P15207 (ANDR_RAT) 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:	Nr3c4

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	902 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 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, SPDEF, SRA1, TGFB1I1, ZNF318 and RREB1. 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 ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its transactivation activity. Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts with RBAK. Interacts via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts with HIP1 (via coiled coil domain) By similarity. Interacts with MACROD1 By similarity. Interacts (via ligand-binding domain) with TRIM68 By similarity. Interacts with TNK2 By similarity. Interacts with USP26 By similarity. Interacts with RNF6 By similarity. Interacts (regulated by RNF6 probably through polyubiquitination) with RNF14; regulates AR transcriptional activity. Interacts with PRMT2 and TRIM24. Interacts with GNB2L1/RACK1 By similarity. Interacts with RANBP10; this interaction enhances hormone-induced AR transcriptional activity By similarity. Interacts with PRPF6 in a hormone-independent way; this interaction enhances hormone-induced AR transcriptional activity. Interacts with STK4/MST1 By similarity. Interacts with ZIPK/DAPK3 By similarity. Interacts with LPXN By similarity. Interacts with MAK By similarity. Part of a complex containing AR, MAK and NCOA3 By similarity. 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Disease	Disease mutation
Domain	Zinc-finger
Ligand	DNA-binding Lipid-binding Metal-binding Steroid-binding Zinc
Molecular function	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 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 sex differentiation Inferred from mutant phenotype Ref.3. Source: RGD 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 sequence or structural similarity. Source: UniProtKB negative regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of integrin biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB 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 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: Compara positive regulation of integrin biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of intracellular estrogen receptor signaling pathway Inferred from electronic annotation. Source: Compara 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 from RNA polymerase III promoter Inferred from electronic annotation. Source: Compara prostate gland epithelium morphogenesis Inferred from electronic annotation. Source: Compara prostate gland growth Inferred from electronic annotation. Source: Compara protein oligomerization Inferred from electronic annotation. Source: Compara 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 sequence or structural similarity. Source: UniProtKB 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 expression pattern PubMed 15596216. Source: RGD tertiary branching involved in mammary gland duct morphogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	axon 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 plasma membrane Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	androgen binding Inferred from mutant phenotype Ref.3. Source: RGD androgen receptor activity Inferred from sequence or structural similarity. Source: UniProtKB beta-catenin binding Inferred from sequence or structural similarity. Source: UniProtKB chromatin binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding Inferred from electronic annotation. Source: Compara 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 902

902

Androgen receptor

PRO_0000053712

Regions

DNA binding

541 – 614

74

Nuclear receptor

Zinc finger

542 – 562

21

NR C4-type

Zinc finger

578 – 602

25

NR C4-type

Region

1 – 540

540

Modulating

Region

534 – 902

369

Interaction with LPXN By similarity

Region

554 – 644

91

Interaction with HIPK3

Region

607 – 902

296

Interaction with KAT7 By similarity

Region

673 – 902

230

Ligand-binding

Compositional bias

63 – 67

5

Poly-Arg

Compositional bias

174 – 195

22

Poly-Gln

Compositional bias

370 – 376

7

Poly-Pro

Compositional bias

394 – 400

7

Poly-Ala

Compositional bias

444 – 450

7

Poly-Gly

Sites

Binding site

688

1

Androgen

Binding site

735

1

Androgen

Binding site

860

1

Androgen

Site

703

1

Interaction with coactivator LXXL motif By similarity

Site

880

1

Interaction with coactivator FXXLF motif By similarity

Amino acid modifications

Modified residue

61

1

Phosphoserine; by CDK9 By similarity

Modified residue

75

1

Phosphoserine By similarity

Modified residue

221

1

Phosphotyrosine; by CSK By similarity

Modified residue

265

1

Phosphotyrosine; by CSK and TNK2 By similarity

Modified residue

305

1

Phosphotyrosine; by CSK By similarity

Modified residue

344

1

Phosphotyrosine; by CSK By similarity

Modified residue

355

1

Phosphotyrosine; by CSK By similarity

Modified residue

360

1

Phosphotyrosine; by CSK By similarity

Modified residue

361

1

Phosphotyrosine; by CSK and TNK2 By similarity

Modified residue

391

1

Phosphotyrosine; by CSK By similarity

Modified residue

517

1

Phosphotyrosine; by CSK By similarity

Modified residue

534

1

Phosphotyrosine; by CSK By similarity

Modified residue

633

1

Phosphoserine; by STK4/MST1 By similarity

Modified residue

898

1

Phosphotyrosine; by CSK By similarity

Cross-link

384

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

503

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

828

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

830

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant

735

1

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

Experimental info

Sequence conflict

195

1

Missing in AAA40734. Ref.3

Sequence conflict

389

1

S → L in AAA40759. Ref.2

Secondary structure

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902

Helix Strand Turn

Details...

Beta strand

543 – 545

3

Beta strand

551 – 553

3

Beta strand

556 – 558

3

Helix

560 – 570

11

Beta strand

579 – 582

4

Turn

588 – 593

6

Helix

595 – 605

11

Helix

655 – 663

9

Beta strand

674 – 676

3

Helix

680 – 703

24

Helix

708 – 710

3

Helix

713 – 740

28

Beta strand

743 – 748

6

Beta strand

751 – 753

3

Helix

755 – 760

6

Helix

764 – 779

16

Helix

784 – 795

12

Beta strand

797 – 800

4

Helix

807 – 826

20

Beta strand

827 – 829

3

Helix

833 – 866

34

Helix

867 – 869

3

Helix

876 – 884

9

Helix

886 – 890

5

Beta strand

893 – 896

4

Sequences

	Sequence		Length	Mass (Da)
	P15207 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 43F4064759FDCBED	FASTA	902	98,218
	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

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.

IPI

IPI00207089.

PIR

B40494.

RefSeq

NP_036634.1. NM_012502.1.

UniGene

Rn.9813.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I37	X-ray	2.00	A	647-902	[»]
1I38	X-ray	2.00	A	647-902	[»]
1R4I	X-ray	3.10	A/B	533-637	[»]
1XNN	X-ray	2.20	A	647-902	[»]
2IHQ	X-ray	2.00	A	647-902	[»]
2NW4	X-ray	3.00	A	647-902	[»]
3G0W	X-ray	1.95	A	647-902	[»]

ProteinModelPortal

P15207.

SMR

P15207. Positions 538-611, 646-901.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5963N.

IntAct

P15207. 1 interaction.

STRING

10116.ENSRNOP00000009129.

PTM databases

PhosphoSite

P15207.

Proteomic databases

PaxDb

P15207.

PRIDE

P15207.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000009129; ENSRNOP00000009129; ENSRNOG00000005639.

GeneID

24208.

KEGG

rno:24208.

Organism-specific databases

CTD

367.

RGD

2147. Ar.

Phylogenomic databases

eggNOG

NOG245477.

GeneTree

ENSGT00700000104072.

HOGENOM

HOG000254783.

HOVERGEN

HBG007583.

InParanoid

P15207.

KO

K08557.

OrthoDB

EOG4XPQFV.

Gene expression databases

Genevestigator

P15207.

GermOnline

ENSRNOG00000005639. Rattus norvegicus.

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. 1 hit.
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

P15207.

ChEMBL

CHEMBL3072.

EvolutionaryTrace

P15207.

NextBio

602605.

Entry information

Entry name

ANDR_RAT

Accession

Primary (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:	April 3, 2013
This is version 150 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program