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A7X8C2 (PRGR_HYLLA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismHylobates lar (Common gibbon) (White-handed gibbon)
Taxonomic identifier9580 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHylobatidaeHylobates

Protein attributes

Sequence length932 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 is involved in activation of c-SRC/MAPK signaling on hormone stimulation By similarity.

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-344 by ERK1/2 MAPK. Interacts with PRMT2 By similarity.

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 By similarity.

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-293 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-387. Phosphorylation on Ser-102 and Ser-344 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162 and Ser-190 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Phosphorylation at Ser-162 and Ser-293, but not at Ser-190, is impaired during the G2/M phase of the cell cycle. Phosphorylation on Ser-344 by ERK1/2 MAPK is required for interaction with SP1 By similarity.

Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-387, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-293 By similarity.

Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-293 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.

Sequence similarities

Belongs to the nuclear hormone receptor family.

Contains 1 nuclear receptor DNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 932932Progesterone receptor
PRO_0000375855

Regions

DNA binding566 – 63873Nuclear receptor
Zinc finger566 – 58621NR C4-type
Zinc finger602 – 62625NR C4-type
Region1 – 565565Modulating, Pro-Rich
Region680 – 932253Steroid-binding
Motif183 – 1875Nuclear localization signal Potential

Amino acid modifications

Modified residue201Phosphoserine By similarity
Modified residue811Phosphoserine By similarity
Modified residue1301Phosphoserine By similarity
Modified residue1621Phosphoserine By similarity
Modified residue1901Phosphoserine By similarity
Modified residue2131Phosphoserine By similarity
Modified residue2931Phosphoserine; by MAPK1 By similarity
Modified residue3441Phosphoserine; by MAPK By similarity
Modified residue6751Phosphoserine By similarity
Cross-link7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link530Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
A7X8C2 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 93845B89631D5DCB

FASTA93298,903
        10         20         30         40         50         60 
MTELKAKGPR APHVAGGPPS PEVGSPLLCR PAAGQFPGSQ TSDTLPEVSA IPISLDGLLF 

        70         80         90        100        110        120 
PRPCQGQDPS YEKTQDQQSL SDVEGAYSRA EATRGAGGSS SSPPEKESGL LDSVLDTLLA 

       130        140        150        160        170        180 
PSGPRQSQPS PPACEVTSSW SLFGPELPED PPAAPATQGV LSPLMSRSGG KAGDSSGTAA 

       190        200        210        220        230        240 
AHKVLPQGLS PSRQLLLPAS GSPHWSGAPV KPSPQPAAVE VEEEDGSESE DSAGPLLKGK 

       250        260        270        280        290        300 
PRALGGAAAG GAAAVPPGAA AGGVALVPKE DSRFSAPRVA LVEQDAPMAP GRSPLATTVM 

       310        320        330        340        350        360 
DFIHVPILPL NHALLAARTR QLLEDENYDG GAGAASAFAP PRSSPSASST PVAVGDFPDC 

       370        380        390        400        410        420 
AYPPDVEPKD DAYPLYGDFQ PPALKIKEEE EGAEASARTP RSYLVAGANP AAFPDFPLGP 

       430        440        450        460        470        480 
PPPLPPRAPP SRPGEAAVTA APASASVSSA SSSGSTLECI LYKAEGAPPQ QGPFAPPPSK 

       490        500        510        520        530        540 
APGAGGCLPP RDGLPSTAAS ASAAGAAPAL YPALRLNGLP QLGYQAAVLK EGLPQVYPPY 

       550        560        570        580        590        600 
LNYLRPDSEA SQSPQYSFES LPQKICLICG DEASGCHYGV LTCGSCKVFF KRAMEGQHNY 

       610        620        630        640        650        660 
LCAGRNDCIV DKIRRKNCPA CRLRKCCQAG MVLGGRKFKK FNKVRVVRAL DAVALPQPVG 

       670        680        690        700        710        720 
IPNESQVLSQ RITFSPGQDI QLIPPLINLL MSIEPDVIYA GHDNTKPDTS SSLLTSLNQL 

       730        740        750        760        770        780 
GERQLLSVVK WSKSLPGFRN LHIDDQITLI QYSWMSLMVF GLGWRSYKHV SGQMLYFAPD 

       790        800        810        820        830        840 
LILNEQRMKE SSFYSLCLTM WQIPQEFVKL QVSQEEFLCM KVLLLLNTIP LEGLRSQTQF 

       850        860        870        880        890        900 
EEMRASYIRE LIKAIGLRQK GVVSSSQRFY QLTKLLDNLH DLVKQLHLYC LNTFIQSRAL 

       910        920        930 
SVEFPEMMSE VIAAQLPKIL AGMVKPLLFH KK 

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References

[1]"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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ234984 Genomic DNA. Translation: ABB72144.1.

3D structure databases

ProteinModelPortalA7X8C2.
SMRA7X8C2. Positions 562-639, 681-931.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEA7X8C2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. SSF48508. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePRGR_HYLLA
AccessionPrimary (citable) accession number: A7X8C2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 26, 2009
Last sequence update: October 23, 2007
Last modified: March 19, 2014
This is version 33 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