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P19091

- ANDR_MOUSE

UniProt

P19091 - ANDR_MOUSE

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Protein
Androgen receptor
Gene
Ar, Nr3c4
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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 sitei685 – 6851Androgen
Sitei700 – 7001Interaction with coactivator LXXL motif By similarity
Binding sitei732 – 7321Androgen
Binding sitei857 – 8571Androgen
Sitei877 – 8771Interaction with coactivator FXXLF motif By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi538 – 61174Nuclear receptor
Add
BLAST
Zinc fingeri539 – 55921NR C4-type
Add
BLAST
Zinc fingeri575 – 59925NR C4-type
Add
BLAST

GO - Molecular functioni

  1. POU domain binding Source: UniProtKB
  2. androgen binding Source: Ensembl
  3. androgen receptor activity Source: UniProtKB
  4. beta-catenin binding Source: UniProtKB
  5. enzyme binding Source: BHF-UCL
  6. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
  7. protein binding Source: UniProtKB
  8. sequence-specific DNA binding Source: MGI
  9. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  10. transcription regulatory region DNA binding Source: UniProtKB
  11. zinc ion binding Source: InterPro

GO - Biological processi

  1. Leydig cell differentiation Source: MGI
  2. activation of prostate induction by androgen receptor signaling pathway Source: MGI
  3. androgen receptor signaling pathway Source: MGI
  4. cellular process Source: MGI
  5. epithelial cell differentiation involved in prostate gland development Source: MGI
  6. epithelial cell morphogenesis Source: MGI
  7. fertilization Source: MGI
  8. in utero embryonic development Source: MGI
  9. intracellular receptor signaling pathway Source: BHF-UCL
  10. lateral sprouting involved in mammary gland duct morphogenesis Source: MGI
  11. male genitalia morphogenesis Source: MGI
  12. male gonad development Source: MGI
  13. male somatic sex determination Source: MGI
  14. mammary gland alveolus development Source: MGI
  15. morphogenesis of an epithelial fold Source: MGI
  16. multicellular organism growth Source: MGI
  17. negative regulation of epithelial cell proliferation Source: MGI
  18. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  19. negative regulation of integrin biosynthetic process Source: UniProtKB
  20. organ formation Source: MGI
  21. positive regulation of MAPK cascade Source: MGI
  22. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  23. positive regulation of cell proliferation Source: UniProtKB
  24. positive regulation of insulin-like growth factor receptor signaling pathway Source: MGI
  25. positive regulation of intracellular estrogen receptor signaling pathway Source: MGI
  26. positive regulation of phosphorylation Source: UniProtKB
  27. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  28. positive regulation of transcription, DNA-templated Source: UniProtKB
  29. prostate gland epithelium morphogenesis Source: MGI
  30. prostate gland growth Source: MGI
  31. protein oligomerization Source: MGI
  32. regulation of catalytic activity Source: MGI
  33. regulation of developmental growth Source: MGI
  34. regulation of establishment of protein localization to plasma membrane Source: UniProtKB
  35. regulation of gene expression Source: MGI
  36. regulation of prostatic bud formation Source: MGI
  37. regulation of systemic arterial blood pressure Source: MGI
  38. regulation of transcription from RNA polymerase II promoter Source: MGI
  39. regulation of transcription, DNA-templated Source: MGI
  40. reproductive structure development Source: MGI
  41. reproductive system development Source: MGI
  42. response to insulin Source: Ensembl
  43. seminiferous tubule development Source: MGI
  44. single fertilization Source: MGI
  45. spermatogenesis Source: MGI
  46. tertiary branching involved in mammary gland duct morphogenesis Source: MGI
  47. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:88064. Ar.

Subcellular locationi

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.

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. dendrite Source: Ensembl
  4. nuclear chromatin Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: MGI
  7. protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 899899Androgen receptor
PRO_0000053707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611Phosphoserine; by CDK9 By similarity
Modified residuei75 – 751Phosphoserine By similarity
Modified residuei218 – 2181Phosphotyrosine; by CSK By similarity
Modified residuei262 – 2621Phosphotyrosine; by CSK and TNK2 By similarity
Modified residuei302 – 3021Phosphotyrosine; by CSK By similarity
Modified residuei341 – 3411Phosphotyrosine; by CSK By similarity
Modified residuei352 – 3521Phosphotyrosine; by CSK By similarity
Modified residuei357 – 3571Phosphotyrosine; by CSK By similarity
Modified residuei358 – 3581Phosphotyrosine; by CSK and TNK2 By similarity
Cross-linki381 – 381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei388 – 3881Phosphotyrosine; by CSK By similarity
Cross-linki500 – 500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei514 – 5141Phosphotyrosine; by CSK By similarity
Modified residuei531 – 5311Phosphotyrosine; by CSK By similarity
Modified residuei630 – 6301Phosphoserine; by STK4/MST1 By similarity
Cross-linki825 – 825Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki827 – 827Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei895 – 8951Phosphotyrosine; by CSK By 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-514 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-381 (major) and Lys-500 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.

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP19091.

PTM databases

PhosphoSiteiP19091.

Expressioni

Gene expression databases

BgeeiP19091.
CleanExiMM_AR.
GenevestigatoriP19091.

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, 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 RBAK. Interacts via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. Interacts with HIP1 (via coiled coil domain). Interacts with SLC30A9 and RAD54L2/ARIP4. Interacts with MACROD1. 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 hormone-induced AR transcriptional activity. Interacts with PRPF6 in a hormone-independent way; this interaction enhances hormone-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 CRY1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Casp8O891102EBI-1776062,EBI-851690

Protein-protein interaction databases

BioGridi198179. 16 interactions.
DIPiDIP-41803N.
IntActiP19091. 2 interactions.
MINTiMINT-151935.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi652 – 6598
Helixi677 – 70125
Helixi705 – 7073
Helixi710 – 73627
Beta strandi740 – 7456
Beta strandi748 – 7503
Helixi752 – 7576
Helixi761 – 77616
Helixi781 – 79212
Beta strandi794 – 7996
Helixi804 – 82320
Helixi831 – 84414
Helixi846 – 86217
Turni863 – 8686
Helixi873 – 88715
Beta strandi890 – 8934

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QPYX-ray2.50A649-899[»]
ProteinModelPortaliP19091.
SMRiP19091. Positions 534-898.

Miscellaneous databases

EvolutionaryTraceiP19091.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 537537Modulating By similarity
Add
BLAST
Regioni531 – 899369Interaction with LPXN By similarity
Add
BLAST
Regioni551 – 64191Interaction with HIPK3 By similarity
Add
BLAST
Regioni604 – 899296Interaction with KAT7 By similarity
Add
BLAST
Regioni670 – 899230Ligand-binding
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 675Poly-Arg
Compositional biasi174 – 19320Poly-Gln
Add
BLAST
Compositional biasi367 – 3737Poly-Pro
Compositional biasi391 – 3977Poly-Ala
Compositional biasi441 – 4477Poly-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.

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG245477.
GeneTreeiENSGT00730000110451.
HOGENOMiHOG000254783.
HOVERGENiHBG007583.
InParanoidiP19091.
KOiK08557.
OMAiCSTDLKD.
OrthoDBiEOG7J17Z7.
PhylomeDBiP19091.
TreeFamiTF350286.

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.

P19091-1 [UniParc]FASTAAdd to Basket

« Hide

MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAANIAPP    50
GACLQQRQET SPRRRRRQQH TEDGSPQAHI RGPTGYLALE EEQQPSQQQA 100
ASEGHPESSC LPEPGAATAP GKGLPQQPPA PPDQDDSAAP STLSLLGPTF 150
PGLSSCSADI KDILNEAGTM QLLQQQQQQQ QHQQQHQQHQ QQQEVISEGS 200
SARAREATGA PSSSKDSYLG GNSTISDSAK ELCKAVSVSM GLGVEALEHL 250
SPGEQLRGDC MYASLLGGPP AVRPTPCAPL PECKGLPLDE GPGKSTEETA 300
EYSSFKGGYA KGLEGESLGC SGSSEAGSSG TLEIPSSLSL YKSGALDEAA 350
AYQNRDYYNF PLALSGPPHP PPPTHPHARI KLENPLDYGS AWAAAAAQCR 400
YGDLGSLHGG SVAGPSTGSP PATTSSSWHT LFTAEEGQLY GPGGGGGSSS 450
PSDAGPVAPY GYTRPPQGLT SQESDYSASE VWYPGGVVNR VPYPSPNCVK 500
SEMGPWMENY SGPYGDMRLD STRDHVLPID YYFPPQKTCL ICGDEASGCH 550
YGALTCGSCK VFFKRAAEGK QKYLCASRND CTIDKFRRKN CPSCRLRKCY 600
EAGMTLGARK LKKLGNLKLQ EEGENSNAGS PTEDPSQKMT VSHIEGYECQ 650
PIFLNVLEAI EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK 700
ALPGFRNLHV DDQMAVIQYS WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF 750
NEYRMHKSRM YSQCVRMRHL SQEFGWLQIT PQEFLCMKAL LLFSIIPVDG 800
LKNQKFFDEL RMNYIKELDR IIACKRKNPT SCSRRFYQLT KLLDSVQPIA 850
RELHQFTFDL LIKSHMVSVD FPEMMAEIIS VQVPKILSGK VKPIYFHTQ 899
Length:899
Mass (Da):98,194
Last modified:November 1, 1990 - v1
Checksum:iFD9EE07C07F7A568
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S56585 mRNA. Translation: AAB19916.1.
X53779 mRNA. Translation: CAA37795.1.
M37890 mRNA. Translation: AAA37234.1.
X59592 mRNA. Translation: CAA42160.1.
CCDSiCCDS30294.1.
PIRiA35895.
RefSeqiNP_038504.1. NM_013476.3.
UniGeneiMm.39005.
Mm.394224.
Mm.439657.

Genome annotation databases

EnsembliENSMUST00000052837; ENSMUSP00000052648; ENSMUSG00000046532.
GeneIDi11835.
KEGGimmu:11835.
UCSCiuc009tuv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S56585 mRNA. Translation: AAB19916.1 .
X53779 mRNA. Translation: CAA37795.1 .
M37890 mRNA. Translation: AAA37234.1 .
X59592 mRNA. Translation: CAA42160.1 .
CCDSi CCDS30294.1.
PIRi A35895.
RefSeqi NP_038504.1. NM_013476.3.
UniGenei Mm.39005.
Mm.394224.
Mm.439657.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QPY X-ray 2.50 A 649-899 [» ]
ProteinModelPortali P19091.
SMRi P19091. Positions 534-898.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198179. 16 interactions.
DIPi DIP-41803N.
IntActi P19091. 2 interactions.
MINTi MINT-151935.

Chemistry

BindingDBi P19091.
ChEMBLi CHEMBL3056.
GuidetoPHARMACOLOGYi 628.

PTM databases

PhosphoSitei P19091.

Proteomic databases

PRIDEi P19091.

Protocols and materials databases

DNASUi 11835.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000052837 ; ENSMUSP00000052648 ; ENSMUSG00000046532 .
GeneIDi 11835.
KEGGi mmu:11835.
UCSCi uc009tuv.1. mouse.

Organism-specific databases

CTDi 367.
MGIi MGI:88064. Ar.

Phylogenomic databases

eggNOGi NOG245477.
GeneTreei ENSGT00730000110451.
HOGENOMi HOG000254783.
HOVERGENi HBG007583.
InParanoidi P19091.
KOi K08557.
OMAi CSTDLKD.
OrthoDBi EOG7J17Z7.
PhylomeDBi P19091.
TreeFami TF350286.

Miscellaneous databases

EvolutionaryTracei P19091.
NextBioi 279763.
PROi P19091.
SOURCEi Search...

Gene expression databases

Bgeei P19091.
CleanExi MM_AR.
Genevestigatori P19091.

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. "Molecular cloning of androgen receptors from divergent species with a polymerase chain reaction technique: complete cDNA sequence of the mouse androgen receptor and isolation of androgen receptor cDNA probes from dog, guinea pig and clawed frog."
    He W.W., Fischer L.M., Sun S., Bilhartz D.L., Zhu X., Young C.Y.F., Kelley D.B., Tindall D.J.
    Biochem. Biophys. Res. Commun. 171:697-704(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "Structure and size distribution of the androgen receptor mRNA in wild-type and Tfm/Y mutant mice."
    Gaspar M.L., Meo T., Tosi M.
    Mol. Endocrinol. 4:1600-1610(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The mouse androgen receptor. Functional analysis of the protein and characterization of the gene."
    Faber P.W., King A., van Rooij H.C.J., Brinkmann A.O., de Both N.J., Trapman J.
    Biochem. J. 278:269-278(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "A frameshift mutation destabilizes androgen receptor messenger RNA in the Tfm mouse."
    Charest N.J., Zhou Z., Lubahn D.B., Olsen K.L., Wilson E.M., French F.S.
    Mol. Endocrinol. 5:573-581(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Novel ATPase of SNF2-like protein family interacts with androgen receptor and modulates androgen-dependent transcription."
    Rouleau N., Domans'kyi A., Reeben M., Moilanen A.-M., Havas K., Kang Z., Owen-Hughes T., Palvimo J.J., Jaenne O.A.
    Mol. Biol. Cell 13:2106-2119(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD54L2.
    Strain: Swiss Webster.
    Tissue: Embryo.
  6. "Dyrk1A potentiates steroid hormone-induced transcription via the chromatin remodeling factor Arip4."
    Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.
    Mol. Cell. Biol. 24:5821-5834(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD54L2.
  7. Cited for: INTERACTION WITH ZNF318.
  8. "GAC63, a GRIP1-dependent nuclear receptor coactivator."
    Chen Y.-H., Kim J.H., Stallcup M.R.
    Mol. Cell. Biol. 25:5965-5972(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC30A9.
  9. "Cryptochromes mediate rhythmic repression of the glucocorticoid receptor."
    Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W., Downes M., Evans R.M.
    Nature 480:552-556(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRY1.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 649-899 IN COMPLEX WITH NCOA2 AND DIHYDROTESTOSTERONE.

Entry informationi

Entry nameiANDR_MOUSE
AccessioniPrimary (citable) accession number: P19091
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 162 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi