.2839965820313 
Location:380-436IPR000972:OCTAMER 
Evalue:0 
Location:181-196IPR000972:OCTAMER 
Evalue:0 
Location:205-220IPR000972:OCTAMER 
Evalue:0 
Location:229-241
SequencesProtein: PO2F1_HUMAN (743 aa)
mRNA: NM_002697
Local Annotation
Synapse Ontology
The formation of a synapse.
sdb:0034 synaptogenesis  (Evidence:domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 18 residues, 165456766-165456819Exon2: 35 residues, 165539334-165539435Exon3: 24 residues, 165568330-165568396Exon4: 35 residues, 165601327-165601428Exon5: 20 residues, 165606021-165606075Exon6: 42 residues, 165607777-165607897Exon7: 65 residues, 165609968-165610157Exon8: 44 residues, 165611889-165612016Exon9: 33 residues, 165619717-165619812Exon10: 60 residues, 165625448-165625622Exon11: 49 residues, 165632146-165632288Exon12: 48 residues, 165633854-165633994Exon13: 62 residues, 165635046-165635226Exon14: 37 residues, 165637311-165637417Exon15: 117 residues, 165647819-165648165Exon16: 31 residues, 165648886-165648975Exon17: 195 residues, 165651360-165651941Exon18: 2 residues, -Jump to PO2F1_HUMAN  
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