IndraLab

Statements

BRAF is kinase-active.
19 21 |
BRAF-V600E is kinase-active. 10 / 38
19 19 |
bel
"From mutations file"
15294323
bel
"From mutations file"
15688405
bel
"From mutations file"
15009714
bel
"From mutations file"
15294323
bel
"From mutations file"
12794760
bel
"From mutations file"
14961576
bel
"From mutations file"
12794760
bel
"From mutations file"
12819038
bel
"From mutations file"
14602780
bel
"From mutations file"
12778069
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."
16170185
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 is active.
18 6 | 2
BRAF phosphorylated on T373 is active. 10 / 13
13 |
biopax:pid
No evidence text available
1386920
biopax:pid
No evidence text available
1386920
biopax:pid
No evidence text available
1386920
biopax:pid
No evidence text available
12917261
biopax:pid
No evidence text available
15632082
biopax:pid
No evidence text available
1386920
biopax:pid
No evidence text available
9560161
biopax:pid
No evidence text available
11278445
biopax:pid
No evidence text available
12917261
biopax:pid
No evidence text available
12917261
BRAF phosphorylated on S579 is active. 5 / 5
5 |
biopax:pid
No evidence text available
16135787
biopax:pid
No evidence text available
8073291
biopax:pid
No evidence text available
14970219
biopax:pid
No evidence text available
18567582
biopax:pid
No evidence text available
17563371
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."
7706312
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."
21779497
signor
"BRAF kinase is a downstream target of KRAS and activates the MAPK pathway."
18098337
BRAF-V600E is active. 2 / 2
| 2
trips
"The mechanism of activation of monomeric B-Raf V600E."
34188782
trips
"The biological significance of BRAF V600E oncogenic activation is not well established in this type of tumour."
18098337
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."
21779497
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."
23791108
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."
21779497
BRAF is inactive.
2 15 |
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."
10869359
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"
10869359
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"
10869359
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 aminoterminal regulatory domain, at both the conserved and unique phosphorylation sites. Akt phosphorylated b-raf on s364 and s428 to inactivate its kinase activity."
10869359
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"
10869359
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"
10869359
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."
16508002
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."
19933846
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."
16508002
BRAF phosphorylated on S429 is inactive. 2 / 2
2 |
signor
"Akt phosphorylates both S364 and S428. Akt downregulates B-Raf activity in vivo"
10869359
signor
"Direct phosphorylation of B-Raf by PKA exerts a negative effect on its kinase activity, essentially via phosphorylation of Ser429"
11510412
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"
10869359
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"
10869359
BRAF phosphorylated on T401, T753, S750, and S151 is inactive. 2 / 2
2 |
biopax:pid
No evidence text available
19541618
biopax:pid
No evidence text available
19541618
BRAF phosphorylated on S365 is inactive. 1 / 1
1 |
signor
"Akt phosphorylates both S364 and S428. Akt downregulates B-Raf activity in vivo"
10869359
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."
21135229
BRAF is kinase-inactive.
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."