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Protein

Androgen receptor

Gene

AR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3.9 Publications
Isoform 3 and isoform 4 lack the C-terminal ligand-binding domain and may therefore constitutively activate the transcription of a specific set of genes independently of steroid hormones.1 Publication

Miscellaneous

In the absence of ligand, steroid hormone receptors are thought to be weakly associated with nuclear components; hormone binding greatly increases receptor affinity. The hormone-receptor complex appears to recognize discrete DNA sequences upstream of transcriptional start sites.
Transcriptional activity is enhanced by binding to RANBP9.
The level of tyrosine phosphorylation may serve as a diagnostic tool to predict patient outcome in response to hormone-ablation therapy. Inhibition of tyrosine phosphorylation may be an effective intervention target for hormone-refractory prostate cancer.

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

AIM-100 (4-amino-5,6-biaryl-furo[2,3-d]pyrimidine) suppresses TNK2-mediated phosphorylation at Tyr-269. Inhibits the binding of the Tyr-269 phosphorylated form to androgen-responsive enhancers (AREs) and its transcriptional activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei706AndrogenCombined sources4 Publications1
Binding sitei753AndrogenCombined sources4 Publications1
Binding sitei878AndrogenCombined sources4 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi560 – 632Nuclear receptorPROSITE-ProRule annotationAdd BLAST73
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri560 – 580NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri596 – 620NR C4-typePROSITE-ProRule annotationAdd BLAST25

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandLipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-4090294 SUMOylation of intracellular receptors
R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-HSA-5689880 Ub-specific processing proteases
R-HSA-8940973 RUNX2 regulates osteoblast differentiation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P10275

SIGNOR Signaling Network Open Resource

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SIGNORi
P10275

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P10275 Predicted

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000001553

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Androgen receptor
Alternative name(s):
Dihydrotestosterone receptor
Nuclear receptor subfamily 3 group C member 4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AR
Synonyms:DHTR, NR3C4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000169083.15

Human Gene Nomenclature Database

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HGNCi
HGNC:644 AR

Online Mendelian Inheritance in Man (OMIM)

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MIMi
313700 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P10275

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Androgen insensitivity syndrome (AIS)74 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn X-linked recessive form of pseudohermaphroditism due end-organ resistance to androgen. Affected males have female external genitalia, female breast development, blind vagina, absent uterus and female adnexa, and abdominal or inguinal testes, despite a normal 46,XY karyotype.
See also OMIM:300068
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_009224196Q → R in AIS. 1 Publication1
Natural variantiVAR_009225257L → P in AIS. 1 Publication1
Natural variantiVAR_009226392P → R in AIS. 1 PublicationCorresponds to variant dbSNP:rs773996740Ensembl.1
Natural variantiVAR_009227392P → S in AIS. Corresponds to variant dbSNP:rs201934623EnsemblClinVar.1
Natural variantiVAR_009228445Q → R in AIS; unknown pathological significance. 1 Publication1
Natural variantiVAR_009719492G → S in AIS. 1
Natural variantiVAR_009722549P → S in AIS. 1 PublicationCorresponds to variant dbSNP:rs137852588EnsemblClinVar.1
Natural variantiVAR_009723560C → Y in AIS. 1 Publication1
Natural variantiVAR_009727572Y → C in AIS. 1 Publication1
Natural variantiVAR_009728574A → D in AIS. 1
Natural variantiVAR_009731577C → F in AIS. 1 Publication1
Natural variantiVAR_009732577C → R in AIS. 1 Publication1
Natural variantiVAR_009733580C → F in AIS; reduced transcription and DNA binding. 1 PublicationCorresponds to variant dbSNP:rs137852586EnsemblClinVar.1
Natural variantiVAR_009734580C → Y in AIS. 1
Natural variantiVAR_009736582V → F in AIS. 2 Publications1
Natural variantiVAR_009739583Missing in AIS. 1 Publication1
Natural variantiVAR_009740586R → K in AIS. 1
Natural variantiVAR_009743597A → T in AIS; abolishes dimerization. 2 PublicationsCorresponds to variant dbSNP:rs137852569EnsemblClinVar.1
Natural variantiVAR_009746602C → F in AIS. 1 Publication1
Natural variantiVAR_009749612C → Y in AIS. 1
Natural variantiVAR_009752616R → P in AIS. 1
Natural variantiVAR_009750616Missing in AIS. 1 Publication1
Natural variantiVAR_009753617L → P in AIS. 1 Publication1
Natural variantiVAR_004688678L → P in AIS. 1 PublicationCorresponds to variant dbSNP:rs137852579EnsemblClinVar.1
Natural variantiVAR_009764682E → K in AIS. 2 Publications1
Natural variantiVAR_009766685V → I in AIS. 1
Natural variantiVAR_009769689G → E in AIS. 1
Natural variantiVAR_004689693Missing in AIS. 1
Natural variantiVAR_004690696D → H in AIS. 1 Publication1
Natural variantiVAR_004691696D → N in AIS; almost complete loss of androgen binding and transcription activation. 2 Publications1
Natural variantiVAR_004692696D → V in AIS. 1 Publication1
Natural variantiVAR_009771701L → M in AIS. 1
Natural variantiVAR_009772702L → F in AIS. 1
Natural variantiVAR_009774703S → A in AIS. 1
Natural variantiVAR_009775704S → C in AIS. 1
Natural variantiVAR_009776706N → S in AIS. 2 Publications1
Natural variantiVAR_013475706N → Y in AIS. 1 Publication1
Natural variantiVAR_004694708L → R in AIS. 1 PublicationCorresponds to variant dbSNP:rs137852585EnsemblClinVar.1
Natural variantiVAR_009778709G → V in AIS. 1
Natural variantiVAR_009779711R → T in AIS. 1
Natural variantiVAR_009785723L → F in AIS. 1
Natural variantiVAR_009786724P → S in AIS. 1
Natural variantiVAR_009790728N → K in AIS. 1 PublicationCorresponds to variant dbSNP:rs768869912Ensembl.1
Natural variantiVAR_004696733D → N in AIS. 1 Publication1
Natural variantiVAR_004697733D → Y in AIS. 1
Natural variantiVAR_009794742W → R in AIS. 1 Publication1
Natural variantiVAR_013477744G → E in AIS. 1 PublicationCorresponds to variant dbSNP:rs137852600EnsemblClinVar.1
Natural variantiVAR_004701751G → D in AIS; loss of androgen binding. 1 Publication1
Natural variantiVAR_009804752W → R in AIS. 1
Natural variantiVAR_004702753R → Q in AIS. 2 Publications1
Natural variantiVAR_004703755F → V in AIS. 2 Publications1
Natural variantiVAR_009810760S → F in AIS. 1 Publication1
Natural variantiVAR_004704763L → F in AIS; loss of androgen binding. 1 Publication1
Natural variantiVAR_009812764Y → H in AIS. 1 Publication1
Natural variantiVAR_009813765F → L in AIS. 1 Publication1
Natural variantiVAR_004707766A → T in AIS; loss of androgen binding. 4 Publications1
Natural variantiVAR_009814766A → V in AIS. 1
Natural variantiVAR_009815767P → S in AIS. 1
Natural variantiVAR_009816768D → E in AIS. 1 Publication1
Natural variantiVAR_009817769L → P in AIS. 1
Natural variantiVAR_004709775R → C in AIS; frequent mutation; loss of androgen binding. 5 PublicationsCorresponds to variant dbSNP:rs137852562EnsemblClinVar.1
Natural variantiVAR_004710780R → W in AIS. 3 Publications1
Natural variantiVAR_004712785C → Y in AIS; loss of androgen binding and of transactivation. 1 Publication1
Natural variantiVAR_004713788M → V in AIS. 1 PublicationCorresponds to variant dbSNP:rs137852570EnsemblClinVar.1
Natural variantiVAR_009822789R → S in AIS. Corresponds to variant dbSNP:rs1254203917Ensembl.1
Natural variantiVAR_009823791L → F in AIS. 1 Publication1
Natural variantiVAR_004714795F → S in AIS. 1 Publication1
Natural variantiVAR_004716808M → R in AIS; loss of transactivation. 1 Publication1
Natural variantiVAR_004717808M → V in AIS; 25% androgen binding. 1 Publication1
Natural variantiVAR_009828813L → F in AIS. 1 Publication1
Natural variantiVAR_009829821G → A in AIS. 1 Publication1
Natural variantiVAR_004719832R → L in AIS. 1 Publication1
Natural variantiVAR_004720832R → Q in AIS; loss of androgen binding. 3 Publications1
Natural variantiVAR_009832835Y → C in AIS; loss of androgen binding. 1 PublicationCorresponds to variant dbSNP:rs1057521122Ensembl.1
Natural variantiVAR_004721841R → C in AIS. 3 PublicationsCorresponds to variant dbSNP:rs137852577EnsemblClinVar.1
Natural variantiVAR_004723841R → H in AIS. 7 PublicationsCorresponds to variant dbSNP:rs9332969EnsemblClinVar.1
Natural variantiVAR_004724843I → T in AIS. 2 PublicationsCorresponds to variant dbSNP:rs9332970Ensembl.1
Natural variantiVAR_004725856R → C in AIS. 5 PublicationsCorresponds to variant dbSNP:rs886041132EnsemblClinVar.1
Natural variantiVAR_004726856R → H in AIS; strongly reduced transcription activation. 5 PublicationsCorresponds to variant dbSNP:rs9332971EnsemblClinVar.1
Natural variantiVAR_009836857F → L in AIS. Corresponds to variant dbSNP:rs137852598EnsemblClinVar.1
Natural variantiVAR_009837864L → R in AIS. 1
Natural variantiVAR_009838865D → G in AIS. 1 Publication1
Natural variantiVAR_004727865D → N in AIS; loss of androgen binding. 1 Publication1
Natural variantiVAR_009839866S → P in AIS. Corresponds to variant dbSNP:rs137852597EnsemblClinVar.1
Natural variantiVAR_004728867V → E in AIS. 1
Natural variantiVAR_009842872R → G in AIS. 1 Publication1
Natural variantiVAR_013479875H → R in AIS. 1 Publication1
Natural variantiVAR_013480880D → Y in AIS. 1 Publication1
Natural variantiVAR_009846882L → V in AIS. 1 Publication1
Natural variantiVAR_009847887M → V in AIS. Corresponds to variant dbSNP:rs755226547EnsemblClinVar.1
Natural variantiVAR_004733893P → L in AIS. 3 Publications1
Natural variantiVAR_004734896M → T in AIS; low androgen binding and transactivation. 2 Publications1
Natural variantiVAR_009852899I → T in AIS. 1
Natural variantiVAR_009855905P → H in AIS. 1
Natural variantiVAR_009856905P → S in AIS. 1
Natural variantiVAR_004735908L → F in AIS; almost complete loss of transcription activation. 2 Publications1
Natural variantiVAR_009861917F → L in AIS. 1 Publication1
Natural variantiVAR_009862918H → R in AIS. 1
Spinal and bulbar muscular atrophy X-linked 1 (SMAX1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. Caused by trinucleotide CAG repeat expansion. In SMAX1 patients the number of Gln ranges from 38 to 62. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.
Disease descriptionAn X-linked recessive form of spinal muscular atrophy. Spinal muscular atrophy refers to a group of neuromuscular disorders characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAX1 occurs only in men. Age at onset is usually in the third to fifth decade of life, but earlier involvement has been reported. It is characterized by slowly progressive limb and bulbar muscle weakness with fasciculations, muscle atrophy, and gynecomastia. The disorder is clinically similar to classic forms of autosomal spinal muscular atrophy.
See also OMIM:313200
Defects in AR may play a role in metastatic prostate cancer. The mutated receptor stimulates prostate growth and metastases development despite of androgen ablation. This treatment can reduce primary and metastatic lesions probably by inducing apoptosis of tumor cells when they express the wild-type receptor.10 Publications
Androgen insensitivity, partial (PAIS)42 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder that is characterized by hypospadias, hypogonadism, gynecomastia, genital ambiguity, normal XY karyotype, and a pedigree pattern consistent with X-linked recessive inheritance. Some patients present azoospermia or severe oligospermia without other clinical manifestations.
See also OMIM:312300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0046792E → K in PAIS. 1 PublicationCorresponds to variant dbSNP:rs104894742EnsemblClinVar.1
Natural variantiVAR_009721548L → F in PAIS. Corresponds to variant dbSNP:rs139524801Ensembl.1
Natural variantiVAR_009726569G → W in PAIS. 1 Publication1
Natural variantiVAR_009737583F → S in PAIS. 1 Publication1
Natural variantiVAR_009738583F → Y in PAIS. 1 PublicationCorresponds to variant dbSNP:rs137852587EnsemblClinVar.1
Natural variantiVAR_009744598S → G in PAIS; associated with P-618 in a PAIS patient; normal androgen binding; does not activate transcription; impairs DNA binding. 1 PublicationCorresponds to variant dbSNP:rs142280455Ensembl.1
Natural variantiVAR_009747605D → Y in PAIS. 1 Publication1
Natural variantiVAR_009748611N → T in PAIS. 1 Publication1
Natural variantiVAR_009754617L → R in PAIS. 1 Publication1
Natural variantiVAR_009762672P → H in PAIS. 1
Natural variantiVAR_013474683P → T in PAIS. 1 Publication1
Natural variantiVAR_009767687C → R in PAIS. 1
Natural variantiVAR_009768688A → V in PAIS. 1
Natural variantiVAR_009770691Missing in PAIS. 1 Publication1
Natural variantiVAR_009777709G → A in PAIS. 2 Publications1
Natural variantiVAR_013476712Q → E in PAIS. 1 Publication1
Natural variantiVAR_009780713L → F in PAIS. Corresponds to variant dbSNP:rs137852595EnsemblClinVar.1
Natural variantiVAR_009791729L → S in PAIS. 1
Natural variantiVAR_009792734Q → H in PAIS. 1
Natural variantiVAR_009793738I → T in PAIS. 1 Publication1
Natural variantiVAR_004698743M → I in PAIS. 1 Publication1
Natural variantiVAR_009795743M → V in PAIS. 1 Publication1
Natural variantiVAR_009797746M → T in PAIS. 1 Publication1
Natural variantiVAR_009798747V → M in PAIS. 1
Natural variantiVAR_009799749A → D in PAIS. 1
Natural variantiVAR_009807757N → S in PAIS. Corresponds to variant dbSNP:rs141425171Ensembl.1
Natural variantiVAR_009809759N → T in PAIS; 50% reduction in transactivation. 1 Publication1
Natural variantiVAR_009818772N → H in PAIS. 1 PublicationCorresponds to variant dbSNP:rs886041352EnsemblClinVar.1
Natural variantiVAR_009819773E → A in PAIS. 1 Publication1
Natural variantiVAR_009820773E → G in PAIS. 1 Publication1
Natural variantiVAR_004715799Q → E in PAIS, AIS and prostate cancer; reduced transcription activation. 6 PublicationsCorresponds to variant dbSNP:rs137852591EnsemblClinVar.1
Natural variantiVAR_009826807C → Y in PAIS. Corresponds to variant dbSNP:rs1064793480Ensembl.1
Natural variantiVAR_009827808M → T in PAIS. 1 PublicationCorresponds to variant dbSNP:rs137852592EnsemblClinVar.1
Natural variantiVAR_009830822L → V in PAIS. 1
Natural variantiVAR_013478828F → V in PAIS. 1 Publication1
Natural variantiVAR_004722841R → G in PAIS. 1 Publication1
Natural variantiVAR_009229841R → S in PAIS. 1 Publication1
Natural variantiVAR_009833842I → S in PAIS. 1
Natural variantiVAR_009835855R → K in PAIS. 1
Natural variantiVAR_004729867V → L in PAIS. 3 PublicationsCorresponds to variant dbSNP:rs137852564EnsemblClinVar.1
Natural variantiVAR_004731870I → M in PAIS. 2 PublicationsCorresponds to variant dbSNP:rs137852574EnsemblClinVar.1
Natural variantiVAR_009840871A → G in PAIS. 1 Publication1
Natural variantiVAR_009841871A → V in PAIS. 1 PublicationCorresponds to variant dbSNP:rs143040492EnsemblClinVar.1
Natural variantiVAR_009854904V → M in PAIS. 1
Natural variantiVAR_009858910G → R in PAIS. 1 Publication1
Natural variantiVAR_009860912V → L in PAIS. 1 Publication1
Natural variantiVAR_004736914P → S in PAIS. 1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi83S → A: Reduced cell growth. 1 Publication1
Mutagenesisi225Y → F: Decrease of CSK-induced phosphorylation. 1 Publication1
Mutagenesisi269Y → F: Decrease of CSK-induced phosphorylation and phosphorylation by TNK2. Complete loss of TNK2-dependent phosphorylation; when associated with F-365. 2 Publications1
Mutagenesisi309Y → F: Decrease of CSK-induced phosphorylation. 1 Publication1
Mutagenesisi348Y → F: Decrease of CSK-induced phosphorylation. 1 Publication1
Mutagenesisi359Y → F: Decrease of CSK-induced phosphorylation. 1 Publication1
Mutagenesisi364Y → F: Decrease of CSK-induced phosphorylation. 1 Publication1
Mutagenesisi365Y → F: Decrease of CSK-induced phosphorylation and phosphorylation by TNK2. Complete loss of TNK2-dependent phosphorylation; when associated with F-269. 2 Publications1
Mutagenesisi395Y → F: Decrease of CSK-induced phosphorylation. 1 Publication1
Mutagenesisi535Y → F: Greatest decrease of CSK-induced phosphorylation and inhibition of transcriptional activity induced by EGF. 1 Publication1
Mutagenesisi552Y → F: Decrease in CSK-induced phosphorylation. 1 Publication1
Mutagenesisi702L → A: Alters receptor specificity, so that transcription is activated by the antiandrogen cyproterone acetate. 1 Publication1
Mutagenesisi721K → A: Loss of transcription activation in the presence of androgen and of interaction with NCOA2. 2 Publications1
Mutagenesisi742W → L: Strongly decreased transcription activation in the presence of androgen. 1 Publication1
Mutagenesisi846K → R: Prevents ubiquitination by RNF6. Prevents AR transcriptional activation by RNF14 in absence of hormone. 1 Publication1
Mutagenesisi848K → R: Partially prevents ubiquitination by RNF6. 1 Publication1
Mutagenesisi898E → A or Q: Reduced transcription activation in the presence of androgen. 2 Publications1
Mutagenesisi898E → K or R: Loss of transcription activation in the presence of androgen. 2 Publications1
Mutagenesisi916Y → F: Decrease in CSK-induced phosphorylation. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration, Pseudohermaphroditism

Organism-specific databases

DisGeNET

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DisGeNETi
367

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
AR

MalaCards human disease database

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MalaCardsi
AR
MIMi300068 phenotype
312300 phenotype
313200 phenotype

Open Targets

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OpenTargetsi
ENSG00000169083

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
99429 Complete androgen insensitivity syndrome
440 Familial hypospadias
481 Kennedy disease
90797 Partial androgen insensitivity syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA57

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1871

Drug and drug target database

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DrugBanki
DB02932 (2r)-N-[4-Cyano-3-(Trifluoromethyl)Phenyl]-3-[(4-Fluorophenyl)Sulfonyl]-2-Hydroxy-2-Methylpropanamide
DB07422 (2S)-2-hydroxy-2-methyl-N-[4-nitro-3-(trifluoromethyl)phenyl]-3-(pentafluorophenoxy)propanamide
DB07419 (2S)-3-(4-chloro-3-fluorophenoxy)-N-[4-cyano-3-(trifluoromethyl)phenyl]-2-hydroxy-2-methylpropanamide
DB07423 (2S)-3-[4-(acetylamino)phenoxy]-2-hydroxy-2-methyl-N-[4-nitro-3-(trifluoromethyl)phenyl]propanamide
DB07039 (2S)-N-(4-cyano-3-iodophenyl)-3-(4-cyanophenoxy)-2-hydroxy-2-methylpropanamide
DB07454 (R)-3-BROMO-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE
DB01128 Bicalutamide
DB01541 Boldenone
DB01564 Calusterone
DB04839 Cyproterone acetate
DB01406 Danazol
DB01481 Delta1-dihydrotestosterone
DB02901 Dihydrotestosterone
DB01395 Drospirenone
DB00858 Drostanolone
DB08899 Enzalutamide
DB13155 Esculin
DB00687 Fludrocortisone
DB02266 Flufenamic Acid
DB01185 Fluoxymesterone
DB00499 Flutamide
DB01026 Ketoconazole
DB00367 Levonorgestrel
DB05234 LGD2941
DB05094 MDV3100
DB06710 Methyltestosterone
DB02998 Methyltrienolone
DB08804 Nandrolone decanoate
DB00984 Nandrolone phenpropionate
DB00665 Nilutamide
DB09389 Norgestrel
DB00621 Oxandrolone
DB06412 Oxymetholone
DB01708 Prasterone
DB07769 S-3-(4-FLUOROPHENOXY)-2-HYDROXY-2-METHYL-N-[4-NITRO-3-(TRIFLUOROMETHYL)PHENYL]PROPANAMIDE
DB00421 Spironolactone
DB00624 Testosterone
DB01420 Testosterone Propionate
DB08867 Ulipristal

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
628

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
AR

Domain mapping of disease mutations (DMDM)

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DMDMi
113830

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000537041 – 920Androgen receptorAdd BLAST920

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei83Phosphoserine; by CDK91 Publication1
Modified residuei96PhosphoserineCombined sources1
Modified residuei225Phosphotyrosine; by CSK1 Publication1
Modified residuei258PhosphoserineCombined sources1
Modified residuei269Phosphotyrosine; by CSK and TNK23 Publications1
Modified residuei309Phosphotyrosine; by CSK1 Publication1
Modified residuei348Phosphotyrosine; by CSK1 Publication1
Modified residuei359Phosphotyrosine; by CSK1 Publication1
Modified residuei364Phosphotyrosine; by CSK1 Publication1
Modified residuei365Phosphotyrosine; by CSK and TNK22 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei395Phosphotyrosine; by CSK1 Publication1
Cross-linki521Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei535Phosphotyrosine; by CSK1 Publication1
Modified residuei552Phosphotyrosine; by CSK1 Publication1
Modified residuei651Phosphoserine; by STK4/MST11 Publication1
Cross-linki846Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki848Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei916Phosphotyrosine; by CSK1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Sumoylated on Lys-388 (major) and Lys-521. Ubiquitinated. Deubiquitinated by USP26. 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity.3 Publications
Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-535 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression. Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity and may be responsible for androgen-independent progression of prostate cancer. Phosphorylation at Ser-83 by CDK9 regulates AR promoter selectivity and cell growth. Phosphorylation by PAK6 leads to AR-mediated transcription inhibition.6 Publications
Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation.1 Publication

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P10275

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P10275

PeptideAtlas

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PeptideAtlasi
P10275

PRoteomics IDEntifications database

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PRIDEi
P10275

ProteomicsDB human proteome resource

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ProteomicsDBi
52590
52591 [P10275-2]

Consortium for Top Down Proteomics

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TopDownProteomicsi
P10275-1 [P10275-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P10275

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P10275

SwissPalm database of S-palmitoylation events

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SwissPalmi
P10275

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform 2 is mainly expressed in heart and skeletal muscle (PubMed:15634333). Isoform 3 is expressed by basal and stromal cells of prostate (at protein level) (PubMed:19244107).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000169083 Expressed in 199 organ(s), highest expression level in uterine cervix

CleanEx database of gene expression profiles

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CleanExi
HS_AR

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P10275 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P10275 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000001
CAB065764
HPA065701

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds DNA as a homodimer. Part of a ternary complex containing AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the presence of androgen. The ligand binding domain interacts with KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, RBAK, SPDEF, SRA1, TGFB1I1 and RREB1. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its transactivation activity. Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. The AR N-terminal poly-Gln region binds Ran resulting in enhancement of AR-mediated transactivation. Ran-binding decreases as the poly-Gln length increases. Interacts with HIP1 (via coiled coil domain). Interacts (via ligand-binding domain) with TRIM68. Interacts with TNK2. Interacts with USP26. Interacts with RNF6. Interacts (regulated by RNF6 probably through polyubiquitination) with RNF14; regulates AR transcriptional activity. Interacts with PRMT2 and TRIM24. Interacts with RACK1. Interacts with RANBP10; this interaction enhances dihydrotestosterone-induced AR transcriptional activity. Interacts with PRPF6 in a hormone-independent way; this interaction enhances dihydrotestosterone-induced AR transcriptional activity. Interacts with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with LPXN. Interacts with MAK. Part of a complex containing AR, MAK and NCOA3. Interacts with CRY1. Interacts with CCAR1 and GATA2. Interacts with ZNF318 (By similarity). Interacts with BUD31 (PubMed:25091737). Interacts with ARID4A (PubMed:23487765). Interacts with ARID4B (By similarity). Interacts (via NR LBD domain) with ZBTB7A; the interaction is direct and androgen-dependent (PubMed:20812024). Interacts with NCOR1 (PubMed:20812024). Interacts with NCOR2 (PubMed:20812024).By similarity40 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei721Interaction with coactivator LXXL and FXXFY motifs1 Publication1
Sitei898Interaction with coactivator FXXLF and FXXFY motifs1 Publication1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-608057,EBI-375543
ASH2LQ9UBL32EBI-608057,EBI-540797
BLKP514513EBI-608057,EBI-2105445
BLNKQ8WV282EBI-608057,EBI-2623522
BRD4O60885-16EBI-608057,EBI-9345088
BTG2P785434EBI-608057,EBI-1047576
CASP8Q147903EBI-608057,EBI-78060
CCND1P243854EBI-608057,EBI-375001
CREBBPQ927932EBI-608057,EBI-81215
CTDSP2O145953EBI-608057,EBI-2802973
CTNNB1P3522211EBI-608057,EBI-491549
DAXXQ9UER75EBI-608057,EBI-77321
DDCP207112EBI-608057,EBI-1632155
ERGP113084EBI-608057,EBI-79704
FESP073323EBI-608057,EBI-1055635
FGRP097693EBI-608057,EBI-1383732
FKBP4Q027902EBI-608057,EBI-1047444
FOXA1P553173EBI-608057,EBI-3918034
FOXH1O755933EBI-608057,EBI-1759806
Foxo1Q9R1E04EBI-608057,EBI-1371343From Mus musculus.
GRB7Q144513EBI-608057,EBI-970191
GSNP063962EBI-608057,EBI-351506
HDAC4P565244EBI-608057,EBI-308629
HIF1AQ166652EBI-608057,EBI-447269
IFI16Q166663EBI-608057,EBI-2867186
INPPL1O153573EBI-608057,EBI-1384248
JMJD1CQ156522EBI-608057,EBI-1224969
JUNDP175352EBI-608057,EBI-2682803
KAT7O952515EBI-608057,EBI-473199
KDM5DQ9BY662EBI-608057,EBI-1246860
KDM5DQ9BY66-32EBI-608057,EBI-12559887
KLK3P072883EBI-608057,EBI-1220791
KMT2AQ031642EBI-608057,EBI-591370
KMT2DO146862EBI-608057,EB