Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
PR (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
PR a nuclear hormone receptor and transcription factor. Regulates gene expression and affects cellular proliferation and differentiation in target tissues. Two splice-variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein; Nuclear receptor
Cellular Component: nucleoplasm; mitochondrial outer membrane
Molecular Function: protein binding; ligand-dependent nuclear receptor activity; enzyme binding; DNA binding; zinc ion binding; sequence-specific DNA binding; steroid hormone receptor activity; steroid binding; receptor binding
Biological Process: transcription initiation from RNA polymerase II promoter; progesterone receptor signaling pathway; cell-cell signaling; epithelial cell maturation; gene expression; signal transduction; ovulation from ovarian follicle; regulation of epithelial cell proliferation
Reference #:  P06401 (UniProtKB)
Alt. Names/Synonyms: NR3C3; Nuclear receptor subfamily 3 group C member 3; PGR; PRGR; Progesterone receptor
Gene Symbols: PGR
Molecular weight: 98,981 Da
Basal Isoelectric point: 6.09  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PR

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  DISEASE  |  Source  |  NURSA  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
cell adhesion, altered: S294‑p
cell growth, altered: S294‑p, K388‑s
transcription, induced: S81‑p, S102‑p, S162‑p, S190‑p, S294‑p, S345‑p, S400‑p, S676‑p
transcription, inhibited: K388‑s
intracellular localization: S294‑p
molecular association, regulation: S81‑p, S345‑p
protein degradation: S294‑p
sumoylation: S294‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
1 0 K7-s _MTELKAkGPRAPHV
0 1 S20-p HVAGGPPsPEVGSPL
5 0 S81-p TQDQQSLsDVEGAYS
2 1 S102-p GAGGSSSsPPEKDSG
0 1 S130-p GPGQSQPsPPACEVT
5 4 S162-p PATQRVLsPLMSRSG
1 0 K183-a SGTAAAHkVLPRGLs
0 2 K183-u SGTAAAHkVLPRGLs
5 1 S190-p kVLPRGLsPARQLLL
1 0 S213-p SGAPVKPsPQAAAVE
1 0 S227 EVEEEDGSESEESAG
1 0 S276 PKEDSRFSAPRVALV
19 0 S294-p APMAPGRsPLATTVM
1 0 S328 RQLLEDESYDGGAGA
6 1 S345-p AFAPPRSsPCASSTP
2 0 K388-u QPPALKIkEEEEGAE
7 0 K388-s QPPALKIkEEEEGAE
7 0 S400-p GAEASARsPRSYLVA
1 0 K464-m1 TLECILYkAEGAPPQ
1 0 K531-s GYQAAVLkEGLPQVY
1 0 S549-p LNYLRPDsEAsQsPQ
1 0 S552-p LRPDsEAsQsPQYsF
2 0 S554-p PDsEAsQsPQYsFEs
2 0 S558-p AsQsPQYsFEsLPQK
1 0 S561-p sPQYsFEsLPQKICL
2 1 S676-p LSQRFTFsPGQDIQL
3171 : Phospho-Progesterone Receptor (Ser190) Antibody
13736 : Phospho-Progesterone Receptor (Ser294) Antibody
12783 : Phospho-Progesterone Receptor (Ser345) Antibody
  PR iso2  
- gap
- gap
- gap
- gap
- gap
- gap
K19 SGTAAAHKVLPRGLs
K19 SGTAAAHKVLPRGLs
S26-p KVLPRGLsPARQLLL
S49 SGAPVKPSPQAAAVE
S63-p EVEEEDGsESEESAG
S112-p PKEDSRFsAPRVALV
S130-p APMAPGRsPLATTVM
S164-p RQLLEDEsYDGGAGA
S181 AFAPPRSSPCASSTP
K224 QPPALKIKEEEEGAE
K224 QPPALKIKEEEEGAE
S236-p GAEASARsPRSYLVA
K300 TLECILYKAEGAPPQ
K367 GYQAAVLKEGLPQVY
S385 LNYLRPDSEASQsPQ
S388 LRPDSEASQsPQYsF
S390-p PDSEASQsPQYsFES
S394-p ASQsPQYsFESLPQK
S397 sPQYsFESLPQKICL
S512-p LSQRFTFsPGQDIQL
13736 : Phospho-Progesterone Receptor (Ser294) Antibody
  mouse

 
K7 _MTELQAKDPQVLHT
S20 HTSGASPSPPHIGSP
S82 TGDQQSLSDVEGAFS
S102 HREGGRNSRPPEKDS
S131 GPEQSHASPPACEAI
S163 PATKGLLSPLMSRPE
K184 SGTGRGQKVLPKGLS
K184 SGTGRGQKVLPKGLS
S191 KVLPKGLSPPRQLLL
S214 PGAGVKPSPQPAAGE
- gap
S277 PKEDSRFSAPRVSLE
S294-p SPIAPGRsPLATTVV
S328 RQLLEGESYDGGATA
S343 GPFCPPRSPSAPSTP
K386 QTPGLKIKEEEEGAD
K386 QTPGLKIKEEEEGAD
S398 GADAAVRSPRPYLSA
K459 ALECILYKAEAPPTQ
K521 GYQAAVLKDSLPQVY
S539 LNYLRPDSEASQSPQ
S542 LRPDSEASQSPQYGF
S544 PDSEASQSPQYGFDS
G548 ASQSPQYGFDSLPQK
S551 SPQYGFDSLPQKICL
S666 LSQRITFSPNQEIQL
13736 : Phospho-Progesterone Receptor (Ser294) Antibody
  rat

 
K7 _MTELQAKDPRTLHT
S20 HTSGAAPSPTHVGSP
S82 TQNQQSLSDVEGAFS
S98 VEASRRRSRNPRAPE
S130 GPEQSQTSPPACEAI
S162 PATKGLLSPLMSRPE
K183 SGTGAGQKVLPKAVS
K183 SGTGAGQKVLPKAVS
S190 KVLPKAVSPPRQLLL
S213 PGAGVKPSQQPATVE
- gap
S276 PKEDSRFSAPRVSLE
S293 APVAPGRSPLATTVV
S327 RQLLEGDSYDGGAAA
S344 PFAPPRGSPSAPSPP
K387 QPPGLKIKEEEEGTE
K387 QPPGLKIKEEEEGTE
S399 GTEAASRSPRPYLLA
K458 ALECILYKAEGAPPT
K521 GYQAAVLKDSLPQVY
S539 LNYLRPDSEASQSPQ
S542 LRPDSEASQSPQYGF
S544 PDSEASQSPQYGFDS
G548 ASQSPQYGFDSLPQK
S551 SPQYGFDSLPQKICL
S666 LGQRITFSPNQEIQL
13736 : Phospho-Progesterone Receptor (Ser294) Antibody
  chicken

 
K7 _MTEVKSKETRAPSS
S13 SKETRAPSSARDGAV
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S259 SAFGPRSSPSVPAAD
K294 FQSALKIKEEGVGLP
K294 FQSALKIKEEGVGLP
- gap
K335 SLECVLYKAEPPLLP
K385 GFPAAVLKEGLPQLC
T403 LGYVRPDTETSQSSQ
S406 VRPDTETSQSSQYSF
S408 PDTETSQSSQYSFES
S412 TSQSSQYSFESLPQK
S415 SSQYSFESLPQKICL
S529 LTQRLSFSPNQEIPF
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.