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P10275 (ANDR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 215. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Androgen receptor
Alternative name(s):
Dihydrotestosterone receptor
Nuclear receptor subfamily 3 group C member 4
Gene names
Name:AR
Synonyms:DHTR, NR3C4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length919 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Transcription activation is down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. Ref.34 Ref.48 Ref.50 Ref.51 Ref.60 Ref.65 Ref.67

Enzyme regulation

AIM-100 (4-amino-5,6-biaryl-furo[2,3-d]pyrimidine) suppresses TNK2-mediated phosphorylation at Tyr-267. Inhibits the binding of the Tyr-267 phosphorylated form to androgen-responsive enhancers (AREs) and its transcriptional activity. Ref.53

Subunit structure

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, ZNF318 and RREB1. Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its transactivation activity. Interacts with SLC30A9 and RAD54L2/ARIP4 By similarity. 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 GNB2L1/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. Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.37 Ref.38 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.54 Ref.59 Ref.60 Ref.65 Ref.67

Subcellular location

Nucleus. Cytoplasm. Note: Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of GNB2L1. Ref.7 Ref.33 Ref.42 Ref.50

Tissue specificity

Isoform 2 is mainly expressed in heart and skeletal muscle. Ref.7

Domain

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. In the presence of bound steroid the ligand-binding domain interacts with the N-terminal modulating domain, and thereby activates AR transcription factor activity. Agonist binding is required for dimerization and binding to target DNA. The transcription factor activity of the complex formed by ligand-activated AR and DNA is modulated by interactions with coactivator and corepressor proteins. Interaction with RANBP9 is mediated by both the N-terminal domain and the DNA-binding domain. Interaction with EFCAB6/DJBP is mediated by the DNA-binding domain. Ref.59 Ref.65

Post-translational modification

Sumoylated on Lys-386 (major) and Lys-520. Ubiquitinated. Deubiquitinated by USP26. 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity. Ref.50 Ref.52

Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-534 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-81 by CDK9 regulates AR promoter selectivity and cell growth. Phosphorylation by PAK6 leads to AR-mediated transcription inhibition. Ref.36 Ref.39 Ref.45 Ref.51 Ref.53 Ref.54

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. Ref.56

Polymorphism

The poly-Gln region of AR is highly polymorphic and the number of Gln varies in the population (from 17 to 26). A smaller size of the poly-Gln region may be associated with the development of prostate cancer.

The poly-Gly region of AR is polymorphic and ranges from 24 to 31 Gly. A poly-Gly region shorter or equal to 23 may be associated with the development of androgenetic alopecia.

Involvement in disease

Androgen insensitivity syndrome (AIS) [MIM:300068]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.16 Ref.18 Ref.61 Ref.76 Ref.78 Ref.81 Ref.83 Ref.84 Ref.85 Ref.86 Ref.87 Ref.88 Ref.90 Ref.91 Ref.95 Ref.96 Ref.98 Ref.100 Ref.102 Ref.104 Ref.106 Ref.115 Ref.116 Ref.117 Ref.119 Ref.120 Ref.121 Ref.122 Ref.123 Ref.124 Ref.126 Ref.127 Ref.129 Ref.130 Ref.131 Ref.137 Ref.139 Ref.140 Ref.143 Ref.144 Ref.146 Ref.147 Ref.148 Ref.149 Ref.152 Ref.155 Ref.156 Ref.157 Ref.160 Ref.162 Ref.163 Ref.164 Ref.165 Ref.166 Ref.167 Ref.168 Ref.169 Ref.170 Ref.172 Ref.175 Ref.176 Ref.181 Ref.182 Ref.183 Ref.184 Ref.188 Ref.191 Ref.192 Ref.195 Ref.196 Ref.198 Ref.201

Spinal and bulbar muscular atrophy X-linked 1 (SMAX1) [MIM:313200]: An 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.
Note: 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. Ref.200

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.

Androgen insensitivity, partial (PAIS) [MIM:312300]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.79 Ref.82 Ref.85 Ref.88 Ref.90 Ref.92 Ref.97 Ref.99 Ref.100 Ref.101 Ref.104 Ref.110 Ref.111 Ref.112 Ref.113 Ref.114 Ref.116 Ref.118 Ref.121 Ref.123 Ref.127 Ref.131 Ref.135 Ref.137 Ref.139 Ref.141 Ref.142 Ref.145 Ref.149 Ref.154 Ref.161 Ref.164 Ref.169 Ref.173 Ref.174 Ref.177 Ref.178 Ref.180 Ref.182 Ref.184 Ref.187 Ref.195 Ref.196

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.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
Triplet repeat expansion
   DiseaseDisease mutation
Neurodegeneration
Pseudohermaphroditism
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Steroid-binding
Zinc
   Molecular functionActivator
Receptor
   PTMIsopeptide bond
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of prostate induction by androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

androgen receptor signaling pathway

Inferred from direct assay PubMed 19886863PubMed 20048160. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cell growth

Non-traceable author statement PubMed 15572661. Source: UniProtKB

cell proliferation

Non-traceable author statement Ref.23. Source: UniProtKB

cell-cell signaling

Traceable author statement PubMed 10835690. Source: ProtInc

epithelial cell differentiation involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

intracellular receptor signaling pathway

Inferred from direct assay PubMed 17277772. Source: BHF-UCL

lateral sprouting involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

male genitalia morphogenesis

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

male somatic sex determination

Inferred from electronic annotation. Source: Ensembl

mammary gland alveolus development

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelial fold

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 21310825. Source: BHF-UCL

negative regulation of integrin biosynthetic process

Inferred from direct assay PubMed 21310825. Source: BHF-UCL

organ formation

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 21310825. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from direct assay PubMed 17277772. Source: BHF-UCL

positive regulation of insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of integrin biosynthetic process

Inferred from direct assay PubMed 21310825. Source: BHF-UCL

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphorylation

Inferred from mutant phenotype PubMed 21310825. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20048160. Source: UniProtKB

positive regulation of transcription from RNA polymerase III promoter

Inferred from direct assay PubMed 18487222. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11477070. Source: UniProtKB

prostate gland development

Non-traceable author statement Ref.23. Source: UniProtKB

prostate gland epithelium morphogenesis

Inferred from electronic annotation. Source: Ensembl

prostate gland growth

Inferred from electronic annotation. Source: Ensembl

protein oligomerization

Inferred from direct assay PubMed 18468998. Source: MGI

regulation of catalytic activity

Inferred from electronic annotation. Source: Ensembl

regulation of developmental growth

Inferred from electronic annotation. Source: Ensembl

regulation of establishment of protein localization to plasma membrane

Inferred from direct assay PubMed 21310825. Source: BHF-UCL

regulation of prostatic bud formation

Inferred from electronic annotation. Source: Ensembl

regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

sex differentiation

Non-traceable author statement Ref.23. Source: UniProtKB

signal transduction

Traceable author statement PubMed 10835690. Source: ProtInc

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

tertiary branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from direct assay PubMed 15572661. Source: UniProtKB

transport

Traceable author statement PubMed 10835690. Source: ProtInc

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 15572661. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from direct assay PubMed 17277772PubMed 17505061. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 15572661Ref.50. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay PubMed 18468998. Source: MGI

   Molecular_functionDNA binding

Non-traceable author statement Ref.23. Source: UniProtKB

RNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 16120611. Source: BHF-UCL

androgen binding

Non-traceable author statement Ref.23. Source: UniProtKB

androgen receptor activity

Inferred from direct assay PubMed 19886863PubMed 20048160. Source: UniProtKB

beta-catenin binding

Inferred from direct assay PubMed 12799378. Source: BHF-UCL

chromatin binding

Inferred from direct assay PubMed 21730289. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.42. Source: UniProtKB

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 17277772. Source: BHF-UCL

protein dimerization activity

Non-traceable author statement Ref.23. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 11875111. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11477070PubMed 15572661. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 12799378. Source: BHF-UCL

transcription regulatory region DNA binding

Inferred from direct assay PubMed 19886863. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P10275-1)

Also known as: AR-B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P10275-2)

Also known as: AR-A; Variant AR45;

The sequence of this isoform differs from the canonical sequence as follows:
     1-531: Missing.
     532-538: GPYGDMR → MILWLHS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 919919Androgen receptor
PRO_0000053704

Regions

DNA binding559 – 63173Nuclear receptor
Zinc finger559 – 57921NR C4-type
Zinc finger595 – 61925NR C4-type
Region1 – 558558Modulating
Region551 – 919369Interaction with LPXN
Region571 – 66191Interaction with HIPK3 By similarity
Region624 – 919296Interaction with KAT7
Region690 – 919230Ligand-binding
Compositional bias54 – 574Poly-Leu
Compositional bias58 – 8932Gln-rich
Compositional bias58 – 7821Poly-Gln
Compositional bias84 – 896Poly-Gln
Compositional bias193 – 1975Poly-Gln
Compositional bias372 – 38110Poly-Pro
Compositional bias396 – 4027Poly-Ala
Compositional bias449 – 47224Poly-Gly

Sites

Binding site7051Androgen
Binding site7521Androgen
Binding site8771Androgen
Site7201Interaction with coactivator LXXL motif
Site8971Interaction with coactivator FXXLF motif

Amino acid modifications

Modified residue811Phosphoserine; by CDK9 Ref.51
Modified residue941Phosphoserine Ref.55
Modified residue2231Phosphotyrosine; by CSK Ref.39
Modified residue2671Phosphotyrosine; by CSK and TNK2 Ref.39 Ref.45 Ref.53
Modified residue3071Phosphotyrosine; by CSK Ref.39
Modified residue3461Phosphotyrosine; by CSK Ref.39
Modified residue3571Phosphotyrosine; by CSK Ref.39
Modified residue3621Phosphotyrosine; by CSK Ref.39
Modified residue3631Phosphotyrosine; by CSK and TNK2 Ref.39 Ref.45
Modified residue3931Phosphotyrosine; by CSK Ref.39
Modified residue5341Phosphotyrosine; by CSK Ref.39
Modified residue5511Phosphotyrosine; by CSK Ref.39
Modified residue6501Phosphoserine; by STK4/MST1 Ref.54
Modified residue9151Phosphotyrosine; by CSK Ref.39
Cross-link386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28
Cross-link520Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28
Cross-link845Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.50
Cross-link847Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.50

Natural variations

Alternative sequence1 – 531531Missing in isoform 2.
VSP_036889
Alternative sequence532 – 5387GPYGDMR → MILWLHS in isoform 2.
VSP_036890
Natural variant21E → K in PAIS. Ref.145
VAR_004679
Natural variant541L → S in prostate cancer.
VAR_004680
Natural variant571L → Q in prostate cancer.
VAR_004681
Natural variant641Q → R in prostate cancer.
VAR_009711
Natural variant74 – 785Missing.
VAR_004682
Natural variant1121Q → H in prostate cancer.
VAR_009712
Natural variant1801K → R in prostate cancer.
VAR_009713
Natural variant1941Q → R in AIS. Ref.160
VAR_009224
Natural variant2051S → R. Ref.94
VAR_009714
Natural variant2141G → R in AIS; 20% lower transactivation capacity. Ref.167
VAR_009715
Natural variant2551L → P in AIS. Ref.168
VAR_009225
Natural variant2661M → T in prostate cancer.
VAR_009716
Natural variant2691P → S in prostate cancer.
VAR_009717
Natural variant3401P → L in prostate cancer. Ref.107
VAR_009718
Natural variant3901P → R in AIS. Ref.181
VAR_009226
Natural variant3901P → S in AIS.
VAR_009227
Natural variant4431Q → R in AIS; might be a polymorphism. Ref.181
VAR_009228
Natural variant465 – 4728Missing.
VAR_004683
Natural variant4911G → S in AIS.
VAR_009719
Natural variant5281D → G in prostate cancer.
VAR_009720
Natural variant5471L → F in PAIS.
VAR_009721
Natural variant5481P → S in AIS. Ref.147
VAR_009722
Natural variant5591C → Y in AIS. Ref.90
VAR_009723
Natural variant5681G → V in a patient with isolated hypospadias. Ref.133
VAR_009725
Natural variant5681G → W in PAIS. Ref.110
VAR_009726
Natural variant5711Y → C in AIS. Ref.165
VAR_009727
Natural variant5731A → D in AIS; defective DNA binding and transactivation. Ref.146
VAR_009728
Natural variant5741L → P in prostate cancer.
VAR_009729
Natural variant5751T → A in prostate cancer. Ref.194
VAR_009730
Natural variant5761C → F in AIS; lack of DNA binding.
VAR_009731
Natural variant5761C → R in AIS. Ref.90
VAR_009732
Natural variant5791C → F in AIS; reduced transcription and DNA binding. Ref.149
VAR_009733
Natural variant5791C → Y in AIS.
VAR_009734
Natural variant5801K → R in prostate cancer. Ref.194
VAR_009735
Natural variant5811V → F in AIS. Ref.95 Ref.106
VAR_009736
Natural variant5821F → S in PAIS. Ref.116
VAR_009737
Natural variant5821F → Y in PAIS. Ref.149
VAR_009738
Natural variant5821Missing in AIS. Ref.115
VAR_009739
Natural variant5851R → K in AIS.
VAR_009740
Natural variant5861A → V in prostate cancer; somatic mutation. Ref.194
VAR_009741
Natural variant5871A → S in prostate cancer; somatic mutation.
VAR_009742
Natural variant5961A → T in AIS; abolishes dimerization. Ref.135 Ref.191
VAR_009743
Natural variant5971S → G in PAIS; high dissociation rate; associated with P-617 in a PAIS patient; partially restores DNA-binding activity of P-617 mutant receptors. Ref.90
VAR_009744
Natural variant5971S → T in a patient with severe hypospadias. Ref.193
VAR_009745
Natural variant6011C → F in AIS. Ref.117
VAR_009746
Natural variant6041D → Y in PAIS. Ref.116
VAR_009747
Natural variant6071R → Q in PAIS and breast cancer. Ref.92 Ref.139 Ref.173 Ref.182
VAR_004684
Natural variant6081R → K in PAIS and breast cancer; defective nuclear localization. Ref.82 Ref.97 Ref.154
VAR_004685
Natural variant6101N → T in PAIS. Ref.139
VAR_009748
Natural variant6111C → Y in AIS.
VAR_009749
Natural variant6151R → H in AIS and PAIS. Ref.16 Ref.115 Ref.123 Ref.166
VAR_009751
Natural variant6151R → P in AIS.
VAR_009752
Natural variant6151Missing in AIS. Ref.115
VAR_009750
Natural variant6161L → P in AIS. Ref.148
VAR_009753
Natural variant6161L → R in PAIS. Ref.118
VAR_009754
Natural variant6171R → P in AIS and PAIS; loss of DNA-binding activity; associated with G-597 in a PAIS patient. Ref.78 Ref.90
VAR_009755
Natural variant6191C → Y in prostate cancer; loss of DNA binding; somatic mutation. Ref.189 Ref.194
VAR_009756
Natural variant6291R → Q in prostate cancer. Ref.159
VAR_009757
Natural variant6301K → T in prostate cancer.
VAR_009758
Natural variant6451A → D. Ref.171
Corresponds to variant rs1800053 [ dbSNP | Ensembl ].
VAR_004686
Natural variant6471S → N in prostate cancer.
VAR_009760
Natural variant6641I → N in AIS and PAIS.
VAR_004687
Natural variant6701Q → R in prostate cancer.
VAR_009761
Natural variant6711P → H in PAIS.
VAR_009762
Natural variant6721I → T in prostate cancer.
VAR_009763
Natural variant6771L → P in AIS. Ref.130
VAR_004688
Natural variant6811E → K in AIS. Ref.100 Ref.182
VAR_009764
Natural variant6821P → T in PAIS. Ref.196
VAR_013474
Natural variant6831G → A in prostate cancer. Ref.153 Ref.185
VAR_009765
Natural variant6841V → I in AIS.
VAR_009766
Natural variant6861C → R in PAIS.
VAR_009767
Natural variant6871A → V in PAIS.
VAR_009768
Natural variant6881G → E in AIS.
VAR_009769
Natural variant6901Missing in PAIS. Ref.114
VAR_009770
Natural variant6921Missing in AIS.
VAR_004689
Natural variant6951D → H in AIS. Ref.18
VAR_004690
Natural variant6951D → N in AIS; almost complete loss of androgen binding and transcription activation. Ref.18 Ref.201
VAR_004691
Natural variant6951D → V in AIS. Ref.170
VAR_004692
Natural variant7001L → M in AIS.
VAR_009771
Natural variant7011L → F in AIS.
VAR_009772
Natural variant7011L → H in AIS and prostate cancer. Ref.103 Ref.158 Ref.186
VAR_009773
Natural variant7021S → A in AIS.
VAR_009774
Natural variant7031S → C in AIS.
VAR_009775
Natural variant7031S → G in PAIS and AIS. Ref.164
VAR_004693
Natural variant7051N → S in AIS. Ref.91 Ref.127
VAR_009776
Natural variant7051N → Y in AIS. Ref.198
VAR_013475
Natural variant7071L → R in AIS. Ref.143
VAR_004694
Natural variant7081G → A in PAIS. Ref.116 Ref.161
VAR_009777
Natural variant7081G → V in AIS.
VAR_009778
Natural variant7101R → T in AIS.
VAR_009779
Natural variant7111Q → E in PAIS. Ref.196
VAR_013476
Natural variant7121L → F in PAIS.
VAR_009780
Natural variant7151V → M in prostate cancer; gain in function. Ref.105
VAR_009781
Natural variant7171K → E in prostate cancer.
VAR_009782
Natural variant7201K → E in prostate cancer; found in bone metastases.
VAR_009783
Natural variant7211A → T in prostate cancer; somatic mutation.
VAR_009784
Natural variant7221L → F in AIS.
VAR_009785
Natural variant7231P → S in AIS.
VAR_009786
Natural variant7241G → D in AIS and prostate cancer.
VAR_009787
Natural variant7251F → L in a patient with severe hypospadias. Ref.127 Ref.193
VAR_009788
Natural variant7261R → L in prostate cancer. Ref.134
VAR_009789
Natural variant7271N → K in AIS. Ref.122
VAR_009790
Natural variant7281L → S in PAIS.
VAR_009791
Natural variant7301V → M in prostate cancer; increases transcription activation. Ref.93 Ref.132
VAR_004695
Natural variant7321D → N in AIS. Ref.162
VAR_004696
Natural variant7321D → Y in AIS.
VAR_004697
Natural variant7331Q → H in PAIS.
VAR_009792
Natural variant7371I → T in PAIS. Ref.127
VAR_009793
Natural variant7411W → R in AIS. Ref.87
VAR_009794
Natural variant7421M → I in PAIS. Ref.141
VAR_004698
Natural variant7421M → V in PAIS. Ref.123
VAR_009795
Natural variant7431G → E in AIS. Ref.196
VAR_013477
Natural variant7431G → V in PAIS and AIS. Ref.99 Ref.102 Ref.106 Ref.174
VAR_004699
Natural variant7441L → F in AIS and prostate cancer.
VAR_009796
Natural variant7451M → T in PAIS. Ref.123
VAR_009797
Natural variant7461V → M in PAIS.
VAR_009798
Natural variant7481A → D in PAIS.
VAR_009799
Natural variant7481A → T in prostate cancer.
VAR_009800
Natural variant7481A → V in prostate cancer.
VAR_009801
Natural variant7491M → I in prostate cancer.
VAR_009802
Natural variant7491M → V in PAIS and AIS. Ref.84 Ref.91 Ref.157
VAR_004700
Natural variant7501G → D in AIS; loss of androgen binding. Ref.163
VAR_004701
Natural variant7501G → S in prostate cancer.
VAR_009803
Natural variant7511W → R in AIS.
VAR_009804
Natural variant7521R → Q in AIS. Ref.165 Ref.166
VAR_004702
Natural variant7541F → L in PAIS and prostate cancer. Ref.116 Ref.139
VAR_009805
Natural variant7541F → V in AIS. Ref.96 Ref.106
VAR_004703
Natural variant7551T → A in prostate cancer.
VAR_009806
Natural variant7561N → S in PAIS.
VAR_009807
Natural variant7571V → A in prostate cancer. Ref.194
VAR_009808
Natural variant7581N → T in PAIS; 50% reduction in transactivation. Ref.177
VAR_009809
Natural variant7591S → F in AIS. Ref.91
VAR_009810
Natural variant7591S → P in prostate cancer.
VAR_009811
Natural variant7621L → F in AIS; loss of androgen binding. Ref.163
VAR_004704
Natural variant7631Y → C in PAIS and prostate cancer; partial loss of androgen binding. Ref.79 Ref.131 Ref.201
VAR_004705
Natural variant7631Y → H in AIS. Ref.127
VAR_009812
Natural variant7641F → L in AIS. Ref.123
VAR_009813
Natural variant7651A → T in AIS; loss of androgen binding. Ref.83 Ref.162 Ref.163 Ref.169
VAR_004707
Natural variant7651A → V in AIS.
VAR_009814
Natural variant7661P → S in AIS.
VAR_009815
Natural variant7671D → E in AIS. Ref.106
VAR_009816
Natural variant7681L → P in AIS.
VAR_009817
Natural variant7711N → H in PAIS. Ref.116
VAR_009818
Natural variant7721E → A in PAIS. Ref.184
VAR_009819
Natural variant7721E → G in PAIS. Ref.154
VAR_009820
Natural variant7741R → C in AIS; loss of androgen binding; frequent mutation. Ref.76 Ref.77 Ref.81 Ref.157 Ref.165
VAR_004709
Natural variant7741R → H in AIS and PAIS; almost complete loss of androgen binding. Ref.81 Ref.91 Ref.127 Ref.201
VAR_004708
Natural variant7791R → W in AIS. Ref.116 Ref.131 Ref.156
VAR_004710
Natural variant7801M → I in PAIS and AIS. Ref.141 Ref.144 Ref.157
VAR_004711
Natural variant7821S → N in prostate cancer; somatic mutation.
VAR_009821
Natural variant7841C → Y in AIS; loss of androgen binding and of transactivation. Ref.169
VAR_004712
Natural variant7871M → V in AIS. Ref.86
VAR_004713
Natural variant7881R → S in AIS.
VAR_009822
Natural variant7901L → F in AIS. Ref.119
VAR_009823
Natural variant7911S → P in prostate cancer.
VAR_009824
Natural variant7931E → D. Ref.94
VAR_009825
Natural variant7941F → S in AIS. Ref.157
VAR_004714
Natural variant7981Q → E in PAIS, AIS and prostate cancer; reduced transcription activation. Ref.107 Ref.127 Ref.141 Ref.150 Ref.175 Ref.201
VAR_004715
Natural variant8061C → Y in PAIS.
VAR_009826
Natural variant8071M → R in AIS; loss of transactivation. Ref.98
VAR_004716
Natural variant8071M → T in PAIS. Ref.187
VAR_009827
Natural variant8071M → V in AIS; 25% androgen binding. Ref.131
VAR_004717
Natural variant8121L → F in AIS. Ref.192
VAR_009828
Natural variant8141S → N in AIS and PAIS.
VAR_004718
Natural variant8201G → A in AIS. Ref.168
VAR_009829
Natural variant8211L → V in PAIS.
VAR_009830
Natural variant8271F → V in PAIS. Ref.196
VAR_013478
Natural variant8301L → P in prostate cancer.
VAR_009831
Natural variant8311R → L in AIS. Ref.129
VAR_004719
Natural variant8311R → Q in AIS; loss of androgen binding. Ref.76 Ref.129 Ref.192
VAR_004720
Natural variant8341Y → C in AIS; loss of androgen binding. Ref.87
VAR_009832
Natural variant8401R → C in AIS. Ref.120 Ref.141 Ref.174
VAR_004721
Natural variant8401R → G in PAIS. Ref.169
VAR_004722
Natural variant8401R → H in AIS. Ref.100 Ref.111 Ref.112 Ref.118 Ref.120 Ref.124 Ref.139
VAR_004723
Natural variant8401R → S in PAIS. Ref.180
VAR_009229
Natural variant8411I → S in PAIS.
VAR_009833
Natural variant8421I → T in AIS. Ref.100 Ref.139
VAR_004724
Natural variant8461R → G in prostate cancer. Ref.194
VAR_009834
Natural variant8541R → K in PAIS.
VAR_009835
Natural variant8551R → C in AIS. Ref.91 Ref.106 Ref.131 Ref.140 Ref.160
VAR_004725
Natural variant8551R → H in AIS; strongly reduced transcription activation. Ref.101 Ref.139 Ref.141 Ref.152 Ref.201
VAR_004726
Natural variant8561F → L in AIS.
VAR_009836
Natural variant8631L → R in AIS.
VAR_009837
Natural variant8641D → G in AIS. Ref.91
VAR_009838
Natural variant8641D → N in AIS; loss of androgen binding. Ref.163
VAR_004727
Natural variant8651S → P in AIS.
VAR_009839
Natural variant8661V → E in AIS.
VAR_004728
Natural variant8661V → L in PAIS. Ref.82 Ref.100 Ref.104
VAR_004729
Natural variant8661V → M in AIS and prostate cancer. Ref.4 Ref.76 Ref.104 Ref.139
VAR_004730
Natural variant8691I → M in PAIS. Ref.101 Ref.141
VAR_004731
Natural variant8701A → G in PAIS. Ref.161
VAR_009840
Natural variant8701A → V in PAIS. Ref.113
VAR_009841
Natural variant8711R → G in AIS. Ref.184
VAR_009842
Natural variant8741H → R in AIS. Ref.196
VAR_013479
Natural variant8741H → Y in prostate cancer; increases affinity for testosterone, androgen sensitivity and transcription activation. Ref.65
VAR_009843
Natural variant8771T → A in prostate cancer; alters receptor specificity so that transcription is activated by antiandrogens, such as cyproterone acetate; found in bone metastases. Ref.61 Ref.64 Ref.75 Ref.89 Ref.103 Ref.109 Ref.151 Ref.179 Ref.186
VAR_004732
Natural variant8771T → S in prostate cancer.
VAR_009844
Natural variant8791D → Y in AIS. Ref.196
VAR_013480
Natural variant8801L → Q in prostate cancer.
VAR_009845
Natural variant8811L → V in AIS. Ref.126
VAR_009846
Natural variant8861M → V in AIS.
VAR_009847
Natural variant8891V → M in AIS and PAIS. Ref.118 Ref.155
VAR_009848
Natural variant8901D → N in prostate cancer. Ref.179
VAR_009849
Natural variant8911F → L in prostate cancer.
VAR_009850
Natural variant8921P → L in AIS. Ref.172 Ref.183 Ref.188
VAR_004733
Natural variant8951M → T in AIS; low androgen binding and transactivation. Ref.61 Ref.169
VAR_004734
Natural variant8961A → T in prostate cancer.
VAR_009851
Natural variant8981I → T in AIS.
VAR_009852
Natural variant9021Q → R in prostate cancer.
VAR_009853
Natural variant9031V → M in PAIS.
VAR_009854
Natural variant9041P → H in AIS.
VAR_009855
Natural variant9041P → S in AIS.
VAR_009856
Natural variant9071L → F in AIS; almost complete loss of transcription activation. Ref.163 Ref.201
VAR_004735
Natural variant9091G → E in prostate cancer.
VAR_009857
Natural variant9091G → R in PAIS. Ref.142
VAR_009858
Natural variant9101K → R in prostate cancer. Ref.158
VAR_009859
Natural variant9111V → L in PAIS. Ref.178
VAR_009860
Natural variant9131P → S in PAIS.
VAR_004736
Natural variant9161F → L in AIS. Ref.164
VAR_009861
Natural variant9171H → R in AIS.
VAR_009862
Natural variant9191Q → R in prostate cancer.
VAR_009863

Experimental info

Mutagenesis811S → A: Reduced cell growth. Ref.51
Mutagenesis2231Y → F: Decrease of CSK-induced phosphorylation. Ref.39
Mutagenesis2671Y → F: Decrease of CSK-induced phosphorylation and phosphorylation by TNK2. Complete loss of TNK2-dependent phosphorylation; when associated with F-363. Ref.39 Ref.45
Mutagenesis3071Y → F: Decrease of CSK-induced phosphorylation. Ref.39
Mutagenesis3461Y → F: Decrease of CSK-induced phosphorylation. Ref.39
Mutagenesis3571Y → F: Decrease of CSK-induced phosphorylation. Ref.39
Mutagenesis3621Y → F: Decrease of CSK-induced phosphorylation. Ref.39
Mutagenesis3631Y → F: Decrease of CSK-induced phosphorylation and phosphorylation by TNK2. Complete loss of TNK2-dependent phosphorylation; when associated with F-267. Ref.39 Ref.45
Mutagenesis3931Y → F: Decrease of CSK-induced phosphorylation. Ref.39
Mutagenesis5341Y → F: Greatest decrease of CSK-induced phosphorylation and inhibition of transcriptional activity induced by EGF. Ref.39
Mutagenesis5511Y → F: Decrease in CSK-induced phosphorylation. Ref.39
Mutagenesis7011L → A: Alters receptor specificity, so that transcription is activated by the antiandrogen cyproterone acetate. Ref.64
Mutagenesis7201K → A: Loss of transcription activation in the presence of androgen and of interaction with NCOA2. Ref.60 Ref.65
Mutagenesis7411W → L: Strongly decreased transcription activation in the presence of androgen. Ref.61
Mutagenesis8451K → R: Prevents ubiquitination by RNF6. Prevents AR transcriptional activation by RNF14 in absence of hormone. Ref.50
Mutagenesis8471K → R: Partially prevents ubiquitination by RNF6. Ref.50
Mutagenesis8971E → A or Q: Reduced transcription activation in the presence of androgen. Ref.60 Ref.65
Mutagenesis8971E → K or R: Loss of transcription activation in the presence of androgen. Ref.60 Ref.65
Mutagenesis9151Y → F: Decrease in CSK-induced phosphorylation. Ref.39
Sequence conflict1661G → A in AAA51780. Ref.5
Sequence conflict2121A → R Ref.3
Sequence conflict2121A → R in AAA51771. Ref.6
Sequence conflict2121A → R in AAA51772. Ref.6
Sequence conflict4751G → E in AAA51775. Ref.2
Sequence conflict4751G → E in AAA51770. Ref.12
Sequence conflict5651E → K in AAA51774. Ref.14
Sequence conflict6341L → P in AAB21256. Ref.18
Sequence conflict6341L → P in AAB21257. Ref.18
Sequence conflict6751N → I in AAB21256. Ref.18
Sequence conflict6751N → I in AAB21257. Ref.18
Sequence conflict8101L → M in AAA51780. Ref.5

Secondary structure

....................................... 919
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (AR-B) [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 93B096927740B6FF

FASTA91998,989
        10         20         30         40         50         60 
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GASLLLLQQQ 

        70         80         90        100        110        120 
QQQQQQQQQQ QQQQQQQQET SPRQQQQQQG EDGSPQAHRR GPTGYLVLDE EQQPSQPQSA 

       130        140        150        160        170        180 
LECHPERGCV PEPGAAVAAS KGLPQQLPAP PDEDDSAAPS TLSLLGPTFP GLSSCSADLK 

       190        200        210        220        230        240 
DILSEASTMQ LLQQQQQEAV SEGSSSGRAR EASGAPTSSK DNYLGGTSTI SDNAKELCKA 

       250        260        270        280        290        300 
VSVSMGLGVE ALEHLSPGEQ LRGDCMYAPL LGVPPAVRPT PCAPLAECKG SLLDDSAGKS 

       310        320        330        340        350        360 
TEDTAEYSPF KGGYTKGLEG ESLGCSGSAA AGSSGTLELP STLSLYKSGA LDEAAAYQSR 

       370        380        390        400        410        420 
DYYNFPLALA GPPPPPPPPH PHARIKLENP LDYGSAWAAA AAQCRYGDLA SLHGAGAAGP 

       430        440        450        460        470        480 
GSGSPSAAAS SSWHTLFTAE EGQLYGPCGG GGGGGGGGGG GGGGGGGGGG GGEAGAVAPY 

       490        500        510        520        530        540 
GYTRPPQGLA GQESDFTAPD VWYPGGMVSR VPYPSPTCVK SEMGPWMDSY SGPYGDMRLE 

       550        560        570        580        590        600 
TARDHVLPID YYFPPQKTCL ICGDEASGCH YGALTCGSCK VFFKRAAEGK QKYLCASRND 

       610        620        630        640        650        660 
CTIDKFRRKN CPSCRLRKCY EAGMTLGARK LKKLGNLKLQ EEGEASSTTS PTEETTQKLT 

       670        680        690        700        710        720 
VSHIEGYECQ PIFLNVLEAI EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK 

       730        740        750        760        770        780 
ALPGFRNLHV DDQMAVIQYS WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF NEYRMHKSRM 

       790        800        810        820        830        840 
YSQCVRMRHL SQEFGWLQIT PQEFLCMKAL LLFSIIPVDG LKNQKFFDEL RMNYIKELDR 

       850        860        870        880        890        900 
IIACKRKNPT SCSRRFYQLT KLLDSVQPIA RELHQFTFDL LIKSHMVSVD FPEMMAEIIS 

       910 
VQVPKILSGK VKPIYFHTQ 

« Hide

Isoform 2 (AR-A) (Variant AR45) [UniParc].

Checksum: 495BAE974B4EFC75
Show »

FASTA38844,643

References

« Hide 'large scale' references
[1]"The human androgen receptor: complementary deoxyribonucleic acid cloning, sequence analysis and gene expression in prostate."
Lubahn D.B., Joseph D.R., Sar M., Tan J., Higgs H.N., Larson R.E., French F.S., Wilson E.M.
Mol. Endocrinol. 2:1265-1275(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Structural analysis of complementary DNA and amino acid sequences of human and rat androgen receptors."
Chang C., Kokontis J., Liao S.
Proc. Natl. Acad. Sci. U.S.A. 85:7211-7215(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Prostate.
[3]"Characterization and expression of a cDNA encoding the human androgen receptor."
Tilley W.D., Marcelli M., Wilson J.D., McPhaul M.J.
Proc. Natl. Acad. Sci. U.S.A. 86:327-331(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Prostate.
[4]"Sequence of the intron/exon junctions of the coding region of the human androgen receptor gene and identification of a point mutation in a family with complete androgen insensitivity."
Lubahn D.B., Brown T.R., Simental J.A., Higgs H.N., Migeon C.J., Wilson E.M., French F.S.
Proc. Natl. Acad. Sci. U.S.A. 86:9534-9538(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AIS MET-866.
[5]"Specific region in hormone binding domain is essential for hormone binding and trans-activation by human androgen receptor."
Govindan M.V.
Mol. Endocrinol. 4:417-427(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT DEL GLY-465--472-GLY.
[6]"Definition of the human androgen receptor gene structure permits the identification of mutations that cause androgen resistance: premature termination of the receptor protein at amino acid residue 588 causes complete androgen resistance."
Marcelli M., Tilley W.D., Wilson C.M., Griffin J.E., Wilson J.D., McPhaul M.J.
Mol. Endocrinol. 4:1105-1116(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Prostate.
[7]"Androgen receptor function is modulated by the tissue-specific AR45 variant."
Ahrens-Fath I., Politz O., Geserick C., Haendler B.
FEBS J. 272:74-84(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[8]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), POLYMORPHISM OF POLY-GLY REGION.
[11]"The N-terminal domain of the human androgen receptor is encoded by one, large exon."
Faber P.W., Kuiper G.G.J.M., van Rooij H.C.J., van der Korput J.A.G.M., Brinkmann A.O., Trapman J.
Mol. Cell. Endocrinol. 61:257-262(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-538.
[12]"Molecular cloning of human and rat complementary DNA encoding androgen receptors."
Chang C., Kokontis J., Liao S.
Science 240:324-326(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-919 (ISOFORM 1).
[13]Lu J., Danielsen M.
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-475, POLYMORPHISM OF POLY-GLY REGION.
Tissue: Blood.
[14]"Cloning, structure and expression of a cDNA encoding the human androgen receptor."
Trapman J., Klaassen P., Kuiper G.G.J.M., van der Korput J.A.G.M., Faber P.W., van Rooij H.C.J., Geurts van Kessel A., Voorhorst M.M., Mulder E., Brinkmann A.O.
Biochem. Biophys. Res. Commun. 153:241-248(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 468-919 (ISOFORM 1).
[15]"Structural organization of the human androgen receptor gene."
Kuiper G.G., Faber P.W., van Rooij H.C., van der Korput J.A., Ris-Stalpers C., Klaassen P., Trapman J., Brinkmann A.O.
J. Mol. Endocrinol. 2:R1-R4(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 536-540; 587-591; 626-630; 722-726; 770-774; 814-817 AND 866-870.
[16]"A point mutation in the second zinc finger of the DNA-binding domain of the androgen receptor gene causes complete androgen insensitivity in two siblings with receptor-positive androgen resistance."
Mowszowicz I., Lee H.-J., Chen H.-T., Mestayer C., Portois M.-C., Cabrol S., Mauvais-Jarvis P., Chang C.
Mol. Endocrinol. 7:861-869(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 557-624 (ISOFORMS 1/2), VARIANT AIS HIS-615.
Tissue: Fibroblast.
[17]"Cloning of human androgen receptor complementary DNA and localization to the X chromosome."
Lubahn D.B., Joseph D.R., Sullivan P.M., Willard H.F., French F.S., Wilson E.M.
Science 240:327-330(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 559-624 (ISOFORMS 1/2).
[18]"Substitution of aspartic acid-686 by histidine or asparagine in the human androgen receptor leads to a functionally inactive protein with altered hormone-binding characteristics."
Ris-Stalpers C., Trifiro M.A., Kuiper G.G.J.M., Jenster G., Romalo G., Sai T., van Rooij H.C.J., Kaufman M., Rosenfield R.L., Liao S., Schweikert H.-U., Trapman J., Pinsky L., Brinkmann A.O.
Mol. Endocrinol. 5:1562-1569(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 629-723, VARIANTS AIS ASN-695 AND HIS-695.
[19]"Trinucleotide repeat polymorphism in the androgen receptor gene (AR)."
Sleddens H.F.B.M., Oostra B.A., Brinkmann A.O., Trapman J.
Nucleic Acids Res. 20:1427-1427(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM OF POLY-GLN REGION.
[20]"The CAG repeat within the androgen receptor gene and its relationship to prostate cancer."
Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D., Brufsky A., Talcott J., Hennekens C.H., Kantoff P.W.
Proc. Natl. Acad. Sci. U.S.A. 94:3320-3323(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM OF POLY-GLN REGION.
[21]Erratum
Giovannucci E., Stampfer M.J., Krithivas K., Brown M., Dahl D., Brufsky A., Talcott J., Hennekens C.H., Kantoff P.W.
Proc. Natl. Acad. Sci. U.S.A. 94:8272-8272(1997)
[22]"PQBP-1, a novel polyglutamine tract binding protein, inhibits transcription activation by Brn-2 and affects cell survival."
Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y., Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.
Hum. Mol. Genet. 8:977-987(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PQBP1.
Tissue: Brain.
[23]"Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate."
Fujimoto N., Yeh S., Kang H.-Y., Inui S., Chang H.-C., Mizokami A., Chang C.
J. Biol. Chem. 274:8316-8321(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TGFB1I1.
[24]"Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription."
Poukka H., Aarnisalo P., Karvonen U., Palvimo J.J., Jaenne O.A.
J. Biol. Chem. 274:19441-19446(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBE2I.
[25]"The linkage of Kennedy's neuron disease to ARA24, the first identified androgen receptor polyglutamine region-associated coactivator."
Hsiao P.-W., Lin D.-L., Nakao R., Chang C.
J. Biol. Chem. 274:20229-20234(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAN.
[26]"PDEF, a novel prostate epithelium-specific ets transcription factor, interacts with the androgen receptor and activates prostate-specific antigen gene expression."
Oettgen P., Finger E., Sun Z., Akbarali Y., Thamrongsak U., Boltax J., Grall F., Dube A., Weiss A., Brown L., Quinn G., Kas K., Endress G., Kunsch C., Libermann T.A.
J. Biol. Chem. 275:1216-1225(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPDEF.
[27]"Androgen receptor interacts with a novel MYST protein, HBO1."
Sharma M., Zarnegar M., Li X., Lim B., Sun Z.
J. Biol. Chem. 275:35200-35208(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KAT7.
[28]"Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)."
Poukka H., Karvonen U., Jaenne O.A., Palvimo J.J.
Proc. Natl. Acad. Sci. U.S.A. 97:14145-14150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-386 AND LYS-520.
[29]"RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor."
Rao M.A., Cheng H., Quayle A.N., Nishitani H., Nelson C.C., Rennie P.S.
J. Biol. Chem. 277:48020-48027(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP9.
[30]"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."
Zhao Y., Goto K., Saitoh M., Yanase T., Nomura M., Okabe T., Takayanagi R., Nawata H.
J. Biol. Chem. 277:30031-30039(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRPF6.
[31]"Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade."
Wong C.-W., McNally C., Nickbarg E., Komm B.S., Cheskis B.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14783-14788(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PELP1.
[32]"hZimp10 is an androgen receptor co-activator and forms a complex with SUMO-1 at replication foci."
Sharma M., Li X., Wang Y., Zarnegar M., Huang C.-Y., Palvimo J.J., Lim B., Sun Z.
EMBO J. 22:6101-6114(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZMIZ1.
[33]"The scaffolding protein RACK1 interacts with androgen receptor and promotes cross-talk through a protein kinase C signaling pathway."
Rigas A.C., Ozanne D.M., Neal D.E., Robson C.N.
J. Biol. Chem. 278:46087-46093(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GNB2L1, SUBCELLULAR LOCATION.
[34]"The retinoblastoma protein-associated transcription repressor RBaK interacts with the androgen receptor and enhances its transcriptional activity."
Hofman K., Swinnen J.V., Claessens F., Verhoeven G., Heyns W.
J. Mol. Endocrinol. 31:583-596(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RBAK.
[35]"DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex."
Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.
Mol. Cancer Res. 1:247-261(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EFCAB6.
[36]"Mechanism of p21-activated kinase 6-mediated inhibition of androgen receptor signaling."
Schrantz N., da Silva Correia J., Fowler B., Ge Q., Sun Z., Bokoch G.M.
J. Biol. Chem. 279:1922-1931(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PAK6.
[37]"Huntingtin interacting protein 1 modulates the transcriptional activity of nuclear hormone receptors."
Mills I.G., Gaughan L., Robson C., Ross T., McCracken S., Kelly J., Neal D.E.
J. Cell Biol. 170:191-200(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIP1.
[38]"hZimp7, a novel PIAS-like protein, enhances androgen receptor-mediated transcription and interacts with SWI/SNF-like BAF complexes."
Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B., Sun Z.
Mol. Endocrinol. 19:2915-2929(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZMIZ2.
[39]"Regulation of androgen receptor activity by tyrosine phosphorylation."
Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I., Kong X., Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R., Veenstra T.D., Chen H., Qiu Y.
Cancer Cell 10:309-319(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-223; TYR-267; TYR-307; TYR-346; TYR-357; TYR-362; TYR-363; TYR-393; TYR-534; TYR-551 AND TYR-915, MUTAGENESIS OF TYR-223; TYR-267; TYR-307; TYR-346; TYR-357; TYR-362; TYR-363; TYR-393; TYR-534; TYR-551 AND TYR-915, IDENTIFICATION BY MASS SPECTROMETRY.
[40]Erratum
Guo Z., Dai B., Jiang T., Xu K., Xie Y., Kim O., Nesheiwat I., Kong X., Melamed J., Handratta V.D., Njar V.C., Brodie A.M., Yu L.-R., Veenstra T.D., Chen H., Qiu Y.
Cancer Cell 11:97-97(2007)
[41]"Male germ cell-associated kinase, a male-specific kinase regulated by androgen, is a coactivator of androgen receptor in prostate cancer cells."
Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M., Shi X.B., deVere White R.W., Chen H.W., Tepper C.G., Kung H.J.
Cancer Res. 66:8439-8447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAK, SUBUNIT.
[42]"PRMT2, a member of the protein arginine methyltransferase family, is a coactivator of the androgen receptor."
Meyer R., Wolf S.S., Obendorf M.
J. Steroid Biochem. Mol. Biol. 107:1-14(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRMT2, SUBCELLULAR LOCATION.
[43]"The zinc finger protein Ras-responsive element binding protein-1 is a coregulator of the androgen receptor: implications for the role of the Ras pathway in enhancing androgenic signaling in prostate cancer."
Mukhopadhyay N.K., Cinar B., Mukhopadhyay L., Lutchman M., Ferdinand A.S., Kim J., Chung L.W.K., Adam R.M., Ray S.K., Leiter A.B., Richie J.P., Liu B.C.-S., Freeman M.R.
Mol. Endocrinol. 21:2056-2070(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RREB1.
[44]"RanBP10 acts as a novel coactivator for the androgen receptor."
Harada N., Yokoyama T., Yamaji R., Nakano Y., Inui H.
Biochem. Biophys. Res. Commun. 368:121-125(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP10.
[45]"Activated Cdc42-associated kinase Ack1 promotes prostate cancer progression via androgen receptor tyrosine phosphorylation."
Mahajan N.P., Liu Y., Majumder S., Warren M.R., Parker C.E., Mohler J.L., Earp H.S., Whang Y.E.
Proc. Natl. Acad. Sci. U.S.A. 104:8438-8443(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TNK2, PHOSPHORYLATION AT TYR-267 AND TYR-363 BY TNK2, MUTAGENESIS OF TYR-267 AND TYR-363.
[46]"TRIM68 regulates ligand-dependent transcription of androgen receptor in prostate cancer cells."
Miyajima N., Maruyama S., Bohgaki M., Kano S., Shigemura M., Shinohara N., Nonomura K., Hatakeyama S.
Cancer Res. 68:3486-3494(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM68.
[47]"Leupaxin, a novel coactivator of the androgen receptor, is expressed in prostate cancer and plays a role in adhesion and invasion of prostate carcinoma cells."
Kaulfuss S., Grzmil M., Hemmerlein B., Thelen P., Schweyer S., Neesen J., Bubendorf L., Glass A.G., Jarry H., Auber B., Burfeind P.
Mol. Endocrinol. 22:1606-1621(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LPXN.
[48]"ZIP kinase plays a crucial role in androgen receptor-mediated transcription."
Leister P., Felten A., Chasan A.I., Scheidtmann K.H.
Oncogene 27:3292-3300(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ZIPK/DAPK3.
[49]"TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells."
Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., Imamura M., Hatakeyama S.
Biochim. Biophys. Acta 1793:1828-1836(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM24.
[50]"Regulation of androgen receptor transcriptional activity and specificity by RNF6-induced ubiquitination."
Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z., Chen H., Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z., Veenstra T.D., Qiu Y.
Cancer Cell 15:270-282(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, POLYUBIQUITINATION AT LYS-845 AND LYS-847 BY RNF6, MUTAGENESIS OF LYS-845 AND LYS-847, INTERACTION WITH RNF14 AND RNF6, SUBCELLULAR LOCATION.
[51]"CDK9 regulates AR promoter selectivity and cell growth through serine 81 phosphorylation."
Gordon V., Bhadel S., Wunderlich W., Zhang J., Ficarro S.B., Mollah S.A., Shabanowitz J., Hunt D.F., Xenarios I., Hahn W.C., Conaway M., Carey M.F., Gioeli D.
Mol. Endocrinol. 24:2267-2280(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN AR KINASE, PHOSPHORYLATION AT SER-81 BY CDK9, MUTAGENESIS OF SER-81, INTERACTION WITH CDK9.
[52]"The deubiquitinating enzyme USP26 is a regulator of androgen receptor signaling."
Dirac A.M., Bernards R.
Mol. Cancer Res. 8:844-854(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION, INTERACTION WITH USP26.
[53]"Effect of Ack1 tyrosine kinase inhibitor on ligand-independent androgen receptor activity."
Mahajan K., Challa S., Coppola D., Lawrence H., Luo Y., Gevariya H., Zhu W., Chen Y.A., Lawrence N.J., Mahajan N.P.
Prostate 70:1274-1285(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-267, ENZYME REGULATION.
[54]"MST1 is a multifunctional caspase-independent inhibitor of androgenic signaling."
Cinar B., Collak F.K., Lopez D., Akgul S., Mukhopadhyay N.K., Kilicarslan M., Gioeli D.G., Freeman M.R.
Cancer Res. 71:4303-4313(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-650, INTERACTION WITH STK4/MST1.
[55]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[56]"DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors."
Pedram A., Razandi M., Deschenes R.J., Levin E.R.
Mol. Biol. Cell 23:188-199(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION.
[57]"Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations."
Matias P.M., Donner P., Coelho R., Thomaz M., Peixoto C., Macedo S., Otto N., Joschko S., Scholz P., Wegg A., Baesler S., Schaefer M., Egner U., Carrondo M.A.
J. Biol. Chem. 275:26164-26171(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 657-919.
[58]"Structural basis for the glucocorticoid response in a mutant human androgen receptor (AR(ccr)) derived from an androgen-independent prostate cancer."
Matias P.M., Carrondo M.A., Coelho R., Thomaz M., Zhao X.Y., Wegg A., Crusius K., Egner U., Donner P.
J. Med. Chem. 45:1439-1446(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 670-917.
[59]"Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance."
He B., Gampe R.T. Jr., Kole A.J., Hnat A.T., Stanley T.B., An G., Stewart E.L., Kalman R.I., Minges J.T., Wilson E.M.
Mol. Cell 16:425-438(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 671-919 IN COMPLEXES WITH N-TERMINAL MODULATING DOMAIN AND NCOA2, INTERACTION WITH NCOA1, CHARACTERIZATION OF VARIANT PROSTATE CANCER M-730.
[60]"The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor."
Estebanez-Perpina E., Moore J.M.R., Mar E., Delgado-Rodrigues E., Nguyen P., Baxter J.D., Buehrer B.M., Webb P., Fletterick R.J., Guy R.K.
J. Biol. Chem. 280:8060-8068(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 669-919 IN COMPLEXES WITH DIHYDROTESTOSTERONE AND NCOA1; NCOA2; NCOA3 AND NCOA4, FUNCTION, INTERACTION WITH NCOA1; NCOA2; NCOA3 AND NCOA4, MUTAGENESIS OF LYS-720 AND GLU-897.
[61]"Structural basis for accommodation of nonsteroidal ligands in the androgen receptor."
Bohl C.E., Miller D.D., Chen J., Bell C.E., Dalton J.T.
J. Biol. Chem. 280:37747-37754(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 664-919 IN COMPLEXES WITH NONSTEROIDAL LIGANDS, MUTAGENESIS OF TRP-741, CHARACTERIZATION OF VARIANT PROSTATE CANCER ALA-877, CHARACTERIZATION OF VARIANT AIS THR-895.
[62]"Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity."
Pereira de Jesus-Tran K., Cote P.-L., Cantin L., Blanchet J., Labrie F., Breton R.
Protein Sci. 15:987-999(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 654-919 IN COMPLEXES WITH TESTOSTERONE; DIHYDROTESTOSTERONE AND TETRAHYDROGESTRINONE.
[63]"Interaction between the androgen receptor and a segment of its corepressor SHP."
Jouravel N., Sablin E., Arnold L.A., Guy R.K., Fletterick R.J.
Acta Crystallogr. D 63:1198-1200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 671-918 IN COMPLEX WITH NR0B2.
[64]"Crystal structure of the T877A human androgen receptor ligand-binding domain complexed to cyproterone acetate provides insight for ligand-induced conformational changes and structure-based drug design."
Bohl C.E., Wu Z., Miller D.D., Bell C.E., Dalton J.T.
J. Biol. Chem. 282:13648-13655(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 671-919 OF MUTANT ALA-877 IN COMPLEX WITH THE ANTIANDROGEN CYPROTERONE ACETATE, CHARACTERIZATION OF VARIANT PROSTATE CANCER ALA-877, MUTAGENESIS OF LEU-701.
[65]"Modulation of androgen receptor activation function 2 by testosterone and dihydrotestosterone."
Askew E.B., Gampe R.T. Jr., Stanley T.B., Faggart J.L., Wilson E.M.
J. Biol. Chem. 282:25801-25816(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 663-919 OF WILD-TYPE AND MUTANT TYR-874 IN COMPLEX WITH TESTOSTERONE AND NCOA2, ACTIVATION BY THE N-TERMINAL MODULATING DOMAIN, INTERACTION WITH NCOA2 AND MAGEA11, FUNCTION, MUTAGENESIS OF LYS-720 AND GLU-897, CHARACTERIZATION OF VARIANT PROSTATE CANCER TYR-874.
[66]"Structural characterization of the human androgen receptor ligand-binding domain complexed with EM5744, a rationally designed steroidal ligand bearing a bulky chain directed toward helix 12."
Cantin L., Faucher F., Couture J.-F., de Jesus-Tran K.P., Legrand P., Ciobanu L.C., Frechette Y., Labrecque R., Singh S.M., Labrie F., Breton R.
J. Biol. Chem. 282:30910-30919(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 654-919 IN COMPLEX WITH EM5744.
[67]"A surface on the androgen receptor that allosterically regulates coactivator binding."
Estebanez-Perpina E., Arnold L.A., Nguyen P., Rodrigues E.D., Mar E., Bateman R., Pallai P., Shokat K.M., Baxter J.D., Guy R.K., Webb P., Fletterick R.J.
Proc. Natl. Acad. Sci. U.S.A. 104:16074-16079(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 669-919 IN COMPLEXES WITH SYNTHETIC LIGANDS, FUNCTION, INTERACTION WITH NCOA2.
[68]"Androgen resistance due to mutation of the androgen receptor."
Pinsky L., Trifiro M.A., Kaufman M., Beitel L.K., Mhatre A., Kazemi-Esfarjani P., Sabbaghian N., Lumbroso R., Alvarado C., Vasiliou M., Gottlieb B.
Clin. Invest. Med. 15:456-472(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[69]"Molecular genetics of human androgen insensitivity."
Brown T.R., Scherer P.A., Chang Y.-T., Migeon C.J., Ghirri P., Murono K., Zhou Z.
Eur. J. Pediatr. 152 Suppl. 2:S62-S69(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS AIS.
[70]"Mutations of androgen receptor gene in androgen insensitivity syndromes."
Sultan C., Lumbroso S., Poujol N., Belon C., Boudon C., Lobaccaro J.-M.
J. Steroid Biochem. Mol. Biol. 46:519-530(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[71]"The androgen receptor gene mutations database."
Patterson M.N., Hughes I.A., Gottlieb B., Pinsky L.
Nucleic Acids Res. 22:3560-3562(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[72]"Androgen receptor mutations."
Brinkmann A.O., Jenster G., Ris-Stalpers C., van der Korput J.A.G.M., Bruggenwirth H.T., Boehmer A.L.M., Trapman J.
J. Steroid Biochem. Mol. Biol. 53:443-448(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[73]"The androgen receptor gene mutations database."
Gottlieb B., Trifiro M.A., Lumbroso R., Vasiliou D.M., Pinsky L.
Nucleic Acids Res. 25:158-162(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[74]"The androgen receptor gene mutations database: 2012 update."
Gottlieb B., Beitel L.K., Nadarajah A., Paliouras M., Trifiro M.
Hum. Mutat. 33:887-894(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[75]"A mutation in the ligand binding domain of the androgen receptor of human LNCaP cells affects steroid binding characteristics and response to anti-androgens."
Veldscholte J., Ris-Stalpers C., Kuiper G.G.J.M., Jenster G., Berrevoets C.A., Claassen E., van Rooij H.C.J., Trapman J., Brinkmann A.O., Mulder E.
Biochem. Biophys. Res. Commun. 173:534-540(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LNCAP ALA-877.
[76]"Functional characterization of naturally occurring mutant androgen receptors from subjects with complete androgen insensitivity."
Brown T.R., Lubahn D.B., Wilson E.M., French F.S., Migeon C.J., Corfen J.L.
Mol. Endocrinol. 4:1759-1772(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS CYS-774; GLN-831 AND MET-866.
[77]"Androgen resistance associated with a mutation of the androgen receptor at amino acid 772 (Arg-->Cys) results from a combination of decreased messenger ribonucleic acid levels and impairment of receptor function."
Marcelli M., Tilley W.D., Zoppi S., Griffin J.E., Wilson J.D., McPhaul M.J.
J. Clin. Endocrinol. Metab. 73:318-325(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-774.
[78]"A mutation in the DNA-binding domain of the androgen receptor gene causes complete testicular feminization in a patient with receptor-positive androgen resistance."
Marcelli M., Zoppi S., Grino P.B., Griffin J.E., Wilson J.D., McPhaul M.J.
J. Clin. Invest. 87:1123-1126(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS PRO-617.
[79]"Molecular basis of androgen resistance in a family with a qualitative abnormality of the androgen receptor and responsive to high-dose androgen therapy."
McPhaul M.J., Marcelli M., Tilley W.D., Griffin J.E., Isidro-Gutierrez R.F., Wilson J.D.
J. Clin. Invest. 87:1413-1421(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS CYS-763.
[80]"Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy."
la Spada A.R., Wilson E.M., Lubahn D.B., Harding A.E., Fischbeck K.H.
Nature 352:77-79(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: POLY-GLN REGION EXPANSION, INVOLVEMENT IN SPINAL AND BULBAR MUSCULAR ATROPHY.
[81]"Replacement of arginine 773 by cysteine or histidine in the human androgen receptor causes complete androgen insensitivity with different receptor phenotypes."
Prior L., Bordet S., Trifiro M.A., Mhatre A., Kaufman M., Pinsky L., Wrogemann K., Belsham D.D., Pereira F., Greenberg C.R., Trapman J., Brinkmann A.O., Chang C., Liao S.
Am. J. Hum. Genet. 51:143-155(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS CYS-774 AND HIS-774.
[82]"Point mutations detected in the androgen receptor gene of three men with partial androgen insensitivity syndrome."
Saunders P.T., Padayachi T., Tincello D.G., Shalet S.M., Wu F.C.
Clin. Endocrinol. (Oxf.) 37:214-220(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS LYS-608 AND LEU-866.
[83]"A unique point mutation in the androgen receptor gene in a family with complete androgen insensitivity syndrome."
Sweet C.R., Behzadian M.A., McDonough P.G.
Fertil. Steril. 58:703-707(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS THR-765.
[84]"Point mutation in the steroid-binding domain of the androgen receptor gene in a family with complete androgen insensitivity syndrome (CAIS)."
Jakubiczka S., Werder E.A., Wieacker P.
Hum. Genet. 90:311-312(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS VAL-749.
[85]"Androgen receptor gene mutations identified by SSCP in fourteen subjects with androgen insensitivity syndrome."
Batch J.A., Williams D.M., Davies H.R., Brown B.D., Evans B.A.J., Hughes I.A., Patterson M.N.
Hum. Mol. Genet. 1:497-503(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS, VARIANTS PAIS.
[86]"A single amino acid substitution (Met-786-->Val) in the steroid-binding domain of human androgen receptor leads to complete androgen insensitivity syndrome."
Nakao R., Haji M., Yanase T., Ogo A., Takayanagi R., Katsube T., Fukumaki Y., Nawata H.
J. Clin. Endocrinol. Metab. 74:1152-1157(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS VAL-787.
[87]"Immunoreactive androgen receptor expression in subjects with androgen resistance."
Wilson C.M., Griffin J.E., Wilson J.D., Marcelli M., Zoppi S., McPhaul M.J.
J. Clin. Endocrinol. Metab. 75:1474-1478(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS ARG-741 AND CYS-834.
[88]"Mutations in the ligand-binding domain of the androgen receptor gene cluster in two regions of the gene."
McPhaul M.J., Marcelli M., Zoppi S., Wilson C.M., Griffin J.E., Wilson J.D.
J. Clin. Invest. 90:2097-2101(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS, VARIANTS PAIS.
[89]"The androgen receptor in LNCaP cells contains a mutation in the ligand binding domain which affects steroid binding characteristics and response to antiandrogens."
Veldscholte J., Berrevoets C.A., Ris-Stalpers C., Kuiper G.G.J.M., Jenster G., Trapman J., Brinkmann A.O., Mulder E.
J. Steroid Biochem. Mol. Biol. 41:665-669(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER ALA-877.
[90]"Amino acid substitutions in the DNA-binding domain of the human androgen receptor are a frequent cause of receptor-binding positive androgen resistance."
Zoppi S., Marcelli M., Deslypere J.-P., Griffin J.E., Wilson J.D., McPhaul M.J.
Mol. Endocrinol. 6:409-415(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS TYR-559 AND ARG-576, VARIANTS PAIS GLY-597 AND PRO-617.
[91]"Single base mutations in the human androgen receptor gene causing complete androgen insensitivity: rapid detection by a modified denaturing gradient gel electrophoresis technique."
De Bellis A., Quigley C.A., Cariello N.F., el-Awady M.K., Sar M., Lane M.V., Wilson E.M., French F.S.
Mol. Endocrinol. 6:1909-1920(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS SER-705; VAL-749; PHE-759; HIS-774; CYS-855 AND GLY-864.
[92]"A germline mutation in the androgen receptor gene in two brothers with breast cancer and Reifenstein syndrome."
Wooster R., Mangion J., Eeles R., Smith S., Dowsett M., Averill D., Barrett-Lee P., Easton D.F., Ponder B.A., Stratton M.R.
Nat. Genet. 2:132-134(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS/BREAST CANCER GLN-607.
[93]"Androgen receptor gene mutations in human prostate cancer."
Newmark J.R., Hardy D.O., Tonb D.C., Carter B.S., Epstein J.I., Isaacs W.B., Brown T.R., Barrack E.R.
Proc. Natl. Acad. Sci. U.S.A. 89:6319-6323(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MET-730.
[94]"Sequence variation in the androgen receptor gene is not a common determinant of male sexual orientation."
Macke J.P., Hu N., Hu S., Bailey M., King V.L., Brown T., Hamer D., Nathans J.
Am. J. Hum. Genet. 53:844-852(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-205 AND ASP-793.
[95]"A new mutation within the deoxyribonucleic acid-binding domain of the androgen receptor gene in a family with complete androgen insensitivity syndrome."
Lumbroso S., Lobaccaro J.-M., Belon C., Martin D., Chaussain J.-L., Sultan C.
Fertil. Steril. 60:814-819(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS PHE-581.
[96]"An exonic point mutation creates a MaeIII site in the androgen receptor gene of a family with complete androgen insensitivity syndrome."
Lobaccaro J.-M., Lumbroso S., Ktari R., Dumas R., Sultan C.
Hum. Mol. Genet. 2:1041-1043(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS VAL-754.
[97]"Androgen receptor gene mutation in male breast cancer."
Lobaccaro J.-M., Lumbroso S., Belon C., Galtier-Dereure F., Bringer J., Lesimple T., Namer M., Cutuli B.F., Pujol H., Sultan C.
Hum. Mol. Genet. 2:1799-1802(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS/BREAST CANCER LYS-608.
[98]"A single-base substitution in exon 6 of the androgen receptor gene causing complete androgen insensitivity: the mutated receptor fails to transactivate but binds to DNA in vitro."
Adeyemo O., Kallio P.J., Palvimo J.J., Kontula K., Jaenne O.A.
Hum. Mol. Genet. 2:1809-1812(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS ARG-807.
[99]"A single amino acid substitution (Gly743 --> Val) in the steroid-binding domain of the human androgen receptor leads to Reifenstein syndrome."
Nakao R., Yanase T., Sakai Y., Haji M., Nawata H.
J. Clin. Endocrinol. Metab. 77:103-107(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS VAL-743.
[100]"Single strand conformation polymorphism analysis of androgen receptor gene mutations in patients with androgen insensitivity syndromes: application for diagnosis, genetic counseling, and therapy."
Hiort O., Huang Q., Sinnecker G.H., Sadeghi-Nejad A., Kruse K., Wolfe H.J., Yandell D.W.
J. Clin. Endocrinol. Metab. 77:262-266(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS LYS-681 AND THR-842, VARIANTS PAIS HIS-840 AND LEU-866.
[101]"Mutations of the androgen receptor gene identified in perineal hypospadias."
Batch J.A., Evans B.A.J., Hughes I.A., Patterson M.N.
J. Med. Genet. 30:198-201(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS HIS-855 AND MET-869.
[102]"Complete androgen insensitivity syndrome associated with a de novo mutation of the androgen receptor gene detected by single strand conformation polymorphism."
Lobaccaro J.-M., Lumbroso S., Berta P., Chaussain J.-L., Sultan C.
J. Steroid Biochem. Mol. Biol. 44:211-216(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS VAL-743.
[103]"Androgen receptor gene mutations in human prostate cancer."
Suzuki H., Sato N., Watabe Y., Masai M., Seino S., Shimazaki J.
J. Steroid Biochem. Mol. Biol. 46:759-765(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER HIS-701 AND ALA-877.
[104]"Substitution of valine-865 by methionine or leucine in the human androgen receptor causes complete or partial androgen insensitivity, respectively with distinct androgen receptor phenotypes."
Kazemi-Esfarjani P., Beitel L.K., Trifiro M.A., Kaufman M., Rennie P., Sheppard P., Matusik R., Pinsky L.
Mol. Endocrinol. 7:37-46(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS MET-866, VARIANT PAIS LEU-866.
[105]"Mutant androgen receptor detected in an advanced-stage prostatic carcinoma is activated by adrenal androgens and progesterone."
Culig Z., Hobisch A., Cronauer M.V., Cato A.C.B., Hittmair A., Radmayr C., Eberle J., Bartsch G., Klocker H.
Mol. Endocrinol. 7:1541-1550(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER MET-715.
[106]"Androgen receptor (AR) gene mutations in 6 families with androgen insensitivity syndrome (Abstract #114)."
Lobaccaro J.-M., Lumbroso S., Belon C., Chaussain J.L., Toublanc J.E., Leheup B., Sultan C.
Pediatr. Res. Suppl. 33:S22-S22(1993)
Cited for: VARIANTS AIS PHE-581; VAL-743; VAL-754; GLU-767 AND CYS-855.
[107]"Androgen receptor gene mutations and p53 gene analysis in advanced prostate cancer."
Castagnaro M., Yandell D.W., Dockhorn-Dworniczak B., Wolfe H.J., Poremba C.
Verh. Dtsch. Ges. Pathol. 77:119-123(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER LEU-340 AND GLU-798.
[108]"Microsatellite mutation (CAG24-->18) in the androgen receptor gene in human prostate cancer."
Schoenberg M.P., Hakimi J.M., Wang S., Bova G.S., Epstein J.I., Fischbeck K.H., Isaacs W.B., Walsh P.C., Barrack E.R.
Biochem. Biophys. Res. Commun. 198:74-80(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: POLY-GLN REGION CONTRACTION, INVOLVEMENT IN PROSTATE CANCER.
[109]"Frequent detection of codon 877 mutation in the androgen receptor gene in advanced prostate cancers."
Gaddipati J.P., McLeod D.G., Heidenberg H.B., Sesterhenn I.A., Finger M.J., Moul J.W., Srivastava S.
Cancer Res. 54:2861-2864(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER ALA-877.
[110]"Molecular prenatal diagnosis of partial androgen insensitivity syndrome based on the Hind III polymorphism of the androgen receptor gene."
Lobaccaro J.-M., Belon C., Lumbroso S., Olewniczack G., Carre-Pigeon F., Job J.C., Chaussain J.L., Toublanc J.E., Sultan C.
Clin. Endocrinol. (Oxf.) 40:297-302(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS TRP-568.
[111]"Molecular prenatal exclusion of familial partial androgen insensitivity (Reifenstein syndrome)."
Lumbroso S., Lobaccaro J.-M., Belon C., Amram S., Bachelard B., Garandeau P., Sultan C.
Eur. J. Endocrinol. 130:327-332(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS HIS-840.
[112]"Single amino acid substitution (840Arg-->His) in the hormone-binding domain of the androgen receptor leads to incomplete androgen insensitivity syndrome associated with a thermolabile androgen receptor."
Imasaki K., Hasegawa T., Okabe T., Sakai Y., Haji M., Takayanagi R., Nawata H.
Eur. J. Endocrinol. 130:569-574(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS HIS-840.
[113]"Molecular characterization of the androgen receptor gene in boys with hypospadias."
Hiort O., Klauber G., Cendron M., Sinnecker G.H., Keim L., Schwinger E., Wolfe H.J., Yandell D.W.
Eur. J. Pediatr. 153:317-321(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS VAL-870.
[114]"Partial androgen insensitivity (PAIS) in a large eskimo kindred caused by a delD690 mutation in the androgen receptor (AR) gene (Abstract #244)."
Schwartz M., Skovby F., Mueller J., Nielsen O., Skakkebaek N.E.
Horm. Res. 41:117-117(1994)
Cited for: VARIANT PAIS ASP-690 DEL.
[115]"Complete androgen insensitivity due to mutations in the probable alpha-helical segments of the DNA-binding domain in the human androgen receptor."
Beitel L.K., Prior L., Vasiliou D.M., Gottlieb B., Kaufman M., Lumbroso R., Alvarado C., McGillivray B., Trifiro M.A., Pinsky L.
Hum. Mol. Genet. 3:21-27(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS PHE-582 DEL; ARG-615 DEL AND HIS-615.
[116]"Detection of point mutations in the androgen receptor gene using non-isotopic single strand conformation polymorphism analysis."
Hiort O., Wodtke A., Struve D., Zoellner A., Sinnecker G.H.
Hum. Mol. Genet. 3:1163-1166(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS SER-582; TYR-604; ALA-708; LEU-754 AND HIS-771, VARIANT AIS TRP-779.
[117]"Two mutations causing complete androgen insensitivity: a frame-shift in the steroid binding domain and a Cys-->Phe substitution in the second zinc finger of the androgen receptor."
Baldazzi L., Baroncini C., Pirazzoli P., Balsamo A., Capelli M., Marchetti G., Bernardi F., Cacciari E.
Hum. Mol. Genet. 3:1169-1170(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS PHE-601.
[118]"Characterization of mutant androgen receptors causing partial androgen insensitivity syndrome."
De Bellis A., Quigley C.A., Marschke K.B., el-Awady M.K., Lane M.V., Smith E.P., Sar M., Wilson E.M., French F.S.
J. Clin. Endocrinol. Metab. 78:513-522(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS ARG-616; HIS-840 AND MET-889.
[119]"An androgen receptor mutation causing androgen resistance in undervirilized male syndrome."
Tsukada T., Inoue M., Tachibana S., Nakai Y., Takebe H.
J. Clin. Endocrinol. Metab. 79:1202-1207(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS PHE-790.
[120]"Substitution of arginine-839 by cysteine or histidine in the androgen receptor causes different receptor phenotypes in cultured cells and coordinate degrees of clinical androgen resistance."
Beitel L.K., Kazemi-Esfarjani P., Kaufman M., Lumbroso R., DiGeorge A.M., Killinger D.W., Trifiro M.A., Pinsky L.
J. Clin. Invest. 94:546-554(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS CYS-840 AND HIS-840.
[121]"Amino acid substitutions in the hormone-binding domain of the human androgen receptor alter the stability of the hormone receptor complex."
Marcelli M., Zoppi S., Wilson C.M., Griffin J.E., McPhaul M.J.
J. Clin. Invest. 94:1642-1650(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS, VARIANTS PAIS.
[122]"Pregnancy after hormonal correction of severe spermatogenic defect due to mutation in androgen receptor gene."
Yong E.L., Ng S.C., Roy A.C., Yun G., Ratnam S.S.
Lancet 344:826-827(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS LYS-727.
[123]"A practical approach to the detection of androgen receptor gene mutations and pedigree analysis in families with X-linked androgen insensitivity."
Ris-Stalpers C., Hoogenboezem T., Sleddens H.F.B.M., Verleun-Mooijman M.C.T., Degenhart H.J., Drop S.L.S., Halley D.J.J., Oosterwijk J.C., Hodgins M.B., Trapman J., Brinkmann A.O.
Pediatr. Res. 36:227-234(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS HIS-615 AND LEU-764, VARIANTS PAIS VAL-742 AND THR-745.
[124]"A frame-shift mutation of the androgen receptor gene in a patient with receptor-negative complete testicular feminization: comparison with a single base substitution in a receptor-reduced incomplete form."
Imai A., Ohno T., Iida K., Ohsuye K., Okano Y., Tamaya T.
Ann. Clin. Biochem. 32:482-486(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS HIS-840.
[125]"Prevalence of androgen receptor gene mutations in latent prostatic carcinomas from Japanese men."
Takahashi H., Furusato M., Allsbrook W.C. Jr., Nishii H., Wakui S., Barrett J.C., Boyd J.
Cancer Res. 55:1621-1624(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER.
[126]"Genetic counselling in complete androgen insensitivity syndrome: trinucleotide repeat polymorphisms, single-strand conformation polymorphism and direct detection of two novel mutations in the androgen receptor gene."
Davies H.R., Hughes I.A., Patterson M.N.
Clin. Endocrinol. (Oxf.) 43:69-77(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS VAL-881.
[127]"Androgen receptor defects: historical, clinical, and molecular perspectives."
Quigley C.A., De Bellis A., Marschke K.B., el-Awady M.K., Wilson E.M., French F.S.
Endocr. Rev. 16:271-321(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS SER-705 AND HIS-763, VARIANTS PAIS LEU-725; THR-737; HIS-774 AND GLU-798.
[128]Erratum
Quigley C.A., De Bellis A., Marschke K.B., el-Awady M.K., Wilson E.M., French F.S.
Endocr. Rev. 16:546-546(1995)
[129]"Characterization of alternative amino acid substitutions at arginine 830 of the androgen receptor that cause complete androgen insensitivity in three families."
Shkolny D.L., Brown T.R., Punnett H.H., Kaufman M., Trifiro M.A., Pinsky L.
Hum. Mol. Genet. 4:515-521(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS LEU-831 AND GLN-831.
[130]"Leu-676-Pro mutation of the androgen receptor causes complete androgen insensitivity syndrome in a large Hutterite kindred."
Belsham D.D., Pereira F., Greenberg C.R., Liao S., Wrogemann K.
Hum. Mutat. 5:28-33(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS PRO-677.
[131]"Human androgen insensitivity due to point mutations encoding amino acid substitutions in the androgen receptor steroid-binding domain."
Murono K., Mendonca B.B., Arnhold I.J.P., Rigon A.C.M.M., Migeon C.J., Brown T.R.
Hum. Mutat. 6:152-162(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS CYS-763, VARIANTS AIS TRP-779; VAL-807 AND CYS-855.
[132]"Mutant androgen receptors in prostatic tumors distinguish between amino-acid-sequence requirements for transactivation and ligand binding."
Peterziel H., Culig Z., Stober J., Hobisch A., Radmayr C., Bartsch G., Klocker H., Cato A.C.B.
Int. J. Cancer 63:544-550(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER MET-730.
[133]"Mutations of the androgen receptor coding sequence are infrequent in patients with isolated hypospadias."
Allera A., Herbst M.A., Griffin J.E., Wilson J.D., Schweikert H.-U., McPhaul M.J.
J. Clin. Endocrinol. Metab. 80:2697-2699(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-568.
[134]"Mutated human androgen receptor gene detected in a prostatic cancer patient is also activated by estradiol."
Elo J.P., Kvist L., Leinonen K., Isomaa V., Henttu P., Lukkarinen O., Vihko P.
J. Clin. Endocrinol. Metab. 80:3494-3500(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER LEU-726.
[135]"A single amino acid exchange abolishes dimerization of the androgen receptor and causes Reifenstein syndrome."
Gast A., Neuschmid-Kaspar F., Klocker H., Cato A.C.B.
Mol. Cell. Endocrinol. 111:93-98(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS THR-596.
[136]"Mutation of the androgen-receptor gene in metastatic androgen-independent prostate cancer."
Taplin M.-E., Bubley G.J., Shuster T.D., Frantz M.E., Spooner A.E., Ogata G.K., Keer H.N., Balk S.P.
N. Engl. J. Med. 332:1393-1398(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER.
[137]"The clinical and molecular spectrum of androgen insensitivity syndromes."
Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.
Am. J. Med. Genet. 63:218-222(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS AND PAIS.
[138]"Mutations in the androgen receptor gene are associated with progression of human prostate cancer to androgen independence."
Tilley W.D., Buchanan G., Hickey T.E., Bentel J.M.
Clin. Cancer Res. 2:277-285(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER.
[139]"Clinical and biochemical investigations and molecular analysis of subjects with mutations in the androgen receptor gene."
Weidemann W., Linck B., Haupt H., Mentrup B., Romalo G., Stockklauser K., Brinkmann A.O., Schweikert H.-U., Spindler K.D.
Clin. Endocrinol. (Oxf.) 45:733-739(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS GLN-607; THR-610; LEU-754; HIS-840; THR-842 AND HIS-855, VARIANT AIS MET-866.
[140]"Rapid detection of a mutation hot-spot in the human androgen receptor."
Malmgren H., Gustavsson J., Tuvemo T., Dahl N.
Clin. Genet. 50:202-205(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS CYS-855.
[141]"Functional analysis of six androgen receptor mutations identified in patients with partial androgen insensitivity syndrome."
Bevan C.L., Brown B.B., Davies H.R., Evans B.A.J., Hughes I.A., Patterson M.N.
Hum. Mol. Genet. 5:265-273(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS ILE-742; ILE-780; GLU-798; CYS-840; HIS-855 AND MET-869.
[142]"Partial androgen insensitivity caused by an androgen receptor mutation at amino acid 907 (Gly-->Arg) that results in decreased ligand binding affinity and reduced androgen receptor messenger ribonucleic acid levels."
Choong C.S., Sturm M.J., Strophair J.A., McCulloch R.K., Tilley W.D., Leedman P.J., Hurley D.M.
J. Clin. Endocrinol. Metab. 81:236-243(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS ARG-909.
[143]"A novel substitution (Leu707Arg) in exon 4 of the androgen receptor gene causes complete androgen resistance."
Lumbroso S., Lobaccaro J.-M., Georget V., Leger J., Poujol N., Terouanne B., Evain-Brion D., Czernichow P., Sultan C.
J. Clin. Endocrinol. Metab. 81:1984-1988(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS ARG-707.
[144]"Different phenotypes in a family with androgen insensitivity caused by the same M780I point mutation in the androgen receptor gene."
Rodien P., Mebarki F., Mowszowicz I., Chaussain J.L., Young J., Morel Y., Schaison G.
J. Clin. Endocrinol. Metab. 81:2994-2998(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS ILE-780.
[145]"A novel missense mutation in the amino-terminal domain of the human androgen receptor gene in a family with partial androgen insensitivity syndrome causes reduced efficiency of protein translation."
Choong C.S., Quigley C.A., French F.S., Wilson E.M.
J. Clin. Invest. 98:1423-1431(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS LYS-2.
[146]"Molecular basis of androgen insensitivity."
Bruggenwirth H.T., Boehmer A.L.M., Verleun-Mooijman M.C.T., Hoogenboezem T., Kleijer W.J., Otten B.J., Trapman J., Brinkmann A.O.
J. Steroid Biochem. Mol. Biol. 58:569-575(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS ASP-573.
[147]"Androgen receptor gene mutations are rarely associated with isolated penile hypospadias."
Sutherland R.W., Wiener J.S., Hicks J.P., Marcelli M., Gonzales E.T. Jr., Roth D.R., Lamb D.J.
J. Urol. 156:828-831(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS SER-548.
[148]"Molecular modeling and in vitro investigations of the human androgen receptor DNA-binding domain: application for the study of two mutations."
Lobaccaro J.-M., Poujol N., Chiche L., Lumbroso S., Brown T.R., Sultan C.
Mol. Cell. Endocrinol. 116:137-147(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS PRO-616.
[149]"Androgen insensitivity syndrome due to new mutations in the DNA-binding domain of the androgen receptor."
Imasaki K., Okabe T., Murakami H., Tanaka Y., Haji M., Takayanagi R., Nawata H.
Mol. Cell. Endocrinol. 120:15-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS PHE-579, VARIANT PAIS TYR-582.
[150]"Low incidence of androgen receptor gene mutations in human prostatic tumors using single strand conformation polymorphism analysis."
Evans B.A.J., Harper M.E., Daniells C.E., Watts C.E., Matenhelia S., Green J., Griffiths K.
Prostate 28:162-171(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER GLU-798.
[151]"Codon 877 mutation in the androgen receptor gene in advanced prostate cancer: relation to antiandrogen withdrawal syndrome."
Suzuki H., Akakura K., Komiya A., Aida S., Akimoto S., Shimazaki J.
Prostate 29:153-158(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER ALA-877.
[152]"Germ-line and somatic mosaicism in the androgen insensitivity syndrome: implications for genetic counseling."
Boehmer A.L.M., Brinkmann A.O., Niermeijer M.F., Bakker L., Halley D.J.J., Drop S.L.S.
Am. J. Hum. Genet. 60:1003-1006(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS HIS-855.
[153]"Androgen receptor gene amplification: a possible molecular mechanism for androgen deprivation therapy failure in prostate cancer."
Koivisto P., Kononen J., Palmberg C., Tammela T., Hyytinen E., Isola J., Trapman J., Cleutjens K., Noordzij A., Visakorpi T., Kallioniemi O.-P.
Cancer Res. 57:314-319(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER ALA-683.
[154]"Correlation of clinical, endocrine and molecular abnormalities with in vivo responses to high-dose testosterone in patients with partial androgen insensitivity syndrome."
Tincello D.G., Saunders P.T., Hodgins M.B., Simpson N.B., Edwards C.R., Hargreaves T.B., Wu F.C.
Clin. Endocrinol. (Oxf.) 46:497-506(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS LYS-608 AND GLY-772.
[155]"Molecular analysis of androgen resistance syndromes in Egyptian patients."
Essawi M., Gad Y.Z., el-Rouby O., Temtamy S.A., Sabour Y.A., el-Awady M.K.
Dis. Markers 13:99-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS MET-889.
[156]"Functional assessment and clinical classification of androgen sensitivity in patients with mutations of the androgen receptor gene."
Sinnecker G.H., Hiort O., Nitsche E.M., Holterhus P.M., Kruse K.
Eur. J. Pediatr. 156:7-14(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS TRP-779.
[157]"Mutations of the androgen receptor gene in patients with complete androgen insensitivity."
Jakubiczka S., Nedel S., Werder E.A., Schleiermacher E., Theile U., Wolff G., Wieacker P.
Hum. Mutat. 9:57-61(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS VAL-749; CYS-774; ILE-780 AND SER-794.
[158]"Genetic alterations of androgen receptor gene in Japanese human prostate cancer."
Watanabe M., Ushijima T., Shiraishi T., Yatani R., Shimazaki J., Kotake T., Sugimura T., Nagao M.
Jpn. J. Clin. Oncol. 27:389-393(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER IN POLY-GLN REGION; HIS-701 AND ARG-910.
[159]"Androgen receptor gene mutations in prostate cancer."
Wang C., Uchida T.
Nihon Hinyokika Gakkai Zasshi 88:550-556(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER GLN-629.
[160]"DNA analysis of the androgen receptor gene in two cases with complete androgen insensitivity syndrome."
Komori S., Sakata K., Tanaka H., Shima H., Koyama K.
J. Obstet. Gynaecol. Res. 23:277-281(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS ARG-194 AND CYS-855.
[161]"Etiologic classification of severe hypospadias: implications for prognosis and management."
Albers N., Ulrichs C., Gluer S., Hiort O., Sinnecker G.H., Mildenberger H., Brodehl J.
J. Pediatr. 131:386-392(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS ALA-708 AND GLY-870.
[162]"Complete androgen insensitivity syndrome. Molecular characterization in two Chinese women."
Ko T.M., Yang Y.S., Wu M.Y., Kao C.H., Hsu P.M., Chuang S.M., Lee T.Y.
J. Reprod. Med. 42:424-428(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS ASN-732 AND THR-765.
[163]"Wide variation in androgen receptor dysfunction in complete androgen insensitivity syndrome."
Bevan C.L., Hughes I.A., Patterson M.N.
J. Steroid Biochem. Mol. Biol. 61:19-26(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS ASP-750; PHE-762; THR-765; ASN-864 AND PHE-907.
[164]"Androgen receptor point mutations as the underlying molecular defect in 2 patients with androgen insensitivity syndrome."
Radmayr C., Culig Z., Glatzl J., Neuschmid-Kaspar F., Bartsch G., Klocker H.
J. Urol. 158:1553-1556(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS GLY-703, VARIANT AIS LEU-916.
[165]"Molecular analysis of the androgen receptor gene in 4 patients with complete androgen insensitivity."
Komori S., Kasumi H., Sakata K., Tanaka H., Hamada K., Koyama K.
Arch. Gynecol. Obstet. 261:95-100(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS CYS-571; GLN-752 AND CYS-774.
[166]"Mutations of androgen receptor gene in Brazilian patients with male pseudohermaphroditism."
Cabral D.F., Maciel-Guerra A.T., Hackel C.
Braz. J. Med. Biol. Res. 31:775-778(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS HIS-615 AND GLN-752.
[167]"Analysis of the transactivation domain of the androgen receptor in patients with male infertility."
Wang Q., Ghadessy F.J., Yong E.L.
Clin. Genet. 54:185-192(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS ARG-214.
[168]"One additional mutation at exon A amplifies thermolability of androgen receptor in a case with complete androgen insensitivity syndrome."
Tanaka H., Komori S., Sakata K., Shima H., Koyama K.
Gynecol. Endocrinol. 12:75-82(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS PRO-255 AND ALA-820.
[169]"Functional characterisation of mutations in the ligand-binding domain of the androgen receptor gene in patients with androgen insensitivity syndrome."
Lundberg Giwercman Y., Nikoshkov A., Lindsten K., Bystroem B., Pousette A., Chibalin A.V., Arvidsson S., Tiulpakov A., Semitcheva T.V., Peterkova V., Hagenfeldt K., Ritzen E.M., Wedell A.
Hum. Genet. 103:529-531(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS THR-765; TYR-784 AND THR-895, VARIANT PAIS GLY-840.
[170]"A new missense substitution at a mutational hot spot of the androgen receptor in siblings with complete androgen insensitivity syndrome."
Doerk T., Schnieders F., Jakubiczka S., Wieacker P., Schroeder-Kurth T., Schmidtke J.
Hum. Mutat. 11:337-339(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS VAL-695.
[171]"An androgen receptor gene mutation (A645D) in a boy with a normal phenotype."
Nordenskjoeld A., Soederhaell S.
Hum. Mutat. 11:339-339(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-645.
[172]"Single amino acid substitution in the hormone-binding domain of the androgen receptor in a family with complete androgen insensitivity syndrome (CAIS)."
Knoke I., Jakubiczka S., Rohrer T., Hanimann B., Werder E.A., Wieacker P.
Hum. Mutat. 12:220-220(1998)
Cited for: VARIANT AIS LEU-892.
[173]"Response to androgen treatment in a patient with partial androgen insensitivity and a mutation in the deoxyribonucleic acid-binding domain of the androgen receptor."
Weidemann W., Peters B., Romalo G., Spindler K.D., Schweikert H.-U.
J. Clin. Endocrinol. Metab. 83:1173-1176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS GLN-607.
[174]"Trafficking of androgen receptor mutants fused to green fluorescent protein: a new investigation of partial androgen insensitivity syndrome."
Georget V., Terouanne B., Lumbroso S., Nicolas J.C., Sultan C.
J. Clin. Endocrinol. Metab. 83:3597-3603(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS VAL-743 AND CYS-840.
[175]"Azoospermia associated with a mutation in the ligand-binding domain of an androgen receptor displaying normal ligand binding, but defective trans-activation."
Wang Q., Ghadessy F.J., Trounson A., de Kretser D., McLachlan R., Ng S.C., Yong E.L.
J. Clin. Endocrinol. Metab. 83:4303-4309(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS GLU-798.
[176]"Inherited and de novo androgen receptor gene mutations: investigation of single-case families."
Hiort O., Sinnecker G.H., Holterhus P.M., Nitsche E.M., Kruse K.
J. Pediatr. 132:939-943(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS.
[177]"Partial androgen insensitivity and correlations with the predicted three dimensional structure of the androgen receptor ligand-binding domain."
Yong E.L., Tut T.G., Ghadessy F.J., Prins G., Ratnam S.S.
Mol. Cell. Endocrinol. 137:41-50(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS THR-758.
[178]"A new point mutation of the androgen receptor gene in a patient with partial androgen resistance and severe oligozoospermia."
Knoke I., Jakubiczka S., Lehnert H., Wieacker P.
Andrologia 31:199-201(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS LEU-911.
[179]"Selection for androgen receptor mutations in prostate cancers treated with androgen antagonist."
Taplin M.-E., Bubley G.J., Ko Y.J., Small E.J., Upton M., Rajeshkumar B., Balk S.P.
Cancer Res. 59:2511-2515(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER ALA-877 AND ASN-890.
[180]"A novel point mutation (R840S) in the androgen receptor in a Brazilian family with partial androgen insensitivity syndrome."
Melo K.F.S., Latronico A.C., Costa E.M.F., Billerbeck A.E.C., Mendonca B.B., Arnhold I.J.P.
Hum. Mutat. 14:353-353(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS SER-840.
[181]"Analysis of exon 1 mutations in the androgen receptor gene."
Gottlieb B., Vasiliou D.M., Lumbroso R., Beitel L.K., Pinsky L., Trifiro M.A.
Hum. Mutat. 14:527-539(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS ARG-390 AND ARG-443.
[182]"Androgen receptor gene mutations in 46,XY females with germ cell tumours."
Chen C.P., Chern S.R., Wang T.Y., Wang W., Wang K.L., Jeng C.J.
Hum. Reprod. 14:664-670(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS GLN-607, VARIANT AIS LYS-681.
[183]"A case of complete testicular feminization: laparoscopic orchiectomy and analysis of androgen receptor gene mutation."
Kanayama H., Naroda T., Inoue Y., Kurokawa Y., Kagawa S.
Int. J. Urol. 6:327-330(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS LEU-892.
[184]"Discordant measures of androgen-binding kinetics in two mutant androgen receptors causing mild or partial androgen insensitivity, respectively."
Shkolny D.L., Beitel L.K., Ginsberg J., Pekeles G., Arbour L., Pinsky L., Trifiro M.A.
J. Clin. Endocrinol. Metab. 84:805-810(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS ALA-772, VARIANT AIS GLY-871.
[185]"Androgen receptor gene mutations in hormone-refractory prostate cancer."
Wallen M.J., Linja M., Kaartinen K., Schleutker J., Visakorpi T.
J. Pathol. 189:559-563(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER IN POLY-GLN REGION AND ALA-683.
[186]"Two mutations identified in the androgen receptor of the new human prostate cancer cell line MDA PCa 2a."
Zhao X.Y., Boyle B., Krishnan A.V., Navone N.M., Peehl D.M., Feldman D.
J. Urol. 162:2192-2199(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER HIS-701 AND ALA-877.
[187]"Directed pharmacological therapy of ambiguous genitalia due to an androgen receptor gene mutation."
Ong Y.C., Wong H.B., Adaikan G., Yong E.L.
Lancet 354:1444-1445(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PAIS THR-807.
[188]"An androgen receptor mutation in the direct vicinity of the proposed C-terminal alpha-helix of the ligand binding domain containing the AF-2 transcriptional activating function core is associated with complete androgen insensitivity."
Peters I., Weidemann W., Romalo G., Knorr D., Schweikert H.-U., Spindler K.D.
Mol. Cell. Endocrinol. 148:47-53(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS LEU-892.
[189]"A C619Y mutation in the human androgen receptor causes inactivation and mislocalization of the receptor with concomitant sequestration of SRC-1."
Nazareth L.V., Stenoien D.L., Bingman W.E. III, James A.J., Wu C., Zhang Y., Edwards D.P., Mancini M., Marcelli M., Lamb D.J., Weigel N.L.
Mol. Endocrinol. 13:2065-2075(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PROSTATE CANCER TYR-619.
[190]Erratum
Nazareth L.V., Stenoien D.L., Bingman W.E. III, James A.J., Wu C., Zhang Y., Edwards D.P., Mancini M., Marcelli M., Lamb D.J., Weigel N.L.
Mol. Endocrinol. 14:544-544(2000)
[191]"Clinical and molecular spectrum of somatic mosaicism in androgen insensitivity syndrome."
Holterhus P.M., Wiebel J., Sinnecker G.H., Bruggenwirth H.T., Sippell W.G., Brinkmann A.O., Kruse K., Hiort O.
Pediatr. Res. 46:684-690(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS THR-596.
[192]"Point mutations in the steroid-binding domain of the androgen receptor gene of five Japanese patients with androgen insensitivity syndrome."
Yaegashi N., Uehara S., Senoo M., Sato J., Fujiwara J., Funato T., Sasaki T., Yajima A.
Tohoku J. Exp. Med. 187:263-272(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS PHE-812 AND GLN-831.
[193]"Screening for mutations in candidate genes for hypospadias."
Nordenskjoeld A., Friedman E., Tapper-Persson M., Soederhaell C., Leviav A., Svensson J., Anvret M.
Urol. Res. 27:49-55(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS THR-597 AND LEU-725.
[194]"Androgen receptor mutations in prostate cancer."
Marcelli M., Ittmann M., Mariani S., Sutherland R.W., Nigam R., Murthy L., Zhao Y., DiConcini D., Puxeddu E., Esen A., Eastham J., Weigel N.L., Lamb D.J.
Cancer Res. 60:944-949(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PROSTATE CANCER ALA-575; ARG-580; VAL-586; TYR-619; ALA-757 AND GLY-846.
[195]"Phenotypic features, androgen receptor binding, and mutational analysis in 278 clinical cases reported as androgen insensitivity syndrome."
Ahmed S.F., Cheng A., Dovey L., Hawkins J.R., Martin H., Rowland J., Shimura N., Tait A.D., Hughes I.A.
J. Clin. Endocrinol. Metab. 85:658-665(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AIS AND PAIS.
[196]"Eight novel mutations of the androgen receptor gene in patients with androgen insensitivity syndrome."
Chavez B., Mendez J.P., Ulloa-Aguirre A., Larrea F., Vilchis F.
J. Hum. Genet. 46:560-565(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PAIS THR-682 AND GLU-711, VARIANTS AIS GLU-743; VAL-827; ARG-874 AND TYR-879.
[197]"Polymorphism of the androgen receptor gene is associated with male pattern baldness."
Ellis J.A., Stebbing M., Harrap S.B.
J. Invest. Dermatol. 116:452-455(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AGA.
[198]"Characterization of a novel receptor mutation A->T at exon 4 in complete androgen insensitivity syndrome and a carrier sibling via bidirectional polymorphism sequence analysis."
Sills E.S., Sholes T.E., Perloe M., Kaplan C.R., Davis J.G., Tucker M.J.
Int. J. Mol. Med. 9:45-48(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AIS TYR-705.
[199]"Genetic variation in the human androgen receptor gene is the major determinant of common early-onset androgenetic alopecia."
Hillmer A.M., Hanneken S., Ritzmann S., Becker T., Freudenberg J., Brockschmidt F.F., Flaquer A., Freudenberg-Hua Y., Jamra R.A., Metzen C., Heyn U., Schweiger N., Betz R.C., Blaumeiser B., Hampe J., Schreiber S., Schulze T.G., Hennies H.C. expand/collapse author list , Schumacher J., Propping P., Ruzicka T., Cichon S., Wienker T.F., Kruse R., Noethen M.M.
Am. J. Hum. Genet. 77:140-148(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN AGA.
[200]"A family with early-onset and rapidly progressive X-linked spinal and bulbar muscular atrophy."
Echaniz-Laguna A., Rousso E., Anheim M., Cossee M., Tranchant C.
Neurology 64:1458-1460(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SMAX1.
[201]"Human androgen receptor gene ligand-binding-domain mutations leading to disrupted interaction between the N- and C-terminal domains."
Jaeaeskelaeinen J., Deeb A., Schwabe J.W., Mongan N.P., Martin H., Hughes I.A.
J. Mol. Endocrinol. 36:361-368(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS AIS ASN-695; CYS-763; HIS-774; GLU-798; HIS-855 AND PHE-907.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20132 mRNA. Translation: AAA51729.1.
M23263 mRNA. Translation: AAA51775.1.
M27430 expand/collapse EMBL AC list , M27423, M27424, M27425, M27426, M27427, M27428, M27429 Genomic DNA. Translation: AAA51886.1.
M34233 mRNA. Translation: AAA51780.1.
M21748 mRNA. Translation: AAA51771.1.
M35851 expand/collapse EMBL AC list , M35844, M35845, M35846, M35847, M35848, M35849, M35850 Genomic DNA. Translation: AAA51772.1.
AX453758 Unassigned DNA. No translation available.
AL049564, AL158016, AL356358 Genomic DNA. Translation: CAI43080.1.
AL158016, AL049564, AL356358 Genomic DNA. Translation: CAI40853.1.
AL356358, AL049564, AL158016 Genomic DNA. Translation: CAI40496.1.
CH471132 Genomic DNA. Translation: EAX05380.1.
BC132975 mRNA. Translation: AAI32976.1.
L29496 mRNA. Translation: AAA51770.1.
U16371 Genomic DNA. Translation: AAB60346.1.
M20260 mRNA. Translation: AAA51774.1.
S79366 Genomic DNA. Translation: AAB21256.2.
S79366 Genomic DNA. Translation: AAB21257.2.
PIRA39248.
RefSeqNP_000035.2. NM_000044.3.
NP_001011645.1. NM_001011645.2.
UniGeneHs.76704.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E3GX-ray2.40A657-919[»]
1GS4X-ray1.95A670-917[»]
1T5ZX-ray2.30A669-919[»]
1T63X-ray2.07A669-919[»]
1T65X-ray1.66A669-919[»]
1XJ7X-ray2.70A663-919[»]
1XOWX-ray1.80A671-919[»]
B20-30[»]
1XQ3X-ray2.25A671-919[»]
1Z95X-ray1.80A672-916[»]
2AM9X-ray1.64A654-919[»]
2AMAX-ray1.90A654-919[»]
2AMBX-ray1.75A654-919[»]
2AO6X-ray1.89A671-919[»]
2AX6X-ray1.50A664-919[»]
2AX7X-ray1.90A664-919[»]
2AX8X-ray1.70A664-919[»]
2AX9X-ray1.65A664-919[»]
2AXAX-ray1.80A664-919[»]
2HVCX-ray2.10A669-918[»]
2OZ7X-ray1.80A671-919[»]
2PIOX-ray2.03A669-919[»]
2PIPX-ray1.80L669-919[»]
2PIQX-ray2.40A669-919[»]
2PIRX-ray2.10A669-919[»]
2PITX-ray1.76A669-919[»]
2PIUX-ray2.12A669-919[»]
2PIVX-ray1.95A669-919[»]
2PIWX-ray2.58A669-919[»]
2PIXX-ray2.40A669-919[»]
2PKLX-ray2.49A669-919[»]
2PNUX-ray1.65A654-919[»]
2Q7IX-ray1.87A663-919[»]
B20-30[»]
2Q7JX-ray1.90A663-919[»]
2Q7KX-ray1.80A663-919[»]
B20-30[»]
2Q7LX-ray1.92A663-919[»]
2YHDX-ray2.20A671-919[»]
2YLOX-ray2.50A664-919[»]
2YLPX-ray2.30A664-919[»]
2YLQX-ray2.40A664-919[»]
2Z4JX-ray2.60A671-918[»]
3B5RX-ray1.80A671-919[»]
3B65X-ray1.80A671-919[»]
3B66X-ray1.65A671-919[»]
3B67X-ray1.90A671-919[»]
3B68X-ray1.90A671-919[»]
3BTRX-ray2.60B621-635[»]
3L3XX-ray1.55A670-918[»]
3L3ZX-ray2.00A670-918[»]
3RLJX-ray1.90A671-917[»]
3RLLX-ray1.70A671-917[»]
3V49X-ray1.70A654-919[»]
B21-31[»]
3V4AX-ray1.95A671-919[»]
B21-31[»]
3ZQTX-ray2.29A664-919[»]
4HLWX-ray2.50A664-919[»]
DisProtDP00492.
ProteinModelPortalP10275.
SMRP10275. Positions 555-918.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106862. 209 interactions.
DIPDIP-125N.
IntActP10275. 58 interactions.
MINTMINT-94801.
STRING9606.ENSP00000363822.

Chemistry

BindingDBP10275.
ChEMBLCHEMBL1871.
DrugBankDB01128. Bicalutamide.
DB04839. Cyproterone.
DB00858. Dromostanolone.
DB01216. Finasteride.
DB01185. Fluoxymesterone.
DB00499. Flutamide.
DB00984. Nandrolone.
DB00665. Nilutamide.
DB00621. Oxandrolone.
DB00624. Testosterone.
GuidetoPHARMACOLOGY628.

PTM databases

PhosphoSiteP10275.

Polymorphism databases

DMDM113830.

Proteomic databases

PaxDbP10275.
PRIDEP10275.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396043; ENSP00000379358; ENSG00000169083. [P10275-2]
GeneID367.
KEGGhsa:367.

Organism-specific databases

CTD367.
GeneCardsGC0XP066763.
H-InvDBHIX0056152.
HGNCHGNC:644. AR.
HPACAB000001.
MIM300068. phenotype.
312300. phenotype.
313200. phenotype.
313700. gene.
neXtProtNX_P10275.
Orphanet99429. Complete androgen insensitivity syndrome.
440. Familial hypospadias.
481. Kennedy disease.
90797. Partial androgen insensitivity syndrome.
PharmGKBPA57.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245477.
HOVERGENHBG007583.
InParanoidP10275.
KOK08557.
OrthoDBEOG7J17Z7.
PhylomeDBP10275.
TreeFamTF350286.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP10275.

Gene expression databases

ArrayExpressP10275.
BgeeP10275.
CleanExHS_AR.
GenevestigatorP10275.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR001103. Andrgn_rcpt.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF02166. Androgen_recep. 2 hits.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00521. ANDROGENR.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAR. human.
EvolutionaryTraceP10275.
GeneWikiAndrogen_receptor.
GenomeRNAi367.
NextBio1531.
PMAP-CutDBB1AKD7.
PROP10275.
SOURCESearch...

Entry information

Entry nameANDR_HUMAN
AccessionPrimary (citable) accession number: P10275
Secondary accession number(s): A2RUN2, B1AKD7, Q9UD95
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 215 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM