Recently visited
Please sign in to see a list of articles you recently visited.
Recently updated
 SOX9
Homo sapiens
 HIF1A
Homo sapiens
 Pax6
Mus musculus
 PAX6
Homo sapiens
 Snai2
Mus musculus
 PPARA
Homo sapiens
 Ppara
Mus musculus
 Thrb
Mus musculus
 SNAI2
Homo sapiens
 Tbr1
Mus musculus
Transcription Factor Encyclopedia  BETA
Comments (post)
There are no comments posted here... Yet.
Overview
No annotation is available in this section for this article. The content below is taken from a related TF, PAX6 (Homo sapiens).

Pax6 is present in both vertebrate and invertebrate. It is highly conserved; its coding sequence is 96% identical to zebrafish pax(zf-a) protein[1][2]. Pax6 belongs to the paired homeobox family. It contains a 128 amino acid long paired domain (PD), a 61 amino acid long homeodomain (HD); the PD and HD domain are linked by a 78 amino acid glycine-rich hinge region (Gln/Gly), and C-terminal of Pax6 is enriched for Pro/Ser/Thr amino acids (PST)[3].

The PD consists of independent amino-terminal and carboxyl-terminal subdomains. The N subdomain contains a short β motif and three α helices that fold like a homeodomain. The C subdomain also contains three α helices with a related homeodomain-like fold [4]. DNA binding is mediated mainly through N subdomain; C subdomain binding may predominate when N subdomain binding is disrupted by insertion of 14 amino acids between second and third alpha helices in Pax6 isoform 5a [4]. The HD domain consists of helix-turn-helix structure that binds to the palindromic recognition sequence as a cooperative dimer. Together, PD and HD domains can bind DNA independently or cooperatively [5] [6][7][8]. Transcription is activated by PST domain which possesses a transactivation function [9].

References
  1. Krauss S et al. Zebrafish pax[zf-a]: a paired box-containing gene expressed in the neural tube. EMBO J., 10(12):3609-19. (PMID 1718739)
  2. Püschel AW et al. Sequence and expression pattern of pax-6 are highly conserved between zebrafish and mice. Development, 114(3):643-51. (PMID 1352238)
  3. Glaser T et al. Genomic structure, evolutionary conservation and aniridia mutations in the human PAX6 gene. Nat. Genet., 2(3):232-9. (PMID 1345175)
  4. Xu HE et al. Crystal structure of the human Pax6 paired domain-DNA complex reveals specific roles for the linker region and carboxy-terminal subdomain in DNA binding. Genes Dev., 13(10):1263-75. (PMID 10346815)
  5. Epstein J et al. Identification of a Pax paired domain recognition sequence and evidence for DNA-dependent conformational changes. J. Biol. Chem., 269(11):8355-61. (PMID 8132558)
  1. Czerny T and Busslinger M. DNA-binding and transactivation properties of Pax-6: three amino acids in the paired domain are responsible for the different sequence recognition of Pax-6 and BSAP (Pax-5). Mol. Cell. Biol., 15(5):2858-71. (PMID 7739566)
  2. Jun S and Desplan C. Cooperative interactions between paired domain and homeodomain. Development, 122(9):2639-50. (PMID 8787739)
  3. Simpson TI and Price DJ. Pax6; a pleiotropic player in development. Bioessays, 24(11):1041-51. (PMID 12386935)
  4. Tang HK et al. Dissection of the transactivation function of the transcription factor encoded by the eye developmental gene PAX6. J. Biol. Chem., 273(13):7210-21. (PMID 9516413)
Structures
About this section
This section contains 3D PDB models of structural predictions for this transcription factor. METHODS: The template selection protocol follows that of Morozov and Siggia, in which templates are selected to optimize similarity of DNA-binding residues (Morozov AV, Siggia ED. PNAS 104(17):7068-73). This has been shown to increase modeling accuracy at the DNA-binding interface. For all solved structures containing DNA, amino acids within 4A of DNA (DNA-binding residues) are stored. Pfam domain hits of each DNA-bound chain are detected by hmmer, and each hit is added to a list mapping domain family name to chain hits. Pfam domain hits of each unsolved structure are detected by HMMER. For each identified Pfam family, the unsolved sequence is aligned to all solved family members (putative templates). Alignments are scored based on similarity of the DNA-binding residues in the template to the aligned residues of the unsolved sequence. For each subsequence of the unsolved protein identified as a DNA-binding domain, the top scoring template is selected. For sequences known to form homodimers, a homodimeric template is selected. The model is constructed from the template using Modeller 9v2. DNA bound to the template is added to the model by superimposition of the solved and modeled structures.
There are no structures here... Yet.
Family
Helix-Turn-Helix Group » Homeodomain Family
Alx1
Mus musculus
 Arx
Mus musculus
Barx1
Mus musculus
Barx2
Mus musculus
Cdx1
Mus musculus
 CDX2
Homo sapiens
 Cdx2
Mus musculus
CRX
Homo sapiens
Crx
Mus musculus
Cux1
Mus musculus
Cux2
Mus musculus
 DLX1
Homo sapiens
 Dlx1
Mus musculus
 Dlx2
Mus musculus
 DLX2
Homo sapiens
 DLX3
Homo sapiens
 Dlx3
Mus musculus
 DLX4
Homo sapiens
 Dlx4
Mus musculus
 DLX5
Homo sapiens
 Dlx5
Mus musculus
 DLX6
Homo sapiens
 Dlx6
Mus musculus
Dmbx1
Mus musculus
EMX1
Homo sapiens
Emx1
Mus musculus
EMX2
Homo sapiens
Emx2
Mus musculus
En1
Mus musculus
En2
Mus musculus
Esx1
Mus musculus
Gbx2
Mus musculus
Gsc
Mus musculus
Gsx1
Mus musculus
Gsx2
Mus musculus
Hesx1
Mus musculus
Hmx2
Mus musculus
Hnf1a
Mus musculus
 HNF1B
Homo sapiens
 Hnf1b
Mus musculus
Hoxa1
Mus musculus
Hoxa10
Mus musculus
Hoxa11
Mus musculus
Hoxa2
Mus musculus
Hoxa3
Mus musculus
Hoxa5
Mus musculus
Hoxa7
Mus musculus
Hoxa9
Mus musculus
Hoxb1
Mus musculus
Hoxb2
Mus musculus
Hoxb3
Mus musculus
HOXB4
Homo sapiens
Hoxb4
Mus musculus
Hoxb5
Mus musculus
Hoxb7
Mus musculus
Hoxb8
Mus musculus
Hoxb9
Mus musculus
Hoxc10
Mus musculus
Hoxc11
Mus musculus
Hoxc4
Mus musculus
Hoxc6
Mus musculus
Hoxd1
Mus musculus
Hoxd10
Mus musculus
Hoxd13
Mus musculus
Hoxd3
Mus musculus
Hoxd4
Mus musculus
Hoxd8
Mus musculus
Hoxd9
Mus musculus
 ISL1
Homo sapiens
 Isl1
Mus musculus
Isl2
Mus musculus
Lbx1
Mus musculus
Lcor
Mus musculus
Lhx1
Mus musculus
Lhx2
Mus musculus
 LHX3
Homo sapiens
 Lhx3
Mus musculus
 LHX4
Homo sapiens
 Lhx4
Mus musculus
Lhx5
Mus musculus
 LMX1A
Homo sapiens
 LMX1B
Homo sapiens
 Lmx1b
Mus musculus
Meis2
Mus musculus
Meox1
Mus musculus
Meox2
Mus musculus
Mixl1
Mus musculus
Msx1
Mus musculus
Msx2
Mus musculus
Nanog
Mus musculus
Nkx2-1
Mus musculus
Nkx2-3
Mus musculus
Nkx2-5
Mus musculus
Nkx2-6
Mus musculus
Nkx2-9
Mus musculus
NKX3-1
Homo sapiens
Nkx3-1
Mus musculus
Nkx3-2
Mus musculus
Nkx6-1
Mus musculus
Nkx6-2
Mus musculus
 ONECUT1
Homo sapiens
 Onecut1
Mus musculus
Onecut2
Mus musculus
Onecut3
Mus musculus
OTX1
Homo sapiens
Otx2
Mus musculus
Pax1
Mus musculus
PAX2
Homo sapiens
Pax2
Mus musculus
PAX3
Homo sapiens
 PAX4
Homo sapiens
 Pax4
Mus musculus
Pax5
Mus musculus
 PAX6
Homo sapiens
 Pax6
Mus musculus
PAX7
Homo sapiens
Pax7
Mus musculus
 PAX8
Homo sapiens
 Pax8
Mus musculus
Pax9
Mus musculus
 PBX1
Homo sapiens
 Pbx1
Mus musculus
Pbx3
Mus musculus
Pdx1
Mus musculus
Phox2a
Mus musculus
Phox2b
Mus musculus
Pitx1
Mus musculus
Pitx3
Mus musculus
Pknox1
Mus musculus
 Pou1f1
Mus musculus
Pou2f1
Mus musculus
Pou2f2
Mus musculus
Pou3f1
Mus musculus
Pou3f2
Mus musculus
Pou3f4
Mus musculus
Pou4f1
Mus musculus
Pou4f3
Mus musculus
Pou5f1
Mus musculus
Pou6f1
Mus musculus
 Prop1
Mus musculus
Prrx2
Mus musculus
Prrxl1
Mus musculus
Rax
Mus musculus
Satb1
Mus musculus
Satb2
Mus musculus
Six1
Mus musculus
Six2
Mus musculus
 SIX3
Homo sapiens
 Six3
Mus musculus
Six4
Mus musculus
 SIX6
Homo sapiens
 Six6
Mus musculus
TEAD1
Homo sapiens
Tead1
Mus musculus
TEAD2
Homo sapiens
Tead2
Mus musculus
TEAD3
Homo sapiens
Tead3
Mus musculus
TEAD4
Homo sapiens
Tead4
Mus musculus
Tgif1
Mus musculus
 TLX1
Homo sapiens
 Tlx1
Mus musculus
Tlx2
Mus musculus
Vsx1
Mus musculus
Vsx2
Mus musculus
Zhx1
Mus musculus
Zhx2
Mus musculus
 
Figures
No annotation is available in this section for this article. The content below is taken from a related TF, PAX6 (Homo sapiens).
FIGURE 5 Pax6 structure
A schematic representation of the human Pax-6. Pax6 protein is separated to distinct regions: paired domain (PD), glycine-rich linker (Gln/Gly), homeodomain (HD) and Proline/Serine/Threonine domain (PST). An alternative splicing event could lead to the insertion of exon 5a to the paired domain.
This figure was created by the authors of this article. The authors of this article have provided the assurance that this figure constitutes their original work.