P10275 (ANDR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Androgen receptor

Alternative name(s):
Dihydrotestosterone receptor
Nuclear receptor subfamily 3 group C member 4

Gene names

Name:	AR
Synonyms:	DHTR, NR3C4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	919 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism Triplet repeat expansion
Disease	Disease mutation Neurodegeneration Pseudohermaphroditism
Domain	Zinc-finger
Ligand	DNA-binding Lipid-binding Metal-binding Steroid-binding Zinc
Molecular function	Activator Receptor
PTM	Isopeptide bond Lipoprotein Palmitate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of prostate induction by androgen receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara lateral sprouting involved in mammary gland duct morphogenesis Inferred from electronic annotation. Source: Compara male genitalia morphogenesis Inferred from electronic annotation. Source: Compara male gonad development Inferred from electronic annotation. Source: Compara male somatic sex determination Inferred from electronic annotation. Source: Compara mammary gland alveolus development Inferred from electronic annotation. Source: Compara morphogenesis of an epithelial fold Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from direct assay PubMed 21310825. Source: BHF-UCL negative regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of integrin biosynthetic process Inferred from direct assay PubMed 21310825. Source: BHF-UCL organ formation Inferred from electronic annotation. Source: Compara positive regulation of MAPK cascade Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara 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 prostate gland development Non-traceable author statement Ref.23. Source: UniProtKB prostate gland epithelium morphogenesis Inferred from electronic annotation. Source: Compara prostate gland growth Inferred from electronic annotation. Source: Compara protein oligomerization Inferred from direct assay PubMed 18468998. Source: MGI regulation of catalytic activity Inferred from electronic annotation. Source: Compara regulation of developmental growth Inferred from electronic annotation. Source: Compara 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: Compara regulation of systemic arterial blood pressure Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from electronic annotation. Source: Compara sex differentiation Non-traceable author statement Ref.23. Source: UniProtKB tertiary branching involved in mammary gland duct morphogenesis Inferred from electronic annotation. Source: Compara transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transport Traceable author statement PubMed 10835690. Source: ProtInc
Cellular_component	axon Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay PubMed 15572661. Source: UniProtKB dendrite Inferred from electronic annotation. Source: Compara nuclear chromatin Inferred from direct assay PubMed 17277772PubMed 17505061. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from electronic annotation. Source: Compara protein complex Inferred from direct assay PubMed 18468998. Source: MGI
Molecular_function	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 protein dimerization activity Non-traceable author statement Ref.23. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: Compara 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BTG2	P78543	4	EBI-608057,EBI-1047576
CREBBP	Q92793	2	EBI-608057,EBI-81215
CTNNB1	P35222	8	EBI-608057,EBI-491549
DAXX	Q9UER7	5	EBI-608057,EBI-77321
DDC	P20711	2	EBI-608057,EBI-1632155
ERG	P11308	2	EBI-608057,EBI-79704
Foxo1	Q9R1E0	4	EBI-608057,EBI-1371343	From a different organism.
HDAC4	P56524	4	EBI-608057,EBI-308629
HIF1A	Q16665	2	EBI-608057,EBI-447269
JMJD1C	Q15652	2	EBI-608057,EBI-1224969
KAT7	O95251	5	EBI-608057,EBI-473199
MAK	P20794	5	EBI-608057,EBI-3911321
MDM2	Q00987	2	EBI-608057,EBI-389668
NCOA2	Q15596	2	EBI-608057,EBI-81236
NCOA6	Q14686	2	EBI-608057,EBI-78670
PARK7	Q99497	6	EBI-608057,EBI-1164361
PRDX1	Q06830	3	EBI-608057,EBI-353193
RNF14	Q9UBS8	2	EBI-608057,EBI-2130308
RNF6	Q9Y252	10	EBI-608057,EBI-2341483
SUMO1	P63165	7	EBI-608057,EBI-80140

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 919

919

Androgen receptor

PRO_0000053704

Regions

DNA binding

559 – 631

73

Nuclear receptor

Zinc finger

559 – 579

21

NR C4-type

Zinc finger

595 – 619

25

NR C4-type

Region

1 – 558

558

Modulating

Region

551 – 919

369

Interaction with LPXN

Region

571 – 661

91

Interaction with HIPK3 By similarity

Region

624 – 919

296

Interaction with KAT7

Region

690 – 919

230

Ligand-binding

Compositional bias

54 – 57

4

Poly-Leu

Compositional bias

58 – 89

32

Gln-rich

Compositional bias

58 – 78

21

Poly-Gln

Compositional bias

84 – 89

6

Poly-Gln

Compositional bias

193 – 197

5

Poly-Gln

Compositional bias

372 – 381

10

Poly-Pro

Compositional bias

396 – 402

7

Poly-Ala

Compositional bias

449 – 472

24

Poly-Gly

Sites

Binding site

705

1

Androgen

Binding site

752

1

Androgen

Binding site

877

1

Androgen

Site

720

1

Interaction with coactivator LXXL motif

Site

897

1

Interaction with coactivator FXXLF motif

Amino acid modifications

Modified residue

81

1

Phosphoserine; by CDK9 Ref.51

Modified residue

94

1

Phosphoserine Ref.55

Modified residue

223

1

Phosphotyrosine; by CSK Ref.39

Modified residue

267

1

Phosphotyrosine; by CSK and TNK2 Ref.39 Ref.45 Ref.53

Modified residue

307

1

Phosphotyrosine; by CSK Ref.39

Modified residue

346

1

Phosphotyrosine; by CSK Ref.39

Modified residue

357

1

Phosphotyrosine; by CSK Ref.39

Modified residue

362

1

Phosphotyrosine; by CSK Ref.39

Modified residue

363

1

Phosphotyrosine; by CSK and TNK2 Ref.39 Ref.45

Modified residue

393

1

Phosphotyrosine; by CSK Ref.39

Modified residue

534

1

Phosphotyrosine; by CSK Ref.39

Modified residue

551

1

Phosphotyrosine; by CSK Ref.39

Modified residue

650

1

Phosphoserine; by STK4/MST1 Ref.54

Modified residue

915

1

Phosphotyrosine; by CSK Ref.39

Cross-link

386

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28

Cross-link

520

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28

Cross-link

845

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.50

Cross-link

847

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.50

Natural variations

Alternative sequence

1 – 531

531

Missing in isoform 2.

VSP_036889

Alternative sequence

532 – 538

7

GPYGDMR → MILWLHS in isoform 2.

VSP_036890

Natural variant

2

1

E → K in PAIS. Ref.145

VAR_004679

Natural variant

54

1

L → S in prostate cancer.

VAR_004680

Natural variant

57

1

L → Q in prostate cancer.

VAR_004681

Natural variant

64

1

Q → R in prostate cancer.

VAR_009711

Natural variant

74 – 78

5

Missing.

VAR_004682

Natural variant

112

1

Q → H in prostate cancer.

VAR_009712

Natural variant

180

1

K → R in prostate cancer.

VAR_009713

Natural variant

194

1

Q → R in AIS. Ref.160

VAR_009224

Natural variant

205

1

S → R. Ref.94

VAR_009714

Natural variant

214

1

G → R in AIS; 20% lower transactivation capacity. Ref.167

VAR_009715

Natural variant

255

1

L → P in AIS. Ref.168

VAR_009225

Natural variant

266

1

M → T in prostate cancer.

VAR_009716

Natural variant

269

1

P → S in prostate cancer.

VAR_009717

Natural variant

340

1

P → L in prostate cancer. Ref.107

VAR_009718

Natural variant

390

1

P → R in AIS. Ref.181

VAR_009226

Natural variant

390

1

P → S in AIS.

VAR_009227

Natural variant

443

1

Q → R in AIS; might be a polymorphism. Ref.181

VAR_009228

Natural variant

465 – 472

8

Missing.

VAR_004683

Natural variant

491

1

G → S in AIS.

VAR_009719

Natural variant

528

1

D → G in prostate cancer.

VAR_009720

Natural variant

547

1

L → F in PAIS.

VAR_009721

Natural variant

548

1

P → S in AIS. Ref.147

VAR_009722

Natural variant

559

1

C → Y in AIS. Ref.90

VAR_009723

Natural variant

568

1

G → V in a patient with isolated hypospadias. Ref.133

VAR_009725

Natural variant

568

1

G → W in PAIS. Ref.110

VAR_009726

Natural variant

571

1

Y → C in AIS. Ref.165

VAR_009727

Natural variant

573

1

A → D in AIS; defective DNA binding and transactivation. Ref.146

VAR_009728

Natural variant

574

1

L → P in prostate cancer.

VAR_009729

Natural variant

575

1

T → A in prostate cancer. Ref.194

VAR_009730

Natural variant

576

1

C → F in AIS; lack of DNA binding.

VAR_009731

Natural variant

576

1

C → R in AIS. Ref.90

VAR_009732

Natural variant

579

1

C → F in AIS; reduced transcription and DNA binding. Ref.149

VAR_009733

Natural variant

579

1

C → Y in AIS.

VAR_009734

Natural variant

580

1

K → R in prostate cancer. Ref.194

VAR_009735

Natural variant

581

1

V → F in AIS. Ref.95 Ref.106

VAR_009736

Natural variant

582

1

F → S in PAIS. Ref.116

VAR_009737

Natural variant

582

1

F → Y in PAIS. Ref.149

VAR_009738

Natural variant

582

1

Missing in AIS. Ref.115

VAR_009739

Natural variant

585

1

R → K in AIS.

VAR_009740

Natural variant

586

1

A → V in prostate cancer; somatic mutation. Ref.194

VAR_009741

Natural variant

587

1

A → S in prostate cancer; somatic mutation.

VAR_009742

Natural variant

596

1

A → T in AIS; abolishes dimerization. Ref.135 Ref.191

VAR_009743

Natural variant

597

1

S → 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 variant

597

1

S → T in a patient with severe hypospadias. Ref.193

VAR_009745

Natural variant

601

1

C → F in AIS. Ref.117

VAR_009746

Natural variant

604

1

D → Y in PAIS. Ref.116

VAR_009747

Natural variant

607

1

R → Q in PAIS and breast cancer. Ref.92 Ref.139 Ref.173 Ref.182

VAR_004684

Natural variant

608

1

R → K in PAIS and breast cancer; defective nuclear localization. Ref.82 Ref.97 Ref.154

VAR_004685

Natural variant

610

1

N → T in PAIS. Ref.139

VAR_009748

Natural variant

611

1

C → Y in AIS.

VAR_009749

Natural variant

615

1

R → H in AIS and PAIS. Ref.16 Ref.115 Ref.123 Ref.166

VAR_009751

Natural variant

615

1

R → P in AIS.

VAR_009752

Natural variant

615

1

Missing in AIS. Ref.115

VAR_009750

Natural variant

616

1

L → P in AIS. Ref.148

VAR_009753

Natural variant

616

1

L → R in PAIS. Ref.118

VAR_009754

Natural variant

617

1

R → 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 variant

619

1

C → Y in prostate cancer; loss of DNA binding; somatic mutation. Ref.189 Ref.194

VAR_009756

Natural variant

629

1

R → Q in prostate cancer. Ref.159

VAR_009757

Natural variant

630

1

K → T in prostate cancer.

VAR_009758

Natural variant

645

1

A → D. Ref.171
Corresponds to variant rs1800053 [ dbSNP | Ensembl ].

VAR_004686

Natural variant

647

1

S → N in prostate cancer.

VAR_009760

Natural variant

664

1

I → N in AIS and PAIS.

VAR_004687

Natural variant

670

1

Q → R in prostate cancer.

VAR_009761

Natural variant

671

1

P → H in PAIS.

VAR_009762

Natural variant

672

1

I → T in prostate cancer.

VAR_009763

Natural variant

677

1

L → P in AIS. Ref.130

VAR_004688

Natural variant

681

1

E → K in AIS. Ref.100 Ref.182

VAR_009764

Natural variant

682

1

P → T in PAIS. Ref.196

VAR_013474

Natural variant

683

1

G → A in prostate cancer. Ref.153 Ref.185

VAR_009765

Natural variant

684

1

V → I in AIS.

VAR_009766

Natural variant

686

1

C → R in PAIS.

VAR_009767

Natural variant

687

1

A → V in PAIS.

VAR_009768

Natural variant

688

1

G → E in AIS.

VAR_009769

Natural variant

690

1

Missing in PAIS. Ref.114

VAR_009770

Natural variant

692

1

Missing in AIS.

VAR_004689

Natural variant

695

1

D → H in AIS. Ref.18

VAR_004690

Natural variant

695

1

D → N in AIS; almost complete loss of androgen binding and transcription activation. Ref.18 Ref.201

VAR_004691

Natural variant

695

1

D → V in AIS. Ref.170

VAR_004692

Natural variant

700

1

L → M in AIS.

VAR_009771

Natural variant

701

1

L → F in AIS.

VAR_009772

Natural variant

701

1

L → H in AIS and prostate cancer. Ref.103 Ref.158 Ref.186

VAR_009773

Natural variant

702

1

S → A in AIS.

VAR_009774

Natural variant

703

1

S → C in AIS.

VAR_009775

Natural variant

703

1

S → G in PAIS and AIS. Ref.164

VAR_004693

Natural variant

705

1

N → S in AIS. Ref.91 Ref.127

VAR_009776

Natural variant

705

1

N → Y in AIS. Ref.198

VAR_013475

Natural variant

707

1

L → R in AIS. Ref.143

VAR_004694

Natural variant

708

1

G → A in PAIS. Ref.116 Ref.161

VAR_009777

Natural variant

708

1

G → V in AIS.

VAR_009778

Natural variant

710

1

R → T in AIS.

VAR_009779

Natural variant

711

1

Q → E in PAIS. Ref.196

VAR_013476

Natural variant

712

1

L → F in PAIS.

VAR_009780

Natural variant

715

1

V → M in prostate cancer; gain in function. Ref.105

VAR_009781

Natural variant

717

1

K → E in prostate cancer.

VAR_009782

Natural variant

720

1

K → E in prostate cancer; found in bone metastases.

VAR_009783

Natural variant

721

1

A → T in prostate cancer; somatic mutation.

VAR_009784

Natural variant

722

1

L → F in AIS.

VAR_009785

Natural variant

723

1

P → S in AIS.

VAR_009786

Natural variant

724

1

G → D in AIS and prostate cancer.

VAR_009787

Natural variant

725

1

F → L in a patient with severe hypospadias. Ref.127 Ref.193

VAR_009788

Natural variant

726

1

R → L in prostate cancer. Ref.134

VAR_009789

Natural variant

727

1

N → K in AIS. Ref.122

VAR_009790

Natural variant

728

1

L → S in PAIS.

VAR_009791

Natural variant

730

1

V → M in prostate cancer; increases transcription activation. Ref.93 Ref.132

VAR_004695

Natural variant

732

1

D → N in AIS. Ref.162

VAR_004696

Natural variant

732

1

D → Y in AIS.

VAR_004697

Natural variant

733

1

Q → H in PAIS.

VAR_009792

Natural variant

737

1

I → T in PAIS. Ref.127

VAR_009793

Natural variant

741

1

W → R in AIS. Ref.87

VAR_009794

Natural variant

742

1

M → I in PAIS. Ref.141

VAR_004698

Natural variant

742

1

M → V in PAIS. Ref.123

VAR_009795

Natural variant

743

1

G → E in AIS. Ref.196

VAR_013477

Natural variant

743

1

G → V in PAIS and AIS. Ref.99 Ref.102 Ref.106 Ref.174

VAR_004699

Natural variant

744

1

L → F in AIS and prostate cancer.

VAR_009796

Natural variant

745

1

M → T in PAIS. Ref.123

VAR_009797

Natural variant

746

1

V → M in PAIS.

VAR_009798

Natural variant

748

1

A → D in PAIS.

VAR_009799

Natural variant

748

1

A → T in prostate cancer.

VAR_009800

Natural variant

748

1

A → V in prostate cancer.

VAR_009801

Natural variant

749

1

M → I in prostate cancer.

VAR_009802

Natural variant

749

1

M → V in PAIS and AIS. Ref.84 Ref.91 Ref.157

VAR_004700

Natural variant

750

1

G → D in AIS; loss of androgen binding. Ref.163

VAR_004701

Natural variant

750

1

G → S in prostate cancer.

VAR_009803

Natural variant

751

1

W → R in AIS.

VAR_009804

Natural variant

752

1

R → Q in AIS. Ref.165 Ref.166

VAR_004702

Natural variant

754

1

F → L in PAIS and prostate cancer. Ref.116 Ref.139

VAR_009805

Natural variant

754

1

F → V in AIS. Ref.96 Ref.106

VAR_004703

Natural variant

755

1

T → A in prostate cancer.

VAR_009806

Natural variant

756

1

N → S in PAIS.

VAR_009807

Natural variant

757

1

V → A in prostate cancer. Ref.194

VAR_009808

Natural variant

758

1

N → T in PAIS; 50% reduction in transactivation. Ref.177

VAR_009809

Natural variant

759

1

S → F in AIS. Ref.91

VAR_009810

Natural variant

759

1

S → P in prostate cancer.

VAR_009811

Natural variant

762

1

L → F in AIS; loss of androgen binding. Ref.163

VAR_004704

Natural variant

763

1

Y → C in PAIS and prostate cancer; partial loss of androgen binding. Ref.79 Ref.131 Ref.201

VAR_004705

Natural variant

763

1

Y → H in AIS. Ref.127

VAR_009812

Natural variant

764

1

F → L in AIS. Ref.123

VAR_009813

Natural variant

765

1

A → T in AIS; loss of androgen binding. Ref.83 Ref.162 Ref.163 Ref.169

VAR_004707

Natural variant

765

1

A → V in AIS.

VAR_009814

Natural variant

766

1

P → S in AIS.

VAR_009815

Natural variant

767

1

D → E in AIS. Ref.106

VAR_009816

Natural variant

768

1

L → P in AIS.

VAR_009817

Natural variant

771

1

N → H in PAIS. Ref.116

VAR_009818

Natural variant

772

1

E → A in PAIS. Ref.184

VAR_009819

Natural variant

772

1

E → G in PAIS. Ref.154

VAR_009820

Natural variant

774

1

R → C in AIS; loss of androgen binding; frequent mutation. Ref.76 Ref.77 Ref.81 Ref.157 Ref.165

VAR_004709

Natural variant

774

1

R → H in AIS and PAIS; almost complete loss of androgen binding. Ref.81 Ref.91 Ref.127 Ref.201

VAR_004708

Natural variant

779

1

R → W in AIS. Ref.116 Ref.131 Ref.156

VAR_004710

Natural variant

780

1

M → I in PAIS and AIS. Ref.141 Ref.144 Ref.157

VAR_004711

Natural variant

782

1

S → N in prostate cancer; somatic mutation.

VAR_009821

Natural variant

784

1

C → Y in AIS; loss of androgen binding and of transactivation. Ref.169

VAR_004712

Natural variant

787

1

M → V in AIS. Ref.86

VAR_004713

Natural variant

788

1

R → S in AIS.

VAR_009822

Natural variant

790

1

L → F in AIS. Ref.119

VAR_009823

Natural variant

791

1

S → P in prostate cancer.

VAR_009824

Natural variant

793

1

E → D. Ref.94

VAR_009825

Natural variant

794

1

F → S in AIS. Ref.157

VAR_004714

Natural variant

798

1

Q → 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 variant

806

1

C → Y in PAIS.

VAR_009826

Natural variant

807

1

M → R in AIS; loss of transactivation. Ref.98

VAR_004716

Natural variant

807

1

M → T in PAIS. Ref.187

VAR_009827

Natural variant

807

1

M → V in AIS; 25% androgen binding. Ref.131

VAR_004717

Natural variant

812

1

L → F in AIS. Ref.192

VAR_009828

Natural variant

814

1

S → N in AIS and PAIS.

VAR_004718

Natural variant

820

1

G → A in AIS. Ref.168

VAR_009829

Natural variant

821

1

L → V in PAIS.

VAR_009830

Natural variant

827

1

F → V in PAIS. Ref.196

VAR_013478

Natural variant

830

1

L → P in prostate cancer.

VAR_009831

Natural variant

831

1

R → L in AIS. Ref.129

VAR_004719

Natural variant

831

1

R → Q in AIS; loss of androgen binding. Ref.76 Ref.129 Ref.192

VAR_004720

Natural variant

834

1

Y → C in AIS; loss of androgen binding. Ref.87

VAR_009832

Natural variant

840

1

R → C in AIS. Ref.120 Ref.141 Ref.174

VAR_004721

Natural variant

840

1

R → G in PAIS. Ref.169

VAR_004722

Natural variant

840

1

R → H in AIS. Ref.100 Ref.111 Ref.112 Ref.118 Ref.120 Ref.124 Ref.139

VAR_004723

Natural variant

840

1

R → S in PAIS. Ref.180

VAR_009229

Natural variant

841

1

I → S in PAIS.

VAR_009833

Natural variant

842

1

I → T in AIS. Ref.100 Ref.139

VAR_004724

Natural variant

846

1

R → G in prostate cancer. Ref.194

VAR_009834

Natural variant

854

1

R → K in PAIS.

VAR_009835

Natural variant

855

1

R → C in AIS. Ref.91 Ref.106 Ref.131 Ref.140 Ref.160

VAR_004725

Natural variant

855

1

R → H in AIS; strongly reduced transcription activation. Ref.101 Ref.139 Ref.141 Ref.152 Ref.201

VAR_004726

Natural variant

856

1

F → L in AIS.

VAR_009836

Natural variant

863

1

L → R in AIS.

VAR_009837

Natural variant

864

1

D → G in AIS. Ref.91

VAR_009838

Natural variant

864

1

D → N in AIS; loss of androgen binding. Ref.163

VAR_004727

Natural variant

865

1

S → P in AIS.

VAR_009839

Natural variant

866

1

V → E in AIS.

VAR_004728

Natural variant

866

1

V → L in PAIS. Ref.82 Ref.100 Ref.104

VAR_004729

Natural variant

866

1

V → M in AIS and prostate cancer. Ref.4 Ref.76 Ref.104 Ref.139

VAR_004730

Natural variant

869

1

I → M in PAIS. Ref.101 Ref.141

VAR_004731

Natural variant

870

1

A → G in PAIS. Ref.161

VAR_009840

Natural variant

870

1

A → V in PAIS. Ref.113

VAR_009841

Natural variant

871

1

R → G in AIS. Ref.184

VAR_009842

Natural variant

874

1

H → R in AIS. Ref.196

VAR_013479

Natural variant

874

1

H → Y in prostate cancer; increases affinity for testosterone, androgen sensitivity and transcription activation. Ref.65

VAR_009843

Natural variant

877

1

T → 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 variant

877

1

T → S in prostate cancer.

VAR_009844

Natural variant

879

1

D → Y in AIS. Ref.196

VAR_013480

Natural variant

880

1

L → Q in prostate cancer.

VAR_009845

Natural variant

881

1

L → V in AIS. Ref.126

VAR_009846

Natural variant

886

1

M → V in AIS.

VAR_009847

Natural variant

889

1

V → M in AIS and PAIS. Ref.118 Ref.155

VAR_009848

Natural variant

890

1

D → N in prostate cancer. Ref.179

VAR_009849

Natural variant

891

1

F → L in prostate cancer.

VAR_009850

Natural variant

892

1

P → L in AIS. Ref.172 Ref.183 Ref.188

VAR_004733

Natural variant

895

1

M → T in AIS; low androgen binding and transactivation. Ref.61 Ref.169

VAR_004734

Natural variant

896

1

A → T in prostate cancer.

VAR_009851

Natural variant

898

1

I → T in AIS.

VAR_009852

Natural variant

902

1

Q → R in prostate cancer.

VAR_009853

Natural variant

903

1

V → M in PAIS.

VAR_009854

Natural variant

904

1

P → H in AIS.

VAR_009855

Natural variant

904

1

P → S in AIS.

VAR_009856

Natural variant

907

1

L → F in AIS; almost complete loss of transcription activation. Ref.163 Ref.201

VAR_004735

Natural variant

909

1

G → E in prostate cancer.

VAR_009857

Natural variant

909

1

G → R in PAIS. Ref.142

VAR_009858

Natural variant

910

1

K → R in prostate cancer. Ref.158

VAR_009859

Natural variant

911

1

V → L in PAIS. Ref.178

VAR_009860

Natural variant

913

1

P → S in PAIS.

VAR_004736

Natural variant

916

1

F → L in AIS. Ref.164

VAR_009861

Natural variant

917

1

H → R in AIS.

VAR_009862

Natural variant

919

1

Q → R in prostate cancer.

VAR_009863

Experimental info

Mutagenesis

81

1

S → A: Reduced cell growth. Ref.51

Mutagenesis

223

1

Y → F: Decrease of CSK-induced phosphorylation. Ref.39

Mutagenesis

267

1

Y → 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

Mutagenesis

307

1

Y → F: Decrease of CSK-induced phosphorylation. Ref.39

Mutagenesis

346

1

Y → F: Decrease of CSK-induced phosphorylation. Ref.39

Mutagenesis

357

1

Y → F: Decrease of CSK-induced phosphorylation. Ref.39

Mutagenesis

362

1

Y → F: Decrease of CSK-induced phosphorylation. Ref.39

Mutagenesis

363

1

Y → 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

Mutagenesis

393

1

Y → F: Decrease of CSK-induced phosphorylation. Ref.39

Mutagenesis

534

1

Y → F: Greatest decrease of CSK-induced phosphorylation and inhibition of transcriptional activity induced by EGF. Ref.39

Mutagenesis

551

1

Y → F: Decrease in CSK-induced phosphorylation. Ref.39

Mutagenesis

701

1

L → A: Alters receptor specificity, so that transcription is activated by the antiandrogen cyproterone acetate. Ref.64

Mutagenesis

720

1

K → A: Loss of transcription activation in the presence of androgen and of interaction with NCOA2. Ref.60 Ref.65

Mutagenesis

741

1

W → L: Strongly decreased transcription activation in the presence of androgen. Ref.61

Mutagenesis

845

1

K → R: Prevents ubiquitination by RNF6. Prevents AR transcriptional activation by RNF14 in absence of hormone. Ref.50

Mutagenesis

847

1

K → R: Partially prevents ubiquitination by RNF6. Ref.50

Mutagenesis

897

1

E → A or Q: Reduced transcription activation in the presence of androgen. Ref.60 Ref.65

Mutagenesis

897

1

E → K or R: Loss of transcription activation in the presence of androgen. Ref.60 Ref.65

Mutagenesis

915

1

Y → F: Decrease in CSK-induced phosphorylation. Ref.39

Sequence conflict

166

1

G → A in AAA51780. Ref.5

Sequence conflict

212

1

A → R Ref.3

Sequence conflict

212

1

A → R in AAA51771. Ref.6

Sequence conflict

212

1

A → R in AAA51772. Ref.6

Sequence conflict

475

1

G → E in AAA51775. Ref.2

Sequence conflict

475

1

G → E in AAA51770. Ref.12

Sequence conflict

565

1

E → K in AAA51774. Ref.14

Sequence conflict

634

1

L → P in AAB21256. Ref.18

Sequence conflict

634

1

L → P in AAB21257. Ref.18

Sequence conflict

675

1

N → I in AAB21256. Ref.18

Sequence conflict

675

1

N → I in AAB21257. Ref.18

Sequence conflict

810

1

L → M in AAA51780. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

919

Helix Strand Turn

Details...

Beta strand

666 – 668

3

Helix

672 – 680

9

Beta strand

691 – 693

3

Helix

697 – 720

24

Helix

725 – 727

3

Helix

730 – 757

28

Beta strand

760 – 765

6

Beta strand

768 – 770

3

Helix

772 – 777

6

Helix

781 – 796

16

Helix

801 – 812

12

Beta strand

814 – 817

4

Helix

824 – 842

19

Turn

843 – 845

3

Helix

850 – 883

34

Helix

884 – 886

3

Helix

893 – 901

9

Helix

903 – 907

5

Beta strand

910 – 913

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (AR-B) [UniParc]. Last modified April 1, 1990. Version 2. Checksum: 93B096927740B6FF	FASTA	919	98,989
	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
	Isoform 2 (AR-A) (Variant AR45) [UniParc]. Checksum: 495BAE974B4EFC75	FASTA	388	44,643
	10 20 30 40 50 60 MILWLHSLET ARDHVLPIDY YFPPQKTCLI CGDEASGCHY GALTCGSCKV FFKRAAEGKQ 70 80 90 100 110 120 KYLCASRNDC TIDKFRRKNC PSCRLRKCYE AGMTLGARKL KKLGNLKLQE EGEASSTTSP 130 140 150 160 170 180 TEETTQKLTV SHIEGYECQP IFLNVLEAIE PGVVCAGHDN NQPDSFAALL SSLNELGERQ 190 200 210 220 230 240 LVHVVKWAKA LPGFRNLHVD DQMAVIQYSW MGLMVFAMGW RSFTNVNSRM LYFAPDLVFN 250 260 270 280 290 300 EYRMHKSRMY SQCVRMRHLS QEFGWLQITP QEFLCMKALL LFSIIPVDGL KNQKFFDELR 310 320 330 340 350 360 MNYIKELDRI IACKRKNPTS CSRRFYQLTK LLDSVQPIAR ELHQFTFDLL IKSHMVSVDF 370 380 PEMMAEIISV QVPKILSGKV KPIYFHTQ

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY.
[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. , 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.

Web resources

Androgen receptor gene mutations database

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Wikipedia

Androgen receptor entry

X-chromosome gene database, androgen receptor (AR)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M20132 mRNA. Translation: AAA51729.1.
M23263 mRNA. Translation: AAA51775.1.
M27430 , M27423, M27424, M27425, M27426, M27427, M27428, M27429 Genomic DNA. Translation: AAA51886.1.
M34233 mRNA. Translation: AAA51780.1.
M21748 mRNA. Translation: AAA51771.1.
M35851 , 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.

IPI

IPI00020070.
IPI00982907.

PIR

A39248.

RefSeq

NP_000035.2. NM_000044.3.
NP_001011645.1. NM_001011645.2.

UniGene

Hs.76704.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E3G	X-ray	2.40	A	657-919	[»]
1GS4	X-ray	1.95	A	670-917	[»]
1T5Z	X-ray	2.30	A	669-919	[»]
1T63	X-ray	2.07	A	669-919	[»]
1T65	X-ray	1.66	A	669-919	[»]
1XJ7	X-ray	2.70	A	663-919	[»]
1XOW	X-ray	1.80	A	671-919	[»]
			B	20-30	[»]
1XQ3	X-ray	2.25	A	671-919	[»]
1Z95	X-ray	1.80	A	672-916	[»]
2AM9	X-ray	1.64	A	654-919	[»]
2AMA	X-ray	1.90	A	654-919	[»]
2AMB	X-ray	1.75	A	654-919	[»]
2AO6	X-ray	1.89	A	671-919	[»]
2AX6	X-ray	1.50	A	664-919	[»]
2AX7	X-ray	1.90	A	664-919	[»]
2AX8	X-ray	1.70	A	664-919	[»]
2AX9	X-ray	1.65	A	664-919	[»]
2AXA	X-ray	1.80	A	664-919	[»]
2HVC	X-ray	2.10	A	669-918	[»]
2OZ7	X-ray	1.80	A	671-919	[»]
2PIO	X-ray	2.03	A	669-919	[»]
2PIP	X-ray	1.80	L	669-919	[»]
2PIQ	X-ray	2.40	A	669-919	[»]
2PIR	X-ray	2.10	A	669-919	[»]
2PIT	X-ray	1.76	A	669-919	[»]
2PIU	X-ray	2.12	A	669-919	[»]
2PIV	X-ray	1.95	A	669-919	[»]
2PIW	X-ray	2.58	A	669-919	[»]
2PIX	X-ray	2.40	A	669-919	[»]
2PKL	X-ray	2.49	A	669-919	[»]
2PNU	X-ray	1.65	A	654-919	[»]
2Q7I	X-ray	1.87	A	663-919	[»]
			B	20-30	[»]
2Q7J	X-ray	1.90	A	663-919	[»]
2Q7K	X-ray	1.80	A	663-919	[»]
			B	20-30	[»]
2Q7L	X-ray	1.92	A	663-919	[»]
2YHD	X-ray	2.20	A	671-919	[»]
2YLO	X-ray	2.50	A	664-919	[»]
2YLP	X-ray	2.30	A	664-919	[»]
2YLQ	X-ray	2.40	A	664-919	[»]
2Z4J	X-ray	2.60	A	671-918	[»]
3B5R	X-ray	1.80	A	671-919	[»]
3B65	X-ray	1.80	A	671-919	[»]
3B66	X-ray	1.65	A	671-919	[»]
3B67	X-ray	1.90	A	671-919	[»]
3B68	X-ray	1.90	A	671-919	[»]
3BTR	X-ray	2.60	B	621-635	[»]
3L3X	X-ray	1.55	A	670-918	[»]
3L3Z	X-ray	2.00	A	670-918	[»]
3RLJ	X-ray	1.90	A	671-917	[»]
3RLL	X-ray	1.70	A	671-917	[»]
3V49	X-ray	1.70	A	654-919	[»]
			B	21-31	[»]
3V4A	X-ray	1.95	A	671-919	[»]
			B	21-31	[»]
3ZQT	X-ray	2.29	A	664-919	[»]
4HLW	X-ray	2.50	A	664-919	[»]

DisProt

DP00492.

ProteinModelPortal

P10275.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-125N.

IntAct

P10275. 40 interactions.

MINT

MINT-94801.

STRING

9606.ENSP00000363822.

PTM databases

PhosphoSite

P10275.

Polymorphism databases

DMDM

113830.

Proteomic databases

PaxDb

P10275.

PRIDE

P10275.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374690; ENSP00000363822; ENSG00000169083.
ENST00000396043; ENSP00000379358; ENSG00000169083.

GeneID

367.

KEGG

hsa:367.

Organism-specific databases

CTD

367.

GeneCards

GC0XP066763.

H-InvDB

HIX0056152.

HGNC

HGNC:644. AR.

HPA

CAB000001.

MIM

300068. phenotype.
312300. phenotype.
313200. phenotype.
313700. gene.

neXtProt

NX_P10275.

Orphanet

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

PharmGKB

PA57.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG245477.

HOVERGEN

HBG007583.

InParanoid

P10275.

KO

K08557.

OrthoDB

EOG4XPQFV.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.
hnf3apathway. FOXA1 transcription factor network.
ar_tf_pathway. Regulation of Androgen receptor activity.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P10275.

Bgee

P10275.

CleanEx

HS_AR.

Genevestigator

P10275.

GermOnline

ENSG00000169083. Homo sapiens.

Family and domain databases

Gene3D

1.10.565.10. 2 hits.
3.30.50.10. 1 hit.

InterPro

IPR001103. 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]

Pfam

PF02166. Androgen_recep. 2 hits.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR00521. ANDROGENR.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P10275.

ChEMBL

CHEMBL1871.

ChiTaRS

AR. human.

DrugBank

DB01128. Bicalutamide.
DB04839. Cyproterone.
DB00858. Dromostanolone.
DB01216. Finasteride.
DB01185. Fluoxymesterone.
DB00499. Flutamide.
DB00984. Nandrolone.
DB00665. Nilutamide.
DB00621. Oxandrolone.
DB00624. Testosterone.

EvolutionaryTrace

P10275.

GenomeRNAi

367.

NextBio

1531.

PMAP-CutDB

B1AKD7.

SOURCE

Search...

Entry information

Entry name

ANDR_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 205 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.