Summary: Androgen receptor
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Androgen receptor Edit Wikipedia article
Structure of the ligand binding domain of the androgen receptor (rainbow cartoon) complexed with testosterone (white sticks).
|External IDs||IUPHAR: ChEMBL: GeneCards:|
|RNA expression pattern|
crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor nh2-terminal peptide, ar20-30, and r1881
The androgen receptor (AR), also known as NR3C4 (nuclear receptor subfamily 3, group C, member 4), is a type of nuclear receptor that is activated by binding of either of the androgenic hormones testosterone or dihydrotestosterone  in the cytoplasm and then translocating into the nucleus. The androgen receptor is most closely related to the progesterone receptor, and progestins in higher dosages can block the androgen receptor.
The main function of the androgen receptor is as a DNA-binding transcription factor that regulates gene expression; however, the androgen receptor has other functions as well. Androgen regulated genes are critical for the development and maintenance of the male sexual phenotype.
Effect on development
In some cell types, testosterone interacts directly with androgen receptors, whereas, in others, testosterone is converted by 5-alpha-reductase to dihydrotestosterone, an even more potent agonist for androgen receptor activation. Testosterone appears to be the primary androgen receptor-activating hormone in the Wolffian duct, whereas dihydrotestosterone is the main androgenic hormone in the urogenital sinus, urogenital tubercle, and hair follicles. Hence, testosterone is responsible primarily for the development of male primary sexual characteristics, whereas dihydrotestosterone is responsible for secondary male characteristics.
Androgens cause slow epiphysis, or maturation of the bones, but more of the potent epiphysis effect comes from the estrogen produced by aromatization of androgens. Steroid users of teen age may find that their growth had been stunted by androgen and/or estrogen excess. People with too little sex hormones can be short during puberty but end up taller as adults as in androgen insensitivity syndrome or estrogen insensitivity syndrome.
Also, AR knockout-mice studies have shown that AR is essential for normal female fertility, being required for development and full functionality of the ovarian follicles and ovulation, working through both intra-ovarian and neuroendocrine mechanisms.
Mechanism of action
The primary mechanism of action for androgen receptors is direct regulation of gene transcription. The binding of an androgen to the androgen receptor results in a conformational change in the receptor that, in turn, causes dissociation of heat shock proteins, transport from the cytosol into the cell nucleus, and dimerization. The androgen receptor dimer binds to a specific sequence of DNA known as a hormone response element. Androgen receptors interact with other proteins in the nucleus, resulting in up- or down-regulation of specific gene transcription. Up-regulation or activation of transcription results in increased synthesis of messenger RNA, which, in turn, is translated by ribosomes to produce specific proteins. One of the known target genes of androgen receptor activation is insulin-like growth factor I (IGF-1). Thus, changes in levels of specific proteins in cells is one way that androgen receptors control cell behavior.
One function of androgen receptor that is independent of direct binding to its target DNA sequence, is facilitated by recruitment via other DNA-binding proteins. One example is serum response factor, a protein that activates several genes that cause muscle growth.
Androgen receptor is modified by acetylation, which directly promotes contact independent growth of prostate cancer cells.
More recently, androgen receptors have been shown to have a second mode of action. As has been also found for other steroid hormone receptors such as estrogen receptors, androgen receptors can have actions that are independent of their interactions with DNA. Androgen receptors interact with certain signal transduction proteins in the cytoplasm. Androgen binding to cytoplasmic androgen receptors can cause rapid changes in cell function independent of changes in gene transcription, such as changes in ion transport. Regulation of signal transduction pathways by cytoplasmic androgen receptors can indirectly lead to changes in gene transcription, for example, by leading to phosphorylation of other transcription factors.
The androgen insensitivity syndrome, formerly known as testicular feminization, is caused by a mutation of the androgen receptor gene located on the X chromosome (locus:Xq11-Xq12). The androgen receptor seems to affect neuron physiology and is defective in Kennedy's disease. In addition, point mutations and trinucleotide repeat polymorphisms has been linked to a number of additional disorders.
- AR-A - 87 kDa - N-terminus truncated (lacks the first 187 amino acids), which results from in vitro proteolysis.
- AR-B - 110 kDa - full length
- A/B) - N-terminal regulatory domain contains:
- activation function 1 (AF-1) between residues 101 and 370 required for full ligand activated transcriptional activity
- activation function 5 (AF-5) between residues 360-485 is responsible for the constitutive activity (activity without bound ligand)
- dimerization surface involving residues 1-36 (containing the FXXLF motif where F = phenylalanine, L = leucine, and X = any amino acid residue) and 370-494, both of which interact with the LBD in an intramolecular head-to-tail interaction
- C) - DNA binding domain (DBD)
- D) - Hinge region - flexible region that connects the DBD with the LBD; along with the DBD, contains a ligand dependent nuclear localization signal
- E) - Ligand binding domain (LBD) containing
- F) - C-terminal domain
Androgen receptor has been shown to interact with:
- Calmodulin 1,
- Caveolin 1,
- CREB-binding protein,
- Cyclin D1,
- Cyclin-dependent kinase 7,
- Death associated protein 6,
- Deleted in Colorectal Cancer,
- Epidermal growth factor receptor,
- Retinoblastoma protein,
- Small heterodimer partner,
- Testicular receptor 2,
- Testicular receptor 4,
- UXT, and
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- Nishimura K, Ting HJ, Harada Y, Tokizane T, Nonomura N, Kang HY, Chang HC, Yeh S, Miyamoto H, Shin M, Aozasa K, Okuyama A, Chang C (August 2003). "Modulation of androgen receptor transactivation by gelsolin: a newly identified androgen receptor coregulator". Cancer Res. 63 (16): 4888–94. PMID 12941811.
- Rigas AC, Ozanne DM, Neal DE, Robson CN (November 2003). "The scaffolding protein RACK1 interacts with androgen receptor and promotes cross-talk through a protein kinase C signaling pathway". J. Biol. Chem. 278 (46): 46087–93. doi:10.1074/jbc.M306219200. PMID 12958311.
- Wang L, Lin HK, Hu YC, Xie S, Yang L, Chang C (July 2004). "Suppression of androgen receptor-mediated transactivation and cell growth by the glycogen synthase kinase 3 beta in prostate cells". J. Biol. Chem. 279 (31): 32444–52. doi:10.1074/jbc.M313963200. PMID 15178691.
- Gaughan L, Logan IR, Cook S, Neal DE, Robson CN (July 2002). "Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor". J. Biol. Chem. 277 (29): 25904–13. doi:10.1074/jbc.M203423200. PMID 11994312.
- Veldscholte J, Berrevoets CA, Brinkmann AO, Grootegoed JA, Mulder E (March 1992). "Anti-androgens and the mutated androgen receptor of LNCaP cells: differential effects on binding affinity, heat-shock protein interaction, and transcription activation". Biochemistry 31 (8): 2393–9. doi:10.1021/bi00123a026. PMID 1540595.
- Nemoto T, Ohara-Nemoto Y, Ota M (September 1992). "Association of the 90-kDa heat shock protein does not affect the ligand-binding ability of androgen receptor". J. Steroid Biochem. Mol. Biol. 42 (8): 803–12. doi:10.1016/0960-0760(92)90088-Z. PMID 1525041.
- Bai S, He B, Wilson EM (February 2005). "Melanoma Antigen Gene Protein MAGE-11 Regulates Androgen Receptor Function by Modulating the Interdomain Interaction". Mol. Cell. Biol. 25 (4): 1238–57. doi:10.1128/MCB.25.4.1238-1257.2005. PMC 548016. PMID 15684378.
- Bai S, Wilson EM (March 2008). "Epidermal Growth Factor-Dependent Phosphorylation and Ubiquitinylation of MAGE-11 Regulates Its Interaction with the Androgen Receptor". Mol. Cell. Biol. 28 (6): 1947–63. doi:10.1128/MCB.01672-07. PMC 2268407. PMID 18212060.
- Wang Q, Sharma D, Ren Y, Fondell JD (November 2002). "A coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expression". J. Biol. Chem. 277 (45): 42852–8. doi:10.1074/jbc.M206061200. PMID 12218053.
- Sharma M, Zarnegar M, Li X, Lim B, Sun Z (November 2000). "Androgen receptor interacts with a novel MYST protein, HBO1". J. Biol. Chem. 275 (45): 35200–8. doi:10.1074/jbc.M004838200. PMID 10930412.
- Ueda T, Mawji NR, Bruchovsky N, Sadar MD (October 2002). "Ligand-independent activation of the androgen receptor by interleukin-6 and the role of steroid receptor coactivator-1 in prostate cancer cells". J. Biol. Chem. 277 (41): 38087–94. doi:10.1074/jbc.M203313200. PMID 12163482.
- Bevan CL, Hoare S, Claessens F, Heery DM, Parker MG (December 1999). "The AF1 and AF2 Domains of the Androgen Receptor Interact with Distinct Regions of SRC1". Mol. Cell. Biol. 19 (12): 8383–92. PMC 84931. PMID 10567563.
- Wang Q, Udayakumar TS, Vasaitis TS, Brodie AM, Fondell JD (April 2004). "Mechanistic relationship between androgen receptor polyglutamine tract truncation and androgen-dependent transcriptional hyperactivity in prostate cancer cells". J. Biol. Chem. 279 (17): 17319–28. doi:10.1074/jbc.M400970200. PMID 14966121.
- He B, Wilson EM (March 2003). "Electrostatic Modulation in Steroid Receptor Recruitment of LXXLL and FXXLF Motifs". Mol. Cell. Biol. 23 (6): 2135–50. doi:10.1128/MCB.23.6.2135-2150.2003. PMC 149467. PMID 12612084.
- Tan JA, Hall SH, Petrusz P, French FS (September 2000). "Thyroid receptor activator molecule, TRAM-1, is an androgen receptor coactivator". Endocrinology 141 (9): 3440–50. doi:10.1210/en.141.9.3440. PMID 10965917.
- Gnanapragasam VJ, Leung HY, Pulimood AS, Neal DE, Robson CN (December 2001). "Expression of RAC 3, a steroid hormone receptor co-activator in prostate cancer". Br. J. Cancer 85 (12): 1928–36. doi:10.1054/bjoc.2001.2179. PMC 2364015. PMID 11747336.
- He B, Minges JT, Lee LW, Wilson EM (March 2002). "The FXXLF motif mediates androgen receptor-specific interactions with coregulators". J. Biol. Chem. 277 (12): 10226–35. doi:10.1074/jbc.M111975200. PMID 11779876.
- Alen P, Claessens F, Schoenmakers E, Swinnen JV, Verhoeven G, Rombauts W, Peeters B (January 1999). "Interaction of the putative androgen receptor-specific coactivator ARA70/ELE1alpha with multiple steroid receptors and identification of an internally deleted ELE1beta isoform". Mol. Endocrinol. 13 (1): 117–28. doi:10.1210/me.13.1.117. PMID 9892017.
- Yeh S, Chang C (May 1996). "Cloning and characterization of a specific coactivator, ARA70, for the androgen receptor in human prostate cells". Proc. Natl. Acad. Sci. U.S.A. 93 (11): 5517–21. doi:10.1073/pnas.93.11.5517. PMC 39278. PMID 8643607.
- Miyamoto H, Yeh S, Wilding G, Chang C (June 1998). "Promotion of agonist activity of antiandrogens by the androgen receptor coactivator, ARA70, in human prostate cancer DU145 cells". Proc. Natl. Acad. Sci. U.S.A. 95 (13): 7379–84. doi:10.1073/pnas.95.13.7379. PMC 22623. PMID 9636157.
- Yeh S, Lin HK, Kang HY, Thin TH, Lin MF, Chang C (May 1999). "From HER2/Neu signal cascade to androgen receptor and its coactivators: A novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells". Proc. Natl. Acad. Sci. U.S.A. 96 (10): 5458–63. doi:10.1073/pnas.96.10.5458. PMC 21881. PMID 10318905.
- Zhou ZX, He B, Hall SH, Wilson EM, French FS (February 2002). "Domain interactions between coregulator ARA(70) and the androgen receptor (AR)". Mol. Endocrinol. 16 (2): 287–300. doi:10.1210/me.16.2.287. PMID 11818501.
- Gao T, Brantley K, Bolu E, McPhaul MJ (October 1999). "RFG (ARA70, ELE1) interacts with the human androgen receptor in a ligand-dependent fashion, but functions only weakly as a coactivator in cotransfection assays". Mol. Endocrinol. 13 (10): 1645–56. doi:10.1210/me.13.10.1645. PMID 10517667.
- Goo YH, Na SY, Zhang H, Xu J, Hong S, Cheong J, Lee SK, Lee JW (February 2004). "Interactions between activating signal cointegrator-2 and the tumor suppressor retinoblastoma in androgen receptor transactivation". J. Biol. Chem. 279 (8): 7131–5. doi:10.1074/jbc.M312563200. PMID 14645241.
- Liao G, Chen LY, Zhang A, Godavarthy A, Xia F, Ghosh JC, Li H, Chen JD (February 2003). "Regulation of androgen receptor activity by the nuclear receptor corepressor SMRT". J. Biol. Chem. 278 (7): 5052–61. doi:10.1074/jbc.M206374200. PMID 12441355.
- Dotzlaw H, Moehren U, Mink S, Cato AC, Iñiguez Lluhí JA, Baniahmad A (April 2002). "The amino terminus of the human AR is target for corepressor action and antihormone agonism". Mol. Endocrinol. 16 (4): 661–73. doi:10.1210/me.16.4.661. PMID 11923464.
- Zhang Y, Fondell JD, Wang Q, Xia X, Cheng A, Lu ML, Hamburger AW (August 2002). "Repression of androgen receptor mediated transcription by the ErbB-3 binding protein, Ebp1". Oncogene 21 (36): 5609–18. doi:10.1038/sj.onc.1205638. PMID 12165860.
- Yang F, Li X, Sharma M, Zarnegar M, Lim B, Sun Z (May 2001). "Androgen receptor specifically interacts with a novel p21-activated kinase, PAK6". J. Biol. Chem. 276 (18): 15345–53. doi:10.1074/jbc.M010311200. PMID 11278661.
- Lee SR, Ramos SM, Ko A, Masiello D, Swanson KD, Lu ML, Balk SP (January 2002). "AR and ER interaction with a p21-activated kinase (PAK6)". Mol. Endocrinol. 16 (1): 85–99. doi:10.1210/me.16.1.85. PMID 11773441.
- Pero R, Lembo F, Palmieri EA, Vitiello C, Fedele M, Fusco A, Bruni CB, Chiariotti L (February 2002). "PATZ attenuates the RNF4-mediated enhancement of androgen receptor-dependent transcription". J. Biol. Chem. 277 (5): 3280–5. doi:10.1074/jbc.M109491200. PMID 11719514.
- Kotaja N, Aittomäki S, Silvennoinen O, Palvimo JJ, Jänne OA (December 2000). "ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation". Mol. Endocrinol. 14 (12): 1986–2000. doi:10.1210/me.14.12.1986. PMID 11117529.
- Moilanen AM, Karvonen U, Poukka H, Yan W, Toppari J, Jänne OA, Palvimo JJ (February 1999). "A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins". J. Biol. Chem. 274 (6): 3700–4. doi:10.1074/jbc.274.6.3700. PMID 9920921.
- Zhao Y, Goto K, Saitoh M, Yanase T, Nomura M, Okabe T, Takayanagi R, Nawata H (August 2002). "Activation function-1 domain of androgen receptor contributes to the interaction between subnuclear splicing factor compartment and nuclear receptor compartment. Identification of the p102 U5 small nuclear ribonucleoprotein particle-binding protein as a coactivator for the receptor". J. Biol. Chem. 277 (33): 30031–9. doi:10.1074/jbc.M203811200. PMID 12039962.
- Lin HK, Hu YC, Lee DK, Chang C (October 2004). "Regulation of androgen receptor signaling by PTEN (phosphatase and tensin homolog deleted on chromosome 10) tumor suppressor through distinct mechanisms in prostate cancer cells". Mol. Endocrinol. 18 (10): 2409–23. doi:10.1210/me.2004-0117. PMID 15205473.
- Wang L, Hsu CL, Ni J, Wang PH, Yeh S, Keng P, Chang C (March 2004). "Human Checkpoint Protein hRad9 Functions as a Negative Coregulator To Repress Androgen Receptor Transactivation in Prostate Cancer Cells". Mol. Cell. Biol. 24 (5): 2202–13. doi:10.1128/MCB.24.5.2202-2213.2004. PMC 350564. PMID 14966297.
- Rao MA, Cheng H, Quayle AN, Nishitani H, Nelson CC, Rennie PS (December 2002). "RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor". J. Biol. Chem. 277 (50): 48020–7. doi:10.1074/jbc.M209741200. PMID 12361945.
- Beitel LK, Elhaji YA, Lumbroso R, Wing SS, Panet-Raymond V, Gottlieb B, Pinsky L, Trifiro MA (August 2002). "Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity". J. Mol. Endocrinol. 29 (1): 41–60. doi:10.1677/jme.0.0290041. PMID 12200228.
- Lu J, Danielsen M (November 1998). "Differential regulation of androgen and glucocorticoid receptors by retinoblastoma protein". J. Biol. Chem. 273 (47): 31528–33. doi:10.1074/jbc.273.47.31528. PMID 9813067.
- Yeh S, Miyamoto H, Nishimura K, Kang H, Ludlow J, Hsiao P, Wang C, Su C, Chang C (July 1998). "Retinoblastoma, a tumor suppressor, is a coactivator for the androgen receptor in human prostate cancer DU145 cells". Biochem. Biophys. Res. Commun. 248 (2): 361–7. doi:10.1006/bbrc.1998.8974. PMID 9675141.
- Miyamoto H, Rahman M, Takatera H, Kang HY, Yeh S, Chang HC, Nishimura K, Fujimoto N, Chang C (February 2002). "A dominant-negative mutant of androgen receptor coregulator ARA54 inhibits androgen receptor-mediated prostate cancer growth". J. Biol. Chem. 277 (7): 4609–17. doi:10.1074/jbc.M108312200. PMID 11673464.
- Kang HY, Yeh S, Fujimoto N, Chang C (March 1999). "Cloning and characterization of human prostate coactivator ARA54, a novel protein that associates with the androgen receptor". J. Biol. Chem. 274 (13): 8570–6. doi:10.1074/jbc.274.13.8570. PMID 10085091.
- Moilanen AM, Poukka H, Karvonen U, Häkli M, Jänne OA, Palvimo JJ (September 1998). "Identification of a Novel RING Finger Protein as a Coregulator in Steroid Receptor-Mediated Gene Transcription". Mol. Cell. Biol. 18 (9): 5128–39. PMC 109098. PMID 9710597.
- Poukka H, Aarnisalo P, Santti H, Jänne OA, Palvimo JJ (January 2000). "Coregulator small nuclear RING finger protein (SNURF) enhances Sp1- and steroid receptor-mediated transcription by different mechanisms". J. Biol. Chem. 275 (1): 571–9. doi:10.1074/jbc.275.1.571. PMID 10617653.
- Liu Y, Kim BO, Kao C, Jung C, Dalton JT, He JJ (May 2004). "Tip110, the human immunodeficiency virus type 1 (HIV-1) Tat-interacting protein of 110 kDa as a negative regulator of androgen receptor (AR) transcriptional activation". J. Biol. Chem. 279 (21): 21766–73. doi:10.1074/jbc.M314321200. PMID 15031286.
- Chipuk JE, Cornelius SC, Pultz NJ, Jorgensen JS, Bonham MJ, Kim SJ, Danielpour D (January 2002). "The androgen receptor represses transforming growth factor-beta signaling through interaction with Smad3". J. Biol. Chem. 277 (2): 1240–8. doi:10.1074/jbc.M108855200. PMID 11707452.
- Hayes SA, Zarnegar M, Sharma M, Yang F, Peehl DM, ten Dijke P, Sun Z (March 2001). "SMAD3 represses androgen receptor-mediated transcription". Cancer Res. 61 (5): 2112–8. PMID 11280774.
- Kang HY, Huang KE, Chang SY, Ma WL, Lin WJ, Chang C (November 2002). "Differential modulation of androgen receptor-mediated transactivation by Smad3 and tumor suppressor Smad4". J. Biol. Chem. 277 (46): 43749–56. doi:10.1074/jbc.M205603200. PMID 12226080.
- Gobinet J, Auzou G, Nicolas JC, Sultan C, Jalaguier S (December 2001). "Characterization of the interaction between androgen receptor and a new transcriptional inhibitor, SHP". Biochemistry 40 (50): 15369–77. doi:10.1021/bi011384o. PMID 11735420.
- Unni E, Sun S, Nan B, McPhaul MJ, Cheskis B, Mancini MA, Marcelli M (October 2004). "Changes in androgen receptor nongenotropic signaling correlate with transition of LNCaP cells to androgen independence". Cancer Res. 64 (19): 7156–68. doi:10.1158/0008-5472.CAN-04-1121. PMID 15466214.
- Powell SM, Christiaens V, Voulgaraki D, Waxman J, Claessens F, Bevan CL (March 2004). "Mechanisms of androgen receptor signalling via steroid receptor coactivator-1 in prostate". Endocr. Relat. Cancer 11 (1): 117–30. doi:10.1677/erc.0.0110117. PMID 15027889.
- Yuan X, Lu ML, Li T, Balk SP (December 2001). "SRY interacts with and negatively regulates androgen receptor transcriptional activity". J. Biol. Chem. 276 (49): 46647–54. doi:10.1074/jbc.M108404200. PMID 11585838.
- Matsuda T, Junicho A, Yamamoto T, Kishi H, Korkmaz K, Saatcioglu F, Fuse H, Muraguchi A (April 2001). "Cross-talk between signal transducer and activator of transcription 3 and androgen receptor signaling in prostate carcinoma cells". Biochem. Biophys. Res. Commun. 283 (1): 179–87. doi:10.1006/bbrc.2001.4758. PMID 11322786.
- Ueda T, Bruchovsky N, Sadar MD (March 2002). "Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways". J. Biol. Chem. 277 (9): 7076–85. doi:10.1074/jbc.M108255200. PMID 11751884.
- Ting HJ, Yeh S, Nishimura K, Chang C (January 2002). "Supervillin associates with androgen receptor and modulates its transcriptional activity". Proc. Natl. Acad. Sci. U.S.A. 99 (2): 661–6. doi:10.1073/pnas.022469899. PMC 117362. PMID 11792840.
- Mu X, Chang C (October 2003). "TR2 orphan receptor functions as negative modulator for androgen receptor in prostate cancer cells PC-3". Prostate 57 (2): 129–33. doi:10.1002/pros.10282. PMID 12949936.
- Lee YF, Shyr CR, Thin TH, Lin WJ, Chang C (December 1999). "Convergence of two repressors through heterodimer formation of androgen receptor and testicular orphan receptor-4: A unique signaling pathway in the steroid receptor superfamily". Proc. Natl. Acad. Sci. U.S.A. 96 (26): 14724–9. doi:10.1073/pnas.96.26.14724. PMC 24715. PMID 10611280.
- Wang X, Yang Y, Guo X, Sampson ER, Hsu CL, Tsai MY, Yeh S, Wu G, Guo Y, Chang C (May 2002). "Suppression of androgen receptor transactivation by Pyk2 via interaction and phosphorylation of the ARA55 coregulator". J. Biol. Chem. 277 (18): 15426–31. doi:10.1074/jbc.M111218200. PMID 11856738.
- Hsiao PW, Chang C (August 1999). "Isolation and characterization of ARA160 as the first androgen receptor N-terminal-associated coactivator in human prostate cells". J. Biol. Chem. 274 (32): 22373–9. doi:10.1074/jbc.274.32.22373. PMID 10428808.
- Miyajima N, Maruyama S, Bohgaki M, Kano S, Shigemura M, Shinohara N, Nonomura K, Hatakeyama S (May 2008). "TRIM68 regulates ligand-dependent transcription of androgen receptor in prostate cancer cells". Cancer Res. 68 (9): 3486–94. doi:10.1158/0008-5472.CAN-07-6059. PMID 18451177.
- Poukka H, Aarnisalo P, Karvonen U, Palvimo JJ, Jänne OA (July 1999). "Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription". J. Biol. Chem. 274 (27): 19441–6. doi:10.1074/jbc.274.27.19441. PMID 10383460.
- Müller JM, Isele U, Metzger E, Rempel A, Moser M, Pscherer A, Breyer T, Holubarsch C, Buettner R, Schüle R (February 2000). "FHL2, a novel tissue-specific coactivator of the androgen receptor". EMBO J. 19 (3): 359–69. doi:10.1093/emboj/19.3.359. PMC 305573. PMID 10654935.
- Cheng S, Brzostek S, Lee SR, Hollenberg AN, Balk SP (July 2002). "Inhibition of the dihydrotestosterone-activated androgen receptor by nuclear receptor corepressor". Mol. Endocrinol. 16 (7): 1492–501. doi:10.1210/me.16.7.1492. PMID 12089345.
- Hodgson MC, Astapova I, Cheng S, Lee LJ, Verhoeven MC, Choi E, Balk SP, Hollenberg AN (February 2005). "The androgen receptor recruits nuclear receptor CoRepressor (N-CoR) in the presence of mifepristone via its N and C termini revealing a novel molecular mechanism for androgen receptor antagonists". J. Biol. Chem. 280 (8): 6511–9. doi:10.1074/jbc.M408972200. PMID 15598662.
- Markus SM, Taneja SS, Logan SK, Li W, Ha S, Hittelman AB, Rogatsky I, Garabedian MJ (February 2002). "Identification and Characterization of ART-27, a Novel Coactivator for the Androgen Receptor N Terminus". Mol. Biol. Cell 13 (2): 670–82. doi:10.1091/mbc.01-10-0513. PMC 65658. PMID 11854421.
- Sharma M, Li X, Wang Y, Zarnegar M, Huang CY, Palvimo JJ, Lim B, Sun Z (November 2003). "hZimp10 is an androgen receptor co-activator and forms a complex with SUMO-1 at replication foci". EMBO J. 22 (22): 6101–14. doi:10.1093/emboj/cdg585. PMC 275443. PMID 14609956.
- GeneReviews/NCBI/NIH/UW entry on Androgen Insensitivity Syndrome
- OMIM entries on Androgen Insensitivity Syndrome
- GeneReviews/NIH/NCBI/UW entry on Spinal and Bulbar Muscular Atrophy, Kennedy's Disease, SBMA, X-Linked Spinal and Bulbar Muscular Atrophy
- OMIM entries on Spinal and Bulbar Muscular Atrophy, Kennedy's Disease, SBMA, X-Linked Spinal and Bulbar Muscular Atrophy
- Androgen Receptors at the US National Library of Medicine Medical Subject Headings (MeSH)
- Brinkmann AO. "Androgen physiology: receptor and metabolic disorders". In Robert McLachlan, editor. Endocrinology of Male Reproduction. Endotext.org. Retrieved 2008-04-29.
- Gottlieb B (2007-07-24). "The Androgen Receptor Gene Mutations Database Server". McGill University. Archived from the original on 22 April 2008. Retrieved 2008-04-29.
- Thompson J (2006-09-30). "Molecular Mechanisms of Androgen Receptor Interactions". Helsinki University Biomedical Dissertations No. 80. University of Helsinki. Archived from the original on 6 April 2008. Retrieved 2008-04-29.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Androgen receptor Provide feedback
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This tab holds annotation information from the InterPro database.
InterPro entry IPR001103
Steroid or nuclear hormone receptors (NRs) constitute an important super-family of transcription regulators that are involved in diverse physiological functions, including control of embryonic development, cell differentiation and homeostasis. Members include the steroid hormone receptors and receptors for thyroid hormone, retinoids and 1,25-dihydroxy-vitamin D3. The proteins function as dimeric molecules in the nucleus to regulate the transcription of target genes in a ligand-responsive manner [PUBMED:7899080, PUBMED:8165128].
NRs are extremely important in medical research, a large number of them being implicated in diseases such as cancer, diabetes and hormone resistance syndromes. Many do not yet have a defined ligand and are accordingly termed "orphan" receptors. More than 300 NRs have been described to date and a new system has recently been introduced in an attempt to rationalise the increasingly complex set of names used to describe superfamily members.
The androgen receptor (AR) consists of 3 functional and structural domains: an N-terminal (modulatory) domain; a DNA binding domain (INTERPRO) that mediates specific binding to target DNA sequences (ligand-responsive elements); and a hormone binding domain. The N-terminal domain (NTD) is unique to the androgen receptors and spans approximately the first 530 residues; the highly-conserved DNA-binding domain is smaller (around 65 residues) and occupies the central portion of the protein; and the hormone ligand binding domain (LBD) lies at the receptor C terminus. In the absence of ligand, steroid hormone receptors are thought to be weakly associated with nuclear components; hormone binding greatly increases receptor affinity.
The LBDs of steroid hormone receptors fold into 12 helices that form a ligand-binding pocket. When an agonist is bound, helix 12 folds over the pocket to enclose the ligand [PUBMED:12089231]. When an antagonist is unbound, helix 12 is positioned away from the pocket in a way that interferes with the binding of coactivators to a groove in the hormone-binding domain formed after ligand binding. In AR, ligand binding that induces folding of helix 12 to overlie the pocket discloses a groove that binds a region of the NTD. Coactivator molecules can also bind to this groove, but the predominant site for coactivator binding to AR is in the NTD. AR ligand resides in a pocket and primarily contacts helices 4, 5, and 10. The DNA-binding region includes eight cysteine residues that form two coordination complexes, each composed of four cysteines and a Zn2+ ion. These two zinc fingers form the structure that binds to the major groove of DNA. The second zinc finger stabilises the binding complex by hydrophobic interactions with the first finger and contributes to specificity of receptor DNA binding. It is also necessary for receptor dimerisation that occurs during DNA binding
Defects in the androgen receptor cause testicular feminisation syndrome, androgen insensibility syndrome (AIS) [PUBMED:1307250, PUBMED:1569163]. AIS may be complete (CAIS), where external genitalia are phenotypically female; partial (PAIS), where genitalia are substantively ambiguous; or mild (MAIS), where external genitalia are normal male, or nearly so. Defects in the receptor also cause X-linked spinal and bulbar muscular atrophy (also known as Kennedy's disease).
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||nucleus (GO:0005634)|
|Molecular function||DNA binding (GO:0003677)|
|androgen receptor activity (GO:0004882)|
|steroid binding (GO:0005496)|
|Biological process||regulation of transcription, DNA-dependent (GO:0006355)|
|androgen receptor signaling pathway (GO:0030521)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
The graphic that is shown by default represents the longest sequence with a given architecture. Each row contains the following information:
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You can also change the order in which sequences are listed in the alignment, change how insertions are represented, alter the characters that are used to represent gaps in sequences and, finally, choose whether to download the alignment or to view it in your browser directly.
You may find that large alignments cause problems for the viewers and the reformatting tool, so we also provide all alignments in Stockholm format. You can download either the plain text alignment, or a gzipped version of it.
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
If you find these logos useful in your own work, please consider citing the following article:
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
|Author:||Mian N, Bateman A|
|Number in seed:||3|
|Number in full:||248|
|Average length of the domain:||263.10 aa|
|Average identity of full alignment:||50 %|
|Average coverage of the sequence by the domain:||56.51 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
This chart is a modified "sunburst" visualisation of the species tree for this family. It shows each node in the tree as a separate arc, arranged radially with the superkingdoms at the centre and the species arrayed around the outermost ring.
How the sunburst is generated
The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
In order to reduce the complexity of the representation, we reduce the number of taxonomic levels that we show. We consider only the following eight major taxonomic levels:
Colouring and labels
Segments of the tree are coloured approximately according to their superkingdom. For example, archeal branches are coloured with shades of orange, eukaryotes in shades of purple, etc. The colour assignments are shown under the sunburst controls. Where space allows, the name of the taxonomic level will be written on the arc itself.
As you move your mouse across the sunburst, the current node will be highlighted. In the top section of the controls panel we show a summary of the lineage of the currently highlighed node. If you pause over an arc, a tooltip will be shown, giving the name of the taxonomic level in the title and a summary of the number of sequences and species below that node in the tree.
Anomalies in the taxonomy tree
There are some situations that the sunburst tree cannot easily handle and for which we have work-arounds in place.
Missing taxonomic levels
Some species in the taxonomic tree may not have one or more of the main eight levels that we display. For example, Bos taurus is not assigned an order in the NCBI taxonomic tree. In such cases we mark the omitted level with, for example, "No order", in both the tooltip and the lineage summary.
Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
So that these nodes are not simply omitted from the sunburst tree, we group them together in a separate branch (or segment of the sunburst tree). Since we cannot determine the lineage for these unmapped species, we show all levels between the superkingdom and the species as "uncategorised".
Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
Too many species/sequences
For large species trees, you may see blank regions in the outer layers of the sunburst. These occur when there are large numbers of arcs to be drawn in a small space. If an arc is less than approximately one pixel wide, it will not be drawn and the space will be left blank. You may still be able to get some information about the species in that region by moving your mouse across the area, but since each arc will be very small, it will be difficult to accurately locate a particular species.
The tree shows the occurrence of this domain across different species. More...
We show the species tree in one of two ways. For smaller trees we try to show an interactive representation, which allows you to select specific nodes in the tree and view them as an alignment or as a set of Pfam domain graphics.
Unfortunately we have found that there are problems viewing the interactive tree when the it becomes larger than a certain limit. Furthermore, we have found that Internet Explorer can become unresponsive when viewing some trees, regardless of their size. We therefore show a text representation of the species tree when the size is above a certain limit or if you are using Internet Explorer to view the site.
If you are using IE you can still load the interactive tree by clicking the "Generate interactive tree" button, but please be aware of the potential problems that the interactive species tree can cause.
For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.
Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.
We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Androgen_recep domain has been found. There are 3 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
Loading structure mapping...