ARAF

For other meanings, see Araf (disambiguation).

V-raf murine sarcoma 3611 viral oncogene homolog
PDB rendering based on 1wxm.
Available structures PDB 1wxm
Identifiers
Symbols	ARAF; A-RAF; ARAF1; PKS2; RAFA1
External IDs	OMIM: 311010 MGI: 88065 HomoloGene: 1249 GeneCards: ARAF Gene
EC number	2.7.11.1
Gene Ontology Molecular function • nucleotide binding • protein kinase activity • protein serine/threonine kinase activity • protein serine/threonine kinase activity • receptor signaling protein activity • protein binding • ATP binding • metal ion binding Cellular component • cellular_component • insoluble fraction • mitochondrion • cytosol Biological process • protein modification process • protein phosphorylation • protein phosphorylation • positive regulation of peptidyl-serine phosphorylation • intracellular signal transduction • negative regulation of apoptosis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	369	11836
Ensembl	ENSG00000078061	ENSMUSG00000001127
UniProt	P10398	Q3TQI2
RefSeq (mRNA)	NM_001654.3	NM_009703
RefSeq (protein)	NP_001645.1	NP_033833
Location (UCSC)	Chr X: 47.42 – 47.43 Mb	Chr X: 20.37 – 20.44 Mb
PubMed search	[1]	[2]

Serine/threonine-protein kinase A-Raf or simply A-Raf is an enzyme that in humans is encoded by the ARAF gene. A-Raf is a member of the Raf kinase family of serine/threonine-specific protein kinases.

Interactions

ARAF has been shown to interact with:

• EFEMP1,
• MAP2K2,
• PRPF6,
• RRAS,
• TIMM44, and
• TH1L.

Further reading

• Belanger BF, Williams WJ, Yin TC (1976). "A flexible renewal process simulator for neural spike trains". IEEE transactions on bio-medical engineering 23 (3): 262–6. doi:10.1109/TBME.1976.324641. PMID 1262038. 
• Popescu NC, Mark GE (1989). "Localization of the pKs gene, a raf related sequence on human chromosomes X and 7". Oncogene 4 (4): 517–9. PMID 2717185. 
• Beck TW, Huleihel M, Gunnell M, et al. (1987). "The complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus". Nucleic Acids Res. 15 (2): 595–609. doi:10.1093/nar/15.2.595. PMC 340454. PMID 3029685. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=340454. 
• Papin C, Eychène A, Brunet A, et al. (1995). "B-Raf protein isoforms interact with and phosphorylate Mek-1 on serine residues 218 and 222". Oncogene 10 (8): 1647–51. PMID 7731720. 
• Lee JE, Beck TW, Brennscheidt U, et al. (1994). "The complete sequence and promoter activity of the human A-raf-1 gene (ARAF1)". Genomics 20 (1): 43–55. doi:10.1006/geno.1994.1125. PMID 8020955. 
• Alessi DR, Saito Y, Campbell DG, et al. (1994). "Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1". EMBO J. 13 (7): 1610–9. PMC 394991. PMID 8157000. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=394991. 
• Gardner AM, Vaillancourt RR, Johnson GL (1993). "Activation of mitogen-activated protein kinase/extracellular signal-regulated kinase kinase by G protein and tyrosine kinase oncoproteins". J. Biol. Chem. 268 (24): 17896–901. PMID 8394352. 
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474. 
• Wu X, Noh SJ, Zhou G, et al. (1996). "Selective activation of MEK1 but not MEK2 by A-Raf from epidermal growth factor-stimulated Hela cells". J. Biol. Chem. 271 (6): 3265–71. doi:10.1074/jbc.271.6.3265. PMID 8621729. 
• Boldyreff B, Issinger OG (1997). "A-Raf kinase is a new interacting partner of protein kinase CK2 beta subunit". FEBS Lett. 403 (2): 197–9. doi:10.1016/S0014-5793(97)00010-0. PMID 9042965. 
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146. 
• Yuryev A, Ono M, Goff SA, et al. (2000). "Isoform-Specific Localization of A-RAF in Mitochondria". Mol. Cell. Biol. 20 (13): 4870–8. doi:10.1128/MCB.20.13.4870-4878.2000. PMC 85938. PMID 10848612. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85938. 
• King TR, Fang Y, Mahon ES, Anderson DH (2000). "Using a phage display library to identify basic residues in A-Raf required to mediate binding to the Src homology 2 domains of the p85 subunit of phosphatidylinositol 3'-kinase". J. Biol. Chem. 275 (46): 36450–6. doi:10.1074/jbc.M004720200. PMID 10967104. 
• Fang Y, Johnson LM, Mahon ES, Anderson DH (2002). "Two phosphorylation-independent sites on the p85 SH2 domains bind A-Raf kinase". Biochem. Biophys. Res. Commun. 290 (4): 1267–74. doi:10.1006/bbrc.2002.6347. PMID 11812000. 
• Yin XL, Chen S, Yan J, et al. (2002). "Identification of interaction between MEK2 and A-Raf-1". Biochim. Biophys. Acta 1589 (1): 71–6. doi:10.1016/S0167-4889(01)00188-4. PMID 11909642. 
• Yin XL, Chen S, Gu JX (2002). "Identification of TH1 as an interaction partner of A-Raf kinase". Mol. Cell. Biochem. 231 (1–2): 69–74. doi:10.1023/A:1014437024129. PMID 11952167. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Yuryev A, Wennogle LP (2003). "Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis". Genomics 81 (2): 112–25. doi:10.1016/S0888-7543(02)00008-3. PMID 12620389. 
• Liu W, Shen X, Yang Y, et al. (2004). "Trihydrophobin 1 is a new negative regulator of A-Raf kinase". J. Biol. Chem. 279 (11): 10167–75. doi:10.1074/jbc.M307994200. PMID 14684750.