

Swiss-PO
Variant π | Detail![]() |
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A2 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Acetylation description: N-acetylalanine link to source |
N20T | source: Jackson Laboratoryβ[10.05.19] description: BRAF N20T does not lie within any known functional domains of the Braf protein (UniProt.org). N20T has not been characterized in the scientific literature and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
V47_M438del | source: Jackson Laboratoryβ[10.05.19] description: BRAF V47_M438del results in the deletion of 392 amino acids of the Braf protein from amino acids 47 to 438 (UniProt.org). V47_M438del (reported as internal deletion of exons 2-10) has not been characterized, however, due to the deletion of the CR1 autoinhibitory domain and preservation of the protein kinase domain (PMID: 23890088, PMID: 22113612, PMID: 29171936), V47_M438del is predicted to lead to a gain of Braf protein function. link to source |
V47_D380del | source: Jackson Laboratoryβ[10.05.19] description: BRAF V47_D380del results in the deletion of 334 amino acids of the Braf protein from amino acids 47 to 380 (UniProt.org). V47_D380del (reported as internal deletion of exons 2-8) has been associated with resistance to Mek inhibitors in a patient (PMID: 29171936), and is predicted to lead to a gain of Braf protein function due to the deletion of the CR1 autoinhibitory domain and preservation of the protein kinase domain (PMID: 23890088, PMID: 22113612). link to source |
V47_G327del | source: Jackson Laboratoryβ[10.05.19] description: BRAF V47_G327del results in the deletion of 281 amino acids of the Braf protein from amino acids 47 to 327 (UniProt.org). V47_G327del (reported as internal deletion of exons 2-7) has not been characterized, however, due to the deletion of the CR1 autoinhibitory domain and preservation of the protein kinase domain (PMID: 23890088, PMID: 22113612, PMID: 29171936), V47_G327del is predicted to lead to a gain of Braf protein function. link to source |
V47_G393del | source: Jackson Laboratoryβ[10.05.19] description: BRAF V47_G393del results in the deletion of 347 amino acids of the Braf protein from amino acids 47 to 393 (UniProt.org). V47_G393del (reported as internal deletion of exons 2-9) has not been characterized, however, due to the deletion of the CR1 autoinhibitory domain and preservation of the protein kinase domain (PMID: 23890088, PMID: 22113612, PMID: 29171936), V47_G393del is predicted to lead to a gain of Braf protein function. link to source |
N49I | source: Jackson Laboratoryβ[10.05.19] description: BRAF N49I lies within the protein kinase domain of the Braf protein (UniProt.org). N49I has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
M53I | source: Jackson Laboratoryβ[10.05.19] description: BRAF M53I does not lie within any known functional domains of the Braf protein (UniProt.org). M53I results in increased transformation ability compared to wild-type Braf in one of two cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
L64I | source: Jackson Laboratoryβ[10.05.19] description: BRAF L64I lies within the protein kinase domain of the Braf protein (UniProt.org). L64I has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
G69S | source: Jackson Laboratoryβ[10.05.19] description: BRAF G69S does not lie within any known functional domains of the Braf protein (UniProt.org). G69S results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
A81_D380del | source: Jackson Laboratoryβ[10.05.19] description: BRAF A81_D380del results in the deletion of 300 amino acids of the Braf protein from amino acids 81 to 380 (UniProt.org). A81_D380del (reported as internal deletion of exons 3-8) has not been characterized, however, due to the deletion of the CR1 autoinhibitory domain and preservation of the protein kinase domain (PMID: 23890088, PMID: 22113612, PMID: 29171936), A81_D380del is predicted to lead to a gain of Braf protein function. link to source |
A81_M438del | source: Jackson Laboratoryβ[10.05.19] description: BRAF A81_M438del results in the deletion of 358 amino acids of the Braf protein from amino acids 81 to 438 (UniProt.org). A81_M438del (reported as internal deletion of exons 3-10) has not been characterized, however, due to the deletion of the CR1 autoinhibitory domain and preservation of the protein kinase domain (PMID: 23890088, PMID: 22113612, PMID: 29171936), A81_M438del is predicted to lead to a gain of Braf protein function. link to source |
G104E | source: Jackson Laboratoryβ[10.05.19] description: BRAF G104E lies within the protein kinase domain of the Braf protein (UniProt.org). G104E has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
P141L | source: Jackson Laboratoryβ[10.05.19] description: BRAF P141L lies within the protein kinase domain of the Braf protein (UniProt.org). P141L has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
S151 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphoserine link to source |
P162S | source: Jackson Laboratoryβ[10.05.19] description: BRAF P162S lies within the protein kinase domain of the Braf protein (UniProt.org). P162S has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
V169_D380del | source: Jackson Laboratoryβ[10.05.19] description: BRAF V169_D380del results in the deletion of 212 amino acids of the Braf protein from amino acids 169 to 380 (UniProt.org). V169_D380del (reported as internal deletion of exons 4-8) has not been characterized, however, due to the deletion of the CR1 autoinhibitory domain and preservation of the protein kinase domain (PMID: 23890088, PMID: 22113612, PMID: 29171936), V169_D380del is predicted to lead to a gain of Braf protein function. link to source |
V169_G327del | source: Jackson Laboratoryβ[10.05.19] description: BRAF V169_G327del results in the deletion of 159 amino acids of the Braf protein from amino acids 169 to 327 (UniProt.org). V169_G327del (reported as internal deletion of exons 4-7) has not been characterized, however, due to the deletion of the CR1 autoinhibitory domain and preservation of the protein kinase domain (PMID: 23890088, PMID: 22113612, PMID: 29171936), V169_G327del is predicted to lead to a gain of Braf protein function. link to source |
R188T | source: Jackson Laboratoryβ[10.05.19] description: BRAF R188T lies within the protein kinase domain of the Braf protein (UniProt.org). R188T has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
G203_G393del | source: Jackson Laboratoryβ[10.05.19] description: BRAF G203_G393del results in the deletion of 91 amino acids of the Braf protein from amino acids 203 to 393 (UniProt.org). G203_G393del (reported as internal deletion of exons 5-9) has not been characterized, however, due to the disruption of the CR1 autoinhibitory domain and preservation of the protein kinase domain (PMID: 23890088, PMID: 22113612, PMID: 29171936), G203_G393del is predicted to lead to a gain of Braf protein function. link to source |
K205Q | source: Jackson Laboratoryβ[10.05.19] description: BRAF K205Q lies within the protein kinase domain of the Braf protein (UniProt.org). K205Q has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
V226L | source: Jackson Laboratoryβ[10.05.19] description: BRAF V226L lies within the Ras-binding domain of the Braf protein (UniProt.org). V226L has not been characterized in the scientific literature and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
E228V | source: Jackson Laboratoryβ[10.05.19] description: BRAF E228V lies within the protein kinase domain of the Braf protein (UniProt.org). E228V has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
R239Q | source: Jackson Laboratoryβ[10.05.19] description: BRAF R239Q lies within the phorbol-ester/DAG-type zinc finger domain of the Braf protein (UniProt.org). R239Q has been identified in the scientific literature (PMID: 29903896), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Jan 2019). link to source |
T241P | source: Jackson Laboratoryβ[10.05.19] description: BRAF T241P does not lie within any known functional domains of the Braf protein (UniProt.org). T241P is only weakly activating of MEK and ERK and does not induce transformation in cell culture (PMID: 19206169), but in one of two cell lines, T241P did increase cell proliferation and cell viability compared to wild-type Braf (PMID: 29533785). link to source |
L245F | source: Jackson Laboratoryβ[10.05.19] description: BRAF L245F lies within the Phorbol-ester/DAG-type zinc finger domain of the Braf protein (UniProt.org). L245F results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
F247L | source: Jackson Laboratoryβ[10.05.19] description: BRAF F247L lies within the phorbol-ester/DAG-type zinc finger region of the Braf protein (UniProt.org). F247L confers a gain of function to Braf, as indicated by activation of downstream MAPK signaling and is transforming in cultured cells (PMID: 28512244, PMID: 29533785). link to source |
Q257H | source: Jackson Laboratoryβ[10.05.19] description: BRAF Q257H lies within the Phorbol-ester/DAG-type zinc finger region of the Braf protein (UniProt.org). Q257H has been identified in sequencing studies (PMID: 28852190, PMID: 27147599), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
Q257R | source: Jackson Laboratoryβ[10.05.19] description: BRAF Q257R lies within the phorbol-ester/DAG-type zinc finger region of the BRAF protein (UniProt.org). Q257R confers a gain of function to the Braf protein as demonstrated by increased kinase activity and activation of downstream Mek signaling in cell cuture, and activation of ELK in reporter assays (PMID: 16474404, PMID: 16439621). link to source |
G258V | source: Jackson Laboratoryβ[10.05.19] description: BRAF G258V lies within the protein kinase domain of the Braf protein (UniProt.org). G258V has not been biochemically characterized, but results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
F259L | source: Jackson Laboratoryβ[10.05.19] description: BRAF F259L lies within the protein kinase domain of the Braf protein (UniProt.org). F259L has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
Q262R | source: Jackson Laboratoryβ[10.05.19] description: BRAF Q262R lies within the Phorbol-ester/DAG-type zinc finger region of the Braf protein (UniProt.org). Q262R has not been characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
H269Y | source: Jackson Laboratoryβ[10.05.19] description: BRAF H269Y lies within the Phorbol-ester/DAG-type zinc finger domain of the Braf protein (UniProt.org). H269Y has not been biochemically characterized, but results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
R271H | source: Jackson Laboratoryβ[10.05.19] description: BRAF R271H lies within the protein kinase domain of the Braf protein (UniProt.org). R271H has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
E275K | source: Jackson Laboratoryβ[10.05.19] description: BRAF E275K lies within the phorbol-ester/DAG-type zinc finger region of the Braf protein (UniProt.org). E275K results in decreased activation of Mek and Erk (PMID: 19206169), but also demonstrates similar cell proliferation and viability as compared to wild-type Braf in culture (PMID: 29533785), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
D287H | source: Jackson Laboratoryβ[10.05.19] description: BRAF D287H does not lie within any known functional domains of the Braf protein (UniProt.org). D287H results in impaired Braf kinase activity, but leads to Ras-dependent activation of Erk in cell culture (PMID: 26343582, PMID: 28783719). link to source |
F294L | source: Jackson Laboratoryβ[10.05.19] description: BRAF F294L lies within the protein kinase domain of the Braf protein (UniProt.org). F294L has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
A320T | source: Jackson Laboratoryβ[10.05.19] description: BRAF A320T lies within the protein kinase domain of the Braf protein (UniProt.org). A320T has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
S333 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphoserine link to source |
P341S | source: Jackson Laboratoryβ[10.05.19] description: BRAF P341S lies within the protein kinase domain of the Braf protein (UniProt.org). P341S has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
R347* | source: Jackson Laboratoryβ[10.05.19] description: BRAF R347* results in a premature truncation of the of the 766 aa Braf protein at aa 347 (UniProt.org). Due to the loss of a portion of the protein kinase domain (UniProt.org), R347* is predicted to lead to a loss of Braf protein function. link to source |
P348T | source: Jackson Laboratoryβ[10.05.19] description: BRAF P348T lies within the protein kinase domain of the Braf protein (UniProt.org). P348T has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
S363F | source: Jackson Laboratoryβ[10.05.19] description: BRAF S363F does not lie within any known functional domains of the Braf protein (UniProt.org). S363F has been identified in the scientific literature (PMID: 29903896), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Jan 2019). link to source |
S364L | source: Jackson Laboratoryβ[10.05.19] description: BRAF S364L lies within the protein kinase domain of the Braf protein (UniProt.org). S364L has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
S365 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphoserine; by SGK1 link to source |
P367S | source: Jackson Laboratoryβ[10.05.19] description: BRAF P367S does not lie within any known functional domains of the Braf protein (UniProt.org). P367S results in increased transformation ability compared to wild-type Braf in one of two cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
P367L | source: Jackson Laboratoryβ[10.05.19] description: BRAF P367L does not lie within any known functional domains of the Braf protein (UniProt.org). P367L has been identified in sequencing studies (PMID: 26317466), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Feb 2019). link to source |
P367R | source: Jackson Laboratoryβ[10.05.19] description: BRAF P367R does not lie within any known functional domains within the Braf protein (UniProt.org). P367R confers a gain of function to the Braf protein as indicated by increased Erk phosphorylation in culture and tumor formation in animal models, and demonstrates resistance to Egfr inhibitors in culture (PMID: 27478040). link to source |
T373 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphothreonine; by autocatalysis link to source |
D380H | source: Jackson Laboratoryβ[10.05.19] description: BRAF D380H lies within the protein kinase domain of the Braf protein (UniProt.org). D380H has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
R389C | source: Jackson Laboratoryβ[10.05.19] description: BRAF R389C lies within the protein kinase domain of the Braf protein (UniProt.org). R389C has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
T396 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphothreonine link to source |
S399 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphoserine link to source |
T401I | source: Jackson Laboratoryβ[10.05.19] description: BRAF T401I lies within the protein kinase domain of the Braf protein (UniProt.org). T401I has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
T401 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphothreonine link to source |
P403fs | source: Jackson Laboratoryβ[10.05.19] description: BRAF P403fs results in a change in the amino acid sequence of the Braf protein beginning at aa 403 of 766, likely resulting in premature truncation of the functional protein (UniProt.org). Due to the loss of the protein kinase domain (UniProt.org), P403fs is predicted to lead to a loss of Braf protein function. link to source |
P407L | source: Jackson Laboratoryβ[10.05.19] description: BRAF P407L lies within the protein kinase domain of the Braf protein (UniProt.org). P407L has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
S419Y | source: Jackson Laboratoryβ[10.05.19] description: BRAF S419Y lies within the protein kinase domain of the Braf protein (UniProt.org). S419Y has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
G421V | source: Jackson Laboratoryβ[10.05.19] description: BRAF G421V lies within the protein kinase domain of the Braf protein (UniProt.org). G421V has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
R444W | source: Jackson Laboratoryβ[10.05.19] description: BRAF R444W does not lie within any known functional domains of the Braf protein (UniProt.org). R444W has been identified in sequencing studies (PMID: 15578519), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
S446 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphoserine link to source |
S447 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphoserine link to source |
W450* | source: Jackson Laboratoryβ[10.05.19] description: BRAF W450* results in a premature truncation the Braf protein at amino acid 450 of 766 (UniProt.org). Due to the loss of the protein kinase domain (UniProt.org), R450* is predicted to lead to a loss of Braf protein function. link to source |
P453T | source: Jackson Laboratoryβ[10.05.19] description: BRAF P453T does not lie within any known functional domains of the Braf protein (UniProt.org). P453T has been identified in sequencing studies (PMID: 27717198, PMID: 16404419), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
V459L | source: Jackson Laboratoryβ[10.05.19] description: BRAF V459L lies within the protein kinase domain of the Braf protein (UniProt.org). V459L results in impaired Braf kinase activity and leads to Ras-dependent activation of Erk in culture (PMID: 28783719), however, in two different cell lines, induces similar cell proliferation and cell viability as compared to wild-type Braf (PMID: 29533785), and therefore, its effect on Braf protein function is unknown. link to source |
R462K | source: Jackson Laboratoryβ[10.05.19] description: BRAF R462K lies within the protein kinase domain of the Braf protein (UniProt.org). R462K has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
R462I | source: Jackson Laboratoryβ[10.05.19] description: BRAF R462I lies within the protein kinase domain of the Braf protein (UniProt.org). R462I results in activation of Braf and increased Erk signaling in cell culture (PMID: 15035987) but, in two different cell lines, induced similar cell proliferation and cell viability as wild-type Braf (PMID: 29533785), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
I463S | source: Jackson Laboratoryβ[10.05.19] description: BRAF I463S lies within the protein kinase domain of the Braf protein (UniProt.org). I463S results in an intermediate increase in Braf kinase activity compared to wild-type Braf and increased Erk activation in cell culture (PMID: 15035987). link to source |
I463T | source: Jackson Laboratoryβ[10.05.19] description: BRAF I463T lies within the protein kinase domain of the Braf protein (UniProt.org). I463T has been identified in the scientific literature (PMID: 28829677), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
G464V | source: SwissProtβ[10.05.19] description: Increased activity ; function (Protein serine/threonine kinase activity). Higher basal activity. Induces cell transformation. link to source source: Jackson Laboratoryβ[10.05.19] description: BRAF G464V (also reported as G463V) lies within the protein kinase domain of the Braf protein (UniProt.org). G464V results in increased Braf kinase activity and increased downstream Mek and Erk activation (PMID: 12068308, PMID: 26343582), and in one of two cell lines, increased cell proliferation and viability compared to wild-type Braf in culture (PMID: 29533785). link to source |
G464R | source: Jackson Laboratoryβ[10.05.19] description: BRAF G464R (also reported as G463R) lies within the protein kinase domain of the Braf protein (UniProt.org). G464R results in increased Braf kinase activity, increased downstream Erk signaling (PMID: 15046639), and induces cell proliferation and cell viability in culture (PMID: 29533785). link to source |
G464E | source: Jackson Laboratoryβ[10.05.19] description: BRAF G464E (also reported as G463E) lies within the protein kinase domain of the Braf protein (UniProt.org). G464E results in increased Braf kinase activity and activation of MEK and ERK (PMID: 15035987, PMID: 23680146), and in one of two cell lines, increased cell proliferation and cell viability compared to wild-type Braf in culture (PMID: 29533785). link to source |
S465A | source: Jackson Laboratoryβ[10.05.19] description: BRAF S465A lies within the protein kinase domain of the Braf protein (UniProt.org). S465A results in basal Mek phosphorylation and Mek phosphorylation upon Ras activation to similar levels of wild-type Braf in culture (PMID: 27034005), and therefore, is predicted to have no effect on Braf protein function. link to source |
S465E | source: Jackson Laboratoryβ[10.05.19] description: BRAF S465E lies within the protein kinase domain of the Braf protein (UniProt.org). S465E results in basal Mek phosphorylation similar to wild-type Braf but decreased Mek phosphorylation upon Ras activation in culture (PMID: 27034005), and therefore, is predicted to lead to a loss of Braf protein function. link to source |
S465D | source: Jackson Laboratoryβ[10.05.19] description: BRAF S465D lies within the protein kinase domain of the Braf protein (UniProt.org). S465D results in basal Mek phosphorylation and Mek phosphorylation upon Ras activation to similar levels of wild-type Braf in culture (PMID: 27034005), and therefore, is predicted to have no effect on Braf protein function. link to source |
G466A | source: Jackson Laboratoryβ[10.05.19] description: BRAF G466A (also reported as G465A) lies within the protein kinase domain of the Braf protein (UniProt.org). The functional effect of G466A (also reported as G465A) on Braf is unclear as it has been characterized both as having intermediate Braf kinase activity (PMID: 15035987) and low Braf kinase activity (PMID: 28783719), leads to Ras-dependent activation of downstream Erk in cell culture (PMID: 28783719), and in one of two cell lines increased cell proliferation and cell viability compared to wild-type Braf (PMID: 29533785). link to source |
G466E | source: Jackson Laboratoryβ[10.05.19] description: BRAF G466E lies within the protein kinase domain of the Braf protein (UniProt.org). G466E results in impaired Braf kinase activity, but paradoxically increases Erk signaling through C-raf activation in cell culture and Xenopus embryos (PMID: 15035987), however, induces similar cell proliferation and cell viability as wild-type Braf (PMID: 29533785), and therefore, its effect on Braf protein function is unknown. link to source |
G466V | source: Jackson Laboratoryβ[10.05.19] description: BRAF G466V lies within the protein kinase domain of the Braf protein (UniProt.org). G466V results in impaired Braf kinase activity, but paradoxically activates MEK and ERK through transactivation of CRAF in cell culture (PMID: 22649091, PMID: 28783719), and in one of two cell lines, G466V decreased cell proliferation and cell viability as compared to wild-type Braf (PMID: 29533785). link to source |
G466R | source: Jackson Laboratoryβ[10.05.19] description: BRAF G466R (previously reported as G465R) lies within the glycine-rich loop in the protein kinase domain of the Braf protein (PMID: 14681681). G466R results in impaired Braf kinase activity, but activates Erk signaling in cell culture (PMID: 15046639), and in one of two cell lines, G466R decreased cell proliferation and cell viability compared to wild-type Braf (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
S467A | source: Jackson Laboratoryβ[10.05.19] description: BRAF S467A lies within the protein kinase domain of the Braf protein (UniProt.org). S467A confers a gain of function to the Braf protein as demonstrated by increased kinase activity and activation of downstream Mek signaling (PMID: 23680146, PMID: 16439621). link to source |
S467L | source: Jackson Laboratoryβ[10.05.19] description: BRAF S467L lies within the protein kinase domain of the Braf protein (UniProt.org). S467L results in impaired Braf kinase activity, but leads to Ras-dependent activation of Erk in cell culture (PMID: 28783719), and in two different cell lines, S467L increased cell proliferation and cell viability as compared to wild-type Braf (PMID: 29533785), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
F468C | source: Jackson Laboratoryβ[10.05.19] description: BRAF F468C (also referred to as F467C) lies within the protein kinase domain of the Braf protein (UniProt.org). F468C confers a gain of function to the Braf protein as demonstrated by increased Braf kinase activity and downstream Erk phosphorylation, activation of NFkappaB signaling in reporter assays, and transformation of cultured cells (PMID: 15150094). link to source |
G469A | source: SwissProtβ[10.05.19] description: Increased activity ; function (Protein serine/threonine kinase activity). Higher basal kinase activity. Induces cell transformation. link to source source: Jackson Laboratoryβ[10.05.19] description: BRAF G469A is a hotspot mutation within the protein kinase domain of the Braf protein (UniProt.org). G469A results in increased Braf kinase activity and downstream activation of Erk, and is transforming in cell culture (PMID: 19010912, PMID: 12068308, PMID: 29533785). link to source |
G469del | source: Jackson Laboratoryβ[10.05.19] description: BRAF G469del results in the deletion of an amino acid in the protein kinase domain of the Braf protein at amino acid 469 (UniProt.org). G469del demonstrates decreased Braf kinase activity, does not activate downstream ERK, and is minimally transforming in cell culture (PMID: 23833300). link to source |
G469R | source: Jackson Laboratoryβ[10.05.19] description: BRAF G469R is a hotspot mutation within the protein kinase domain of the Braf protein (UniProt.org). G469R demonstrates intermediate BRAF kinase activity (PMID: 28783719) and results in constitutive ERK activation in cell culture (PMID: 24920063), and in one of two cell lines leads to increased cell proliferation and cell viability compared to wild-type Braf (PMID: 29533785), and is therefore predicted to confer a gain of function to the Braf protein. link to source |
G469E | source: Jackson Laboratoryβ[10.05.19] description: BRAF G469E is a hotspot mutation within the protein kinase domain of the Braf protein (UniProt.org). The functional effect of G469E on Braf is unclear as it has been characterized as having both low Braf kinase activity (PMID: 28783719) and intermediate Braf kinase activity (PMID: 15035987), results in Ras-dependent activation of ERK signaling in cell culture (PMID: 28783719), and in one of two cell lines, G469E increased cell proliferation and cell viability as compared to wild-type Braf (PMID: 29533785). link to source |
G469V | source: Jackson Laboratoryβ[10.05.19] description: BRAF G469V is a hotspot mutation within the protein kinase domain of the Braf protein (UniProt.org). G469V results in increased Braf kinase activity and activation of downstream MEK and ERK in cell culture (PMID: 28947956, PMID: 26343582, PMID: 28783719), and in one of two cell lines, increased cell proliferation and cell viability compared to wild-type Braf (PMID: 29533785). link to source |
G469L | source: Jackson Laboratoryβ[10.05.19] description: BRAF G469L is a hotspot mutation lies within the protein kinase domain of the Braf protein (UniProt.org). G469L has been identified in the scientific literature (PMID: 24035431, PMID: 26301799, PMID: 26200454), but has not been biochemically characterized, and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
G469S | source: Jackson Laboratoryβ[10.05.19] description: BRAF G469S is a hotspot mutation within the protein kinase domain of the Braf protein (UniProt.org). G469S results in increased Erk phosphorylation (PMID: 27478040) and induces increased cell proliferation and cell viability compared to wild-type Braf in culture (PMID: 29533785). link to source |
T470K | source: Jackson Laboratoryβ[10.05.19] description: BRAF T470K lies within the protein kinase domain of the Braf protein (UniProt.org). T470K has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
V471F | source: Jackson Laboratoryβ[10.05.19] description: BRAF V471F lies within the protein kinase domain of the Braf protein (UniProt.org). V471F results in a loss of Braf kinase activity, however, results in dimerization-dependent activation of Erk signaling and is weakly transforming in cultured cells (PMID: 25348715). link to source |
V471I | source: Jackson Laboratoryβ[10.05.19] description: BRAF V471I lies within the protein kinase domain of the Braf protein (UniProt.org). V471I has been identified in sequencing studies (PMID: 28188106, PMID: 23103869), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
Y472C | source: Jackson Laboratoryβ[10.05.19] description: BRAF Y472C lies within the protein kinase domain of the Braf protein (UniProt.org). Y472C results in impaired Braf kinase activity, but paradoxically increases Mek and Erk signaling through C-raf transactivation (PMID: 22649091), however, in two different cell lines, Y472C induces similar cell proliferation and cell viability as compared to wild-type Braf (PMID: 29533785), and therefore, its effect on Braf protein function is unknown. link to source |
G478C | source: Jackson Laboratoryβ[10.05.19] description: BRAF G478C lies within the protein kinase domain of the Braf protein (UniProt.org). G478C demonstrates a lack of Braf kinase activity in cell culture (PMID: 22926515), and therefore is predicted to confer a loss of function to the Braf protein. link to source |
K483E | source: Jackson Laboratoryβ[10.05.19] description: BRAF K483E lies within the protein kinase domain of the Braf protein (UniProt.org). K483E results in increased transformation compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), but also results in ERK1/2 phosphorylation level similar to wild-type Braf in culture (PMID: 27799065), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
K483M | source: Jackson Laboratoryβ[10.05.19] description: BRAF K483M (also reported as K482M) lies within an ATP binding site in the protein kinase domain of the Braf protein (UniProt.org). K483M results in a loss of Braf kinase activity, however, has been demonstrated to both activate MEK through CRAF (PMID: 16508002, PMID: 23533272), and lack ability to activate ERK and CRAF in cell culture and in Xenopus (PMID: 15035987), and therefore, its effect on Braf protein function is unknown. link to source |
L485_P490delinsF | source: Jackson Laboratoryβ[10.05.19] description: BRAF L485_P490delinsF results in a deletion of six amino acids near the alphaC-helix region of the Braf protein kinase domain combined with the insertion of one new amino acid in the same location (PMID: 26732095). L485_P490delinsF is associated with increased Erk phosphorylation in human tumor samples (PMID: 29544532), and increased activation of MEK/ERK signaling in combination with L485_P490delinsY in cultured cells (PMID: 26732095), and therefore is predicted to confer a gain of function to the Braf protein. link to source |
L485_P490delinsY | source: Jackson Laboratoryβ[10.05.19] description: BRAF L485_P490delinsY results in a deletion of six amino acids near the alphaC-helix region of the Braf protein kinase domain combined with the insertion of one new amino acid in the same location (PMID: 26732095). L485_P490delinsY is associated with increased MEK/ERK activation in cells also harboring L485_P490delinsF, and similar deletions result in Braf activation (PMID: 26732095), and therefore, L485_P490delinsY is predicted to confer a gain of function to the Braf protein. link to source |
L485W | source: Jackson Laboratoryβ[10.05.19] description: BRAF L485W lies within the protein kinase domain of the Braf protein (UniProt.org). L485W results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
L485_Q494del | source: Jackson Laboratoryβ[10.05.19] description: BRAF L485_Q494del results in the deletion of ten amino acids within the beta-3/alpha-C helix loop in the protein kinase domain of the Braf protein (PMID: 26732095, UniProt.org). L485_Q494del has not been characterized, however, is predicted to result in a gain of function due to other characterized BRAF deletions in the same region (PMID: 26732095). link to source |
L485Y | source: Jackson Laboratoryβ[10.05.19] description: BRAF L485Y lies within the protein kinase domain of the Braf protein (UniProt.org). L485Y has been demonstrated to confer resistance to Raf inhibitor in cell culture (PMID: 19276360), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
L485_P490del | source: Jackson Laboratoryβ[10.05.19] description: BRAF L485_P490del results in the deletion of six amino acids within the beta-3/alpha-C helix loop in the protein kinase domain of the Braf protein (PMID: 26732095, UniProt.org). L485_P490del confers a gain of function to the Braf protein as demonstrated by increased kinase activity, phosphorylation of downstream Mek and Erk, and transformation ability in cell culture (PMID: 26732095, PMID: 26996308), and is associated with resistance to vemurafenib in cell culture (PMID: 26996308). link to source |
L485F | source: Jackson Laboratoryβ[10.05.19] description: BRAF L485F lies within the protein kinase domain of the Braf protein (UniProt.org). L485F confers a gain of function to the Braf protein as demonstrated by increased kinase activity and activation of downstream Mek and Erk in cell culture (PMID: 16439621), and in one of two cell lines, L485F increased cell proliferation and cell viability compared to wild-type Braf (PMID: 29533785). link to source |
N486_A489delinsK | source: Jackson Laboratoryβ[10.05.19] description: BRAF N486_A489delinsK results in a deletion of 4 amino acids in the protein kinase domain of the Braf protein from amino acids 486 to 489, combined with the insertion of a lysine (K) at the same site (UniProt.org). N486_A489delinsK has been identified in sequencing studies (PMID: 29247016), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Feb 2019). link to source |
N486_P490del | source: Jackson Laboratoryβ[10.05.19] description: BRAF N486_P490del results in the deletion of five amino acids near the alphaC-helix region of the kinase domain (PMID: 26732095). N486_P490del confers a gain of function to the Braf protein as indicated by activation of the MAPK signaling pathway and increased cell proliferation in culture (PMID: 26732095). link to source |
N486_T491delinsK | source: Jackson Laboratoryβ[10.05.19] description: BRAF N486_T491delinsK results in a deletion of 6 amino acids in the protein kinase domain of the Braf protein from amino acids 486 to 491, combined with the insertion of a lysine (K) at the same site (UniProt.org). N486_A491delinsK confers a gain of function to Braf, as indicated by increased ERK activation and transformation of cultured cells (PMID: 30867592). link to source |
N486D | source: Jackson Laboratoryβ[10.05.19] description: BRAF N486D lies within the protein kinase domain of the Braf protein (UniProt.org). N486D results in increased transformation ability compared to wild-type Braf in one of two cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
V487_P492delinsA | source: Jackson Laboratoryβ[10.05.19] description: BRAF V487_P492delinsA results in a deletion of six amino acids near the alphaC-helix region of the kinase domain of the Braf protein combined with the insertion of one new amino acid in the same location (PMID: 26732095). V487_P492delinsA confers a gain of function to the Braf protein as indicated by increased pathway signaling and cell proliferation in culture (PMID: 26732095). link to source |
T488_Q493delinsK | source: Jackson Laboratoryβ[10.05.19] description: BRAF T488_Q493delinsK results in the deletion of six amino acids near the alphaC-helix region of the Braf protein kinase domain combined with the insertion of one new amino acid in the same location (PMID: 26732095). T488_Q493delinsK has not been characterized, however, is predicted to result in a gain of function due to other characterized BRAF deletions in the same region (PMID: 26732095). link to source |
T488_P492del | source: Jackson Laboratoryβ[10.05.19] description: BRAF T488_P492del results in the deletion of five amino acids near the alphaC-helix region of the protein kinase domain in the Braf protein from amino acids 488 to 492 (PMID: 26732095). T488_P492del results in activation of Mek in cell culture (PMID: 26996308), and similar Braf deletions are activating (PMID: 26996308, PMID: 26732095), and therefore T488_P492del is predicted to confer a gain of function to the Braf function. link to source |
P490_Q494del | source: Jackson Laboratoryβ[10.05.19] description: BRAF P490_Q494del results in the deletion of five amino acids near the alphaC-helix region of the protein kinase domain in the Braf protein from amino acids 490 to 494 (PMID: 26732095). P490_Q494del results in activation of Mek in cell culture (PMID: 26996308), and similar Braf deletions are activating (PMID: 26996308, PMID: 26732095), and therefore P490_Q494del is predicted to confer a gain of function to the Braf function. link to source |
K499E | source: Jackson Laboratoryβ[10.05.19] description: BRAF K499E lies within the protein kinase domain of the Braf protein (UniProt.org). K499E confers a gain of function to the Braf protein as demonstrated by increased Braf kinase activity and downstream signaling, activation of ELK-dependent signaling in reporter assays, and foci formation in cultured cells (PMID: 16474404, PMID: 18413255, PMID: 26065894). link to source |
K499N | source: Jackson Laboratoryβ[10.05.19] description: BRAF K499N lies within the protein kinase domain of the Braf protein (UniProt.org). K449N results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
E501K | source: Jackson Laboratoryβ[10.05.19] description: BRAF E501K lies within the protein kinase domain of the Braf protein (UniProt.org). E501K results in ELK transactivation at comparable levels to wild-type Braf in a reporter assay (PMID: 16474404), however, also demonstrates decreased Braf kinase activity in culture (PMID: 17603482), and therefore, its effect on Braf protein function is unknown. link to source |
E501G | source: Jackson Laboratoryβ[10.05.19] description: BRAF E501G lies within the protein kinase domain of the Braf protein (UniProt.org). E501G confers a loss of function to the Braf protein as demonstrated by inability to activate downstream reporter assays, impaired kinase activity and presence in genetic diseases associated with Ras/Raf/Mek dysfunction (PMID: 26065894, PMID: 16474404, PMID: 16439621). link to source |
V504I | source: Jackson Laboratoryβ[10.05.19] description: BRAF V504I lies within the protein kinase domain of the Braf protein (UniProt.org). V504I has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels as wild-type Braf (PMID: 29533785). link to source |
V504_R506dup | source: Jackson Laboratoryβ[10.05.19] description: BRAF V504_R506dup (also referred to as R506_K507insVLR) lies within the protein kinase domain (UniProt.org). V504_R506dup confers a gain of function to the Braf protein as demonstrated by stabilization of Braf homodimers and increased downstream Erk phosphorylation in cultured cells (PMID: 23817572), and is associated with increased Erk1/2 phosphorylation in human tumor samples (PMID: 29544532). link to source |
L505H | source: Jackson Laboratoryβ[10.05.19] description: BRAF L505H lies within the protein kinase domain of the Braf protein (UniProt.org). L505H confers a gain of function to the Braf protein resulting in MEK/ERK activation and oncogenic transformation in cultured cells, and is associated with resistance to RAF inhibitors (PMID: 24283590). link to source |
R509G | source: Jackson Laboratoryβ[10.05.19] description: BRAF R509G lies within the protein kinase domain of the Braf protein (UniProt.org). R509C has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
R509H | source: Jackson Laboratoryβ[10.05.19] description: BRAF R509H lies within the dimerization interface region of the Braf protein (PMID: 22510884). R509H confers a loss of function to the Braf protein, as demonstrated by decreased Braf dimerization and reduced ability to activate downstream Mek signaling in in vitro assays (PMID: 22510884). link to source |
L514V | source: Jackson Laboratoryβ[10.05.19] description: BRAF L514V lies within the protein kinase domain of the Braf protein (UniProt.org). L514V is predicted to lead to a gain of Braf function as indicated by moderate increase of Mek and Erk phosphorylation in culture, enhanced dimerization when expressed in cis with BRAF V600E, and is associated with resistance to Raf inhibitors (PMID: 29880583). link to source |
M517I | source: Jackson Laboratoryβ[10.05.19] description: BRAF M517I lies within the protein kinase domain of the Braf protein (UniProt.org). M517I has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
T529M | source: Jackson Laboratoryβ[10.05.19] description: BRAF T529M lies within the protein kinase domain of the Braf protein (UniProt.org). T529M has been demonstrated to result in resistance to Raf inhibitors in the context of BRAF V600E (PMID: 20538618), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
T529N | source: Jackson Laboratoryβ[10.05.19] description: BRAF T529N lies within the protein kinase domain of the Braf protein (UniProt.org). T529N has been demonstrated to result in resistance to Raf inhibitors in the context of BRAF V600E (PMID: 20538618, PMID: 20807807), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
T529I | source: Jackson Laboratoryβ[10.05.19] description: BRAF T529I is a gatekeeper mutation that lies within the protein kinase domain of the Braf protein (PMID: 20538618). T529I has been demonstrated to result in resistance to Raf inhibitors in the context of BRAF V600E (PMID: 20538618), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Jun 2018). link to source |
W531C | source: Jackson Laboratoryβ[10.05.19] description: BRAF W531C lies within the protein kinase domain of the Braf protein (UniProt.org). W531C results in the weak activation of MEK signaling and does not induce transformation in cell culture (PMID: 19206169), but in two different cell lines, W531C demonstrates increased cell proliferation and viability as compared to wild-type Braf (PMID: 29533785), and therefore, its effect on Braf protein function is unknown. link to source |
Y538H | source: Jackson Laboratoryβ[10.05.19] description: BRAF Y538H lies within the protein kinase domain of the Braf protein (UniProt.org). Y538H has not been characterized in the scientific literature and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
G563D | source: Jackson Laboratoryβ[10.05.19] description: BRAF G563D lies within the protein kinase domain of the Braf protein (UniProt.org). G563D has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture compared to wild-type Braf (PMID: 29533785), and therefore is predicted to confer a loss of function to the Braf protein. link to source |
H568D | source: Jackson Laboratoryβ[10.05.19] description: BRAF H568D lies within the protein kinase domain of the Braf protein (UniProt.org). H568D results in a loss of MEK phosphorylation in cell culture similar to Braf kinase-dead variants (PMID: 29666306), and therefore, is predicted to confer a loss of function to the Braf protein. link to source |
H574Q | source: Jackson Laboratoryβ[10.05.19] description: BRAF H574Q lies within the protein kinase domain of the Braf protein (UniProt.org). H574Q confers a gain of function to the Braf protein as indicated by increased Erk phosphorylation in culture and tumor formation in animal models, and confers resistance to Egfr inhibitors in culture (PMID: 27478040). link to source |
H574N | source: Jackson Laboratoryβ[10.05.19] description: BRAF H574N lies within the protein kinase domain of the Braf protein (UniProt.org). H574N results in Erk phosphorylation at similar levels to wild-type Braf in culture (PMID: 27478040), and is therefore predicted to have no effect on Braf protein function. link to source |
N581K | source: Jackson Laboratoryβ[10.05.19] description: BRAF N581K lies within the protein kinase domain of the Braf protein (UniProt.org). N581K has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
N581D | source: Jackson Laboratoryβ[10.05.19] description: BRAF N581D lies within the protein kinase domain of the Braf protein (UniProt.org). N581D results in transactivation of ELK at comparable levels to wild-type Braf in a reporter assay (PMID: 16474404), and is therefore predicted to have no effect on Braf protein function. link to source |
N581Y | source: Jackson Laboratoryβ[10.05.19] description: BRAF N581Y lies within the protein kinase domain of the Braf protein (UniProt.org). N581Y has been identified in the scientific literature (PMID: 19474002, PMID: 26084293), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Nov 2018). link to source |
N581T | source: Jackson Laboratoryβ[10.05.19] description: BRAF N581T lies within the protein kinase domain of the Braf protein (UniProt.org). N581T has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
N581I | source: Jackson Laboratoryβ[10.05.19] description: BRAF N581I lies within the protein kinase domain of the Braf protein (UniProt.org). N581I results in low Braf kinase activity and Ras-dependent activation of Erk signaling in cell culture (PMID: 28783719), however, also results in increased transformation ability compared to wild-type Braf in culture (PMID: 29533785), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
N581S | source: Jackson Laboratoryβ[10.05.19] description: BRAF N581S lies within the protein kinase domain of the Braf protein (UniProt.org). The functional effect of N581S is unclear as it has been demonstrated to result in intermediate Braf kinase activity (PMID: 15035987), as well as low Braf kinase activity (PMID: 28783719), and results in Ras-dependent activation of ERK signaling in cell culture (PMID: 28783719), however in another study, N581S demonstrated increased transformation ability in one of two different cell lines as compared to wild-type Braf (PMID: 29533785). link to source |
I582M | source: Jackson Laboratoryβ[10.05.19] description: BRAF I582M lies within the protein kinase domain of the Braf protein (UniProt.org). I582M has been identified in sequencing studies (PMID: 30268455, PMID: 15331929), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
L584F | source: Jackson Laboratoryβ[10.05.19] description: BRAF L584F lies within the protein kinase domain of the Braf protein (UniProt.org). L584F results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
H585Y | source: Jackson Laboratoryβ[10.05.19] description: BRAF H585Y lies within the protein kinase domain of the Braf protein (UniProt.org). H585Y has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
E586K | source: Jackson Laboratoryβ[10.05.19] description: BRAF E586K (also reported as E585K) lies within the protein kinase domain of the Braf protein (UniProt.org). E586K results in increased Braf kinase activity, and activation of Mek and Erk in cell culture (PMID: 15035987, PMID: 22510884), and increases cell proliferation and viability compared to wild-type Braf in one of two cell lines (PMID: 29533785). link to source |
D587E | source: Jackson Laboratoryβ[10.05.19] description: BRAF D587E lies within the protein kinase domain of the Braf protein (UniProt.org). D587E has been identified in sequencing studies (PMID: 27034166), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
D587G | source: Jackson Laboratoryβ[10.05.19] description: BRAF D587G lies within the protein kinase domain of the Braf protein (UniProt.org). D587G has been identified in the scientific literature (PMID: 24803665), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
D587A | source: Jackson Laboratoryβ[10.05.19] description: BRAF D587A lies within the protein kinase domain of the Braf protein (UniProt.org). D587A has been identified in sequencing studies (PMID: 14500346), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
V590I | source: Jackson Laboratoryβ[10.05.19] description: BRAF V590I lies within the protein kinase domain of the Braf protein (UniProt.org). V590I has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
I592V | source: Jackson Laboratoryβ[10.05.19] description: BRAF I592V lies within the protein kinase domain of the Braf protein (UniProt.org). I592V has been identified in sequencing studies (PMID: 24710085, PMID: 15331929), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
I592M | source: Jackson Laboratoryβ[10.05.19] description: BRAF I592M lies within the protein kinase domain of the Braf protein (UniProt.org). I592M has been identified in sequencing studies (PMID: 15331929), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
D594_T599dup | source: Jackson Laboratoryβ[10.05.19] description: BRAF D594_T599dup (also referred to as T599_V600insDFGLAT) results in the insertion of six amino acids in the protein kinase domain of the Braf protein between amino acids 599 and 600 (UniProt.org).BRAF D594_T599dup results in increased colony formation and downstream Mek and Erk activation in cultured cells (PMID: 17297294). link to source |
D594A | source: Jackson Laboratoryβ[10.05.19] description: BRAF D594A lies within the protein kinase domain of the Braf protein (UniProt.org). D594A results in a lack of Braf kinase activity (PMID: 20141835, PMID: 20978199, PMID: 28783719), promotes aneupolidy (PMID: 20978199), and in one of two cell lines demonstrated decreased transformation ability compared to wild-type Braf in culture (PMID: 29533785), but leads to activation of Mek and Erk through cooperation with activated RAS and transactivation of CRAF in cell culture and mouse models (PMID: 20141835, PMID: 20978199, PMID: 28783719). link to source |
D594E | source: Jackson Laboratoryβ[10.05.19] description: BRAF D594E lies within the protein kinase domain of the Braf protein (UniProt.org). D594E results in impaired Braf kinase activity, however, results in increased Mek and Erk phosphorylation in the presence of CRAF in cell culture (PMID: 28783719). link to source |
D594G | source: Jackson Laboratoryβ[10.05.19] description: BRAF D594G lies within the protein kinase domain of the Braf protein (UniProt.org). D594G has been demonstrated to result in impaired Braf kinase activity, but leads to increased activation of Erk signaling through CRAF in cell culture (PMID: 18794803, PMID: 28783719), however, has increased transforming ability in one of two cell lines in culture (PMID: 29533785), and therefore its effect on Braf protein function is unknown. link to source |
D594N | source: Jackson Laboratoryβ[10.05.19] description: BRAF D594N lies within the protein kinase domain of the Braf protein (UniProt.org). D594N results in impaired Braf kinase activity, but leads to activation of Erk signaling through CRAF in cell culture (PMID: 28783719), and demonstrates decreased transforming ability compared to wild-type Braf in one of two cell lines in culture (PMID: 29533785), and therefore is predicted to confer a loss of function to the Braf protein. link to source |
D594Y | source: Jackson Laboratoryβ[10.05.19] description: BRAF D594Y lies within the protein kinase domain of the Braf protein (UniProt.org). D594Y has been identified in sequencing studies (PMID: 29106415, PMID: 28486044), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
D594V | source: Jackson Laboratoryβ[10.05.19] description: BRAF D594V lies within the protein kinase domain of the Braf protein (UniProt.org). D594V results in impaired Braf kinase activity, and decreased activation of Erk, Mek, and CRAF in cell culture (PMID: 28947956, PMID: 15035987), and has decreased transforming ability in one of two cell lines compared to wild-type Braf in culture (PMID: 29533785). link to source |
D594H | source: Jackson Laboratoryβ[10.05.19] description: BRAF D594H lies within the protein kinase domain of the Braf protein (UniProt.org). D594H results in a loss of Braf kinase activity, but leads to Ras-dependent activation of Erk signaling through CRAF (PMID: 28783719), and demonstrates decreased transforming activity compared to wild-type Braf in one of two cell lines in culture (PMID: 29533785), and therefore is predicted to confer a loss of function to the Braf protein. link to source |
F595S | source: Jackson Laboratoryβ[10.05.19] description: BRAF F595S lies within the protein kinase domain of the Braf protein (UniProt.org). F595S has been identified in sequencing studies (PMID: 15331929), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
F595L | source: Jackson Laboratoryβ[10.05.19] description: BRAF F595L lies within the protein kinase domain of the Braf protein (UniProt.org). F595L has been demonstrated to result in intermediate Braf kinase activity and is transforming in cell culture (PMID: 15035987, PMID: 26582644, PMID: 29533785), and works cooperatively with oncogenic Ras to activate MEK/ERK signaling (PMID: 26582644), however, has also been demonstrated to have low Braf kinase activity (PMID: 28783719), and therefore its effect on Braf protein function is unknown. link to source |
G596C | source: Jackson Laboratoryβ[10.05.19] description: BRAF G596C lies within the protein kinase domain of the Braf protein (UniProt.org). G596C results in decreased Braf kinase activity, however, leads to activation of downstream MEK and ERK in combination with CRAF in cell culture (PMID: 28947956). link to source |
G596D | source: Jackson Laboratoryβ[10.05.19] description: BRAF G596D lies within the protein kinase domain of the Braf protein (UniProt.org). G596D demonstrates decreased Braf kinase activity in cell culture (PMID: 28783719), and therefore is predicted to confer a loss of function to the Braf protein. link to source |
G596R | source: Jackson Laboratoryβ[10.05.19] description: BRAF G596R lies within the protein kinase domain of the Braf protein, within the DFG motif (PMID: 19735675). G596R results in impaired Braf kinase activity and decreased Mek and Erk phosphorylation, including in the presence of BRAF V600E, is not transforming in culture and does not promote tumor formation in mouse models, but results in activation of Erk in the presence of CRAF (PMID: 19735675, PMID: 28783719), however, in another study demonstrates similar cell proliferation and viability levels to wild-type Braf (PMID: 29533785), and is predicted to confer a loss of function to the Braf protein. link to source |
G596V | source: Jackson Laboratoryβ[10.05.19] description: BRAF G596V lies within the protein kinase domain of the Braf protein (UniProt.org). G596V results in impaired Braf kinase activity and does not activate downstream MEK and ERK in cell culture (PMID: 16439621), but leads to activation of ERK in zebrafish models (PMID: 19376813), and is therefore predicted to lead to a loss of Braf protein function. link to source |
G596S | source: Jackson Laboratoryβ[10.05.19] description: BRAF G596S lies within the protein kinase domain of the Braf protein (UniProt.org). G596S has not been biochemically characterized, but results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
G596fs | source: Jackson Laboratoryβ[10.05.19] description: BRAF G596fs results in a change in the amino acid sequence of the Braf protein beginning at aa 596 of 766, likely resulting in premature truncation of the functional protein (UniProt.org). Due to the disruption of the protein kinase domain (UniProt.org), G596fs is predicted to lead to a loss of Braf protein function. link to source |
L597V | source: SwissProtβ[10.05.19] description: Increased activity ; function (Protein serine/threonine kinase activity). Increased basal kinase activity. Efficiently induces cell transformation. link to source source: Jackson Laboratoryβ[10.05.19] description: BRAF L597V lies within the protein kinase domain of the Braf protein (UniProt.org). L597V results in activation of Braf as indicated by increased phosphorylation of Mek and Erk in cell culture (PMID: 22798288) and and induces cell proliferation and cell viability in culture (PMID: 29533785). link to source |
L597Q | source: Jackson Laboratoryβ[10.05.19] description: BRAF L597Q lies within the protein kinase domain of the Braf protein (UniProt.org). L597Q results in activation of Braf as indicated by increased phosphorylation of Mek and Erk in cell culture (PMID: 22798288) and induces cell proliferation and cell viability in culture (PMID: 29533785). link to source |
L597R | source: Jackson Laboratoryβ[10.05.19] description: BRAF L597R lies within the protein kinase domain of the Braf protein (UniProt.org). L597R results in activation of Braf as indicated by increased phosphorylation of Mek and Erk in cell culture (PMID: 22798288, PMID: 26343582), is associated with Erk activation in a patient tumor sample (PMID: 23715574), and in one of two cell lines, increased cell proliferation and cell viability compared to wild-type Braf (PMID: 29533785). link to source |
L597S | source: Jackson Laboratoryβ[10.05.19] description: BRAF L597S lies within the protein kinase domain of the Braf protein (UniProt.org). L597S results in activation of Braf as indicated by increased phosphorylation of Mek and Erk in cell culture (PMID: 22798288) and induces cell proliferation and cell viability in culture (PMID: 29533785). link to source |
L597P | source: Jackson Laboratoryβ[10.05.19] description: BRAF L597P lies within the protein kinase domain of the Braf protein (UniProt.org). L597P has been identified in sequencing studies (PMID: 30268455, PMID: 24714776), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
A598T | source: Jackson Laboratoryβ[10.05.19] description: BRAF A598T lies within the protein kinase domain of the Braf protein (UniProt.org). A598T demonstrates a lack of Braf kinase activity in culture (PMID: 22926515), and therefore, is predicted to result in a loss of Braf protein function. link to source |
A598V | source: Jackson Laboratoryβ[10.05.19] description: BRAF A598V lies within the protein kinase domain of the Braf protein (UniProt.org). A598V is associated with increased activation of Braf and downstream Mek and Erk in human tumor samples (PMID: 19200582), and is therefore predicted to confer a gain of function to the Braf protein. link to source |
A598S | source: Jackson Laboratoryβ[10.05.19] description: BRAF A598S lies within the protein kinase domain of the Braf protein (UniProt.org). A598S has not been characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
A598_T599insV | source: Jackson Laboratoryβ[10.05.19] description: BRAF A598_T599insV results in the insertion of a valine (V) in the protein kinase domain of the Braf protein between amino acids 598 and 599 (UniProt.org). A598_T599insV results in increased Braf kinase activity, increased downstream Mapk and Mek signaling, and the ability to transform cells in culture (PMID: 16501605). link to source |
A598_T599insARC | source: Jackson Laboratoryβ[10.05.19] description: BRAF A598_T599insARC results in the insertion of 3 amino acids in the protein kinase domain of the Braf protein between amino acids 598 and 599 (UniProt.org). BRAF A598_T599insARC has not been characterized, however other insertions between A598 and T599 are activating thus, A598_T599insARC is predicted to lead to a gain of Braf protein function (PMID: 16501605). link to source |
T599I | source: Jackson Laboratoryβ[10.05.19] description: BRAF T599I (also reported as T598I) lies within the protein kinase domain of the Braf protein (UniProt.org). T599I results in increased Braf kinase activity, increased downstream Erk signaling (PMID: 15035987), and induces cell proliferation and cell viability in culture (PMID: 29533785). link to source |
T599A | source: Jackson Laboratoryβ[10.05.19] description: BRAF T599A lies within the protein kinase domain of the Braf protein (UniProt.org). T599A does not result in increased MEK or ERK phosphorylation and does not transactivate CRAF (PMID: 22506009), and demonstrates decreased transformation ability compared to wild-type Braf in cell culture (PMID: 29533785). link to source |
T599_V600insTT | source: Jackson Laboratoryβ[10.05.19] description: BRAF T599_V600insTT results in the insertion of two threonines (T) in the protein kinase domain of the Braf protein between amino acids 599 and 600 (UniProt.org). T599_V600insTT results in increased Braf kinase activity in an in vitro assay, and increased downstream Mek/Erk signaling in culture (PMID: 21190184). link to source |
T599_V600insETT | source: Jackson Laboratoryβ[10.05.19] description: BRAF T599_V600insETT results in the insertion of 3 amino acids in the protein kinase domain of the Braf protein between amino acids 599 and 600 (UniProt.org). BRAF T599_V600insETT has not been characterized, however other insertions between T599 and V600 are activating thus, T599_V600insETT is predicted to lead to a gain of Braf protein function (PMID: 16501605, PMID: 17297294, PMID: 21190184). link to source |
T599_V600insEAT | source: Jackson Laboratoryβ[10.05.19] description: BRAF T599_V600insEAT results in the insertion of 3 amino acids in the protein kinase domain of the Braf protein between amino acids 599 and 600 (UniProt.org). T599_V600insEAT has not been characterized, however other insertions between T599 and V600 are activating thus, T599_V600insEAT is predicted to lead to a gain of Braf protein function (PMID: 16501605, PMID: 17297294, PMID: 21190184). link to source |
T599K | source: Jackson Laboratoryβ[10.05.19] description: BRAF T599K lies within the protein kinase domain of the Braf protein (UniProt.org). T599K has been identified in sequencing studies (PMID: 30603682), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Feb 2019). link to source |
T599R | source: Jackson Laboratoryβ[10.05.19] description: BRAF T599R lies within the activation loop in the kinase domain of the Braf protein (PMID: 19206169). T599R confers a gain of function on Braf, as indicated by increased MEK and ERK phosphorylation, and is transforming in cell culture (PMID: 19206169, PMID: 29533785). link to source |
T599_V600insT | source: Jackson Laboratoryβ[10.05.19] description: BRAF T599dup (also referred to T599_V600insT) indicates the insertion of the duplicate amino acid, tyrosine (T)-599, in the protein kinase domain of the Braf protein (UniProt.org). T599dup confers a gain of function to the Braf protein as demonstrated by increased kinase activity and phosphorylation of downstream Mek and Erk, and is transforming in cell culture (PMID: 21190184). link to source |
T599_V600insS | source: Jackson Laboratoryβ[10.05.19] description: BRAF T599_V600insS results in the insertion of a serine (S) in the protein kinase domain of the Braf protein between amino acids 599 and 600 (UniProt.org). T599_V600insS has not been characterized in the scientific literature and therefore, its effect on Braf protein function is unknown (PubMed, Feb 2019). link to source |
V600E | source: SwissProtβ[10.05.19] description: Increased activity ; function (Protein serine/threonine kinase activity ; cell population proliferation). Constitutive and elevated kinase activity; loss of regulation by HRAS and PMRT5; efficiently induces cell transformation. link to source source: Jackson Laboratoryβ[10.05.19] description: BRAF V600E (previously reported as V599) lies within the activation segment of the kinase domain of the Braf protein (PMID: 15035987). V600E confers a gain of function to the Braf protein as demonstrated by increased Braf kinase activity, downstream signaling, and the ability to transform cells in culture (PMID: 15035987, PMID: 29533785). link to source |
V600G | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600G (previously reported as V599G) lies within the activation segment of the kinase domain of the Braf protein (PMID: 15035987). V600G confers a gain of function to Braf as indicated by increased phosphorylation of MEK and ERK and activation of ELK in culture (PMID: 20735442, PMID: 26744778), and in one of two cell lines, increased cell proliferation and viability compared to wild-type Braf (PMID: 29533785). link to source |
V600L | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600L (previously reported as V599L) lies within the activation segment of the protein kinase domain of the Braf protein (PMID: 15035987). V600L results in increased cell proliferation and cell viability compared to wild-type Braf in one of two cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
V600K | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600K (previously reported as V599) lies within the activation segment of the kinase domain of the Braf protein (PMID: 15035987). V600K confers a gain of function to the Braf protein as demonstrated by increased kinase activity, downstream signaling, and the ability to transform cells in vitro (PMID: 15035987, PMID: 29533785). link to source |
V600delinsYM | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600delinsYM results in a deletion of valine (V) at amino acid 600 within the protein kinase domain of the Braf protein, combined with the insertion of a tyrosine (Y) and a methionine (M) at the same site (UniProt.org). V600delinsYM results in increased Braf kinase activity, increased downstream signaling, and the ability to transform cells in culture (PMID: 22752848). link to source |
V600D | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600D (previously reported as V599) lies within the activation segment of the kinase domain of the Braf protein (PMID: 15035987). V600D confers a gain of function to the Braf protein as demonstrated by increased kinase activity, downstream signaling, and the ability to transform cells in vitro (PMID: 15035987). link to source |
V600_K601delinsE | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600_K601delinsE results in the deletion of two amino acids formation of a new glutamic acid (E) residue in the protein kinase domain of the Braf protein between amino acids 600 and 601 (UniProt.org, PMID: 22563563). V600_K601delinsE leads to activation of downstream Mek and Erk signaling, increased colony formation (PMID: 17297294), and induces cell proliferation and cell viability in cell culture (PMID: 29533785). link to source |
V600fs | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600fs results in a change in the amino acid sequence of the Braf protein beginning at aa 600 of 766, likely resulting in premature truncation of the functional protein (UniProt.org). Due to the disruption of the protein kinase domain, V600fs is predicted to lead to a loss of Braf protein function (UniProt.org). link to source |
V600R | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600R (previously reported as V599) lies within the activation segment of the kinase domain of the Braf protein (PMID: 15035987). V600R confers a gain of function to the Braf protein as demonstrated by increased Braf kinase activity, downstream signaling, and the ability to transform cells in culture (PMID: 15035987, PMID: 29533785). link to source |
V600_K601insV | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600dup (also referred to as T599_V600insV) indicates the insertion of the duplicate amino acid, valine (V)-600, in the protein kinase domain of the Braf protein (UniProt.org). V600dup confers a gain of function to the Braf protein as demonstrated by increased kinase activity and phosphorylation of downstream Mek and Erk, and is transforming in cell culture (PMID: 21190184). link to source |
V600delinsE/K | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600E/K indicates a mutation that results in the replacement of the valine (V) at amino acid 600 of the Braf protein by either a glutamate (E) or lysine (K). V600E/K mutations are hotspot mutations in Braf that result in increased Braf kinase activity (PMID: 15035987). link to source |
V600Q | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600Q (previously reported as V599Q) lies within the activation segment and the protein kinase domain of the Braf protein (PMID: 15035987). V600Q has been identified in the scientific literature (PMID: 28848703), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
V600M | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600M (previously reported as V599) lies within the activation segment of the kinase domain of the Braf protein (PMID: 15035987). V600M results in intermediate Braf kinase activity in cell culture (PMID: 28783719), and in one of two cell lines increased cell proliferation and cell viability compared to wild-type Braf (PMID: 29533785), and is therefore predicted to confer a gain of function to the Braf protein. link to source |
V600A | source: Jackson Laboratoryβ[10.05.19] description: BRAF V600A (previously reported as V599) lies within the activation segment of the kinase domain of the Braf protein (PMID: 15035987). V600A results in phosphorylated Mek protein levels similar to wild-type Braf and therefore, is predicted to have no effect on Braf protein function (PMID: 26744778). link to source |
K601T | source: Jackson Laboratoryβ[10.05.19] description: BRAF K601T lies within the activation segment in the kinase domain of the Braf protein (PMID: 15343278). K601T results in increased Braf kinase activity in cell culture (PMID: 28783719), and in one of two cell lines increased cell proliferation and cell viability compared to wild-type Braf (PMID: 29533785), and is therefore predicted to confer a gain of function to the Braf protein. link to source |
K601N | source: Jackson Laboratoryβ[10.05.19] description: BRAF K601N lies within the protein kinase domain of the Braf protein (UniProt.org). K601N confers a gain of function on Braf, as indicated by increased phosphorylation of MEK and ERK in cell in culture (PMID: 24434212) and induction of cell proliferation and cell viability in culture (PMID: 29533785). link to source |
K601I | source: Jackson Laboratoryβ[10.05.19] description: BRAF K601I lies within the protein kinase domain of the Braf protein (UniProt.org). K601I has been identified in the scientific literature (PMID: 26682952, PMID: 29176861, PMID: 23555633), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
K601E | source: Jackson Laboratoryβ[10.05.19] description: BRAF K601E lies within the activation segment in the kinase domain of the Braf protein (PMID: 15343278). K601E results in increased Braf kinase activity and downstream activation of MEK and ERK in cell culture (PMID: 22798288, PMID: 28783719) and induces cell proliferation and cell viability in culture (PMID: 29533785). link to source |
K601_S602delinsNT | source: Jackson Laboratoryβ[10.05.19] description: BRAF K601_S602delinsNT results in a deletion of two amino acids in the protein kinase domain of the Braf protein from amino acids 601 to 602, combined with the insertion of an asparagine (N) and a threonine (T) at the same site (UniProt.org). K601_S602delinsNT has not been characterized and therefore, its effect on Braf protein function is unknown (PubMed, Feb 2019). link to source |
K601del | source: Jackson Laboratoryβ[10.05.19] description: BRAF K601del results in the deletion of one amino acid in the protein kinase domain of the Braf protein at amino acid 601 (UniProt.org). K601del has been identified in sequencing studies (PMID: 19152441), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
K601Q | source: Jackson Laboratoryβ[10.05.19] description: BRAF K601Q lies within the activation loop in the kinase domain of the Braf protein (PMID: 19206169). K601Q confers a gain of function on Braf, as indicated by increased MEK and ERK phosphorylation, and is transforming in cell culture (PMID: 19206169, PMID: 29533785). link to source |
S602F | source: Jackson Laboratoryβ[10.05.19] description: BRAF S602F lies within the protein kinase domain of the Braf protein (UniProt.org). S602F has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
R603* | source: Jackson Laboratoryβ[10.05.19] description: BRAF R603* results in a premature truncation within the protein kinase domain of the Braf protein at amino acid 603 of 766 (UniProt.org, PMID: 11032810). Due to the loss of the protein kinase domain (UniProt.org, PMID: 11032810), R603* is predicted to lead to a loss of function. link to source |
W604G | source: Jackson Laboratoryβ[10.05.19] description: BRAF W604G lies within the protein kinase domain of the Braf protein (UniProt.org). W604G has been identified in the scientific literature (PMID: 29769567, PMID: 15331929), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
W604del | source: Jackson Laboratoryβ[10.05.19] description: BRAF W604del results in the deletion of one amino acid in the protein kinase domain of the Braf protein at amino acid 604 (UniProt.org). W604del has been identified in sequencing studies (PMID: 15513360), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
W604R | source: Jackson Laboratoryβ[10.05.19] description: BRAF W604R lies within the protein kinase domain of the Braf protein (UniProt.org). W604R has been identified in sequencing studies (PMID: 28188106, PMID: 21825258, PMID: 23833300), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
S605E | source: Jackson Laboratoryβ[10.05.19] description: BRAF S605E lies within the protein kinase domain of the Braf protein (UniProt.org). S605E results in basal Mek phosphorylation similar to wild-type Braf but moderately decreased Mek phosphorylation upon Ras activation in culture (PMID: 27034005), and therefore, is predicted to lead to a loss of Braf protein function. link to source |
S605F | source: Jackson Laboratoryβ[10.05.19] description: BRAF S605F lies within the protein kinase domain of the Braf protein (UniProt.org). S605F has been identified in sequencing studies (PMID: 15331929), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
S605A | source: Jackson Laboratoryβ[10.05.19] description: BRAF S605A lies within the protein kinase domain of the Braf protein (UniProt.org). S605A results in basal Mek phosphorylation similar to wild-type Braf but moderately decreased Mek phosphorylation upon Ras activation in culture (PMID: 27034005), and therefore, is predicted to lead to a loss of Braf protein function. link to source |
S605G | source: Jackson Laboratoryβ[10.05.19] description: BRAF S605G lies within the protein kinase domain of the Braf protein (UniProt.org). S605G results in basal Mek phosphorylation similar to wild-type Braf but moderately decreased Mek phosphorylation upon Ras activation in culture (PMID: 27034005), and therefore, is predicted to lead to a loss of Braf protein function. link to source |
S605N | source: Jackson Laboratoryβ[10.05.19] description: BRAF S605N lies within the protein kinase domain of the Braf protein (UniProt.org). S605N has been identified in sequencing studies (PMID: 29176861, PMID: 28628916, PMID: 15331929), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
G606A | source: Jackson Laboratoryβ[10.05.19] description: BRAF G606A lies within the protein kinase domain of the Braf protein (UniProt.org). G606A has been identified in sequencing studies (PMID: 21825258), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
G606E | source: Jackson Laboratoryβ[10.05.19] description: BRAF G606E lies within the protein kinase domain of the Braf protein (UniProt.org). G606E has been identified in sequencing studies (PMID: 29320312, PMID: 28936923, PMID: 15331929), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
G606V | source: Jackson Laboratoryβ[10.05.19] description: BRAF G606V lies within the protein kinase domain of the Braf protein (UniProt.org). G606V has been identified in sequencing studies (PMID: 21825258), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
G606W | source: Jackson Laboratoryβ[10.05.19] description: BRAF G606W lies within the protein kinase domain of the Braf protein (UniProt.org). G606W has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
S607F | source: Jackson Laboratoryβ[10.05.19] description: BRAF S607F lies within the protein kinase domain of the Braf protein (UniProt.org). S607F has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
H608R | source: Jackson Laboratoryβ[10.05.19] description: BRAF H608R lies within the protein kinase domain of the Braf protein (UniProt.org). H608R has been identified in sequencing studies (PMID: 15331929), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
Q609H | source: Jackson Laboratoryβ[10.05.19] description: BRAF Q609H lies within the protein kinase domain of the Braf protein (UniProt.org). Q609H has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
Q609E | source: Jackson Laboratoryβ[10.05.19] description: BRAF Q609E lies within the protein kinase domain of the Braf protein (UniProt.org). Q609E results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
E611D | source: Jackson Laboratoryβ[10.05.19] description: BRAF E611D lies within the protein kinase domain of the Braf protein (UniProt.org). E611D has been identified in sequencing studies (PMID: 15935100), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
L613F | source: Jackson Laboratoryβ[10.05.19] description: BRAF L613F lies within the protein kinase domain of the Braf protein (UniProt.org). L613F results in increased transformation ability as compared to wild-type Braf, in one of two cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
G615R | source: Jackson Laboratoryβ[10.05.19] description: BRAF G615R lies within the protein kinase domain of the Braf protein (UniProt.org). G615R has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
L618F | source: Jackson Laboratoryβ[10.05.19] description: BRAF L618F lies within the protein kinase domain of the Braf protein (UniProt.org). L618F has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
W619R | source: Jackson Laboratoryβ[10.05.19] description: BRAF W619R lies within the protein kinase domain of the Braf protein (UniProt.org). W619R has been identified in sequencing studies (PMID: 16179870), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
S637* | source: Jackson Laboratoryβ[10.05.19] description: BRAF S637* results in a premature truncation the Braf protein at amino acid 637 of 766 (UniProt.org). S637* has not been biochemically characterized, however, demonstrates an inability to induce cell viability and proliferation in cell culture (PMID: 29533785), and therefore is predicted to confer a loss of function to the Braf protein. link to source |
V639I | source: Jackson Laboratoryβ[10.05.19] description: BRAF V639I lies within the protein kinase domain of the Braf protein (UniProt.org). V639I has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
E648Q | source: Jackson Laboratoryβ[10.05.19] description: BRAF E648Q lies within the protein kinase domain of the Braf protein (UniProt.org). E648Q has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture compared to wild-type Braf (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
Y656D | source: Jackson Laboratoryβ[10.05.19] description: BRAF Y656D lies within the protein kinase domain of the Braf protein (UniProt.org). Y656D has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
R671Q | source: Jackson Laboratoryβ[10.05.19] description: BRAF R671Q lies within the protein kinase domain of the Braf protein (UniProt.org). R671Q has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
R671 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Alkylation description: Omega-N-methylarginine; by PRMT5 link to source |
P676S | source: Jackson Laboratoryβ[10.05.19] description: BRAF P676S lies within the protein kinase domain of the Braf protein (UniProt.org). P676S has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
L678I | source: Jackson Laboratoryβ[10.05.19] description: BRAF L678I lies within the protein kinase domain of the Braf protein (UniProt.org). L678I has not been biochemically characterized, but demonstrates decreased transformation ability in cell culture (PMID: 29533785), and is therefore predicted to confer a loss of function to the Braf protein. link to source |
V681I | source: Jackson Laboratoryβ[10.05.19] description: BRAF V681I lies within the protein kinase domain of the Braf protein (UniProt.org). V681I has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
E695K | source: Jackson Laboratoryβ[10.05.19] description: BRAF E695K lies within the protein kinase domain of the Braf protein (UniProt.org). E695K has not been biochemically characterized, but results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
K698R | source: Jackson Laboratoryβ[10.05.19] description: BRAF K698R lies within the protein kinase domain of the Braf protein (UniProt.org). K698R has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
L711F | source: Jackson Laboratoryβ[10.05.19] description: BRAF L711F lies within the protein kinase domain of the Braf protein (UniProt.org). L711F has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
A712T | source: Jackson Laboratoryβ[10.05.19] description: BRAF A712T lies within the protein kinase domain of the Braf protein (UniProt.org). A712T has not been biochemically characterized, but results inΓ similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
R719S | source: Jackson Laboratoryβ[10.05.19] description: BRAF R719S lies within the protein kinase domain of the Braf protein (UniProt.org). R719S has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
H725Y | source: Jackson Laboratoryβ[10.05.19] description: BRAF H725Y does not lie with any known functional domains of the Braf protein (UniProt.org). H725Y has not been biochemically characterized, but results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
A728V | source: Jackson Laboratoryβ[10.05.19] description: BRAF A728V (also referred to as A727V) does not lie within any known functional domains of the Braf protein (UniProt.org). A728V results in an intermediate increase in Braf kinase activity compared to wild-type Braf and increased Erk phosphorylation in cell culture (PMID: 15035987). link to source |
S729 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphoserine link to source |
P731T | source: Jackson Laboratoryβ[10.05.19] description: BRAF P731T does not lie within any known functional domains of the Braf protein (UniProt.org). P731T has been identified in the scientific literature (PMID: 29320312), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Feb 2019). link to source |
P731S | source: Jackson Laboratoryβ[10.05.19] description: BRAF P731S does not lie within any known functional domains of the Braf protein (UniProt.org). P731S results in increased transformation ability compared to wild-type Braf in one of two different cell lines in culture (PMID: 29533785), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
S750 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphoserine link to source |
T753 | source: SwissProtβ[20.02.20] impact: PTMβprotein effect: Phosphorylation description: Phosphothreonine; by MAPK1 link to source |
A762E | source: Jackson Laboratoryβ[10.05.19] description: BRAF A762E does not lie within any known functional domains of the Braf protein (UniProt.org). A762E has been demonstrated to confer resistance to Egfr inhibitors in culture (PMID: 27478040), but has not been biochemically characterized and therefore, its effect on Braf protein function is unknown (PubMed, Mar 2019). link to source |
A762V | source: Jackson Laboratoryβ[10.05.19] description: BRAF A762V lies within the protein kinase domain of the Braf protein (UniProt.org). A762V has not been biochemically characterized, but results in similar cell proliferation and viability levels to wild-type Braf in culture (PMID: 29533785), and therefore is predicted to have no effect on Braf protein function. link to source |
3D structure




Hydrogen bonds
Ionic interactions
Cation-Pi interactions
Hydrophobic contacts
Pi-stacking interactions
β
Sequence alignment

IDLabel
.450.452.454.456.458.460.462.464.466.468.470.472.474.476.478.480.482.484.486.488.490.492.494.496.498.500.502.504.506.508.510.512.514.516.518.520.522.524.526.528.530.532.534.536.538.540.542.544.546.548.550.552.554.556.558.560.562.564.566.568.570.572.574.576.578.580.582.584.586.588.590.592.594.596.598.600.602.604.606.608.610.612.614.616.618.620.622.624.626.628.630.632.634.636.638.640.642.644.646.648.650.652.654.656.658.660.662.664.666.668.670.672.674.676.678.680.682.684.686.688.690.692.694.696.698.700.702.704.706.708.710.712.714.716.718.720.722
β
Remarks
Mouse: An unreviewed sequence is presented instead of the reviewed one because it fits better. The sequence starts to fit with the other organisms at residue 16.
Rat: The sequence starts to fit with the other organisms at residue 23.
Dog: The sequence starts to fit with the other organisms at residue 46.
Chicken: An unreviewed sequence is presented instead of the reviewed one because it fits better.
Mouse: An unreviewed sequence is presented instead of the reviewed one because it fits better. The sequence starts to fit with the other organisms at residue 16.
Rat: The sequence starts to fit with the other organisms at residue 23.
Dog: The sequence starts to fit with the other organisms at residue 46.
Chicken: An unreviewed sequence is presented instead of the reviewed one because it fits better.