Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q6QT55

- ANDR_MACMU

UniProt

Q6QT55 - ANDR_MACMU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Androgen receptor

Gene

AR

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed - 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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei681 – 6811AndrogenBy similarity
Sitei696 – 6961Interaction with coactivator LXXL motifBy similarity
Binding sitei728 – 7281AndrogenBy similarity
Binding sitei853 – 8531AndrogenBy similarity
Sitei873 – 8731Interaction with coactivator FXXLF motifBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi534 – 60774Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri535 – 55521NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri571 – 59525NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. androgen receptor activity Source: UniProtKB
  2. beta-catenin binding Source: UniProtKB
  3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
  4. sequence-specific DNA binding Source: InterPro
  5. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  6. steroid binding Source: UniProtKB-KW
  7. transcription regulatory region DNA binding Source: UniProtKB
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. androgen receptor signaling pathway Source: UniProtKB
  2. intracellular receptor signaling pathway Source: BHF-UCL
  3. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  4. negative regulation of integrin biosynthetic process Source: UniProtKB
  5. positive regulation of cell proliferation Source: UniProtKB
  6. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  7. positive regulation of phosphorylation Source: UniProtKB
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  10. regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  11. transcription, DNA-templated Source: UniProtKB
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
OrganismiMacaca mulatta (Rhesus macaque)
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
ProteomesiUP000006718: Unplaced

Subcellular locationi

Nucleus PROSITE-ProRule annotation. 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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nuclear chromatin Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 895895Androgen receptorPRO_0000053706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine; by CDK9By similarity
Modified residuei79 – 791PhosphoserineBy similarity
Modified residuei208 – 2081Phosphotyrosine; by CSKBy similarity
Modified residuei252 – 2521Phosphotyrosine; by CSK and TNK2By similarity
Modified residuei292 – 2921Phosphotyrosine; by CSKBy similarity
Modified residuei331 – 3311Phosphotyrosine; by CSKBy similarity
Modified residuei342 – 3421Phosphotyrosine; by CSKBy similarity
Modified residuei347 – 3471Phosphotyrosine; by CSKBy similarity
Modified residuei348 – 3481Phosphotyrosine; by CSK and TNK2By similarity
Cross-linki371 – 371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei378 – 3781Phosphotyrosine; by CSKBy similarity
Cross-linki496 – 496Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei510 – 5101Phosphotyrosine; by CSKBy similarity
Modified residuei527 – 5271Phosphotyrosine; by CSKBy similarity
Modified residuei626 – 6261Phosphoserine; by STK4/MST1By similarity
Cross-linki821 – 821Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki823 – 823Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei891 – 8911Phosphotyrosine; 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-510 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-371 (major) and Lys-496 (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

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 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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6QT55.
SMRiQ6QT55. Positions 531-604, 639-894.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 533533ModulatingBy similarityAdd
BLAST
Regioni527 – 895369Interaction with LPXNBy similarityAdd
BLAST
Regioni600 – 895296Interaction with KAT7By similarityAdd
BLAST
Regioni666 – 895230Ligand-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 628Poly-Gln
Compositional biasi68 – 747Poly-Gln
Compositional biasi178 – 1825Poly-Gln
Compositional biasi357 – 36610Poly-Pro
Compositional biasi381 – 3877Poly-Ala
Compositional biasi434 – 44815Poly-GlyAdd
BLAST

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 fingeri535 – 55521NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri571 – 59525NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG245477.
HOGENOMiHOG000254783.
HOVERGENiHBG007583.
InParanoidiQ6QT55.
KOiK08557.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR001103. 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]
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.

Q6QT55-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP
60 70 80 90 100
GASLQQQQQQ QQETSPRQQQ QQQQGEDGSP QAHRRGPTGY LVLDEEQQPS
110 120 130 140 150
QPQSAPECHP ERGCVPEPGA AVAAGKGLPQ QLPAPPDEDD SAAPSTLSLL
160 170 180 190 200
GPTFPGLSSC SADLKDILSE ASTMQLLQQQ QQEAVSEGSS SGRAREASGA
210 220 230 240 250
PTSSKDNYLE GTSTISDSAK ELCKAVSVSM GLGVEALEHL SPGEQLRGDC
260 270 280 290 300
MYAPVLGVPP AVRPTPCAPL AECKGSLLDD SAGKSTEDTA EYSPFKGGYT
310 320 330 340 350
KGLEGESLGC SGSAAAGSSG TLELPSTLSL YKSGALDEAA AYQSRDYYNF
360 370 380 390 400
PLALAGPPPP PPPPHPHARI KLENPLDYGS AWAAAAAQCR YGDLASLHGA
410 420 430 440 450
GAAGPGSGSP SAAASSSWHT LFTAEEGQLY GPCGGGGGGG GGGGGGAGEA
460 470 480 490 500
GAVAPYGYTR PPQGLAGQEG DFTAPDVWYP GGMVSRVPYP SPTCVKSEMG
510 520 530 540 550
PWMDSYSGPY GDMRLETARD HVLPIDYYFP PQKTCLICGD EASGCHYGAL
560 570 580 590 600
TCGSCKVFFK RAAEGKQKYL CASRNDCTID KFRRKNCPSC RLRKCYEAGM
610 620 630 640 650
TLGARKLKKL GNLKLQEEGE ASSTTSPTEE TAQKLTVSHI EGYECQPIFL
660 670 680 690 700
NVLEAIEPGV VCAGHDNNQP DSFAALLSSL NELGERQLVH VVKWAKALPG
710 720 730 740 750
FRNLHVDDQM AVIQYSWMGL MVFAMGWRSF TNVNSRMLYF APDLVFNEYR
760 770 780 790 800
MHKSRMYSQC VRMRHLSQEF GWLQITPQEF LCMKALLLFS IIPVDGLKNQ
810 820 830 840 850
KFFDELRMNY IKELDRIIAC KRKNPTSCSR RFYQLTKLLD SVQPIARELH
860 870 880 890
QFTFDLLIKS HMVSVDFPEM MAEIISVQVP KILSGKVKPI YFHTQ
Length:895
Mass (Da):96,537
Last modified:July 5, 2004 - v1
Checksum:i40D2A5BA0CA8B598
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY526325 mRNA. Translation: AAS19691.1.
AF092930 mRNA. Translation: AAD16104.1.
RefSeqiNP_001028083.1. NM_001032911.1.
UniGeneiMmu.3464.

Genome annotation databases

GeneIDi574293.
KEGGimcc:574293.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY526325 mRNA. Translation: AAS19691.1 .
AF092930 mRNA. Translation: AAD16104.1 .
RefSeqi NP_001028083.1. NM_001032911.1.
UniGenei Mmu.3464.

3D structure databases

ProteinModelPortali Q6QT55.
SMRi Q6QT55. Positions 531-604, 639-894.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 574293.
KEGGi mcc:574293.

Organism-specific databases

CTDi 367.

Phylogenomic databases

eggNOGi NOG245477.
HOGENOMi HOG000254783.
HOVERGENi HBG007583.
InParanoidi Q6QT55.
KOi K08557.

Miscellaneous databases

NextBioi 19968459.

Family and domain databases

Gene3Di 1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProi 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 ]
Pfami PF02166. Androgen_recep. 1 hit.
PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR00521. ANDROGENR.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Full length cDNA encoding rhesus monkey androgen receptor."
    Chen F., Towler D.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Androgen receptor messenger ribonucleic acid in brains and pituitaries of male rhesus monkeys: studies on distribution, hormonal control, and relationship to luteinizing hormone secretion."
    Abdelgadir S.E., Roselli C.E., Choate J.V., Resko J.A.
    Biol. Reprod. 60:1251-1256(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 767-876.
    Tissue: Prostate.

Entry informationi

Entry nameiANDR_MACMU
AccessioniPrimary (citable) accession number: Q6QT55
Secondary accession number(s): O97891
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: July 5, 2004
Last modified: October 1, 2014
This is version 93 of the entry and version 1 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

External Data

Dasty 3