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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
g O-GlcNAc
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; intracellular membrane-bound organelle; cytoplasm; nucleolus; nucleus
Molecular Function: identical protein binding; ligand-dependent nuclear receptor activity; protein binding; 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; PR; 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.


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Sites Implicated In
cell adhesion, altered: S294‑p
cell growth, altered: S294‑p, K388‑s
transcription, altered: S81‑p, S102‑p, S162‑p, S190‑p, S294‑p, S345‑p, K388‑s, S400‑p, S676‑p
intracellular localization: S294‑p
molecular association, regulation: 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
4 0 S81-p TQDQQSLsDVEGAys
0 1 Y87-p LsDVEGAysRAEATR
0 1 S88-p sDVEGAysRAEATRG
2 1 S102-p GAGGSSSsPPEKDSG
0 1 S130-p GPGQSQPsPPACEVT
5 3 S162-p PATQRVLsPLMSRSG
0 2 K183-u SGTAAAHkVLPRGLs
4 1 S190-p kVLPRGLsPARQLLL
1 0 S213-p SGAPVKPsPQAAAVE
0 1 S229 EEEDGSESEESAGPL
0 1 S232 DGSESEESAGPLLKG
16 0 S294-p APMAPGRsPLATTVM
5 1 S345-p AFAPPRSsPCASSTP
2 0 K388-u QPPALKIkEEEEGAE
7 0 K388-s QPPALKIkEEEEGAE
5 0 S400-p GAEASARsPRSYLVA
0 1 N410 SYLVAGANPAAFPDF
1 0 K531-s GYQAAVLkEGLPQVY
1 0 S549-p LNYLRPDsEAsQsPQ
1 0 S552-p LRPDsEAsQsPQYsF
1 0 S554-p PDsEAsQsPQYsFEs
1 0 S558-p AsQsPQYsFEsLPQK
1 0 S561-p sPQYsFEsLPQKICL
1 1 S676-p LSQRFTFsPGQDIQL
3171 : Phospho-Progesterone Receptor (Ser190) Antibody
  PR iso2  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K19 SGTAAAHKVLPRGLS
S26 KVLPRGLSPARQLLL
S49 SGAPVKPSPQAAAVE
S65 EEEDGSESEESAGPL
S68 DGSESEESAGPLLKG
S130 APMAPGRSPLATTVM
S181 AFAPPRSSPCASSTP
K224 QPPALKIKEEEEGAE
K224 QPPALKIKEEEEGAE
S236 GAEASARSPRSYLVA
N246 SYLVAGANPAAFPDF
K367 GYQAAVLKEGLPQVY
S385 LNYLRPDSEASQSPQ
S388 LRPDSEASQSPQYSF
S390 PDSEASQSPQYSFES
S394 ASQSPQYSFESLPQK
S397 SPQYSFESLPQKICL
S512 LSQRFTFSPGQDIQL
  mouse

 
K7 _MTELQAKDPQVLHT
S20 HTSGASPSPPHIGSP
S82 TGDQQSLSDVEGAFS
F88 LSDVEGAFSGVEATH
S89 SDVEGAFSGVEATHR
- gap
S131 GPEQSHASPPACEAI
S163 PATKGLLSPLMSRPE
K184 SGTGRGQKVLPKGLS
S191 KVLPKGLSPPRQLLL
S214 PGAGVKPSPQPAAGE
T230-p EEDSGLEtEGsASPL
S233-p SGLEtEGsASPLLKS
S294-p SPIAPGRsPLATTVV
- gap
K386 QTPGLKIKEEEEGAD
K386 QTPGLKIKEEEEGAD
S398 GADAAVRSPRPYLSA
S408-p PYLSAGAsSSTFPDF
K521 GYQAAVLKDSLPQVY
S539 LNYLRPDSEASQSPQ
S542 LRPDSEASQSPQYGF
S544 PDSEASQSPQYGFDS
G548 ASQSPQYGFDSLPQK
S551 SPQYGFDSLPQKICL
S666 LSQRITFSPNQEIQL
  rat

 
K7 _MTELQAKDPRTLHT
S20 HTSGAAPSPTHVGSP
S82 TQNQQSLSDVEGAFS
F88 LSDVEGAFSGVEASR
S89 SDVEGAFSGVEASRR
- gap
S130 GPEQSQTSPPACEAI
S162 PATKGLLSPLMSRPE
K183 SGTGAGQKVLPKAVS
S190 KVLPKAVSPPRQLLL
S213 PGAGVKPSQQPATVE
T229 EEDGGLETEGSAGPL
S232 GGLETEGSAGPLLKS
S293 APVAPGRSPLATTVV
S344 PFAPPRGSPSAPSPP
K387 QPPGLKIKEEEEGTE
K387 QPPGLKIKEEEEGTE
S399 GTEAASRSPRPYLLA
S409 PYLLAGASAATFPDF
K521 GYQAAVLKDSLPQVY
S539 LNYLRPDSEASQSPQ
S542 LRPDSEASQSPQYGF
S544 PDSEASQSPQYGFDS
G548 ASQSPQYGFDSLPQK
S551 SPQYGFDSLPQKICL
S666 LGQRITFSPNQEIQL
  chicken

 
K7 _MTEVKSKETRAPSS
S13 SKETRAPSSARDGAV
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S176 RPGPEDASENRAPGL
- gap
G219 AAVEPGAGQDYLHVP
S259 SAFGPRSSPSVPAAD
K294 FQSALKIKEEGVGLP
K294 FQSALKIKEEGVGLP
- gap
A313 PFLGAKAAPADFAQP
K385 GFPAAVLKEGLPQLC
T403 LGYVRPDTETSQSSQ
S406 VRPDTETSQSSQYSF
S408 PDTETSQSSQYSFES
S412 TSQSSQYSFESLPQK
S415 SSQYSFESLPQKICL
S529 LTQRLSFSPNQEIPF
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