ja ARAF

ARAF
PDBに登録されている構造
PDB	オルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧
	1WXM, 2MSE
識別子
記号	ARAF, A-Raf proto-oncogene, serine/threonine kinase, A-RAF, ARAF1, PKS2, RAFA1, Serine/threonine-protein kinase A-Raf
外部ID	OMIM: 311010 MGI: 88065 HomoloGene: 1249 GeneCards: ARAF
遺伝子の位置 (ヒト)
染色体	X染色体
終点	47,571,908 bp
遺伝子の位置 (マウス)
染色体	X染色体 (マウス)
終点	20,726,758 bp
RNA発現パターン
	さらなる参照発現データ
遺伝子オントロジー
分子機能	• トランスフェラーゼ活性; • protein kinase activity; • ヌクレオチド結合; • 金属イオン結合; • キナーゼ活性; • protein serine/threonine kinase activity; • 血漿タンパク結合; • ATP binding; • MAP kinase kinase kinase activity; • mitogen-activated protein kinase kinase binding;
細胞の構成要素	• ミトコンドリア; • 細胞質基質; • 細胞の構成要素;
生物学的プロセス	• intracellular signal transduction; • regulation of TOR signaling; • リン酸化; • negative regulation of apoptotic process; • positive regulation of peptidyl-serine phosphorylation; • MAPK cascade; • タンパク質リン酸化; • regulation of proteasomal ubiquitin-dependent protein catabolic process; • シグナル伝達; • 多細胞個体の発生; • negative regulation of signal transduction; • 細胞分化; • positive regulation of ERK1 and ERK2 cascade;
	出典:Amigo / QuickGO
オルソログ
	369
	11836
	ENSG00000078061
	ENSMUSG00000001127
	P10398,Q96II5
	P04627
	NM_001256196; NM_001256197; NM_001654
	NM_001159645; NM_009703
	NP_001243125; NP_001243126; NP_001645; NP_001243125.1
	NP_001153117; NP_033833
	ウィキデータ
閲覧/編集ヒト	閲覧/編集マウス

セリン/トレオニンタンパク質キナーゼ A-Raf（セリン/トレオニン-タンパクしつキナーゼ・エイラフ、英: Serine/threonine-protein kinase A-Raf）あるいは単純にA-Rafは、ヒトARAF遺伝子にコードされている酵素である^[5]。A-Rafはセリン/トレオニン特異的タンパク質キナーゼ（英語版）のRafキナーゼファミリーのメンバーである^[6]。

相互作用

ARAFは以下のタンパク質と相互作用することが示されている。

脚注

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000078061 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000001127 - Ensembl, May 2017
^ Human PubMed Reference:
^ Mouse PubMed Reference:
^ “Entrez Gene: ARAF V-raf murine sarcoma 3611 viral oncogene homolog”. 2012年1月26日閲覧。
^ Mark GE, Seeley TW, Shows TB, Mountz JD (September 1986). “Pks, a raf-related sequence in humans”. Proc. Natl. Acad. Sci. U.S.A. 83 (17): 6312–6. doi:10.1073/pnas.83.17.6312. PMC 386493. PMID 3529082.
^ ^a ^b ^c ^d ^e Yuryev A, Wennogle LP (February 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.
^ Yin XL, Chen S, Yan J, Hu Y, Gu JX (February 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.
^ ^a ^b ^c Yuryev A, Ono M, Goff SA, Macaluso F, Wennogle LP (July 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.
^ Yin XL, Chen S, Gu JX (February 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.

推薦文献

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.
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.
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.
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.
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.
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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000078061 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000001127 - Ensembl, May 2017

[3] Human PubMed Reference:

[4] Mouse PubMed Reference:

[entrez-5] “Entrez Gene: ARAF V-raf murine sarcoma 3611 viral oncogene homolog”. 2012年1月26日閲覧。

[pmid3529082-6] Mark GE, Seeley TW, Shows TB, Mountz JD (September 1986). “Pks, a raf-related sequence in humans”. Proc. Natl. Acad. Sci. U.S.A. 83 (17): 6312–6. doi:10.1073/pnas.83.17.6312. PMC 386493. PMID 3529082.

[pmid12620389-7] Yuryev A, Wennogle LP (February 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.

[pmid11909642-8] Yin XL, Chen S, Yan J, Hu Y, Gu JX (February 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.

[pmid10848612-9] Yuryev A, Ono M, Goff SA, Macaluso F, Wennogle LP (July 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.

[pmid11952167-10] Yin XL, Chen S, Gu JX (February 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.

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