| + |
MAPKAPK2 |
phosphorylation
|
SRF |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67448 |
Ser103 |
RGLKRSLsEMEIGMV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10318869 |
Mk2 phosphorylates srf in vitro at ser-103 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2A | up-regulates activity 
phosphorylation
|
SRF |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250638 |
Ser103 |
RGLKRSLsEMEIGMV |
|
|
| pmid |
sentence |
| 10753652 |
Skeletal muscle CaMKII enriches in nuclei and phosphorylates myogenic factor SRF at multiple sites. | Microsequencing of these phosphorylated peptides identified that both Ser-103 and a novel residue, Thr-160 in the MADS box of SRF, were sites of phosphorylation. | The location of Thr-160 in the 3-D structure of SRF suggests that its phosphorylation by nuclear CaMKII may directly influence DNA binding of SRF and other MADS box factors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250639 |
Thr160 |
NKLRRYTtFSKRKTG |
|
|
| pmid |
sentence |
| 10753652 |
Skeletal muscle CaMKII enriches in nuclei and phosphorylates myogenic factor SRF at multiple sites. | Microsequencing of these phosphorylated peptides identified that both Ser-103 and a novel residue, Thr-160 in the MADS box of SRF, were sites of phosphorylation. | The location of Thr-160 in the 3-D structure of SRF suggests that its phosphorylation by nuclear CaMKII may directly influence DNA binding of SRF and other MADS box factors. |
|
| Publications: |
2 |
| + |
PRKCA | down-regulates 
phosphorylation
|
SRF |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-234461 |
Ser162 |
LRRYTTFsKRKTGIM |
Mus musculus |
|
| pmid |
sentence |
| 16537394 |
Mimicking phosphorylation of serine-162, a target of protein kinase c-alpha, with an aspartic acid substitution (srf-s162d) completely inhibited srf-dna binding and blocked alpha-actin gene transcription pkc? Highly phosphorylated serine-162. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKDC | up-regulates activity
phosphorylation
|
SRF |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248921 |
Ser435 |
LTVLNAFsQAPSTMQ |
in vitro |
|
| pmid |
sentence |
| 8407951 |
The carboxyl-terminal transcription activation domain was mapped within a 71-amino acid region that contains both DNA-PK phosphorylation sites. Amino acid substitutions that interfered with phosphorylation by DNA-PK at Ser-435/446 in GAL4-SRF fusion proteins were reduced in transactivation potency. From these data we suggest that DNA-PK phosphorylation may modulate SRF activity in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248922 |
Ser446 |
STMQVSHsQVQEPGG |
in vitro |
|
| pmid |
sentence |
| 8407951 |
The carboxyl-terminal transcription activation domain was mapped within a 71-amino acid region that contains both DNA-PK phosphorylation sites. Amino acid substitutions that interfered with phosphorylation by DNA-PK at Ser-435/446 in GAL4-SRF fusion proteins were reduced in transactivation potency. From these data we suggest that DNA-PK phosphorylation may modulate SRF activity in vivo. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CSNK2A1 | up-regulates activity
phosphorylation
|
SRF |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250955 |
Ser77 |
PTAGALYsGSEGDSE |
in vitro |
|
| pmid |
sentence |
| 2046671 |
Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro.| Nevertheless, additional mutation of serines 77 and 79 was required before phosphorylation and enhanced binding were completely abolished. Thus, serines 77 and 79 could also be recognized by CKII if serines 83 and 85 were mutated. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250956 |
Ser79 |
AGALYSGsEGDSESG |
in vitro |
|
| pmid |
sentence |
| 2046671 |
Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro.| Nevertheless, additional mutation of serines 77 and 79 was required before phosphorylation and enhanced binding were completely abolished. Thus, serines 77 and 79 could also be recognized by CKII if serines 83 and 85 were mutated. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250958 |
Ser83 |
YSGSEGDsESGEEEE |
in vitro |
|
| pmid |
sentence |
| 2046671 |
Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro. We report here that serine 83 appears to be the residue phosphorylated by CKII but that three other serines in this region can also be involved in phosphorylation and the enhancement of DNA-binding activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250957 |
Ser85 |
GSEGDSEsGEEEELG |
in vitro |
|
| pmid |
sentence |
| 2046671 |
Casein kinase II (CKII) phosphorylates the mammalian transcription factor serum response factor (SRF) on a serine residue(s) located within a region of the protein spanning amino acids 70 to 92, thereby enhancing its DNA-binding activity in vitro.| Mutation of serine 85 alone had a smaller but significant effect on phosphorylation that may be due to alteration in the protein kinase recognition site. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PRKCA | up-regulates
phosphorylation
|
SRF |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188181 |
Thr159 |
DNKLRRYtTFSKRKT |
Mus musculus |
|
| pmid |
sentence |
| 12809504 |
Myotonic dystrophy protein kinase (DMPK), a muscle- and neuron-restricted kinase, enhanced SRF-mediated promoter activity of the skeletal and cardiac alpha-actin genes in C2C12 myoblasts as well as in nonmyogenic cells. | Threonine 159 in the MADS box alphaI coil was a specific phosphorylation target in vitro as well as in vivo of both DMPK and protein kinase C-alpha. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKACA | up-regulates
phosphorylation
|
SRF |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188177 |
Thr159 |
DNKLRRYtTFSKRKT |
Mus musculus |
|
| pmid |
sentence |
| 12809504 |
Myotonic dystrophy protein kinase (DMPK), a muscle- and neuron-restricted kinase, enhanced SRF-mediated promoter activity of the skeletal and cardiac alpha-actin genes in C2C12 myoblasts as well as in nonmyogenic cells. | Threonine 159 in the MADS box alphaI coil was a specific phosphorylation target in vitro as well as in vivo of both DMPK and protein kinase C-alpha. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKG1 | up-regulates
phosphorylation
|
SRF |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188185 |
Thr159 |
DNKLRRYtTFSKRKT |
Mus musculus |
|
| pmid |
sentence |
| 12809504 |
Myotonic dystrophy protein kinase (DMPK), a muscle- and neuron-restricted kinase, enhanced SRF-mediated promoter activity of the skeletal and cardiac alpha-actin genes in C2C12 myoblasts as well as in nonmyogenic cells. | Threonine 159 in the MADS box alphaI coil was a specific phosphorylation target in vitro as well as in vivo of both DMPK and protein kinase C-alpha. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DMPK | up-regulates
phosphorylation
|
SRF |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236982 |
Thr159 |
DNKLRRYtTFSKRKT |
Mus musculus |
|
| pmid |
sentence |
| 12809504 |
Myotonic dystrophy protein kinase (DMPK), a muscle- and neuron-restricted kinase, enhanced SRF-mediated promoter activity of the skeletal and cardiac alpha-actin genes in C2C12 myoblasts as well as in nonmyogenic cells. | Threonine 159 in the MADS box alphaI coil was a specific phosphorylation target in vitro as well as in vivo of both DMPK and protein kinase C-alpha. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SRF | down-regulates quantity by repression 
transcriptional regulation
|
SERPINE1 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255228 |
|
|
Homo sapiens |
Lung Fibroblast Cell Line |
| pmid |
sentence |
| 15514113 |
We previously demonstrated that serum response factor (SRF), a critical smooth muscle transcription factor, is highly expressed in LAM cells. Here we show that a high SRF level alters the plasminogen (Plg) system. Specifically, overexpression of SRF in human lung fibroblasts upregulated urokinase-type plasminogen activator (uPA) and its substrate Plg, whereas it downregulated plasminogen activator inhibitor (PAI)-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MRTFA | up-regulates
binding
|
SRF |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174264 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21673106 |
Similarly, the myocd-related transcription factor (mrtf) family of proteins, mrtf-a and mrtf-b, are also involved in the transcriptional regulation of contractile gene markers as coactivators of srf. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
MYOCD | up-regulates
binding
|
SRF |
0.789 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174322 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21673106 |
A coactivator of srf, myocd, interacts with srf and activates vsmc expression of contractile genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
SRF | up-regulates quantity by expression 
transcriptional regulation
|
PLAU |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255227 |
|
|
Homo sapiens |
Lung Fibroblast Cell Line |
| pmid |
sentence |
| 15514113 |
We previously demonstrated that serum response factor (SRF), a critical smooth muscle transcription factor, is highly expressed in LAM cells. Here we show that a high SRF level alters the plasminogen (Plg) system. Specifically, overexpression of SRF in human lung fibroblasts upregulated urokinase-type plasminogen activator (uPA) and its substrate Plg, whereas it downregulated plasminogen activator inhibitor (PAI)-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRF | up-regulates quantity by expression
transcriptional regulation
|
ACTA2 |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126923 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15269336 |
The primary goal of the present study was to directly assess the role of the degeneracy of sm ?-Actin cargs in the regulation of smc-selective gene expression in vivo. in addition, our present studies address the possible role of this carg degeneracy, and the smc-selective srf coactivator myocardin, in regulating differential expression of carg-dependent smc genes and growth regulatory genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
SRF | form complex 
binding
|
NKX3-1/SRF |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82090 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10993896 |
A novel complex element containing a juxtaposed nkx-binding site (nke) and an srf-binding element (sre) in the proximal promoter region was found to be necessary for the nkx3-1/srf coactivation of smga transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
MAPKAPK2 | up-regulates
phosphorylation
|
SRF |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166640 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20626350 |
Neverthless, some transcription factors, such as e47, er81, srf and creb are also phosphorylated by mk2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MRTFB | up-regulates activity
binding
|
SRF |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-237671 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 14565952 |
MKL2 binds to and activates SRF similar to myocardin and MKL1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRF | up-regulates
|
IL6 |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255966 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22225874 |
Srf within myofibers modulates Il6 and Cox2/Il4 expressions and, therefore, exerts a paracrine control of satellite cell proliferation and fusion, respectively, which in turn support skeletal muscle hypertrophy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MRTFB | up-regulates
binding
|
SRF |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174316 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21673106 |
Similarly, the myocd-related transcription factor (mrtf) family of proteins, mrtf-a and mrtf-b, are also involved in the transcriptional regulation of contractile gene markers as coactivators of srf. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
SRF | up-regulates quantity by expression
transcriptional regulation
|
CNN1 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174358 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21673106 |
In particular, high expression of vsmc-specific genes, such as smooth muscle -actin (sma), calponin1 (cnn), and sm22 (sm22) are associated with the contractile vsmc phenotype. Transcription of contractile genes is regulated by srf through a dna sequence motif known as the carg box (cc(a/t)6gg), which is present in the promoters of vsmc-specific genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
SRF | up-regulates quantity by expression
transcriptional regulation
|
PLG |
0.249 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255226 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15514113 |
We previously demonstrated that serum response factor (SRF), a critical smooth muscle transcription factor, is highly expressed in LAM cells. Here we show that a high SRF level alters the plasminogen (Plg) system. Specifically, overexpression of SRF in human lung fibroblasts upregulated urokinase-type plasminogen activator (uPA) and its substrate Plg, whereas it downregulated plasminogen activator inhibitor (PAI)-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRF | up-regulates quantity by expression
transcriptional regulation
|
TAGLN |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174393 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21673106 |
The contractile phenotype of smooth muscle (sm) cells is controlled by serum response factor (srf), which drives the expression of sm-specific genes including sm alpha-actin, sm22, and others. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRF | up-regulates
|
PTGS2 |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255965 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22225874 |
Srf within myofibers modulates Il6 and Cox2/Il4 expressions and, therefore, exerts a paracrine control of satellite cell proliferation and fusion, respectively, which in turn support skeletal muscle hypertrophy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRRX1 | up-regulates
binding
|
SRF |
0.454 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52657 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9334314 |
The human homeodomain proteinphox1interacts functionally with serum response factor (srf) to impart serum responsive transcriptional activity to srf-binding sites in a hela cell cotransfection assay. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KLF4 | down-regulates
binding
|
SRF |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174258 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21673106 |
Klf4 antagonizes contractile gene expression through diverse mechanisms including (i) inhibiting the binding of srf-myocd or srf-mrtfs to the carg box by direct association with srf. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
3.0
SRF
- 
- 