C-Raf

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Protein-coding gene in the species Homo sapiens

C-Raf
Symbol RAF1
HGNC ID 9829
Alternative symbols
Entrez Gene
OMIM 164760
RefSeq NM_002880
UniProt P04049
Chromosome 3p25
Locus supplementary data


C-Raf (also known as RAF1) is a protein kinase that is encoded by the RAF1 gene in Homo sapiens. It is a member of the Raf kinase family of serine/threonine-specific protein kinases.

Function[edit]

C-Raf plays a crucial role in the MAPK/ERK pathway, which is involved in the regulation of cell division, differentiation, and secretion. Upon activation by Ras proteins, C-Raf phosphorylates and activates MEK1 and MEK2, which in turn activate ERK1 and ERK2. This signaling cascade is essential for transmitting signals from the cell membrane to the nucleus.

Structure[edit]

C-Raf consists of three conserved regions: CR1, CR2, and CR3. The CR1 region contains the Ras-binding domain (RBD) and the cysteine-rich domain (CRD), which are essential for its interaction with Ras proteins. The CR2 region is a serine/threonine-rich domain that serves as a regulatory region. The CR3 region contains the kinase domain, which is responsible for its enzymatic activity.

Clinical Significance[edit]

Mutations in the RAF1 gene have been associated with several types of cancer, including melanoma, lung cancer, and colorectal cancer. Additionally, mutations in C-Raf are linked to developmental disorders such as Noonan syndrome and LEOPARD syndrome.

Interactions[edit]

C-Raf interacts with several proteins, including:

Research[edit]

Ongoing research is focused on understanding the precise mechanisms of C-Raf activation and its role in various diseases. Inhibitors targeting C-Raf and other components of the MAPK/ERK pathway are being developed as potential therapeutic agents for cancer treatment.

See also[edit]

References[edit]


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