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Protein

Androgen receptor

Gene

AR

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei682 – 6821AndrogenBy similarity
Binding sitei729 – 7291AndrogenBy similarity
Binding sitei854 – 8541AndrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi535 – 60874Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri536 – 55621NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri572 – 59625NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Androgen receptor
Alternative name(s):
Dihydrotestosterone receptor
Nuclear receptor subfamily 3 group C member 4
Gene namesi
Name:AR
Synonyms:NR3C4
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Nucleus By similarity
  • 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 RACK1.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 896896Androgen receptorPRO_0000053710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine; by CDK9By similarity
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei215 – 2151Phosphotyrosine; by CSKBy similarity
Modified residuei248 – 2481PhosphoserineBy similarity
Modified residuei259 – 2591Phosphotyrosine; by CSK and TNK2By similarity
Modified residuei299 – 2991Phosphotyrosine; by CSKBy similarity
Modified residuei338 – 3381Phosphotyrosine; by CSKBy similarity
Modified residuei349 – 3491Phosphotyrosine; by CSKBy similarity
Modified residuei354 – 3541Phosphotyrosine; by CSKBy similarity
Modified residuei355 – 3551Phosphotyrosine; by CSK and TNK2By similarity
Cross-linki378 – 378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei385 – 3851Phosphotyrosine; by CSKBy similarity
Cross-linki497 – 497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei511 – 5111Phosphotyrosine; by CSKBy similarity
Modified residuei528 – 5281Phosphotyrosine; by CSKBy similarity
Modified residuei627 – 6271Phosphoserine; by STK4/MST1By similarity
Cross-linki822 – 822Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki824 – 824Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei892 – 8921Phosphotyrosine; by CSKBy similarity

Post-translational modificationi

Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-511 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-65 by CDK9 regulates AR promoter selectivity and cell growth (By similarity).By similarity
Sumoylated on Lys-378 (major) and Lys-497 (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).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).By similarity

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9GKL7.

Interactioni

Subunit structurei

Binds DNA as a homodimer. Part of a ternary complex containing AR, EFCAB6/DJBP and PARK7. Interacts with HIPK3 and NR0B2 in the presence of androgen. The ligand binding domain interacts with KAT7/HBO1 in the presence of dihydrotestosterone. Interacts with EFCAB6/DJBP, PELP1, PQBP1, RANBP9, RBAK, SPDEF, SRA1, TGFB1I1, 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 RACK1. Interacts with RANBP10; this interaction enhances dihydrotestosterone-induced AR transcriptional activity. Interacts with PRPF6 in a hormone-independent way; this interaction enhances dihydrotestosterone-induced AR transcriptional activity. Interacts with STK4/MST1. Interacts with ZIPK/DAPK3. Interacts with LPXN. Interacts with MAK. Part of a complex containing AR, MAK and NCOA3. Interacts with CRY1. Interacts with CCAR1 and GATA2 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei697 – 6971Interaction with coactivator LXXL motifBy similarity
Sitei874 – 8741Interaction with coactivator FXXLF motifBy similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013166.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 534534ModulatingBy similarityAdd
BLAST
Regioni528 – 896369Interaction with LPXNBy similarityAdd
BLAST
Regioni548 – 63891Interaction with HIPK3By similarityAdd
BLAST
Regioni568 – 896329Interaction with CCAR1By similarityAdd
BLAST
Regioni601 – 896296Interaction with KAT7By similarityAdd
BLAST
Regioni667 – 896230Ligand-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 628Poly-Gln
Compositional biasi69 – 757Poly-Gln
Compositional biasi180 – 18910Poly-Gln
Compositional biasi364 – 37310Poly-Pro
Compositional biasi388 – 3947Poly-Ala
Compositional biasi441 – 4466Poly-Gly

Domaini

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).By similarity

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri536 – 55621NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri572 – 59625NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000037950.
HOVERGENiHBG007583.
InParanoidiQ9GKL7.
KOiK08557.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR001103. Andrgn_rcpt.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF02166. Androgen_recep. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00521. ANDROGENR.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9GKL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVQLGLGRV YPRPPSKTFR GAFQNLFQSV REVIQNPGPR HPEAASAAPP
60 70 80 90 100
GARLQQQQLQ QQETSPRRQQ QQQQQPSEDG SPQVQSRGPT GYLALDEKQQ
110 120 130 140 150
PSQQQSAPEC HPESGCTPEP GAASAASKGL QQQPPAPPDE DDSAAPSTLS
160 170 180 190 200
LLGPTFPGLS SCSTDLKDIL SEAGTMQLLQ QQQQQQQQQE AVSEGNSSGR
210 220 230 240 250
AREATGAPIS SKDSYLGGSS TISDSAKELC KAVSVSMGLG VEALEHLSPG
260 270 280 290 300
EQLRGDCMYA PLLTGPPSVR PTPCAPLAEC KGSLLDDGPG KSNEETAEYS
310 320 330 340 350
PFKAGYTKGL DSESLGCSSG GEAGGSGTLE LPSALSLYKS GALDDVAAYP
360 370 380 390 400
SRDYYNFPLA LAGPPPPPPP PHPHARIKLE NPLDYGSAWA AAAAQCRYGD
410 420 430 440 450
LASLHGGGAP GPGSGSPSAT SSSSWHTLFT AEESQLYGPC GGGGGGSAGE
460 470 480 490 500
AGAVAPYGYT RPPQGLAGQE GDLAIPDIWY PGGVVSRVPY PSPSCVKSEM
510 520 530 540 550
GPWMESYSGP YGDMRLEPTR DHVLPIDYYF PPQKTCLICG DEASGCHYGA
560 570 580 590 600
LTCGSCKVFF KRAAEGKQKY LCASRNDCTI DKFRRKNCPS CRLRKCYEAG
610 620 630 640 650
MTLGARKLKK LGNLKLQEEG EASSATSPTE EPAQKLTVSH IEGYECQPIF
660 670 680 690 700
LNVLEAIEPG VVCAGHDNNQ PDSFAALLSS LNELGERQLV HVVKWAKALP
710 720 730 740 750
GFRNLHVDDQ MAVIQYSWMG LMVFAMGWRS FTNVNSRMLY FAPDLVFNEY
760 770 780 790 800
RMHKSRMYSQ CVRMRHLSQE FGWLQITPQE FLCMKALLLF SIIPVDGLKN
810 820 830 840 850
QKFFDELRMN YIKELDRIIA CKRKNPTSCS RRFYQLTKLL DSVQPIAREL
860 870 880 890
HQFTFDLLIK SHMVSVDFPE MMAEIISVQV PKILSGKVKP IYFHTQ
Length:896
Mass (Da):97,137
Last modified:July 13, 2010 - v3
Checksum:i43DD668E3FFDC796
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131R → W in AAG40566 (PubMed:11086548).Curated
Sequence conflicti75 – 751Missing in AAG40566 (PubMed:11086548).Curated
Sequence conflicti256 – 2561D → G in AAG40566 (PubMed:11086548).Curated
Sequence conflicti323 – 3231A → E in AAG40566 (PubMed:11086548).Curated
Sequence conflicti352 – 3521R → N in AAG37994 (Ref. 1) Curated
Sequence conflicti363 – 3631G → R in AAG40566 (PubMed:11086548).Curated
Sequence conflicti410 – 4101P → S in AAG40566 (PubMed:11086548).Curated
Sequence conflicti820 – 8234ACKR → VMQE in AAG40566 (PubMed:11086548).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF202775 mRNA. Translation: AAG37994.1.
AF161717 mRNA. Translation: AAG40566.1.
RefSeqiNP_999479.2. NM_214314.2.
UniGeneiSsc.6713.

Genome annotation databases

GeneIDi397582.
KEGGissc:397582.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF202775 mRNA. Translation: AAG37994.1.
AF161717 mRNA. Translation: AAG40566.1.
RefSeqiNP_999479.2. NM_214314.2.
UniGeneiSsc.6713.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013166.

Proteomic databases

PaxDbiQ9GKL7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397582.
KEGGissc:397582.

Organism-specific databases

CTDi367.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOGENOMiHOG000037950.
HOVERGENiHBG007583.
InParanoidiQ9GKL7.
KOiK08557.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR001103. Andrgn_rcpt.
IPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF02166. Androgen_recep. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00521. ANDROGENR.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sus scrofa androgen receptor (AR) coding sequence."
    Song J.H., Fahrenkrug S.C., Rohrer G.A., Wise T.H., Ford J.J.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pituitary.
  2. "A highly polymorphic repetitive polypyrimidine/polypurine (CCTTT)n sequence in the 5' untranslated sequence of the porcine androgen receptor gene."
    Trakooljul N., Ponsuksili S., Schellander K., Wimmers K.
    Anim. Genet. 31:288-289(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiANDR_PIG
AccessioniPrimary (citable) accession number: Q9GKL7
Secondary accession number(s): Q9GKN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: July 13, 2010
Last modified: March 16, 2016
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.