Home News About DMDM Database Statistics Research Publications Contact  

 
Click for a Larger Image
  Domain Name: NR_DBD_AR
DNA-binding domain of androgen receptor (AR) is composed of two C4-type zinc fingers. DNA-binding domain of androgen receptor (AR) is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. To regulate gene expression, AR interacts with a palindrome of the core sequence 5'-TGTTCT-3' with a 3-bp spacer. It also binds to the direct repeat 5'-TGTTCT-3' hexamer in some androgen controlled genes. AR is activated by the androgenic hormones, testosterone or dihydrotestosterone, which are responsible for primary and for secondary male characteristics, respectively. The primary mechanism of action of ARs is by direct regulation of gene transcription. The binding of androgen results in a conformational change in the androgen receptor which causes its transport from the cytosol into the cell nucleus, and dimerization. The receptor dimer binds to a hormone response element of AR regulated genes and modulates their expression. Another mode of action of androgen receptor is independent of their interactions with DNA. The receptor interacts directly with signal transduction proteins in the cytoplasm, causing rapid changes in cell function, such as ion transport. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, AR has a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD).
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 71
Total Disease Mutations Found: 52
This domain occurred 46 times on human genes (181 proteins).



  46,XY SEX REVERSAL 3
  ANDROGEN INSENSITIVITY SYNDROME
  ANDROGEN INSENSITIVITY, COMPLETE
  ANDROGEN INSENSITIVITY, PARTIAL, WITH BREAST CANCER
  ANDROGEN INSENSITIVITY, PARTIAL, WITH OR WITHOUT BREAST CANCER
  ENHANCED S-CONE SYNDROME
  GLUCOCORTICOID RESISTANCE, GENERALIZED
  HYPERAPOBETALIPOPROTEINEMIA, SUSCEPTIBILITY TO
  LIPODYSTROPHY, FAMILIAL PARTIAL, TYPE 3
  MATURITY-ONSET DIABETES OF THE YOUNG, TYPE 1
  MICROPHTHALMIA, SYNDROMIC 12
  PSEUDOHYPOALDOSTERONISM, TYPE I, AUTOSOMAL DOMINANT
  RETINITIS PIGMENTOSA 37
  SPERMATOGENIC FAILURE 8 (SPGF8)
  VITAMIN D-DEPENDENT RICKETS, TYPE 2A


Tips:
 If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position.

 The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs.

 Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below.



Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
zinc binding site
DNA binding site
dimer interface










Weblogos are Copyright (c) 2002 Regents of the University of California




Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

   |   1000 Hilltop Circle, Baltimore, MD 21250   |   Department of Biological Sciences   |   Phone: 410-455-2258