Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Proline-, glutamic acid- and leucine-rich protein 1  

UniProtKB / Swiss-Prot ID :  PELP1_MOUSE

Gene Name (Synonyms) : 
Pelp1, Mnar  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus (By similarity). Cytoplasm (By similarity). Note=Also found associated with the plasma membrane (By similarity). 

Protein Function :  Coactivator of estrogen receptor-mediated transcription and a corepressor of other nuclear hormone receptors and sequence- specific transcription factors. Plays a role in estrogen receptor (ER) genomic activity when present in the nuclear compartment by activating the ER target genes in a hormonal stimulation dependent manner. Can facilitate ER non-genomic signaling via SRC and PI3K interaction in the cytosol. Plays a role in E2-mediated cell cycle progression by interacting with RB1. May have important functional implications in ER/growth factor cross-talk. Interacts with several growth factor signaling components including EGFR and HRS. Involved in nuclear receptor signaling via its interaction with AR and NR3C1. May promote tumorigenesis via its interaction with and modulation of several oncogenes including SRC, PI3K, STAT3 and EGFR. Plays a role in cancer cell metastasis via its ability to modulate E2-mediated cytoskeleton changes and cell migration via its interaction with SRC and PI3K (By similarity). 

Protein Sequence MAAAVLSGASAGSPAGAPGGPGGLSAVGSGPRLRLLLLESISGLLQPRTASPVAPVHPPIQWAPHLPGLM...
Predicted Secondary Structure CCCCEECCCCCCCCCCCCCCCCCCCCCCCCCCEEEEHHHHHHHHHCCCCCCCCCCCCCCCCCCCCHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
13PhosphoserineASAGSPAGA
CCCCCCCCC
15.99Phosphositeplus
Link-
13Phosphoserine.ASAGSPAGA
CCCCCCCCC
15.99UniProtKB
Link-
740PhosphoserineHRAGSGEDP
CCCCCCCCC
37.72Phosphositeplus
Link-
749PhosphoserineVLAPSGTPP
CCCCCCCCC
50.09Phosphositeplus
Link-
751PhosphothreonineAPSGTPPPS
CCCCCCCCC
36.64PhosphoELM
Link-
751PhosphothreonineAPSGTPPPS
CCCCCCCCC
36.64Phosphositeplus
Link-
751PhosphothreonineAPSGTPPPS
CCCCCCCCC
36.64SysPTM
Link-
751Phosphothreonine.APSGTPPPS
CCCCCCCCC
36.64UniProtKB
Link-
755PhosphoserineTPPPSIPPD
CCCCCCCCC
54.20Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-751, AND MASSSPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures