A database built with INDRA combining content from numerous readers and databases. This page allows you to curate the loaded statements. For more information please see the manual.

IndraLab

Statements

databases
phosphosite cbn pc11 biopax bel_lc signor biogrid tas lincs_drug hprd trrust | geneways tees isi trips rlimsp medscan sparser reach
reading

ELK1 is active
8 29 | 1
ELK1 phosphorylated on S383 is active. 9 / 9
9 |
signor
"However, both of these stimuli strongly activate two other mapks, jnk1 and jnk2, and stimulate elk-1 transcriptional activity and phosphorylation jnk phosphorylation sites include ser383 and ser389, the major residues whose phosphorylation is responsible for enhancement of elk-1 trascriptional activity."
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"Elk-1 is a member of the e-twenty-six (ets) domain superfamily of transcription factors and has been traditionally associated with mitogen-induced immediate early gene transcription upon phosphorylation by mitogen activated protein kinases (erk/mapk)."
signor
"We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erk1 phosphorylates five c-terminal sites in elk-1 (s324,t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"Subsequent studies with dominant negative elk-1, wild type, and variant gal4-elk-1 fusion proteins confirmed that phosphorylation of elk-1 at serines 383 and 389 in the c-terminal region of elk-1 is an important downstream target associated with activation of an sre by e2. Both e2 (er?-Dependent) and growth factors (er?-Independent) activated the sre in breast cancer cells via the ras/mapk pathway"
signor
"We demonstrate here that elk-1 is barely activated by a third subclass of map kinases (p38), most likely because the critical residues ser383 and ser389 are poorly phosphorylated by p38 map kinase."
signor
"Transfection studies demonstrated that TAO2 stimulates phosphorylation of the TCF Elk1 on the major activating site, Ser383, and that TAO2 stimulates transactivation of Elk1 and the related TCF, Sap1."
signor
"Phosphorylation on ser383 and ser389 of elk-1 by mapk enhances this basal binding but, most importantly, elk-1 exhibits new interactions with p300."
ELK1 phosphorylated on S389 is active. 7 / 7
7 |
signor
"We find that the JNKs are the predominant Elk-1 activation domain kinases in extracts of UV-irradiated cells and that immunopurified JNK1/2 phosphorylate Elk-1 on the same major sites recognized by ERK1/2, that potentiate its transcriptional activity."
signor
"We demonstrate here that elk-1 is barely activated by a third subclass of map kinases (p38), most likely because the critical residues ser383 and ser389 are poorly phosphorylated by p38 map kinase."
signor
"However, both of these stimuli strongly activate two other mapks, jnk1 and jnk2, and stimulate elk-1 transcriptional activity and phosphorylation jnk phosphorylation sites include ser383 and ser389, the major residues whose phosphorylation is responsible for enhancement of elk-1 trascriptional activity."
signor
"We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erki phosphorylates five c-terminal sites in elk-i (s324,t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"However, both of these stimuli strongly activate two other mapks, jnk1 and jnk2, and stimulate elk-1 transcriptional activity and phosphorylation jnk phosphorylation sites include ser383 and ser389, the major residues whose phosphorylation is responsible for enhancement of elk-1 trascriptional activity."
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
ELK1 phosphorylated on S389 and S383 is active. 6 / 6
6 |
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
ELK1 phosphorylated on S422 is active. 3 / 3
3 |
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erki phosphorylates five c-terminal sites in elk-i (s324,t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
ELK1 phosphorylated on T336 is active. 3 / 3
3 |
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erki phosphorylates five c-terminal sites in elk-i (s324,t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
ELK1 phosphorylated on S324 is active. 3 / 3
3 |
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"Erki phosphorylates five c-terminal sites in elk-i (s324, t336, s383, s389 and s422) with varying degrees of efficiency."
signor
"We demonstrate that elk-1, a protein closely related to p62tcf in function, is a nuclear target of two members of the map kinase family, erk1 and erk2, erk1 phosphorylates five c-terminal sites in elk-1 (s324,t336, s383, s389 and s422) with varying degrees of efficiency."
Phosphorylated ELK1 is active. 3 / 3
3 |
signor
"The tcf protein elk-1 is phosphorylated by the jnk and erk groups of mitogen-activated protein (map) kinases causing increased dna binding, ternary complex formation, and transcriptional activation"
signor
"The tcf protein elk-1 is phosphorylated by the jnk and erk groups of mitogen-activated protein (map) kinases causing increased dna binding, ternary complex formation, and transcriptional activation"
signor
"Erk also undergoes rapid translocation into the nucleus, where it phosphorylates and activates a variety of transcription factor targets, including sp1, e2f, elk-1, and ap1."
ELK1 phosphorylated on S324, S389, S383, T336, and S422 is active. 1 / 1
1 |
biopax:pid
No evidence text available
ELK1 phosphorylated on T417 is active. 1 / 1
1 |
signor
"Activated hprp4 phosphorylates residue thr-417 on elk-1 resulting in elk-1 activation."
Tyrosine-phosphorylated ELK1 is active. 1 / 1
1 |
biopax:pid
No evidence text available
ELK1 bound to EP300 is active. 1 / 1
| 1
trips
"We present a novel mechanism of activating such complexes and show that pre-assembled Elk-1-p300 complexes become activated following Elk-1 phosphorylation by changes in Elk-1-p300 interactions rather than recruitment."
ELK1 affects transcription, and True
5 9 |
ELK1 phosphorylated on S383 is transcriptionally active. 9 / 9
5 4 |
bel
"Subsequent studies with dominant negative Elk-1, wild type, and variant GAL4-Elk-1 fusion proteins confirmed that phosphorylation of Elk-1 at serines 383 and 389 in the C-terminal region of Elk-1 is an important downstream target associated with activation of an SRE by E2."
bel
"The NH(2) terminus of MKP-1 was also found to inhibit the activation of the serum response element (SRE) by preventing MAPK-mediated phosphorylation of the regulatory serine 383 residue on Elk-1."
bel
"Elk-1-dependent transactivation is regulated by phosphorylation at serine-383 and -389, and each of the MAPK has been shown to be competent to phosphorylate this nuclear factor at these residues in vitro (33, 34, 35, 36, 37)."
bel
"Subsequent studies with dominant negative Elk-1, wild type, and variant GAL4-Elk-1 fusion proteins confirmed that phosphorylation of Elk-1 at serines 383 and 389 in the C-terminal region of Elk-1 is an important downstream target associated with activation of an SRE by E2."
bel
"Phosphorylation of the C-terminal domain of Elk-1, especially at serine 383, is important for its transactivation activity."
bel
"The NH(2) terminus of MKP-1 was also found to inhibit the activation of the serum response element (SRE) by preventing MAPK-mediated phosphorylation of the regulatory serine 383 residue on Elk-1."
bel
"Indeed, Ser383 plays a vital role, as mutation of Ser383 virtually eliminated hRev7-mediated enhancement of Elk-1 activity (Fig. 4D)."
bel
"Indeed, Ser383 plays a vital role, as mutation of Ser383 virtually eliminated hRev7-mediated enhancement of Elk-1 activity (Fig. 4D)."
bel
"Phosphorylation of the C-terminal domain of Elk-1, especially at serine 383, is important for its transactivation activity."
Phosphorylated ELK1 is transcriptionally active. 4 / 4
4 |
bel
"This approach revealed a previously unrecognized transcriptional target of ELK-1, the human tissue plasminogen activator (tPA)."
bel
"Elk-1-dependent transactivation is regulated by phosphorylation at serine-383 and -389, and each of the MAPK has been shown to be competent to phosphorylate this nuclear factor at these residues in vitro (33, 34, 35, 36, 37)."
bel
"MSK1 induction requires simultaneous activation of both ERK and p38 MAPK. Other downstream targets of p38 MAPK include transcription factors such as Elk1 and myocyte-enhancing factor (MEF) 2, whereby p38 MAPK directly phosphorylates nuclear substrates and augments their activity (Chen et al. 2001)."
bel
"RIP2 directly phosphorylates and activates ERK2 in vivo and in vitro."
Serine-phosphorylated ELK1 is transcriptionally active. 1 / 1
1 |
bel
"GSK PI3K Phase 2, part 1: List of non-position specific phosphorylation effects on parent protein's activity, derived from existing causal assertions of position-specific phosphorylations on the parent protein activity."
ELK1 affects transcription, and False
2 |
ELK1-S383A is transcriptionally inactive. 1 / 1
1 |
bel
"Mutation to alanine of S383, F378 or W379, which virtually abolishes transcriptional activation by Elk-1, does not affect phosphorylation of any sites tested."
ELK1-W379A is transcriptionally inactive. 1 / 1
1 |
bel
"Mutation to alanine of S383, F378 or W379, which virtually abolishes transcriptional activation by Elk-1, does not affect phosphorylation of any sites tested."