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P15207 (ANDR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Androgen receptor
Alternative name(s):
Dihydrotestosterone receptor
Nuclear receptor subfamily 3 group C member 4
Gene names
Name:Ar
Synonyms:Nr3c4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length902 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins. Transcription activation is down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3 By similarity. Ref.9 Ref.10

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. 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. Interacts with CRY1. Ref.4 Ref.5 Ref.7

Subcellular location

Nucleus. Cytoplasm By similarity. 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 By similarity. Ref.4

Tissue specificity

Highest levels in the seminal vesicle, ventral prostate and coagulating gland with lower levels in the kidney and levator ani muscle.

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 By similarity.

Post-translational modification

Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-517 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression By similarity. Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity. Phosphorylation at Ser-61 by CDK9 regulates AR promoter selectivity and cell growth. Phosphorylation by PAK6 leads to AR-mediated transcription inhibition By similarity.

Sumoylated on Lys-384 (major) and Lys-503 By similarity. Ubiquitinated. Deubiquitinated by USP26 By similarity. 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity By similarity.

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 By similarity.

Involvement in disease

Defects in Ar are a cause of androgen insensitivity. Rats with this syndrome are called testicular feminized (TFM). Ref.3

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.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DiseaseDisease mutation
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Steroid-binding
Zinc
   Molecular functionReceptor
   PTMIsopeptide bond
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of prostate induction by androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

androgen receptor signaling pathway

Inferred from mutant phenotype Ref.3. Source: RGD

cellular response to steroid hormone stimulus

Inferred from expression pattern Ref.3. Source: RGD

epithelial cell differentiation involved in prostate gland development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

intracellular receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

lateral sprouting involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

male genitalia morphogenesis

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

male sex differentiation

Inferred from mutant phenotype Ref.3. Source: RGD

male somatic sex determination

Inferred from electronic annotation. Source: Ensembl

mammary gland alveolus development

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelial fold

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of integrin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

organ formation

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

prostate gland epithelium morphogenesis

Inferred from electronic annotation. Source: Ensembl

prostate gland growth

Inferred from electronic annotation. Source: Ensembl

regulation of catalytic activity

Inferred from electronic annotation. Source: Ensembl

regulation of developmental growth

Inferred from electronic annotation. Source: Ensembl

regulation of establishment of protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of prostatic bud formation

Inferred from electronic annotation. Source: Ensembl

regulation of systemic arterial blood pressure

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from expression pattern PubMed 15596216. Source: RGD

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

tertiary branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from direct assay PubMed 12865346. Source: RGD

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from direct assay PubMed 12865346. Source: RGD

nuclear chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Traceable author statement PubMed 12865346. Source: RGD

androgen binding

Inferred from mutant phenotype Ref.3. Source: RGD

androgen receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

androgen receptor binding

Inferred from physical interaction PubMed 9710597. Source: RGD

beta-catenin binding

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 17223690. Source: RGD

receptor binding

Inferred from physical interaction PubMed 11875111. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 902902Androgen receptor
PRO_0000053712

Regions

DNA binding541 – 61474Nuclear receptor
Zinc finger542 – 56221NR C4-type
Zinc finger578 – 60225NR C4-type
Region1 – 540540Modulating
Region534 – 902369Interaction with LPXN By similarity
Region554 – 64491Interaction with HIPK3
Region607 – 902296Interaction with KAT7 By similarity
Region673 – 902230Ligand-binding
Compositional bias63 – 675Poly-Arg
Compositional bias174 – 19522Poly-Gln
Compositional bias370 – 3767Poly-Pro
Compositional bias394 – 4007Poly-Ala
Compositional bias444 – 4507Poly-Gly

Sites

Binding site6881Androgen
Binding site7351Androgen
Binding site8601Androgen
Site7031Interaction with coactivator LXXL motif By similarity
Site8801Interaction with coactivator FXXLF motif By similarity

Amino acid modifications

Modified residue611Phosphoserine; by CDK9 By similarity
Modified residue751Phosphoserine By similarity
Modified residue2211Phosphotyrosine; by CSK By similarity
Modified residue2651Phosphotyrosine; by CSK and TNK2 By similarity
Modified residue3051Phosphotyrosine; by CSK By similarity
Modified residue3441Phosphotyrosine; by CSK By similarity
Modified residue3551Phosphotyrosine; by CSK By similarity
Modified residue3601Phosphotyrosine; by CSK By similarity
Modified residue3611Phosphotyrosine; by CSK and TNK2 By similarity
Modified residue3911Phosphotyrosine; by CSK By similarity
Modified residue5171Phosphotyrosine; by CSK By similarity
Modified residue5341Phosphotyrosine; by CSK By similarity
Modified residue6331Phosphoserine; by STK4/MST1 By similarity
Modified residue8981Phosphotyrosine; by CSK By similarity
Cross-link384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link828Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link830Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant7351R → Q in TFM; has only 10-15% of the androgen-binding capacity of wild-type AR. Ref.3

Experimental info

Sequence conflict1951Missing in AAA40734. Ref.3
Sequence conflict3891S → L in AAA40759. Ref.2

Secondary structure

................................................. 902
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15207 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 43F4064759FDCBED

FASTA90298,218
        10         20         30         40         50         60 
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAASIAPP GACLQQRQET 

        70         80         90        100        110        120 
SPRRRRRQQH PEDGSPQAHI RGTTGYLALE EEQQPSQQQS ASEGHPESGC LPEPGAATAP 

       130        140        150        160        170        180 
GKGLPQQPPA PPDQDDSAAP STLSLLGPTF PGLSSCSADI KDILSEAGTM QLLQQQQQQQ 

       190        200        210        220        230        240 
QQQQQQQQQQ QQQQQEVISE GSSSVRAREA TGAPSSSKDS YLGGNSTISD SAKELCKAVS 

       250        260        270        280        290        300 
VSMGLGVEAL EHLSPGEQLR GDCMYASLLG GPPAVRPTPC APLAECKGLS LDEGPGKGTE 

       310        320        330        340        350        360 
ETAEYSSFKG GYAKGLEGES LGCSGSSEAG SSGTLEIPSS LSLYKSGAVD EAAAYQNRDY 

       370        380        390        400        410        420 
YNFPLALSGP PHPPPPTHPH ARIKLENPSD YGSAWAAAAA QCRYGDLASL HGGSVAGPST 

       430        440        450        460        470        480 
GSPPATASSS WHTLFTAEEG QLYGPGGGGG SSSPSDAGPV APYGYTRPPQ GLASQEGDFS 

       490        500        510        520        530        540 
ASEVWYPGGV VNRVPYPSPS CVKSEMGPWM ENYSGPYGDM RLDSTRDHVL PIDYYFPPQK 

       550        560        570        580        590        600 
TCLICGDEAS GCHYGALTCG SCKVFFKRAA EGKQKYLCAS RNDCTIDKFR RKNCPSCRLR 

       610        620        630        640        650        660 
KCYEAGMTLG ARKLKKLGNL KLQEEGENSS AGSPTEDPSQ KMTVSHIEGY ECQPIFLNVL 

       670        680        690        700        710        720 
EAIEPGVVCA GHDNNQPDSF AALLSSLNEL GERQLVHVVK WAKALPGFRN LHVDDQMAVI 

       730        740        750        760        770        780 
QYSWMGLMVF AMGWRSFTNV NSRMLYFAPD LVFNEYRMHK SRMYSQCVRM RHLSQEFGWL 

       790        800        810        820        830        840 
QITPQEFLCM KALLLFSIIP VDGLKNQKFF DELRMNYIKE LDRIIACKRK NPTSCSRRFY 

       850        860        870        880        890        900 
QLTKLLDSVQ PIARELHQFT FDLLIKSHMV SVDFPEMMAE IISVQVPKIL SGKVKPIYFH 


TQ 

« Hide

References

[1]"The rat androgen receptor: primary structure, autoregulation of its messenger ribonucleic acid, and immunocytochemical localization of the receptor protein."
Tan J., Joseph D.R., Quarmby V.E., Lubahn D.B., Sar M., French F.S., Wilson E.M.
Mol. Endocrinol. 2:1276-1285(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Prostate.
[3]"A single base mutation in the androgen receptor gene causes androgen insensitivity in the testicular feminized rat."
Yarbrough W.G., Quarmby V.E., Simental J.A., Joseph D.R., Sar M., Lubahn D.B., Olsen K.L., French F.S., Wilson E.M.
J. Biol. Chem. 265:8893-8900(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TFM GLN-735.
[4]"Activation of androgen receptor function by a novel nuclear protein kinase."
Moilanen A.-M., Karvonen U., Poukka H., Jaenne O.A., Palvimo J.J.
Mol. Biol. Cell 9:2527-2543(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK3, SUBCELLULAR LOCATION.
Tissue: Testis.
[5]"A novel steroid receptor co-activator protein (SRAP) as an alternative form of steroid receptor RNA-activator gene: expression in prostate cancer cells and enhancement of androgen receptor activity."
Kawashima H., Takano H., Sugita S., Takahara Y., Sugimura K., Nakatani T.
Biochem. J. 369:163-171(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRA1.
[6]"Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone."
Sack J.S., Kish K.F., Wang C., Attar R.M., Kiefer S.E., An Y., Wu G.Y., Scheffler J.E., Salvati M.E., Krystek S.R. Jr., Weinmann R., Einspahr H.M.
Proc. Natl. Acad. Sci. U.S.A. 98:4904-4909(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 647-902 OF MUTANT ALA-860 IN COMPLEX WITH DIHYDROTESTOSTERONE.
[7]"Structural basis of androgen receptor binding to selective androgen response elements."
Shaffer P.L., Jivan A., Dollins D.E., Claessens F., Gewirth D.T.
Proc. Natl. Acad. Sci. U.S.A. 101:4758-4763(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 533-637 IN COMPLEX WITH DNA AND ZINC IONS, SUBUNIT.
[8]"Structure based approach to the design of bicyclic-1H-isoindole-1,3(2H)-dione based androgen receptor antagonists."
Salvati M.E., Balog A., Shan W., Wei D.D., Pickering D., Attar R.M., Geng J., Rizzo C.A., Gottardis M.M., Weinmann R., Krystek S.R., Sack J., An Y., Kish K.
Bioorg. Med. Chem. Lett. 15:271-276(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 647-902 OF MUTANT ALA-860 IN COMPLEX WITH SYNTHETIC ANTAGONIST.
[9]"Discovery of potent, orally-active, and muscle-selective androgen receptor modulators based on an N-aryl-hydroxybicyclohydantoin scaffold."
Sun C., Robl J.A., Wang T.C., Huang Y., Kuhns J.E., Lupisella J.A., Beehler B.C., Golla R., Sleph P.G., Seethala R., Fura A., Krystek S.R. Jr., An Y., Malley M.F., Sack J.S., Salvati M.E., Grover G.J., Ostrowski J., Hamann L.G.
J. Med. Chem. 49:7596-7599(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 647-902 IN COMPLEX WITH SYNTHETIC ANDROGEN ANTAGONIST, FUNCTION.
[10]"Pharmacological and X-ray structural characterization of a novel selective androgen receptor modulator: potent hyperanabolic stimulation of skeletal muscle with hypostimulation of prostate in rats."
Ostrowski J., Kuhns J.E., Lupisella J.A., Manfredi M.C., Beehler B.C., Krystek S.R. Jr., Bi Y., Sun C., Seethala R., Golla R., Sleph P.G., Fura A., An Y., Kish K.F., Sack J.S., Mookhtiar K.A., Grover G.J., Hamann L.G.
Endocrinology 148:4-12(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 647-902 IN COMPLEX WITH THE SYNTHETIC AGONIST MBS-564929, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20133 mRNA. Translation: AAA40733.1.
M23264 mRNA. Translation: AAA40759.1.
J05454 Genomic DNA. Translation: AAA40734.1.
PIRB40494.
RefSeqNP_036634.1. NM_012502.1.
UniGeneRn.9813.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I37X-ray2.00A647-902[»]
1I38X-ray2.00A647-902[»]
1R4IX-ray3.10A/B533-637[»]
1XNNX-ray2.20A647-902[»]
2IHQX-ray2.00A647-902[»]
2NW4X-ray3.00A647-902[»]
3G0WX-ray1.95A647-902[»]
ProteinModelPortalP15207.
SMRP15207. Positions 538-611, 646-901.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246396. 2 interactions.
DIPDIP-5963N.
IntActP15207. 1 interaction.
STRING10116.ENSRNOP00000009129.

Chemistry

BindingDBP15207.
ChEMBLCHEMBL3072.
GuidetoPHARMACOLOGY628.

PTM databases

PhosphoSiteP15207.

Proteomic databases

PaxDbP15207.
PRIDEP15207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000009129; ENSRNOP00000009129; ENSRNOG00000005639.
GeneID24208.
KEGGrno:24208.

Organism-specific databases

CTD367.
RGD2147. Ar.

Phylogenomic databases

eggNOGNOG245477.
GeneTreeENSGT00730000110451.
HOGENOMHOG000254783.
HOVERGENHBG007583.
InParanoidP15207.
KOK08557.
OrthoDBEOG7J17Z7.
PhylomeDBP15207.
TreeFamTF350286.

Gene expression databases

GenevestigatorP15207.

Family and domain databases

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

Other

EvolutionaryTraceP15207.
NextBio602605.
PROP15207.

Entry information

Entry nameANDR_RAT
AccessionPrimary (citable) accession number: P15207
Secondary accession number(s): Q63049
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references