Progesterone receptor - Homo sapiens (Human)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

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Alternative products

Sequence annotation (Features)

Sequences

References

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Cross-references

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Names and origin

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Entry

#Exp.

IntAct

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Reviewed, UniProtKB/Swiss-Prot P06401 (PRGR_HUMAN)

Last modified February 9, 2010. Version 145. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Protein names

Recommended name:
    Progesterone receptor
      Short name=PR
Alternative name(s):
    Nuclear receptor subfamily 3 group C member 3

Gene names

Name:	PGR
Synonyms:	NR3C3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Sequence length	933 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Isoform A is inactive in stimulating c-Src/MAPK signaling on hormone stimulation. Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22
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. Ref.17 Ref.18 Ref.22 Ref.13 Ref.16
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.14 Ref.15 Ref.20 Isoform A: Nucleus. Cytoplasm. Note: Mainly nuclear. Ref.14 Ref.15 Ref.20
Domain	Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal steroid-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.14 Ref.15 Ref.19 Ref.20 Ref.22 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.21 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.17 Ref.18 Ref.19 Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR3 subfamily. Contains 1 nuclear receptor DNA-binding domain.

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Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Lipid-binding Metal-binding Steroid-binding Zinc
Molecular function	Receptor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell-cell signaling Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular function	protein binding Ref.13 Ref.18 Inferred from physical interaction. Source: IntAct receptor binding Inferred from physical interaction. Source: UniProtKB 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. Source: ProtInc transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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With	Entry	#Exp.	IntAct
CUEDC2	Q9H467	5	EBI-78539,EBI-1248228
JDP2	Q8WYK2	1	EBI-78539,EBI-1248415
NCOR2	Q9Y618	1	EBI-78539,EBI-80830
PRMT2	P55345	1	EBI-78539,EBI-78458
SMARCD1	Q96GM5	1	EBI-78539,EBI-358489

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Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 933

933

Progesterone receptor

PRO_0000053693

DNA binding

567 – 639

Nuclear receptor

Zinc finger

567 – 587

NR C4-type

Zinc finger

603 – 627

NR C4-type

Region

1 – 566

566

Modulating, Pro-Rich

Region

681 – 933

253

Steroid-binding

Motif

183 – 187

Nuclear localization signal Potential

Modified residue

Phosphoserine Ref.7

Modified residue

Phosphoserine Ref.8 Ref.9

Modified residue

102

Phosphoserine Ref.7 Ref.9

Modified residue

130

Phosphoserine Ref.7

Modified residue

162

Phosphoserine Ref.15 Ref.7 Ref.8 Ref.9 Ref.10 Ref.21

Modified residue

190

Phosphoserine Ref.15 Ref.7 Ref.10 Ref.11

Modified residue

213

Phosphoserine Ref.7

Modified residue

294

Phosphoserine; by MAPK1 Ref.15 Ref.19 Ref.20 Ref.22 Ref.9 Ref.11 Ref.12

Modified residue

345

Phosphoserine; by MAPK Ref.22 Ref.7 Ref.9

Modified residue

400

Phosphoserine; by CDK2 Ref.14 Ref.22 Ref.10

Modified residue

676

Phosphoserine Ref.7

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.17

Cross-link

388

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.17 Ref.18 Ref.19

Cross-link

388

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Cross-link

531

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.17

Alternative sequence

1 – 164

164

Missing in isoform A.

VSP_003706

Natural variant

A → T: dbSNP rs11571143. Ref.5

VAR_019221

Natural variant

120

A → V: dbSNP rs11571144. Ref.5

VAR_019222

Natural variant

186

P → L: dbSNP rs11571145. Ref.5

VAR_019223

Natural variant

301

M → R: dbSNP rs11571146. Ref.5

VAR_019224

Natural variant

344

S → T: dbSNP rs3740753. Ref.5 Ref.1

VAR_016117

Natural variant

347

C → S: dbSNP rs11571147.

VAR_025555

Natural variant

444

A → S: dbSNP rs11571150. Ref.5

VAR_019225

Natural variant

529

V → L: dbSNP rs11571151. Ref.5

VAR_019226

Natural variant

536

Q → P: dbSNP rs11571152. Ref.5

VAR_019227

Natural variant

625

R → I: dbSNP rs2020874.

VAR_014627

Natural variant

651

L → V: dbSNP rs11571222. Ref.5

VAR_019228

Natural variant

660

V → L: dbSNP rs1042838. Ref.2 Ref.3

VAR_016118

Natural variant

865

S → L: dbSNP rs2020880. Ref.5

VAR_014628

Mutagenesis

K → R: Some loss of sumoylation; when associated with R-531. Complete loss of sumoylation; when associated with R-388 and R-531. Ref.17

Mutagenesis

294

S → 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.19 Ref.20 Ref.12

Mutagenesis

294

S → D: Decreases protein stability and increases progesterone-induced transcriptional activity. Ref.19 Ref.20 Ref.12

Mutagenesis

344

S → 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.22 Ref.12

Mutagenesis

345

S → 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.22 Ref.12

Mutagenesis

388

K → 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.17 Ref.18 Ref.19

Mutagenesis

400

S → A: Abolishes CDK2-induced activity in the absence, but not in the presence, of progestin. Delayed nuclear translocation in presence of progestin. Ref.14 Ref.22

Mutagenesis

531

K → R: Some loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-388. Ref.17

Sequence conflict

226

G → S in CAA36018. Ref.1

Sequence conflict

256

V → S in CAA36018. Ref.1

933

Helix Strand Turn

Details...

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Sequence		Length	Mass (Da)
Isoform B [UniParc]. Last modified March 21, 2006. Version 4. Checksum: 80452E54FF3A0454 Show »	FASTA	933	98,981
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. Checksum: FE676F25282983F3 Show »	FASTA	769	82,295
10 20 30 40 50 60 MSRSGCKVGD SSGTAAAHKV LPRGLSPARQ LLLPASESPH WSGAPVKPSP QAAAVEVEEE 70 80 90 100 110 120 DGSESEESAG PLLKGKPRAL GGAAAGGGAA AVPPGAAAGG VALVPKEDSR FSAPRVALVE 130 140 150 160 170 180 QDAPMAPGRS PLATTVMDFI HVPILPLNHA LLAARTRQLL EDESYDGGAG AASAFAPPRS 190 200 210 220 230 240 SPCASSTPVA VGDFPDCAYP PDAEPKDDAY PLYSDFQPPA LKIKEEEEGA EASARSPRSY 250 260 270 280 290 300 LVAGANPAAF PDFPLGPPPP LPPRATPSRP GEAAVTAAPA SASVSSASSS GSTLECILYK 310 320 330 340 350 360 AEGAPPQQGP FAPPPCKAPG ASGCLLPRDG LPSTSASAAA AGAAPALYPA LGLNGLPQLG 370 380 390 400 410 420 YQAAVLKEGL PQVYPPYLNY LRPDSEASQS PQYSFESLPQ KICLICGDEA SGCHYGVLTC 430 440 450 460 470 480 GSCKVFFKRA MEGQHNYLCA GRNDCIVDKI RRKNCPACRL RKCCQAGMVL GGRKFKKFNK 490 500 510 520 530 540 VRVVRALDAV ALPQPVGVPN ESQALSQRFT FSPGQDIQLI PPLINLLMSI EPDVIYAGHD 550 560 570 580 590 600 NTKPDTSSSL LTSLNQLGER QLLSVVKWSK SLPGFRNLHI DDQITLIQYS WMSLMVFGLG 610 620 630 640 650 660 WRSYKHVSGQ MLYFAPDLIL NEQRMKESSF YSLCLTMWQI PQEFVKLQVS QEEFLCMKVL 670 680 690 700 710 720 LLLNTIPLEG LRSQTQFEEM RSSYIRELIK AIGLRQKGVV SSSQRFYQLT KLLDNLHDLV 730 740 750 760 KQLHLYCLNT FIQSRALSVE FPEMMSEVIA AQLPKILAGM VKPLLFHKK « Hide

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	« Hide 'large scale' referencesShow '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: 2328727] [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: 3551956] [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: 18375150] [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]	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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 11110801] [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.
[8]	"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: 7476977] [Abstract] Cited for: PHOSPHORYLATION AT SER-81 AND SER-162.
[9]	"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: 8702648] [Abstract] Cited for: PHOSPHORYLATION AT SER-81; SER-102; SER-162; SER-294 AND SER-345.
[10]	"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: 9171245] [Abstract] Cited for: PHOSPHORYLATION AT SER-162; SER-190 AND SER-400.
[11]	"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: 10628747] [Abstract] Cited for: PHOSPHORYLATION AT SER-190 AND SER-294.
[12]	"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: 10655479] [Abstract] Cited for: PHOSPHORYLATION AT SER-294, UBIQUITINATION, MUTAGENESIS OF SER-294; SER-344 AND SER-345.
[13]	"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: 12917342] [Abstract] Cited for: INTERACTION WITH SMARD1.
[14]	"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: 15572662] [Abstract] Cited for: PHOSPHORYLATION AT SER-400, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-400.
[15]	"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: 15798179] [Abstract] Cited for: PHOSPHORYLATION AT SER-162; SER-190 AND SER-294, SUBCELLULAR LOCATION, FUNCTION.
[16]	"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: 16478993] [Abstract] Cited for: INTERACTION WITH UNC45A.
[17]	"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: 17020914] [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.
[18]	"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: 17347654] [Abstract] Cited for: INTERACTION WITH CUEDC2, SUMOYLATION AT LYS-388, UBIQUITINATION AT LYS-388, FUNCTION, MUTAGENESIS OF LYS-388.
[19]	"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: 17717077] [Abstract] Cited for: PHOSPHORYLATION AT SER-294, SUMOYLATION AT LYS-388, FUNCTION, MUTAGENESIS OF SER-294 AND LYS-388.
[20]	"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: 17173941] [Abstract] Cited for: PHOSPHORYLATION AT SER-294, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-294.
[21]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, MASS SPECTROMETRY. Tissue: Platelet.
[22]	"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: 18202149] [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.
[23]	"Atomic structure of progesterone complexed with its receptor." Williams S.P., Sigler P.B. Nature 393:392-396(1998) [PubMed: 9620806] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 682-933.
[24]	"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: 15937332] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 676-933.
+	Additional computationally mapped references.

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NIEHS-SNPs

Wikipedia

Progesterone receptor entry

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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.
CH471065 Genomic DNA. Translation: EAW67000.1.

IPI

IPI00219021.
IPI00297419.

PIR

QRHUP. S09971.

RefSeq

NP_000917.3.

UniGene

Hs.32405

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A28	X-ray	1.80	A/B	678-933	[»]
1E3K	X-ray	2.80	A/B	676-933	[»]
1SQN	X-ray	1.45	A/B	673-933	[»]
1SR7	X-ray	1.46	A/B	676-933	[»]
1ZUC	X-ray	2.00	A/B	676-933	[»]
2C7A	X-ray	2.50	A/B	563-640	[»]
2OVH	X-ray	2.00	A	678-933	[»]
2OVM	X-ray	2.60	A	678-933	[»]
2W8Y	X-ray	1.80	A/B	678-933	[»]
3D90	X-ray	2.26	A/B	676-933	[»]
3KBA	X-ray	2.00	A/B	681-933	[»]

ModBase

Search...

DIP

DIP-578N.
DIP-5967N.

IntAct

P06401. 5 interactions.

STRING

P06401.

PhosphoSite

P06401.

PRIDE

P06401.

Ensembl

ENST00000325455; ENSP00000325120; ENSG00000082175; Homo sapiens. [Genome view]

GeneID

5241.

KEGG

hsa:5241.

UCSC

uc001pgh.2. human.

CTD

5241.

GeneCards

GC11M100414.

H-InvDB

HIX0035826.

HGNC

HGNC:8910. PGR.

HPA

CAB000068.
HPA004751.
HPA008428.
HPA017176.

MIM

607311. gene.

PharmGKB

PA266.

GenAtlas

Search...

eggNOG

prNOG12788.

HOGENOM

HBG127128.

HOVERGEN

P06401.

InParanoid

P06401.

OMA

CLLPRDG.

PhylomeDB

P06401.

Reactome

REACT_71. Gene Expression.

ArrayExpress

P06401.

Bgee

P06401.

CleanEx

HS_PGR.

Genevestigator

P06401.

GermOnline

ENSG00000082175. Homo sapiens.

InterPro

IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000128. Progest_rcpt_N.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Gene3D

G3DSA:1.10.565.10. Nucl_hrmn_rcpt_lig_bd. 1 hit.
G3DSA:3.30.50.10. Znf_NHR/GATA. 1 hit.

Pfam

PF00104. Hormone_recep. 1 hit.
PF02161. Prog_receptor. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR00544. PROGESTRONER.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

DrugBank

DB00304. 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.

NextBio

20248.

SOURCE

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Entry name

PRGR_HUMAN

Accession

Primary (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:	February 9, 2010
This is version 145 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

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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

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.

Note: Mainly nuclear. Ref.14 Ref.15 Ref.20