SubmitCancel

Skip Header

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

P06401

- PRGR_HUMAN

UniProt

P06401 - PRGR_HUMAN

(max 400 entries)x

Your basket is currently empty.

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

Protein
Progesterone receptor
Gene
PGR, NR3C3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.8 Publications
Isoform A: inactive in stimulating c-Src/MAPK signaling on hormone stimulation.8 Publications
Isoform 4: Increases mitochondrial membrane potential and cellular respiration upon stimulation by progesterone.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi567 – 63973Nuclear receptor
Add
BLAST
Zinc fingeri567 – 58721NR C4-type
Add
BLAST
Zinc fingeri603 – 62725NR C4-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. enzyme binding Source: UniProtKB
  3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: Ensembl
  4. protein binding Source: UniProtKB
  5. receptor binding Source: UniProtKB
  6. sequence-specific DNA binding Source: InterPro
  7. steroid binding Source: UniProtKB-KW
  8. steroid hormone receptor activity Source: ProtInc
  9. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell-cell signaling Source: ProtInc
  2. epithelial cell maturation Source: Ensembl
  3. gene expression Source: Reactome
  4. negative regulation of gene expression Source: UniProtKB
  5. ovulation from ovarian follicle Source: Ensembl
  6. progesterone receptor signaling pathway Source: Ensembl
  7. regulation of epithelial cell proliferation Source: Ensembl
  8. signal transduction Source: ProtInc
  9. tertiary branching involved in mammary gland duct morphogenesis Source: Ensembl
  10. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_116022. Nuclear signaling by ERBB4.
REACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP06401.

Names & Taxonomyi

Protein namesi
Recommended name:
Progesterone receptor
Short name:
PR
Alternative name(s):
Nuclear receptor subfamily 3 group C member 3
Gene namesi
Name:PGR
Synonyms:NR3C3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:8910. PGR.

Subcellular locationi

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.4 Publications
Isoform A : Nucleus. Cytoplasm
Note: Mainly nuclear.4 Publications
Isoform 4 : Mitochondrion outer membrane 4 Publications

GO - Cellular componenti

  1. mitochondrial outer membrane Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71K → R: Some loss of sumoylation; when associated with R-531. Complete loss of sumoylation; when associated with R-388 and R-531. 1 Publication
Mutagenesisi294 – 2941S → 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. 3 Publications
Mutagenesisi294 – 2941S → D: Decreases protein stability and increases progesterone-induced transcriptional activity. 3 Publications
Mutagenesisi344 – 3441S → 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. 2 Publications
Mutagenesisi345 – 3451S → 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. 2 Publications
Mutagenesisi388 – 3881K → 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. 3 Publications
Mutagenesisi400 – 4001S → A: Abolishes CDK2-induced activity in the absence, but not in the presence, of progestin. Delayed nuclear translocation in presence of progestin. 2 Publications
Mutagenesisi531 – 5311K → R: Some loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-388. 1 Publication

Organism-specific databases

PharmGKBiPA266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 933933Progesterone receptor
PRO_0000053693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei81 – 811Phosphoserine2 Publications
Modified residuei102 – 1021Phosphoserine2 Publications
Modified residuei130 – 1301Phosphoserine1 Publication
Modified residuei162 – 1621Phosphoserine5 Publications
Modified residuei190 – 1901Phosphoserine4 Publications
Modified residuei213 – 2131Phosphoserine1 Publication
Modified residuei294 – 2941Phosphoserine; by MAPK17 Publications
Modified residuei345 – 3451Phosphoserine; by MAPK3 Publications
Cross-linki388 – 388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate3 Publications
Cross-linki388 – 388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei400 – 4001Phosphoserine; by CDK23 Publications
Cross-linki531 – 531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei676 – 6761Phosphoserine1 Publication

Post-translational modificationi

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 SP1.11 Publications
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-294.3 Publications
Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294.3 Publications
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.1 Publication

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP06401.
PaxDbiP06401.
PRIDEiP06401.

PTM databases

PhosphoSiteiP06401.

Expressioni

Gene expression databases

ArrayExpressiP06401.
BgeeiP06401.
CleanExiHS_PGR.
GenevestigatoriP06401.

Organism-specific databases

HPAiCAB000068.
CAB055100.
HPA004751.
HPA008428.
HPA017176.

Interactioni

Subunit structurei

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 PRMT2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUEDC2Q9H4679EBI-78539,EBI-1248228
STAT3P407633EBI-78539,EBI-518675

Protein-protein interaction databases

BioGridi111260. 65 interactions.
DIPiDIP-578N.
DIP-5967N.
IntActiP06401. 8 interactions.
MINTiMINT-1505587.
STRINGi9606.ENSP00000325120.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni568 – 5703
Beta strandi576 – 5783
Beta strandi581 – 5833
Helixi585 – 59612
Turni613 – 6186
Helixi620 – 63011
Helixi686 – 6949
Helixi711 – 73525
Helixi739 – 7413
Helixi744 – 77128
Beta strandi774 – 7796
Beta strandi782 – 7843
Helixi786 – 7883
Helixi792 – 81120
Helixi815 – 82612
Beta strandi828 – 8303
Helixi838 – 85720
Helixi863 – 89634
Helixi898 – 9014
Helixi907 – 92115
Beta strandi925 – 9273

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP06401.
SMRiP06401. Positions 563-933.

Miscellaneous databases

EvolutionaryTraceiP06401.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 566566Modulating, Pro-Rich
Add
BLAST
Regioni681 – 933253Steroid-binding
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi183 – 1875Nuclear localization signal Reviewed prediction

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG273252.
HOGENOMiHOG000290653.
HOVERGENiHBG007583.
InParanoidiP06401.
KOiK08556.
OMAiRPCQGQD.
OrthoDBiEOG751NF2.
PhylomeDBiP06401.
TreeFamiTF106510.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR008946. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF02161. Prog_receptor. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00544. PROGESTRONER.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 2 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform B (identifier: P06401-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MTELKAKGPR APHVAGGPPS PEVGSPLLCR PAAGPFPGSQ TSDTLPEVSA    50
IPISLDGLLF PRPCQGQDPS DEKTQDQQSL SDVEGAYSRA EATRGAGGSS 100
SSPPEKDSGL LDSVLDTLLA PSGPGQSQPS PPACEVTSSW CLFGPELPED 150
PPAAPATQRV LSPLMSRSGC KVGDSSGTAA AHKVLPRGLS PARQLLLPAS 200
ESPHWSGAPV KPSPQAAAVE VEEEDGSESE ESAGPLLKGK PRALGGAAAG 250
GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTV 300
MDFIHVPILP LNHALLAART RQLLEDESYD GGAGAASAFA PPRSSPCASS 350
TPVAVGDFPD CAYPPDAEPK DDAYPLYSDF QPPALKIKEE EEGAEASARS 400
PRSYLVAGAN PAAFPDFPLG PPPPLPPRAT PSRPGEAAVT AAPASASVSS 450
ASSSGSTLEC ILYKAEGAPP QQGPFAPPPC KAPGASGCLL PRDGLPSTSA 500
SAAAAGAAPA LYPALGLNGL PQLGYQAAVL KEGLPQVYPP YLNYLRPDSE 550
ASQSPQYSFE SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN 600
YLCAGRNDCI VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVVRA 650
LDAVALPQPV GVPNESQALS QRFTFSPGQD IQLIPPLINL LMSIEPDVIY 700
AGHDNTKPDT SSSLLTSLNQ LGERQLLSVV KWSKSLPGFR NLHIDDQITL 750
IQYSWMSLMV FGLGWRSYKH VSGQMLYFAP DLILNEQRMK ESSFYSLCLT 800
MWQIPQEFVK LQVSQEEFLC MKVLLLLNTI PLEGLRSQTQ FEEMRSSYIR 850
ELIKAIGLRQ KGVVSSSQRF YQLTKLLDNL HDLVKQLHLY CLNTFIQSRA 900
LSVEFPEMMS EVIAAQLPKI LAGMVKPLLF HKK 933
Length:933
Mass (Da):98,981
Last modified:March 21, 2006 - v4
Checksum:i80452E54FF3A0454
GO
Isoform A (identifier: P06401-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:769
Mass (Da):82,295
Checksum:iFE676F25282983F3
GO
Isoform 3 (identifier: P06401-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-594: Missing.

Show »
Length:339
Mass (Da):38,798
Checksum:i4496D6B5A4EC95FD
GO
Isoform 4 (identifier: P06401-4) [UniParc]FASTAAdd to Basket

Also known as: PR-M

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MTELKAKGPRAPHVAG → MEFIYIYMNFFFFFSV
     17-635: Missing.

Show »
Length:314
Mass (Da):36,318
Checksum:iA85692E905BFB9B3
GO
Isoform 5 (identifier: P06401-5) [UniParc]FASTAAdd to Basket

Also known as: delta4

The sequence of this isoform differs from the canonical sequence as follows:
     636-737: Missing.

Show »
Length:831
Mass (Da):87,747
Checksum:iEC4882171DD1C48B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501A → T.1 Publication
Corresponds to variant rs11571143 [ dbSNP | Ensembl ].
VAR_019221
Natural varianti120 – 1201A → V.1 Publication
Corresponds to variant rs11571144 [ dbSNP | Ensembl ].
VAR_019222
Natural varianti186 – 1861P → L.1 Publication
Corresponds to variant rs11571145 [ dbSNP | Ensembl ].
VAR_019223
Natural varianti301 – 3011M → R.1 Publication
Corresponds to variant rs11571146 [ dbSNP | Ensembl ].
VAR_019224
Natural varianti344 – 3441S → T.2 Publications
Corresponds to variant rs3740753 [ dbSNP | Ensembl ].
VAR_016117
Natural varianti347 – 3471C → S.
Corresponds to variant rs11571147 [ dbSNP | Ensembl ].
VAR_025555
Natural varianti444 – 4441A → S.1 Publication
Corresponds to variant rs11571150 [ dbSNP | Ensembl ].
VAR_019225
Natural varianti529 – 5291V → L.1 Publication
Corresponds to variant rs11571151 [ dbSNP | Ensembl ].
VAR_019226
Natural varianti536 – 5361Q → P.1 Publication
Corresponds to variant rs11571152 [ dbSNP | Ensembl ].
VAR_019227
Natural varianti625 – 6251R → I.
Corresponds to variant rs2020874 [ dbSNP | Ensembl ].
VAR_014627
Natural varianti651 – 6511L → V.1 Publication
Corresponds to variant rs11571222 [ dbSNP | Ensembl ].
VAR_019228
Natural varianti660 – 6601V → L.3 Publications
Corresponds to variant rs1042838 [ dbSNP | Ensembl ].
VAR_016118
Natural varianti865 – 8651S → L.1 Publication
Corresponds to variant rs2020880 [ dbSNP | Ensembl ].
VAR_014628

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 594594Missing in isoform 3.
VSP_046942Add
BLAST
Alternative sequencei1 – 164164Missing in isoform A.
VSP_003706Add
BLAST
Alternative sequencei1 – 1616MTELK…PHVAG → MEFIYIYMNFFFFFSV in isoform 4.
VSP_047454Add
BLAST
Alternative sequencei17 – 635619Missing in isoform 4.
VSP_047455Add
BLAST
Alternative sequencei636 – 737102Missing in isoform 5.
VSP_053543Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261G → S in CAA36018. 1 Publication
Sequence conflicti256 – 2561V → S in CAA36018. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51730 mRNA. Translation: CAA36018.1.
M15716 mRNA. Translation: AAA60081.1.
AF016381 mRNA. Translation: AAD01587.1.
AB084248 mRNA. Translation: BAB91074.1.
DQ234979 Genomic DNA. Translation: ABB72139.1.
AY212933 mRNA. Translation: AAO61671.1.
AK304853 mRNA. Translation: BAG65592.1.
AY525610 Genomic DNA. Translation: AAS00096.1.
AP001533 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66999.1.
CH471065 Genomic DNA. Translation: EAW67000.1.
CCDSiCCDS59229.1. [P06401-3]
CCDS8310.1. [P06401-1]
PIRiS09971. QRHUP.
RefSeqiNP_000917.3. NM_000926.4. [P06401-1]
NP_001189403.1. NM_001202474.3. [P06401-2]
NP_001258090.1. NM_001271161.2.
NP_001258091.1. NM_001271162.1. [P06401-3]
UniGeneiHs.32405.
Hs.742403.

Genome annotation databases

EnsembliENST00000263463; ENSP00000263463; ENSG00000082175. [P06401-5]
ENST00000325455; ENSP00000325120; ENSG00000082175. [P06401-1]
ENST00000534013; ENSP00000436561; ENSG00000082175. [P06401-3]
GeneIDi5241.
KEGGihsa:5241.
UCSCiuc001pgh.2. human. [P06401-1]
uc001pgi.3. human.

Polymorphism databases

DMDMi90110048.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Progesterone receptor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X51730 mRNA. Translation: CAA36018.1 .
M15716 mRNA. Translation: AAA60081.1 .
AF016381 mRNA. Translation: AAD01587.1 .
AB084248 mRNA. Translation: BAB91074.1 .
DQ234979 Genomic DNA. Translation: ABB72139.1 .
AY212933 mRNA. Translation: AAO61671.1 .
AK304853 mRNA. Translation: BAG65592.1 .
AY525610 Genomic DNA. Translation: AAS00096.1 .
AP001533 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66999.1 .
CH471065 Genomic DNA. Translation: EAW67000.1 .
CCDSi CCDS59229.1. [P06401-3 ]
CCDS8310.1. [P06401-1 ]
PIRi S09971. QRHUP.
RefSeqi NP_000917.3. NM_000926.4. [P06401-1 ]
NP_001189403.1. NM_001202474.3. [P06401-2 ]
NP_001258090.1. NM_001271161.2.
NP_001258091.1. NM_001271162.1. [P06401-3 ]
UniGenei Hs.32405.
Hs.742403.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3G8O X-ray 1.90 A/B 673-933 [» ]
3HQ5 X-ray 2.10 A/B 678-933 [» ]
3KBA X-ray 2.00 A/B 681-933 [» ]
3ZR7 X-ray 1.65 A/B 678-933 [» ]
3ZRA X-ray 1.90 A/B 678-933 [» ]
3ZRB X-ray 1.80 A/B 678-933 [» ]
4A2J X-ray 2.00 A/B 678-933 [» ]
4APU X-ray 1.90 A/B 678-933 [» ]
ProteinModelPortali P06401.
SMRi P06401. Positions 563-933.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111260. 65 interactions.
DIPi DIP-578N.
DIP-5967N.
IntActi P06401. 8 interactions.
MINTi MINT-1505587.
STRINGi 9606.ENSP00000325120.

Chemistry

BindingDBi P06401.
ChEMBLi CHEMBL208.
DrugBanki 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.
GuidetoPHARMACOLOGYi 627.

PTM databases

PhosphoSitei P06401.

Polymorphism databases

DMDMi 90110048.

Proteomic databases

MaxQBi P06401.
PaxDbi P06401.
PRIDEi P06401.

Protocols and materials databases

DNASUi 5241.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263463 ; ENSP00000263463 ; ENSG00000082175 . [P06401-5 ]
ENST00000325455 ; ENSP00000325120 ; ENSG00000082175 . [P06401-1 ]
ENST00000534013 ; ENSP00000436561 ; ENSG00000082175 . [P06401-3 ]
GeneIDi 5241.
KEGGi hsa:5241.
UCSCi uc001pgh.2. human. [P06401-1 ]
uc001pgi.3. human.

Organism-specific databases

CTDi 5241.
GeneCardsi GC11M100943.
HGNCi HGNC:8910. PGR.
HPAi CAB000068.
CAB055100.
HPA004751.
HPA008428.
HPA017176.
MIMi 607311. gene.
neXtProti NX_P06401.
PharmGKBi PA266.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG273252.
HOGENOMi HOG000290653.
HOVERGENi HBG007583.
InParanoidi P06401.
KOi K08556.
OMAi RPCQGQD.
OrthoDBi EOG751NF2.
PhylomeDBi P06401.
TreeFami TF106510.

Enzyme and pathway databases

Reactomei REACT_116022. Nuclear signaling by ERBB4.
REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki P06401.

Miscellaneous databases

EvolutionaryTracei P06401.
GeneWikii Progesterone_receptor.
GenomeRNAii 5241.
NextBioi 20248.
PROi P06401.
SOURCEi Search...

Gene expression databases

ArrayExpressi P06401.
Bgeei P06401.
CleanExi HS_PGR.
Genevestigatori P06401.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR008946. 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 ]
Pfami PF00104. Hormone_recep. 1 hit.
PF02161. Prog_receptor. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR00544. PROGESTRONER.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 2 hits.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "Progesterone Receptor, alternative splicing variant, mRNA."
    Hisatomi H., Wakita K., Kohno N., Nagao K., Hirata H., Hikiji K.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    Tissue: Mammary tumor.
  5. "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].
  6. "Cloning and expression of a novel, truncated, progesterone receptor."
    Saner K.J., Welter B.H., Zhang F., Hansen E., Dupont B., Wei Y., Price T.M.
    Mol. Cell. Endocrinol. 200:155-163(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT LEU-660.
    Tissue: Adipose tissue and Aorta.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Uterus.
  8. 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.
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "A truncated progesterone receptor (PR-M) localizes to the mitochondrion and controls cellular respiration."
    Dai Q., Shah A.A., Garde R.V., Yonish B.A., Zhang L., Medvitz N.A., Miller S.E., Hansen E.L., Dunn C.N., Price T.M.
    Mol. Endocrinol. 27:741-753(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 204-217, FUNCTION (ISOFORM 4), SUBCELLULAR LOCATION (ISOFORM 4).
    Tissue: Heart.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. "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.
  29. "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.
  30. "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.

Entry informationi

Entry nameiPRGR_HUMAN
AccessioniPrimary (citable) accession number: P06401
Secondary accession number(s): A7LQ08
, A7X8B0, B4E3T0, Q8TDS3, Q9UPF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: March 21, 2006
Last modified: September 3, 2014
This is version 192 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi