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0BARX2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameBARX2
DescriptionHomeobox protein barh-like 2.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
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
Helix-turn-helix (HTH) motifs are found in all known DNA binding proteinsthat regulate gene expression. The motif consists of approximately 20 residues and is characterised by 2 alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix of the HTH motif 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 . Thefirst helix helps to stabilise the structure . The HTH motif is very similar in sequence and structure to the N-terminal region of the lamda and other repressor proteins.nd has also been identified in many other DNA-binding proteins on the basis of sequence and structural similarity . One of the principal differences between HTH motifs in these different proteins arises from the stereochemical requirement for glycine in the turn.hich is needed to avoid steric interference of the beta-carbon with the main chain: for cro and other repressors the Gly appears to be mandatory.hile for many of the homeoticand other DNA-binding proteins the requirement is relaxed.
  IPR000047:Helix-turn-helix motif, lambda-like repressor
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
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
IPR001356:Homeobox 
Evalue:-27.8239078521729 
Location:109-165
SequencesProtein: BARX2_HUMAN (254 aa)
mRNA: BC069378 NM_003658
Local Annotation
Synapse Ontology
calcium-regulated transcription factor
sdb:0215 calcium-regulated transcription factor  (Evidence:keywords)
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 95 residues, 128751044-128751327Exon2: 102 residues, 128811855-128812156Exon3: 30 residues, 128817939-128818024Exon4: 263 residues, 128826240-128827025Exon5: 2 residues, -Jump to BARX2_HUMANExon1: 80 residues, 128751090-128751327Exon2: 102 residues, 128811855-128812156Exon3: 30 residues, 128817939-128818024Exon4: 107 residues, 128826240-128826556Exon5: 2 residues, -Jump to BARX2_HUMAN  
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