K-ras 2 proto-oncogene protein (GTPase KRas, K-Ras 2, Ki-Ras, c-K-ras, c-Ki-ras, KRAS, KRAS2, RASK2)
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Function
- Ras proteins bind GDP/GTP & possess intrinsic GTPase activity
- interacts with PHLPP (putative)
- alternates between an inactive form bound to GDP & an active form bound to GTP
- activated by a guanine nucleotide-exchange factor (GEF) & inactivated by a GTPase-activating protein (GAP)
- p21ras binds to & activates raf1 protein probably in association with other proteins; raf1 activates MEK which in turn activates MAP kinases
Structure
belongs to the small GTPase superfamily. Ras family
Compartment
cell membrane, lipid-anchor, cytoplasmic side
Alternative splicing
named isoforms=2 isoforms 2A & 2B differ in the C-terminal region encoded by two alternative exons (IVA & IVB) variant in position: 153:D->V (in CFC syndrome)
Pathology
- defects in KRAS are a cause of
- acute myelogenous leukemia
- juvenile myelomonocytic leukemia
- Noonan syndrome 3
- cardiofaciocutaneous syndrome
- KRAS mutations are involved in cancer development, colorectal carcinoma
- KRAS-dependent tumor cells are dependent upon activity of STK33[5]
More general terms
More specific terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/P01116.html
- ↑ Atlas of genetics & cytogenetics in oncology & Haematology http://atlasgeneticsoncology.org/genes/KRASID91.html
- ↑ GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=KRAS
- ↑ SHMPD; Note: The Singapore human mutation and polymorphism database http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=KRAS
- ↑ 5.0 5.1 Scholl C et al Synthetic lethal interaction between oncogenic KRAS dependency and STK33 suppression in human cancer cells. Cell 2009 May 29; 137:821 PMID: https://www.ncbi.nlm.nih.gov/pubmed/19490892