Curated Information
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
Curated Information Page
PubMed Id: 19914168 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Alarcón C, et al. (2009) Nuclear CDKs drive Smad transcriptional activation and turnover in BMP and TGF-beta pathways. Cell 139, 757-69 19914168
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
Download Sites

S187-p - Smad1 (human) ▲
Orthologous residues
Smad1 (human): S187‑p, Smad1 (mouse): S187‑p, Smad1 (rat): S187‑p
Characterization
 Methods used to characterize site in vivo:  immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  cervical cancer, cervical adenocarcinoma
 Relevant cell lines - cell types - tissues:  HaCaT (keratinocyte), HeLa S3 (cervical), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CDK9 (human)
KINASE CDK8 (human)
KINASE ERK2 (human)

S195-p - Smad1 (human) ▲
Orthologous residues
Smad1 (human): S195‑p, Smad1 (mouse): S195‑p, Smad1 (rat): S195‑p
Characterization
 Methods used to characterize site in vivo:  immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  cervical cancer, cervical adenocarcinoma
 Relevant cell lines - cell types - tissues:  HaCaT (keratinocyte), HeLa S3 (cervical), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CDK8 (human)
KINASE ERK2 (human)
KINASE CDK9 (human)

S206-p - Smad1 (human) ▲
Orthologous residues
Smad1 (human): S206‑p, Smad1 (mouse): S206‑p, Smad1 (rat): S206‑p
Characterization
 Methods used to characterize site in vivo:  immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  cervical cancer, cervical adenocarcinoma
 Relevant cell lines - cell types - tissues:  HaCaT (keratinocyte), HeLa S3 (cervical), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CDK9 (human)
KINASE CDK8 (human)
KINASE ERK2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CDK9 (human) siRNA inhibition of enzyme, activation of upstream enzyme
KINASE CDK8 (human) co-immunoprecipitation, siRNA inhibition of enzyme, activation of upstream enzyme
KINASE CDK7 (human) siRNA inhibition of enzyme, activation of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
BMP2 no change compared to control cytoplasmic fraction
BMP2 increase nuclear fraction
TGF-beta no change compared to control cytoplasmic and nuclear fractions
UV increase
BMP2 no change compared to control Smad1C knockin MEFs
UV increase Smad1C knockin MEFs
BMP2 no change compared to control Smad1L knockin MEFs
UV no change compared to control Smad1L knockin MEFs
BMP2 Smad4 (human) increase Smad4 -/- decrease
BMP2 Smad4 (human) no effect upon treatment-induced increase WT
BMP2 FOXO4 (human) increase FoxO4 siRNA decreases
BMP2 SMURF1 iso3 (human) increase Smurf1 siRNA decrease
MG132 BMP2 no effect upon treatment-induced increase
BMP2 no effect upon treatment-induced increase alpha-amanatin
augment treatment-induced decrease
U0126 BMP2 no effect upon treatment-induced increase
SB203580 BMP2 no effect upon treatment-induced increase
SP600125 BMP2 no effect upon treatment-induced increase
U0126, SP600125, SB203580 BMP2 no effect upon treatment-induced increase
flavopiridol BMP2 inhibit treatment-induced increase
TGF-beta no change compared to control cytoplasmic fraction
flavopiridol TGF-beta no change compared to control
TGF-beta increase nuclear fraction
flavopiridol TGF-beta inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  transcription, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
YAP1 (human) WW Induces transcription, altered co-immunoprecipitation

S214-p - Smad1 (human) ▲
Orthologous residues
Smad1 (human): S214‑p, Smad1 (mouse): S214‑p, Smad1 (rat): S214‑p
Characterization
 Methods used to characterize site in vivo:  immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  cervical cancer, cervical adenocarcinoma
 Relevant cell lines - cell types - tissues:  HaCaT (keratinocyte), HeLa S3 (cervical), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CDK9 (human)
KINASE ERK2 (human)
KINASE CDK8 (human)
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
YAP1 (human) WW Induces transcription, altered co-immunoprecipitation

T220-p - Smad2 (human) ▲
Orthologous residues
Smad2 (human): T220‑p, Smad2 (mouse): T220‑p, Smad2 (rat): T220‑p
Characterization
 Methods used to characterize site in vivo:  immunoprecipitation, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  HaCaT (keratinocyte), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
BMP2 no change compared to control
BMP2 no change compared to control cytoplasmic and nuclear fractions
TGF-beta increase nuclear fraction
TGF-beta no change compared to control cytoplasmic fraction
TGF-beta FOXO4 (human) increase FoxO4 siRNA decreases
TGF-beta NEDD4L (human) increase Nedd4L siRNA decreases (slightly)
MG132 decrease slight decrease

T179-p - Smad3 (human) ▲
Orthologous residues
Smad3 (human): T179‑p, Smad3 (mouse): T179‑p, Smad3 (rat): T179‑p
Characterization
 Methods used to characterize site in vivo:  immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  cervical cancer, cervical adenocarcinoma
 Relevant cell lines - cell types - tissues:  HaCaT (keratinocyte), HeLa S3 (cervical), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CDK9 (human)
KINASE CDK8 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CDK9 (human) siRNA inhibition of enzyme, activation of upstream enzyme
KINASE CDK8 (human) siRNA inhibition of enzyme, activation of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
BMP2 no change compared to control
BMP2 no change compared to control cytoplasmic and nuclear fractions
TGF-beta increase nuclear fraction
TGF-beta no change compared to control cytoplasmic fraction
TGF-beta Smad4 (human) increase Smad4 -/- decrease
TGF-beta Smad4 (human) increase Smad4 WT
Downstream Regulation
 Effect of modification (process):  transcription, altered

S204-p - Smad3 (human) ▲
Orthologous residues
Smad3 (human): S204‑p, Smad3 (mouse): S204‑p, Smad3 (rat): S204‑p
Characterization
 Methods used to characterize site in vivo:  immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  cervical cancer, cervical adenocarcinoma
 Relevant cell lines - cell types - tissues:  HaCaT (keratinocyte), HeLa S3 (cervical), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE ERK2 (human)

S208-p - Smad3 (human) ▲
Orthologous residues
Smad3 (human): S208‑p, Smad3 (mouse): S208‑p, Smad3 (rat): S208‑p
Characterization
 Methods used to characterize site in vivo:  immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  cervical cancer, cervical adenocarcinoma
 Relevant cell lines - cell types - tissues:  HaCaT (keratinocyte), HeLa S3 (cervical), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CDK8 (human)
KINASE ERK2 (human)
KINASE CDK9 (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TGF-beta no change compared to control cytoplasmic fraction
flavopiridol TGF-beta no change compared to control
TGF-beta increase nuclear fraction
flavopiridol TGF-beta inhibit treatment-induced increase

S213-p - Smad3 (human) ▲
Orthologous residues
Smad3 (human): S213‑p, Smad3 (mouse): S213‑p, Smad3 (rat): S213‑p
Characterization
 Methods used to characterize site in vivo:  immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  cervical cancer, cervical adenocarcinoma
 Relevant cell lines - cell types - tissues:  HaCaT (keratinocyte), HeLa S3 (cervical), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE ERK2 (human)
KINASE CDK9 (human)
KINASE CDK8 (human)


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.