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P19091 (ANDR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length899 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.

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 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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

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.

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-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.

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
   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_processLeydig cell differentiation

Inferred from mutant phenotype PubMed 19574395. Source: MGI

activation of prostate induction by androgen receptor signaling pathway

Inferred from mutant phenotype PubMed 17317769. Source: MGI

androgen receptor signaling pathway

Inferred from direct assay Ref.6PubMed 15660130. Source: MGI

cellular process

Inferred from direct assay PubMed 12145204. Source: MGI

epithelial cell differentiation involved in prostate gland development

Inferred from mutant phenotype PubMed 17652515. Source: MGI

epithelial cell morphogenesis

Inferred from genetic interaction PubMed 21084446. Source: MGI

fertilization

Inferred from mutant phenotype PubMed 19574395. Source: MGI

in utero embryonic development

Inferred from mutant phenotype PubMed 10319319. Source: MGI

intracellular receptor signaling pathway

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

lateral sprouting involved in mammary gland duct morphogenesis

Inferred from mutant phenotype PubMed 14676301. Source: MGI

male genitalia morphogenesis

Inferred from mutant phenotype PubMed 19282366. Source: MGI

male gonad development

Inferred from mutant phenotype PubMed 10319319PubMed 17317769PubMed 19574395. Source: MGI

male somatic sex determination

Inferred from mutant phenotype PubMed 5452809. Source: MGI

mammary gland alveolus development

Inferred from mutant phenotype PubMed 14676301. Source: MGI

morphogenesis of an epithelial fold

Inferred from mutant phenotype PubMed 17652515. Source: MGI

multicellular organism growth

Inferred from genetic interaction PubMed 19574395. Source: MGI

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 17652515. Source: MGI

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 mutant phenotype PubMed 17317769. Source: MGI

positive regulation of MAPK cascade

Inferred from mutant phenotype PubMed 14676301. Source: MGI

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 mutant phenotype PubMed 14676301. Source: MGI

positive regulation of intracellular estrogen receptor signaling pathway

Inferred from mutant phenotype PubMed 14676301. Source: MGI

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 mutant phenotype PubMed 17652515. Source: MGI

prostate gland growth

Inferred from mutant phenotype PubMed 17317769PubMed 17652515. Source: MGI

protein oligomerization

Inferred from sequence orthology PubMed 18468998. Source: MGI

regulation of catalytic activity

Inferred from mutant phenotype PubMed 17276355. Source: MGI

regulation of developmental growth

Inferred from mutant phenotype PubMed 17317769. Source: MGI

regulation of establishment of protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of gene expression

Inferred from mutant phenotype PubMed 17332066. Source: MGI

regulation of prostatic bud formation

Inferred from genetic interaction PubMed 12941620. Source: MGI

regulation of systemic arterial blood pressure

Inferred from genetic interaction PubMed 18468998. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17332066. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12145204PubMed 14576337. Source: MGI

reproductive structure development

Inferred from mutant phenotype PubMed 17317769. Source: MGI

reproductive system development

Inferred from genetic interaction PubMed 19574395. Source: MGI

response to insulin

Inferred from electronic annotation. Source: Ensembl

seminiferous tubule development

Inferred from mutant phenotype PubMed 19574395. Source: MGI

single fertilization

Inferred from genetic interaction PubMed 21084446. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 18403489PubMed 19574395. Source: MGI

tertiary branching involved in mammary gland duct morphogenesis

Inferred from mutant phenotype PubMed 14676301. Source: MGI

transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 18468998. Source: MGI

protein complex

Inferred from sequence orthology PubMed 18468998. Source: MGI

   Molecular_functionPOU domain binding

Inferred from direct assay PubMed 11997177. Source: UniProtKB

androgen binding

Inferred from electronic annotation. Source: Ensembl

androgen receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

beta-catenin binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 17277772. Source: BHF-UCL

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 PubMed 11997177. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 8119157. Source: MGI

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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Casp8O891102EBI-1776062,EBI-851690

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 899899Androgen receptor
PRO_0000053707

Regions

DNA binding538 – 61174Nuclear receptor
Zinc finger539 – 55921NR C4-type
Zinc finger575 – 59925NR C4-type
Region1 – 537537Modulating By similarity
Region531 – 899369Interaction with LPXN By similarity
Region551 – 64191Interaction with HIPK3 By similarity
Region604 – 899296Interaction with KAT7 By similarity
Region670 – 899230Ligand-binding
Compositional bias63 – 675Poly-Arg
Compositional bias174 – 19320Poly-Gln
Compositional bias367 – 3737Poly-Pro
Compositional bias391 – 3977Poly-Ala
Compositional bias441 – 4477Poly-Gly

Sites

Binding site6851Androgen
Binding site7321Androgen
Binding site8571Androgen
Site7001Interaction with coactivator LXXL motif By similarity
Site8771Interaction with coactivator FXXLF motif By similarity

Amino acid modifications

Modified residue611Phosphoserine; by CDK9 By similarity
Modified residue751Phosphoserine By similarity
Modified residue2181Phosphotyrosine; by CSK By similarity
Modified residue2621Phosphotyrosine; by CSK and TNK2 By similarity
Modified residue3021Phosphotyrosine; by CSK By similarity
Modified residue3411Phosphotyrosine; by CSK By similarity
Modified residue3521Phosphotyrosine; by CSK By similarity
Modified residue3571Phosphotyrosine; by CSK By similarity
Modified residue3581Phosphotyrosine; by CSK and TNK2 By similarity
Modified residue3881Phosphotyrosine; by CSK By similarity
Modified residue5141Phosphotyrosine; by CSK By similarity
Modified residue5311Phosphotyrosine; by CSK By similarity
Modified residue6301Phosphoserine; by STK4/MST1 By similarity
Modified residue8951Phosphotyrosine; by CSK By similarity
Cross-link381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link500Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link825Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link827Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

................................ 899
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19091 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: FD9EE07C07F7A568

FASTA89998,194
        10         20         30         40         50         60 
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAANIAPP GACLQQRQET 

        70         80         90        100        110        120 
SPRRRRRQQH TEDGSPQAHI RGPTGYLALE EEQQPSQQQA ASEGHPESSC LPEPGAATAP 

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

       190        200        210        220        230        240 
QHQQQHQQHQ QQQEVISEGS SARAREATGA PSSSKDSYLG GNSTISDSAK ELCKAVSVSM 

       250        260        270        280        290        300 
GLGVEALEHL SPGEQLRGDC MYASLLGGPP AVRPTPCAPL PECKGLPLDE GPGKSTEETA 

       310        320        330        340        350        360 
EYSSFKGGYA KGLEGESLGC SGSSEAGSSG TLEIPSSLSL YKSGALDEAA AYQNRDYYNF 

       370        380        390        400        410        420 
PLALSGPPHP PPPTHPHARI KLENPLDYGS AWAAAAAQCR YGDLGSLHGG SVAGPSTGSP 

       430        440        450        460        470        480 
PATTSSSWHT LFTAEEGQLY GPGGGGGSSS PSDAGPVAPY GYTRPPQGLT SQESDYSASE 

       490        500        510        520        530        540 
VWYPGGVVNR VPYPSPNCVK SEMGPWMENY SGPYGDMRLD STRDHVLPID YYFPPQKTCL 

       550        560        570        580        590        600 
ICGDEASGCH YGALTCGSCK VFFKRAAEGK QKYLCASRND CTIDKFRRKN CPSCRLRKCY 

       610        620        630        640        650        660 
EAGMTLGARK LKKLGNLKLQ EEGENSNAGS PTEDPSQKMT VSHIEGYECQ PIFLNVLEAI 

       670        680        690        700        710        720 
EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK ALPGFRNLHV DDQMAVIQYS 

       730        740        750        760        770        780 
WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF NEYRMHKSRM YSQCVRMRHL SQEFGWLQIT 

       790        800        810        820        830        840 
PQEFLCMKAL LLFSIIPVDG LKNQKFFDEL RMNYIKELDR IIACKRKNPT SCSRRFYQLT 

       850        860        870        880        890 
KLLDSVQPIA RELHQFTFDL LIKSHMVSVD FPEMMAEIIS VQVPKILSGK VKPIYFHTQ 

« Hide

References

[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]"A zinc finger protein TZF is a novel corepressor of androgen receptor."
Ishizuka M., Kawate H., Takayanagi R., Ohshima H., Tao R.-H., Hagiwara H.
Biochem. Biophys. Res. Commun. 331:1025-1031(2005) [PubMed] [Europe PMC] [Abstract]
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]"A surface on the androgen receptor that allosterically regulates coactivator binding."
Estebanez-Perpina E., Arnold L.A., Nguyen P., Rodrigues E.D., Mar E., Bateman R., Pallai P., Shokat K.M., Baxter J.D., Guy R.K., Webb P., Fletterick R.J.
Proc. Natl. Acad. Sci. U.S.A. 104:16074-16079(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 649-899 IN COMPLEX WITH NCOA2 AND DIHYDROTESTOSTERONE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S56585 mRNA. Translation: AAB19916.1.
X53779 mRNA. Translation: CAA37795.1.
M37890 mRNA. Translation: AAA37234.1.
X59592 mRNA. Translation: CAA42160.1.
CCDSCCDS30294.1.
PIRA35895.
RefSeqNP_038504.1. NM_013476.3.
UniGeneMm.39005.
Mm.394224.
Mm.439657.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QPYX-ray2.50A649-899[»]
ProteinModelPortalP19091.
SMRP19091. Positions 534-898.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198179. 16 interactions.
DIPDIP-41803N.
IntActP19091. 2 interactions.
MINTMINT-151935.

Chemistry

BindingDBP19091.
ChEMBLCHEMBL3056.
GuidetoPHARMACOLOGY628.

PTM databases

PhosphoSiteP19091.

Proteomic databases

PRIDEP19091.

Protocols and materials databases

DNASU11835.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052837; ENSMUSP00000052648; ENSMUSG00000046532.
GeneID11835.
KEGGmmu:11835.
UCSCuc009tuv.1. mouse.

Organism-specific databases

CTD367.
MGIMGI:88064. Ar.

Phylogenomic databases

eggNOGNOG245477.
GeneTreeENSGT00730000110451.
HOGENOMHOG000254783.
HOVERGENHBG007583.
InParanoidP19091.
KOK08557.
OMACSTDLKD.
OrthoDBEOG7J17Z7.
PhylomeDBP19091.
TreeFamTF350286.

Gene expression databases

BgeeP19091.
CleanExMM_AR.
GenevestigatorP19091.

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

EvolutionaryTraceP19091.
NextBio279763.
PROP19091.
SOURCESearch...

Entry information

Entry nameANDR_MOUSE
AccessionPrimary (citable) accession number: P19091
Entry history
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 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot