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6  structures 58  species 1  interaction 131  sequences 11  architectures

Family: Androgen_recep (PF02166)

Summary: Androgen receptor

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Androgen receptor". More...

Androgen receptor Edit Wikipedia article

Available structures
PDB Ortholog search: PDBe RCSB
Aliases AR, AIS, AR8, DHTR, HUMARA, HYSP1, KD, NR3C4, SBMA, SMAX1, TFM, androgen receptor
External IDs OMIM: 313700 MGI: 88064 HomoloGene: 28 GeneCards: AR
RNA expression pattern
PBB GE AR 211110 s at.png

PBB GE AR 211621 at.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)


Location (UCSC) n/a Chr X: 98.15 – 98.32 Mb
PubMed search [2] [3]
View/Edit Human View/Edit Mouse
PDB 1xow EBI.jpg
crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor nh2-terminal peptide, ar20-30, and r1881
Symbol Androgen_recep
Pfam PF02166
InterPro IPR001103
Normal function of the androgen receptor. Testosterone (T) enters the cell and, if 5-alpha-reductase is present, is converted into dihydrotestone (DHT). Upon steroid binding, the androgen receptor (AR) undergoes a conformational change and releases heat-shock proteins (hsps). Phosphorylation (P) occurs before or after steroid binding. The AR translocates to the nucleus where dimerization, DNA binding, and the recruitment of coactivators occur. Target genes are transcribed (mRNA) and translated into proteins.[4][5][6][7]

The androgen receptor (AR), also known as NR3C4 (nuclear receptor subfamily 3, group C, member 4), is a type of nuclear receptor[8] that is activated by binding any of the androgenic hormones, including testosterone and dihydrotestosterone[9] 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.[10][11]

The main function of the androgen receptor is as a DNA-binding transcription factor that regulates gene expression;[12] however, the androgen receptor has other functions as well.[13] 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.[14] 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.[15] 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.[16]

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.[17]

Maintenance of male skeletal integrity

Via the Androgen receptor, androgens play a key role in the maintenance of male skeletal integrity. The regulation of this integrity by androgen receptor (AR) signaling can be attributed to both osteoblasts and osteocytes.[18]

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.[19] 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 the insulin-like growth factor I receptor (IGF-1R).[20] 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.[21]

Androgen receptor is modified by post translational modification through acetylation,[22] which directly promotes AR mediated transactivation, apoptosis[23] and contact independent growth of prostate cancer cells.[24] AR acetylation is induced by androgens [25] and determines recruitment into chromatin.[26] The AR acetylation site is a key target of NAD-dependent and TSA-dependent histone deacetylases [27] and long non coding RNA.[28]


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.[13][29] 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.



In humans, the androgen receptor is encoded by the AR gene located on the X chromosome at Xq11-12.[30][31]

AR deficiencies

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).[32] The androgen receptor seems to affect neuron physiology and is defective in Kennedy's disease.[33][34] In addition, point mutations and trinucleotide repeat polymorphisms has been linked to a number of additional disorders.[35]

CAG repeats

The AR gene contains CAG repeats which affect receptor function, where fewer repeats leads to increased receptor sensitivity to circulating androgens and more repeats leads to decreased receptor sensitivity. Studies have shown that racial variation in CAG repeats exists,[36][37] with African-Americans having fewer repeats than non-Hispanic white Americans.[36] The racial trends in CAG repeats parallels the incidence and mortality of prostate cancer in these groups.


Structural domains of the two isoforms (AR-A and AR-B) of the human androgen receptor. Numbers above the bars refer to the amino acid residues that separate the domains starting from the N-terminus (left) to C-terminus (right). NTD = N-terminal domain, DBD = DNA binding domain. LBD = ligand binding domain. AF = activation function.


Two isoforms of the androgen receptor (A and B) have been identified:[38]

  • AR-A - 87 kDa - N-terminus truncated (lacks the first 187 amino acids), which results from in vitro proteolysis.[39]
  • AR-B - 110 kDa - full length


Like other nuclear receptors, the androgen receptor is modular in structure and is composed of the following functional domains labeled A through F:[40]

  • A/B) - N-terminal regulatory domain contains:[41]
    • 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[42][43][44] head-to-tail interaction[45][46][47]
  • 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[48]
  • E) - Ligand binding domain (LBD) containing
    • activation function 2 (AF-2), responsible for agonist induced activity (activity in the presence of bound agonist)
    • AF-2 binds either the N-terminal FXXFL motif intramolecularly or coactivator proteins (containing the LXXLL or preferably FXXFL motifs)[47]
    • A ligand dependent nuclear export signal[49]
  • F) - C-terminal domain

Splice variants

AR-V7 is an androgen receptor splice variant that can be detected in circulating tumor cells of metastatic prostate cancer patients.[50][51] and is predictive of resistance to some drugs.[52]





As a drug target

The AR is important for therapeutic target in prostate cancer, thus many different inhibitors have been developed, primarily targeting the ligand binding domain of the protein, while inhibitors that target the N-terminal domain of the protein are still under development.[53] AR ligands can either be classified based on their structure (steroidal or nonsteroidal) or based on their ability to activate or inhibit transcription (agonists or antagonists).[54] Sulforaphane, a phytochemical derived from broccoli or the HSP90 inhibitor ganetespib or the NRF2 activator bardoxolone methyl has been shown to degrade both AR and AR-V7 and thus enhance the efficacy of antagonists like enzalutamide.[55][56]


Androgen receptor has been shown to interact with:

See also


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  146. ^ Mu X, Chang C (October 2003). "TR2 orphan receptor functions as negative modulator for androgen receptor in prostate cancer cells PC-3". The Prostate. 57 (2): 129–33. doi:10.1002/pros.10282. PMID 12949936. 
  147. ^ 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". Proceedings of the National Academy of Sciences of the United States of America. 96 (26): 14724–9. doi:10.1073/pnas.96.26.14724. PMC 24715Freely accessible. PMID 10611280. 
  148. ^ 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". The Journal of Biological Chemistry. 277 (18): 15426–31. doi:10.1074/jbc.M111218200. PMID 11856738. 
  149. ^ Hsiao PW, Chang C (August 1999). "Isolation and characterization of ARA160 as the first androgen receptor N-terminal-associated coactivator in human prostate cells". The Journal of Biological Chemistry. 274 (32): 22373–9. doi:10.1074/jbc.274.32.22373. PMID 10428808. 
  150. ^ 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 Research. 68 (9): 3486–94. doi:10.1158/0008-5472.CAN-07-6059. PMID 18451177. 
  151. ^ Poukka H, Aarnisalo P, Karvonen U, Palvimo JJ, Jänne OA (July 1999). "Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription". The Journal of Biological Chemistry. 274 (27): 19441–6. doi:10.1074/jbc.274.27.19441. PMID 10383460. 
  152. ^ 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". The EMBO Journal. 19 (3): 359–69. doi:10.1093/emboj/19.3.359. PMC 305573Freely accessible. PMID 10654935. 
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  154. ^ 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". The Journal of Biological Chemistry. 280 (8): 6511–9. doi:10.1074/jbc.M408972200. PMID 15598662. 
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This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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

No Pfam abstract.

External database links

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).

Gene Ontology

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Domain organisation

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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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...


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.

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Curation and family details

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Curation View help on the curation process

Seed source: IPR001103
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Mian N , Bateman A
Number in seed: 2
Number in full: 131
Average length of the domain: 328.90 aa
Average identity of full alignment: 60 %
Average coverage of the sequence by the domain: 51.91 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.5 23.5
Trusted cut-off 23.7 23.6
Noise cut-off 23.4 23.4
Model length: 484
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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Viroids Viroids Unclassified sequence Unclassified sequence


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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 6 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 sequence.

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