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P06401 (PRGR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 177. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Progesterone receptor
Short name=PR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 3
Gene names
Name:PGR
Synonyms:NR3C3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation. Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Isoform A is inactive in stimulating c-Src/MAPK signaling on hormone stimulation. Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Subunit structure

Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and repesses transcriptional activity. Interacts with PIAS3; the interaction promotes sumoylation of PR in a hormone-dependent manner, inhibits DNA-binding, and alters nuclear export. Interacts with SP1; the interaction requires ligand-induced phosphorylation on Ser-345 by ERK1/2 MAPK. Interacts with PRMT2. Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.23

Subcellular location

Nucleus. Cytoplasm. Note: Nucleoplasmic shuttling is both homone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G1 and G2/M phases. Ref.16 Ref.17 Ref.22

Isoform A: Nucleus. Cytoplasm. Note: Mainly nuclear. Ref.16 Ref.17 Ref.22

Domain

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Post-translational modification

Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G2/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.21 Ref.22 Ref.23

Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294. Ref.19 Ref.20 Ref.21

Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294. Ref.19 Ref.20 Ref.21

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. Ref.24

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
   Coding sequence diversityAlternative splicing
Polymorphism
   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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell-cell signaling

Traceable author statement PubMed 1557371. Source: ProtInc

epithelial cell maturation

Inferred from electronic annotation. Source: Compara

negative regulation of gene expression

Inferred from expression pattern PubMed 21695196. Source: UniProtKB

ovulation from ovarian follicle

Inferred from electronic annotation. Source: Compara

progesterone receptor signaling pathway

Inferred from electronic annotation. Source: Compara

regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Compara

tertiary branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Compara

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionDNA binding

Traceable author statement Ref.2. Source: ProtInc

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from electronic annotation. Source: Compara

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid binding

Inferred from electronic annotation. Source: UniProtKB-KW

steroid hormone receptor activity

Traceable author statement PubMed 10840043. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CUEDC2Q9H4679EBI-78539,EBI-1248228
STAT3P407633EBI-78539,EBI-518675

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P06401-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A (identifier: P06401-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-164: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 933933Progesterone receptor
PRO_0000053693

Regions

DNA binding567 – 63973Nuclear receptor
Zinc finger567 – 58721NR C4-type
Zinc finger603 – 62725NR C4-type
Region1 – 566566Modulating, Pro-Rich
Region681 – 933253Steroid-binding
Motif183 – 1875Nuclear localization signal Potential

Amino acid modifications

Modified residue201Phosphoserine Ref.8
Modified residue811Phosphoserine Ref.9 Ref.10
Modified residue1021Phosphoserine Ref.8 Ref.10
Modified residue1301Phosphoserine Ref.8
Modified residue1621Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.17
Modified residue1901Phosphoserine Ref.8 Ref.11 Ref.12 Ref.17
Modified residue2131Phosphoserine Ref.8
Modified residue2941Phosphoserine; by MAPK1 Ref.10 Ref.12 Ref.13 Ref.17 Ref.21 Ref.22 Ref.23
Modified residue3451Phosphoserine; by MAPK Ref.8 Ref.10 Ref.23
Modified residue4001Phosphoserine; by CDK2 Ref.11 Ref.16 Ref.23
Modified residue6761Phosphoserine Ref.8
Cross-link7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.19
Cross-link388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.19 Ref.20 Ref.21
Cross-link388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross-link531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.19

Natural variations

Alternative sequence1 – 164164Missing in isoform A.
VSP_003706
Natural variant501A → T. Ref.5
Corresponds to variant rs11571143 [ dbSNP | Ensembl ].
VAR_019221
Natural variant1201A → V. Ref.5
Corresponds to variant rs11571144 [ dbSNP | Ensembl ].
VAR_019222
Natural variant1861P → L. Ref.5
Corresponds to variant rs11571145 [ dbSNP | Ensembl ].
VAR_019223
Natural variant3011M → R. Ref.5
Corresponds to variant rs11571146 [ dbSNP | Ensembl ].
VAR_019224
Natural variant3441S → T. Ref.1 Ref.5
Corresponds to variant rs3740753 [ dbSNP | Ensembl ].
VAR_016117
Natural variant3471C → S.
Corresponds to variant rs11571147 [ dbSNP | Ensembl ].
VAR_025555
Natural variant4441A → S. Ref.5
Corresponds to variant rs11571150 [ dbSNP | Ensembl ].
VAR_019225
Natural variant5291V → L. Ref.5
Corresponds to variant rs11571151 [ dbSNP | Ensembl ].
VAR_019226
Natural variant5361Q → P. Ref.5
Corresponds to variant rs11571152 [ dbSNP | Ensembl ].
VAR_019227
Natural variant6251R → I.
Corresponds to variant rs2020874 [ dbSNP | Ensembl ].
VAR_014627
Natural variant6511L → V. Ref.5
Corresponds to variant rs11571222 [ dbSNP | Ensembl ].
VAR_019228
Natural variant6601V → L. Ref.2 Ref.3
Corresponds to variant rs1042838 [ dbSNP | Ensembl ].
VAR_016118
Natural variant8651S → L. Ref.5
Corresponds to variant rs2020880 [ dbSNP | Ensembl ].
VAR_014628

Experimental info

Mutagenesis71K → R: Some loss of sumoylation; when associated with R-531. Complete loss of sumoylation; when associated with R-388 and R-531. Ref.19
Mutagenesis2941S → A: No effect on interaction with CUEDC2. Impaired progesterone-induced transcriptional activity. No CUEDC2- nor progestin-mediated protein degradation. No change in sumoylation; when associated with A-344 and A-345. Ref.13 Ref.21 Ref.22
Mutagenesis2941S → D: Decreases protein stability and increases progesterone-induced transcriptional activity. Ref.13 Ref.21 Ref.22
Mutagenesis3441S → A: No interaction with SP1. No change in progestin-induced protein degradation; when associated with A-345. No change in sumoylation; when associated with A-294 and A-345. Ref.13 Ref.23
Mutagenesis3451S → A: No change in progestin-induced protein degradation; when associated with A-344. No change in sumoylation; when associated with A-294 and A-344. Ref.13 Ref.23
Mutagenesis3881K → R: Great loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-531. Loss of CUEDC2-mediated protein degradation. Increased ligand-dependent transcriptional activity. Ref.19 Ref.20 Ref.21
Mutagenesis4001S → A: Abolishes CDK2-induced activity in the absence, but not in the presence, of progestin. Delayed nuclear translocation in presence of progestin. Ref.16 Ref.23
Mutagenesis5311K → R: Some loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-388. Ref.19
Sequence conflict2261G → S in CAA36018. Ref.1
Sequence conflict2561V → S in CAA36018. Ref.1

Secondary structure

1 ........................................... 933
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified March 21, 2006. Version 4.
Checksum: 80452E54FF3A0454

FASTA93398,981
        10         20         30         40         50         60 
MTELKAKGPR APHVAGGPPS PEVGSPLLCR PAAGPFPGSQ TSDTLPEVSA IPISLDGLLF 

        70         80         90        100        110        120 
PRPCQGQDPS DEKTQDQQSL SDVEGAYSRA EATRGAGGSS SSPPEKDSGL LDSVLDTLLA 

       130        140        150        160        170        180 
PSGPGQSQPS PPACEVTSSW CLFGPELPED PPAAPATQRV LSPLMSRSGC KVGDSSGTAA 

       190        200        210        220        230        240 
AHKVLPRGLS PARQLLLPAS ESPHWSGAPV KPSPQAAAVE VEEEDGSESE ESAGPLLKGK 

       250        260        270        280        290        300 
PRALGGAAAG GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTV 

       310        320        330        340        350        360 
MDFIHVPILP LNHALLAART RQLLEDESYD GGAGAASAFA PPRSSPCASS TPVAVGDFPD 

       370        380        390        400        410        420 
CAYPPDAEPK DDAYPLYSDF QPPALKIKEE EEGAEASARS PRSYLVAGAN PAAFPDFPLG 

       430        440        450        460        470        480 
PPPPLPPRAT PSRPGEAAVT AAPASASVSS ASSSGSTLEC ILYKAEGAPP QQGPFAPPPC 

       490        500        510        520        530        540 
KAPGASGCLL PRDGLPSTSA SAAAAGAAPA LYPALGLNGL PQLGYQAAVL KEGLPQVYPP 

       550        560        570        580        590        600 
YLNYLRPDSE ASQSPQYSFE SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN 

       610        620        630        640        650        660 
YLCAGRNDCI VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVVRA LDAVALPQPV 

       670        680        690        700        710        720 
GVPNESQALS QRFTFSPGQD IQLIPPLINL LMSIEPDVIY AGHDNTKPDT SSSLLTSLNQ 

       730        740        750        760        770        780 
LGERQLLSVV KWSKSLPGFR NLHIDDQITL IQYSWMSLMV FGLGWRSYKH VSGQMLYFAP 

       790        800        810        820        830        840 
DLILNEQRMK ESSFYSLCLT MWQIPQEFVK LQVSQEEFLC MKVLLLLNTI PLEGLRSQTQ 

       850        860        870        880        890        900 
FEEMRSSYIR ELIKAIGLRQ KGVVSSSQRF YQLTKLLDNL HDLVKQLHLY CLNTFIQSRA 

       910        920        930 
LSVEFPEMMS EVIAAQLPKI LAGMVKPLLF HKK

« Hide

Isoform A [UniParc].

Checksum: FE676F25282983F3
Show »

FASTA76982,295

References

« Hide 'large scale' references
[1]"Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B."
Kastner P., Krust A., Turcotte B., Stropp U., Tora L., Gronemeyer H., Chambon P.
EMBO J. 9:1603-1614(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, VARIANT THR-344.
[2]"Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA."
Misrahi M., Atger M., D'Auriol L., Loosfelt H., Meriel C., Fridlansky F., Guiochon-Mantel A., Galibert F., Milgrom E.
Biochem. Biophys. Res. Commun. 143:740-748(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-660.
[3]Kieback D.G., Agoulnik I.U., Tong X.-W.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-660.
[4]"The human progesterone receptor shows evidence of adaptive evolution associated with its ability to act as a transcription factor."
Chen C., Opazo J.C., Erez O., Uddin M., Santolaya-Forgas J., Goodman M., Grossman L.I., Romero R., Wildman D.E.
Mol. Phylogenet. Evol. 47:637-649(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]NIEHS SNPs program
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-50; VAL-120; LEU-186; ARG-301; THR-344; SER-444; LEU-529; PRO-536; VAL-651 AND LEU-865.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites."
Knotts T.A., Orkiszewski R.S., Cook R.G., Edwards D.P., Weigel N.L.
J. Biol. Chem. 276:8475-8483(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 11-22 AND 673-679, PHOSPHORYLATION AT SER-20; SER-102; SER-130; SER-162; SER-190; SER-213; SER-345 AND SER-676, MASS SPECTROMETRY.
[9]"Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor."
Zhang Y., Beck C.A., Poletti A., Edwards D.P., Weigel N.L.
Mol. Endocrinol. 9:1029-1040(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-81 AND SER-162.
[10]"Stoichiometry and site-specific phosphorylation of human progesterone receptor in native target cells and in the baculovirus expression system."
Beck C.A., Zhang Y., Altmann M., Weigel N.L., Edwards D.P.
J. Biol. Chem. 271:19546-19555(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-81; SER-102; SER-162; SER-294 AND SER-345.
[11]"Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo."
Zhang Y., Beck C.A., Poletti A., Clement J.P. IV, Prendergast P., Yip T.-T., Hutchens T.W., Edwards D.P., Weigel N.L.
Mol. Endocrinol. 11:823-832(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-162; SER-190 AND SER-400.
[12]"Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody."
Clemm D.L., Sherman L., Boonyaratanakornkit V., Schrader W.T., Weigel N.L., Edwards D.P.
Mol. Endocrinol. 14:52-65(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-190 AND SER-294.
[13]"Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome."
Lange C.A., Shen T., Horwitz K.B.
Proc. Natl. Acad. Sci. U.S.A. 97:1032-1037(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-294, UBIQUITINATION, MUTAGENESIS OF SER-294; SER-344 AND SER-345.
[14]"Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.
J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRMT2.
[15]"BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMARD1.
[16]"Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase 2."
Pierson-Mullany L.K., Lange C.A.
Mol. Cell. Biol. 24:10542-10557(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-400, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-400.
[17]"Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity."
Narayanan R., Edwards D.P., Weigel N.L.
Mol. Cell. Biol. 25:2885-2898(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-162; SER-190 AND SER-294, SUBCELLULAR LOCATION, FUNCTION.
[18]"GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway."
Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F., Wood W.M., Felts S.J., Horwitz K.B., Toft D.
Mol. Cell. Biol. 26:1722-1730(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UNC45A.
[19]"PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus."
Man J.-H., Li H.-Y., Zhang P.-J., Zhou T., He K., Pan X., Liang B., Li A.-L., Zhao J., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F., Zhang X.-M.
Nucleic Acids Res. 34:5552-5566(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-7; LYS-388 AND LYS-531, INTERACTION WITH PIAS3, FUNCTION, MUTAGENESIS OF LYS-7; LYS-388 AND LYS-531.
[20]"CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome."
Zhang P.-J., Zhao J., Li H.-Y., Man J.-H., He K., Zhou T., Pan X., Li A.-L., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F., Zhang X.-M.
EMBO J. 26:1831-1842(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CUEDC2, SUMOYLATION AT LYS-388, UBIQUITINATION AT LYS-388, FUNCTION, MUTAGENESIS OF LYS-388.
[21]"Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells."
Daniel A.R., Faivre E.J., Lange C.A.
Mol. Endocrinol. 21:2890-2906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-294, SUMOYLATION AT LYS-388, FUNCTION, MUTAGENESIS OF SER-294 AND LYS-388.
[22]"Linkage of progestin and epidermal growth factor signaling: phosphorylation of progesterone receptors mediates transcriptional hypersensitivity and increased ligand-independent breast cancer cell growth."
Daniel A.R., Qiu M., Faivre E.J., Ostrander J.H., Skildum A., Lange C.A.
Steroids 72:188-201(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-294, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-294.
[23]"Progesterone receptor rapid signaling mediates serine 345 phosphorylation and tethering to specificity protein 1 transcription factors."
Faivre E.J., Daniel A.R., Hillard C.J., Lange C.A.
Mol. Endocrinol. 22:823-837(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-294; SER-345 AND SER-400, INTERACTION WITH SP1, FUNCTION, MUTAGENESIS OF SER-344; SER-345 AND SER-400.
[24]"DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors."
Pedram A., Razandi M., Deschenes R.J., Levin E.R.
Mol. Biol. Cell 23:188-199(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION.
[25]"Atomic structure of progesterone complexed with its receptor."
Williams S.P., Sigler P.B.
Nature 393:392-396(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 682-933.
[26]"Molecular and pharmacological properties of a potent and selective novel nonsteroidal progesterone receptor agonist tanaproget."
Zhang Z., Olland A.M., Zhu Y., Cohen J., Berrodin T., Chippari S., Appavu C., Li S., Wilhem J., Chopra R., Fensome A., Zhang P., Wrobel J., Unwalla R.J., Lyttle C.R., Winneker R.C.
J. Biol. Chem. 280:28468-28475(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 676-933.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Progesterone receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X51730 mRNA. Translation: CAA36018.1.
M15716 mRNA. Translation: AAA60081.1.
AF016381 mRNA. Translation: AAD01587.1.
DQ234979 Genomic DNA. Translation: ABB72139.1.
AY525610 Genomic DNA. Translation: AAS00096.1.
AP001533 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67000.1.
IPIIPI00219021.
IPI00297419.
PIRQRHUP. S09971.
RefSeqNP_000917.3. NM_000926.4.
NP_001189403.1. NM_001202474.1.
UniGeneHs.32405.
Hs.742403.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A28X-ray1.80A/B678-933[»]
1E3KX-ray2.80A/B676-933[»]
1SQNX-ray1.45A/B673-933[»]
1SR7X-ray1.46A/B676-933[»]
1ZUCX-ray2.00A/B676-933[»]
2C7AX-ray2.50A/B563-640[»]
2OVHX-ray2.00A678-933[»]
2OVMX-ray2.60A678-933[»]
2W8YX-ray1.80A/B678-933[»]
3D90X-ray2.26A/B676-933[»]
3G8OX-ray1.90A/B673-933[»]
3HQ5X-ray2.10A/B678-933[»]
3KBAX-ray2.00A/B681-933[»]
3ZR7X-ray1.65A/B678-933[»]
3ZRAX-ray1.90A/B678-933[»]
3ZRBX-ray1.80A/B678-933[»]
4A2JX-ray2.00A/B678-933[»]
4APUX-ray1.90A/B678-933[»]
ProteinModelPortalP06401.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-578N.
DIP-5967N.
IntActP06401. 8 interactions.
MINTMINT-1505587.
STRING9606.ENSP00000325120.

PTM databases

PhosphoSiteP06401.

Polymorphism databases

DMDM90110048.

Proteomic databases

PaxDbP06401.
PRIDEP06401.

Protocols and materials databases

DNASU5241.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325455; ENSP00000325120; ENSG00000082175.
GeneID5241.
KEGGhsa:5241.
UCSCuc001pgh.2. human.

Organism-specific databases

CTD5241.
GeneCardsGC11M100943.
HGNCHGNC:8910. PGR.
HPACAB000068.
HPA004751.
HPA008428.
HPA017176.
MIM607311. gene.
neXtProtNX_P06401.
PharmGKBPA266.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG273252.
HOGENOMHOG000290653.
HOVERGENHBG007583.
InParanoidP06401.
KOK08556.
OMARPCQGQD.
PhylomeDBP06401.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP06401.
BgeeP06401.
CleanExHS_PGR.
GenevestigatorP06401.
GermOnlineENSG00000082175. Homo sapiens.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000128. Progest_rcpt.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF02161. Prog_receptor. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00544. PROGESTRONER.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. Str_ncl_receptor. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP06401.
ChEMBLCHEMBL208.
DrugBankDB00304. Desogestrel.
DB01395. Drospirenone.
DB00378. Dydrogesterone.
DB00823. Ethynodiol Diacetate.
DB00294. Etonogestrel.
DB00367. Levonorgestrel.
DB00603. Medroxyprogesterone.
DB00351. Megestrol.
DB00834. Mifepristone.
DB00717. Norethindrone.
DB00957. Norgestimate.
DB00506. Norgestrel.
DB00396. Progesterone.
EvolutionaryTraceP06401.
GenomeRNAi5241.
NextBio20248.
SOURCESearch...

Entry information

Entry namePRGR_HUMAN
AccessionPrimary (citable) accession number: P06401
Secondary accession number(s): A7X8B0, Q9UPF7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: March 21, 2006
Last modified: May 1, 2013
This is version 177 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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