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0PAX6_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePAX6
DescriptionPaired box protein pax-6 (oculorhombin) (aniridia type ii protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0003700 transcription factor activity (TAS)
0007417 central nervous system development (TAS)
0001654 eye development (TAS)
0009887 organogenesis (TAS)
0007601 visual perception (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 paired box is a conserved 124 amino acid N-terminal domain of unknown function that usually.ut not always.recedes a homeobox domain (see ) . Paired box genes are expressed in alternate segments of the developing fruit fly.he observed grouping of segments into pairs depending on the position of the segment in the segmental array.nd not on the identity of the segment as in the case of homeotic genes. This implies that the genes affect different processes from those altered by homeotic genes.
  IPR001523:Paired box protein, N-terminal
Winged helix DNA-binding proteins share a related winged helix-turn-helix DNA-binding motif.here the "wings".r loops.re small beta-sheets. The winged helix motif consists of two wings (W1.2).hree alpha helices (H1.2.3) and three beta-sheets (S1.2.3) arranged in the order H1-S1-H2-H3-S2-W1-S3-W2 . The DNA-recognition helix makes sequence-specific DNA contacts with the major groove of DNA.hile the wings make different DNA contacts.ften with the minor groove or the backbone of DNA. Several winged-helix proteins display an exposed patch of hydrophobic residues thought to mediate protein-protein interactions.Many different proteins with diverse biological functions contain a winged helix DNA-binding domain.ncluding transcriptional repressors such as biotin repressor.exA repressor and the arginine repressor ; transcription factors such as the hepatocyte nuclear factor-3 proteins involved in cell differentiation.eat-shock transcription factor.nd the general transcription factors TFIIE and TFIIF . helicases such as RuvB that promotes branch migration at the Holliday junction.nd CDC6 in the pre-replication complex . endonucleases such as FokI and TnsA ; histones; and Mu transposase.here the flexible wing of the enhancer-binding domain is essential for efficient transposition .
  IPR011991:Winged helix repressor DNA-binding
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
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
IPR001523:PAX 
Evalue:-91.2076083105017 
Location:4-128IPR001356:Homeobox 
Evalue:-30.32790184021 
Location:211-267
SequencesProtein: PAX6_HUMAN (422 aa)
mRNA: NM_000280 NM_001604
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentK08031
  Level 3 annotation:
    paired box protein Pax-6
  Level 2 annotation:
    Maturity onset diabetes of the young
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 370 residues, 31767034-31768143Exon2: 52 residues, 31768833-31768984Exon3: 40 residues, 31771561-31771677Exon4: 52 residues, 31771775-31771926Exon5: 29 residues, 31772155-31772238Exon6: 55 residues, 31772753-31772912Exon7: 57 residues, 31778814-31778980Exon8: 74 residues, 31779684-31779900Exon9: 16 residues, 31779994-31780036Exon10: 45 residues, 31780827-31780958Exon11: 22 residues, 31784525-31784586Exon12: 27 residues, 31784972-31785049Exon13: 64 residues, 31788951-31789139Exon14: 41 residues, 31789336-31789455Exon15: 2 residues, -Jump to PAX6_HUMANExon1: 370 residues, 31767034-31768143Exon2: 52 residues, 31768833-31768984Exon3: 40 residues, 31771561-31771677Exon4: 52 residues, 31771775-31771926Exon5: 29 residues, 31772155-31772238Exon6: 55 residues, 31772753-31772912Exon7: 57 residues, 31778814-31778980Exon8: 74 residues, 31779684-31779900Exon9: 45 residues, 31780827-31780958Exon10: 22 residues, 31784525-31784586Exon11: 27 residues, 31784972-31785049Exon12: 64 residues, 31788951-31789139Exon13: 67 residues, 31789238-31789434Exon14: 2 residues, -Jump to PAX6_HUMAN  
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