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

BRAF affects kinase, and True
19 21 |
BRAF-V600E is kinase-active. 10 / 38
19 19 |
bel
"From mutations file"
bel
"From mutations file"
bel
"From mutations file"
bel
"From mutations file"
bel
"From mutations file"
bel
"From mutations file"
bel
"From mutations file"
bel
"From mutations file"
bel
"From mutations file"
bel
"From mutations file"
Serine-phosphorylated BRAF is kinase-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."
BRAF phosphorylated on S446 is kinase-active. 1 / 1
1 |
bel
"78,136,143 The homologous site on B-Raf, S445, is constitutively phosphorylated, accounting for the higher basal activity of B-Raf."
BRAF is active
18 6 | 1
BRAF phosphorylated on T373 is active. 10 / 13
13 |
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
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
BRAF phosphorylated on S579 is active. 5 / 5
5 |
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
BRAF bound to HRAS is active. 3 / 3
3 |
signor
"Association of B-Raf with immobilized Ras occurred independently of prior stimulation of cells with serum, suggesting that primarily the production of GTP-Ras by mitogen stimulation is critical for the formation of B-Raf_GTP-Ras complexes."
signor
"The raf family of proteins (raf-1, a-raf, and b-raf) is serine/threonine kinases that bind to the effector region of ras-gtp, thus inducing translocation of the protein to the plasma membrane. Once there, raf proteins are activated and phosphorylated by different protein kinases."
signor
"BRAF kinase is a downstream target of KRAS and activates the MAPK pathway."
BRAF bound to NRAS is active. 1 / 1
1 |
signor
"The raf family of proteins (raf-1, a-raf, and b-raf) is serine/threonine kinases that bind to the effector region of ras-gtp, thus inducing translocation of the protein to the plasma membrane. Once there, raf proteins are activated and phosphorylated by different protein kinases."
BRAF bound to RIT1 is active. 1 / 1
1 |
signor
"It is possible that RIT1 interacts with RAF1 and that gain-of-function mutations in RIT1 and RAF1 exert similar effects in heart development."
BRAF bound to KRAS is active. 1 / 1
1 |
signor
"The raf family of proteins (raf-1, a-raf, and b-raf) is serine/threonine kinases that bind to the effector region of ras-gtp, thus inducing translocation of the protein to the plasma membrane. Once there, raf proteins are activated and phosphorylated by different protein kinases."
BRAF-V600E is active. 1 / 1
| 1
trips
"The biological significance of BRAF V600E oncogenic activation is not well established in this type of tumour."
BRAF is not active
2 15 |
BRAF phosphorylated on T753 is inactive. 3 / 3
3 |
signor
"Erk-induced phosphorylation of b-raf on t753 promoted the disassembly of raf heterodimers, and the mutation of t753 prolonged growth factor-induced heterodimerization. The b-raf t753a mutant enhanced differentiation of pc12 cells, which was previously shown to be dependent on sustained erk signaling. Site is critical for v-src dependent modulation of slk kinase activity."
signor
"Erk-induced phosphorylation of b-raf on t753 promoted the disassembly of raf heterodimers, and the mutation of t753 prolonged growth factor-induced heterodimerization. The b-raf t753a mutant enhanced differentiation of pc12 cells, which was previously shown to be dependent on sustained erk signaling. Site is critical for v-src dependent modulation of slk kinase activity."
signor
"Erk-induced phosphorylation of b-raf on t753 promoted the disassembly of raf heterodimers, and the mutation of t753 prolonged growth factor-induced heterodimerization. The b-raf t753a mutant enhanced differentiation of pc12 cells, which was previously shown to be dependent on sustained erk signaling. Site is critical for v-src dependent modulation of slk kinase activity."
BRAF phosphorylated on S428 is inactive. 3 / 3
3 |
signor
"We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf"
signor
"We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf"
signor
"We show that phosphorylation of b-raf by akt occurs at multiple residues within its aminoterminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity."
BRAF phosphorylated on S364 is inactive. 3 / 3
3 |
signor
"We show that phosphorylation of b-raf by akt occurs at multiple residues within its aminoterminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity."
signor
"We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf"
signor
"We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf"
BRAF phosphorylated on S151, T753, T401, and S750 is inactive. 2 / 2
2 |
biopax:pid
No evidence text available
biopax:pid
No evidence text available
BRAF phosphorylated on T440 is inactive. 2 / 2
2 |
signor
"We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf"
signor
"We show that phosphorylation of b-raf by akt occurs at multiple residues within its amino terminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity b-raf contains three akt consensus sites, table i. One site, ser364 is conserved with c-raf;however, two sites, ser428 and thr439, are unique to b-raf"
BRAF phosphorylated on S429 is inactive. 2 / 2
2 |
signor
"Akt phosphorylates both S364 and S428. Akt downregulates B-Raf activity in vivo"
signor
"Direct phosphorylation of B-Raf by PKA exerts a negative effect on its kinase activity, essentially via phosphorylation of Ser429"
BRAF phosphorylated on T401 is inactive. 1 / 1
1 |
signor
"We show that b-raf is a calcineurin substrate;among calcineurin target residues on b-raf is t401, a site of negative feedback phosphorylation by erk1/2. Blocking calcineurin activity in _ cells prevents dephosphorylation of b-raf t401 and decreases b-raf and erk1/2 activities."
BRAF phosphorylated on S365 is inactive. 1 / 1
1 |
signor
"Akt phosphorylates both S364 and S428. Akt downregulates B-Raf activity in vivo"
BRAF affects kinase, and False
1 |
Serine-phosphorylated BRAF is kinase-inactive. 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."