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TRAF6 is a TRAF human protein.

The protein encoded by this gene is a member of the TNF receptor associated factor (TRAF) protein family. TRAF proteins are associated with, and mediate signal transduction from members of the TNF receptor superfamily. This protein mediates the signaling not only from the members of the TNF receptor superfamily, but also from the members of the Toll/IL-1 family. Signals from receptors such as CD40, TNFSF11/TRANCE/RANKL and IL-1 have been shown to be mediated by this protein. This protein also interacts with various protein kinases including IRAK1/IRAK, SRC and PKCzeta, which provides a link between distinct signaling pathways. This protein functions as a signal transducer in the NF-kappaB pathway that activates IkappaB kinase (IKK) in response to proinflammatory cytokines. The interaction of this protein with UBE2N/UBC13, and UBE2V1/UEV1A, which are ubiquitin conjugating enzymes catalyzing the formation of polyubiquitin chains, has been found to be required for IKK activation by this protein. Two alternatively spliced transcript variants encoding identical proteins have been reported.^[1]

Signaling pathway of toll-like receptors. Dashed grey lines represent unknown associations

Interactions[edit]

TRAF6 has been shown to interact with SDCBP,^[2] IRAK2,^[3]^[4] IRAK1,^[2]^[3]^[4]^[5]^[6]^[7]^[8]^[9]^[10] MAP3K7IP2,^[10]^[11]^[12]^[13]^[14]^[15] MAP3K7IP1,^[12]^[13]^[16] TNFRSF13B,^[17] FHL2,^[18] CD40,^[19]^[20] IKBKG,^[15]^[21] RANK,^[22]^[23]^[24]^[25]^[26] HSPB2,^[27] UBE2N,^[28] SIGIRR,^[29] TAX1BP1,^[9] ASK1,^[30]^[31]^[32] PPP4C,^[33] TNFAIP3,^[34]^[35] Sequestosome 1,^[36] MAP3K7^[10]^[11]^[12]^[13]^[16]^[32]^[37] and Ubiquitin C.^[14]^[21]^[33]^[38]^[39]

References[edit]

^ "Entrez Gene: TRAF6 TNF receptor-associated factor 6".
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^ ^a ^b Wesche, H; Gao X, Li X, Kirschning C J, Stark G R, Cao Z (July 1999). "IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family". J. Biol. Chem. (United States) 274 (27): 19403–10. doi:10.1074/jbc.274.27.19403. ISSN 0021-9258. PMID 10383454.
^ ^a ^b Muzio, M; Ni J, Feng P, Dixit V M (November 1997). "IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling". Science (United States) 278 (5343): 1612–5. doi:10.1126/science.278.5343.1612. ISSN 0036-8075. PMID 9374458.
^ Qian, Y; Commane M, Ninomiya-Tsuji J, Matsumoto K, Li X (November 2001). "IRAK-mediated translocation of TRAF6 and TAB2 in the interleukin-1-induced activation of NFkappa B". J. Biol. Chem. (United States) 276 (45): 41661–7. doi:10.1074/jbc.M102262200. ISSN 0021-9258. PMID 11518704.
^ Cao, Z; Xiong J, Takeuchi M, Kurama T, Goeddel D V (October 1996). "TRAF6 is a signal transducer for interleukin-1". Nature (ENGLAND) 383 (6599): 443–6. doi:10.1038/383443a0. ISSN 0028-0836. PMID 8837778.
^ Takatsuna, Hiroshi; Kato Hiroki, Gohda Jin, Akiyama Taishin, Moriya Ayaka, Okamoto Yoshinari, Yamagata Yuriko, Otsuka Masami, Umezawa Kazuo, Semba Kentaro, Inoue Jun-Ichiro (April 2003). "Identification of TIFA as an adapter protein that links tumor necrosis factor receptor-associated factor 6 (TRAF6) to interleukin-1 (IL-1) receptor-associated kinase-1 (IRAK-1) in IL-1 receptor signaling". J. Biol. Chem. (United States) 278 (14): 12144–50. doi:10.1074/jbc.M300720200. ISSN 0021-9258. PMID 12566447.
^ Li, Shyun; Strelow Astrid, Fontana Elizabeth J, Wesche Holger (April 2002). "IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (8): 5567–72. doi:10.1073/pnas.082100399. ISSN 0027-8424. PMC 122810. PMID 11960013.
^ ^a ^b Ling, L; Goeddel D V (August 2000). "T6BP, a TRAF6-interacting protein involved in IL-1 signaling". Proc. Natl. Acad. Sci. U.S.A. (United States) 97 (17): 9567–72. doi:10.1073/pnas.170279097. ISSN 0027-8424. PMC 16905. PMID 10920205.
^ ^a ^b ^c Takaesu, G; Ninomiya-Tsuji J, Kishida S, Li X, Stark G R, Matsumoto K (April 2001). "Interleukin-1 (IL-1) receptor-associated kinase leads to activation of TAK1 by inducing TAB2 translocation in the IL-1 signaling pathway". Mol. Cell. Biol. (United States) 21 (7): 2475–84. doi:10.1128/MCB.21.7.2475-2484.2001. ISSN 0270-7306. PMC 86880. PMID 11259596.
^ ^a ^b Ishitani, Tohru; Takaesu Giichi, Ninomiya-Tsuji Jun, Shibuya Hiroshi, Gaynor Richard B, Matsumoto Kunihiro (Dec. 2003). "Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling". EMBO J. (England) 22 (23): 6277–88. doi:10.1093/emboj/cdg605. ISSN 0261-4189. PMC 291846. PMID 14633987.
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^ ^a ^b ^c Walsh, Matthew C; Kim Gregory K, Maurizio Paul L, Molnar Elizabeth E, Choi Yongwon (2008). "TRAF6 autoubiquitination-independent activation of the NFkappaB and MAPK pathways in response to IL-1 and RANKL". In Unutmaz, Derya. PLoS ONE (United States) 3 (12): e4064. doi:10.1371/journal.pone.0004064. PMC 2603309. PMID 19112497.
^ ^a ^b Ma, Qi; Zhou Li, Shi Huili, Huo Keke (June 2008). "NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-kappaB activation". Cell. Signal. (England) 20 (6): 1044–51. doi:10.1016/j.cellsig.2008.01.015. ISSN 0898-6568. PMID 18299187.
^ ^a ^b Windheim, Mark; Stafford Margaret, Peggie Mark, Cohen Philip (March 2008). "Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptor-associated kinase 1 to facilitate NEMO binding and the activation of IkappaBalpha kinase". Mol. Cell. Biol. (United States) 28 (5): 1783–91. doi:10.1128/MCB.02380-06. PMC 2258775. PMID 18180283.
^ ^a ^b Ninomiya-Tsuji, J; Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K (March 1999). "The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway". Nature (ENGLAND) 398 (6724): 252–6. doi:10.1038/18465. ISSN 0028-0836. PMID 10094049.
^ Xia, X Z; Treanor J, Senaldi G, Khare S D, Boone T, Kelley M, Theill L E, Colombero A, Solovyev I, Lee F, McCabe S, Elliott R, Miner K, Hawkins N, Guo J, Stolina M, Yu G, Wang J, Delaney J, Meng S Y, Boyle W J, Hsu H (July 2000). "TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation". J. Exp. Med. (United States) 192 (1): 137–43. doi:10.1084/jem.192.1.137. ISSN 0022-1007. PMC 1887716. PMID 10880535.
^ Bai, Shuting; Zha Jikun, Zhao Haibo, Ross F Patrick, Teitelbaum Steven L (November 2008). "Tumor necrosis factor receptor-associated factor 6 is an intranuclear transcriptional coactivator in osteoclasts". J. Biol. Chem. (United States) 283 (45): 30861–7. doi:10.1074/jbc.M802525200. ISSN 0021-9258. PMC 2662164. PMID 18768464.
^ Tsukamoto, N; Kobayashi N, Azuma S, Yamamoto T, Inoue J (February 1999). "Two differently regulated nuclear factor kappaB activation pathways triggered by the cytoplasmic tail of CD40". Proc. Natl. Acad. Sci. U.S.A. (United States) 96 (4): 1234–9. doi:10.1073/pnas.96.4.1234. ISSN 0027-8424. PMC 15446. PMID 9990007.
^ Roy, N; Deveraux Q L, Takahashi R, Salvesen G S, Reed J C (Dec. 1997). "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". EMBO J. (ENGLAND) 16 (23): 6914–25. doi:10.1093/emboj/16.23.6914. ISSN 0261-4189. PMC 1170295. PMID 9384571.
^ ^a ^b Lamothe, Betty; Campos Alejandro D, Webster William K, Gopinathan Ambily, Hur Lana, Darnay Bryant G (September 2008). "The RING domain and first zinc finger of TRAF6 coordinate signaling by interleukin-1, lipopolysaccharide, and RANKL". J. Biol. Chem. (United States) 283 (36): 24871–80. doi:10.1074/jbc.M802749200. ISSN 0021-9258. PMC 2529010. PMID 18617513.
^ Mizukami, Junko; Takaesu Giichi, Akatsuka Hiroyuki, Sakurai Hiroaki, Ninomiya-Tsuji Jun, Matsumoto Kunihiro, Sakurai Naoki (February 2002). "Receptor activator of NF-kappaB ligand (RANKL) activates TAK1 mitogen-activated protein kinase kinase kinase through a signaling complex containing RANK, TAB2, and TRAF6". Mol. Cell. Biol. (United States) 22 (4): 992–1000. doi:10.1128/MCB.22.4.992-1000.2002. ISSN 0270-7306. PMC 134634. PMID 11809792.
^ Darnay, B G; Haridas V, Ni J, Moore P A, Aggarwal B B (August 1998). "Characterization of the intracellular domain of receptor activator of NF-kappaB (RANK). Interaction with tumor necrosis factor receptor-associated factors and activation of NF-kappab and c-Jun N-terminal kinase". J. Biol. Chem. (United States) 273 (32): 20551–5. doi:10.1074/jbc.273.32.20551. ISSN 0021-9258. PMID 9685412.
^ Darnay, B G; Ni J, Moore P A, Aggarwal B B (March 1999). "Activation of NF-kappaB by RANK requires tumor necrosis factor receptor-associated factor (TRAF) 6 and NF-kappaB-inducing kinase. Identification of a novel TRAF6 interaction motif". J. Biol. Chem. (United States) 274 (12): 7724–31. doi:10.1074/jbc.274.12.7724. ISSN 0021-9258. PMID 10075662.
^ Galibert, L; Tometsko M E, Anderson D M, Cosman D, Dougall W C (Dec. 1998). "The involvement of multiple tumor necrosis factor receptor (TNFR)-associated factors in the signaling mechanisms of receptor activator of NF-kappaB, a member of the TNFR superfamily". J. Biol. Chem. (United States) 273 (51): 34120–7. doi:10.1074/jbc.273.51.34120. ISSN 0021-9258. PMID 9852070.
^ Kim, H H; Lee D E, Shin J N, Lee Y S, Jeon Y M, Chung C H, Ni J, Kwon B S, Lee Z H (January 1999). "Receptor activator of NF-kappaB recruits multiple TRAF family adaptors and activates c-Jun N-terminal kinase". FEBS Lett. (NETHERLANDS) 443 (3): 297–302. doi:10.1016/S0014-5793(98)01731-1. ISSN 0014-5793. PMID 10025951.
^ Wu, Yifan; Liu Junhong, Zhang Zhengping, Huang Huang, Shen Jiayin, Zhang Shuangquan, Jiang Yong, Luo Lan, Yin Zhimin (January 2009). "HSP27 regulates IL-1 stimulated IKK activation through interacting with TRAF6 and affecting its ubiquitination". Cell. Signal. (England) 21 (1): 143–50. doi:10.1016/j.cellsig.2008.10.001. PMID 18950704.
^ Deng, L; Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen Z J (October 2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell (United States) 103 (2): 351–61. doi:10.1016/S0092-8674(00)00126-4. ISSN 0092-8674. PMID 11057907.
^ Wald, David; Qin Jinzhong, Zhao Zhendong, Qian Youcun, Naramura Mayumi, Tian Liping, Towne Jennifer, Sims John E, Stark George R, Li Xiaoxia (September 2003). "SIGIRR, a negative regulator of Toll-like receptor-interleukin 1 receptor signaling". Nat. Immunol. (United States) 4 (9): 920–7. doi:10.1038/ni968. ISSN 1529-2908. PMID 12925853.
^ Nishitoh, H; Saitoh M, Mochida Y, Takeda K, Nakano H, Rothe M, Miyazono K, Ichijo H (September 1998). "ASK1 is essential for JNK/SAPK activation by TRAF2". Mol. Cell (United States) 2 (3): 389–95. doi:10.1016/S1097-2765(00)80283-X. ISSN 1097-2765. PMID 9774977.
^ Hoeflich, K P; Yeh W C, Yao Z, Mak T W, Woodgett J R (October 1999). "Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1)". Oncogene (ENGLAND) 18 (42): 5814–20. doi:10.1038/sj.onc.1202975. ISSN 0950-9232. PMID 10523862.
^ ^a ^b Mochida, Y; Takeda K, Saitoh M, Nishitoh H, Amagasa T, Ninomiya-Tsuji J, Matsumoto K, Ichijo H (October 2000). "ASK1 inhibits interleukin-1-induced NF-kappa B activity through disruption of TRAF6-TAK1 interaction". J. Biol. Chem. (United States) 275 (42): 32747–52. doi:10.1074/jbc.M003042200. ISSN 0021-9258. PMID 10921914.
^ ^a ^b Chen, Lu; Dong Wei, Zou Tingting, Ouyang Lu, He Guoqing, Liu Yingle, Qi Yipeng (August 2008). "Protein phosphatase 4 negatively regulates LPS cascade by inhibiting ubiquitination of TRAF6". FEBS Lett. (Netherlands) 582 (19): 2843–9. doi:10.1016/j.febslet.2008.07.014. ISSN 0014-5793. PMID 18634786.
^ Heyninck, K; Beyaert R (January 1999). "The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-kappaB activation at the level of TRAF6". FEBS Lett. (NETHERLANDS) 442 (2–3): 147–50. doi:10.1016/S0014-5793(98)01645-7. ISSN 0014-5793. PMID 9928991.
^ Evans, P C; Taylor E R, Coadwell J, Heyninck K, Beyaert R, Kilshaw P J (August 2001). "Isolation and characterization of two novel A20-like proteins". Biochem. J. (England) 357 (Pt 3): 617–23. doi:10.1042/0264-6021:3570617. ISSN 0264-6021. PMC 1221992. PMID 11463333.
^ Sanz, L; Diaz-Meco M T, Nakano H, Moscat J (April 2000). "The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway". EMBO J. (ENGLAND) 19 (7): 1576–86. doi:10.1093/emboj/19.7.1576. ISSN 0261-4189. PMC 310227. PMID 10747026.
^ Sorrentino, Alessandro; Thakur Noopur, Grimsby Susanne, Marcusson Anders, von Bulow Verena, Schuster Norbert, Zhang Shouting, Heldin Carl-Henrik, Landström Maréne (October 2008). "The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner". Nat. Cell Biol. (England) 10 (10): 1199–207. doi:10.1038/ncb1780. PMID 18758450.
^ Newton, Kim; Matsumoto Marissa L, Wertz Ingrid E, Kirkpatrick Donald S, Lill Jennie R, Tan Jenille, Dugger Debra, Gordon Nathaniel, Sidhu Sachdev S, Fellouse Frederic A, Komuves Laszlo, French Dorothy M, Ferrando Ronald E, Lam Cynthia, Compaan Deanne, Yu Christine, Bosanac Ivan, Hymowitz Sarah G, Kelley Robert F, Dixit Vishva M (August 2008). "Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies". Cell (United States) 134 (4): 668–78. doi:10.1016/j.cell.2008.07.039. PMID 18724939.
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External links[edit]

TRAF6 at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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1. エプスタインバーウイルス（EBウイルス）のウイルス学 virology of epstein barr virus
2. 原発性縦隔大細胞型B細胞リンパ腫 primary mediastinal large b cell lymphoma
3. Toll様受容体：疾患および治療における役割 toll like receptors roles in disease and therapy
4. びまん性大細胞型B細胞性リンパ腫および原発性縦隔大細胞型B細胞リンパ腫の病理学 pathobiology of diffuse large b cell lymphoma and primary mediastinal large b cell lymphoma
5. 高IgM症候群 hyperimmunoglobulin m syndromes

English Journal

EGb761 inhibits inflammatory responses in human chondrocytes and shows chondroprotection in osteoarthritic rat knee.

Chen YJ, Tsai KS, Chiu CY, Yang TH, Lin TH, Fu WM, Chen CF, Yang RS, Liu SH.SourceInstitute of Toxicology, College of Medicine, National Taiwan University, Taipei, Taiwan.
Journal of orthopaedic research : official publication of the Orthopaedic Research Society.J Orthop Res.2013 Jul;31(7):1032-8. doi: 10.1002/jor.22339. Epub 2013 Mar 11.
Osteoarthritis (OA) is a degenerative joint disease involving a combination of cartilage degradation and inflammation. EGb761, a standardized extract of Ginkgo biloba leaves, holds an anti-inflammatory potency. Here, we determined whether EGb761 could inhibit lipopolysaccharide (LPS)- and IL-1β-ind
PMID 23483610

Cezanne paints inflammation by regulating ubiquitination.

Abe J, Berk BC.SourceFrom the Aab Cardiovascular Research Institute, University of Rochester, Rochester, NY.
Circulation research.Circ Res.2013 Jun 7;112(12):1526-8. doi: 10.1161/CIRCRESAHA.113.301518.
PMID 23743222
PMID 23564640

Japanese Journal

Expression of TRAF6 Protein and TRAF6 mRNA during Different Stages of Deciduous Tooth Root Physiological Absorption

Zhang Guirong,Zhou Linxi,Ito Koji [他]
Journal of hard tissue biology 22(1), 1-6, 2013-01
NAID 40019635202

ヒトB細胞活性化におけるSykを介したTLR9シグナルの増幅メカニズム (特集 B細胞の機能発現とその制御分子)

岩田慈,山岡邦宏,田中良哉
臨床免疫・アレルギー科 57(5), 513-517, 2012-05
NAID 40019337340

レギュラトリーT細胞とTRAF6 (特集レギュラトリーT細胞の分化と機能発現)

秋山泰身,新澤美穂,秋山伸子
臨床免疫・アレルギー科 57(4), 377-383, 2012-04
NAID 40019309698

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★リンクテーブル★

リンク元	「トール様受容体」「IL-1」「TNF受容体関連因子6」「TNF receptor-associated factor 6」
関連記事	「TRAF」

「トール様受容体」

TNF receptor-associated factor 6, E3 ubiquitin protein ligase
	; PDB rendering based on 1lb4.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1LB4, 1LB5, 1LB6, 2ECI, 2JMD, 3HCS, 3HCT, 3HCU
Identifiers
Symbols	TRAF6; MGC:3310; RNF85
External IDs	OMIM: 602355 MGI: 108072 HomoloGene: 3395 GeneCards: TRAF6 Gene
Gene Ontology
Molecular function	• ubiquitin-protein ligase activity; • signal transducer activity; • protein binding; • zinc ion binding; • protein kinase binding; • mitogen-activated protein kinase kinase kinase binding; • ubiquitin protein ligase binding; • thioesterase binding; • histone deacetylase binding; • protein kinase B binding; • protein N-terminus binding;
Cellular component	• nucleus; • nucleolus; • cytoplasm; • lipid particle; • cytosol; • plasma membrane; • cell cortex; • internal side of plasma membrane; • endosome membrane; • nuclear membrane; • CD40 receptor complex; • perinuclear region of cytoplasm;
Biological process	• negative regulation of transcription from RNA polymerase II promoter; • activation of MAPK activity; • protein polyubiquitination; • ossification; • neural tube closure; • toll-like receptor signaling pathway; • positive regulation of T cell cytokine production; • MyD88-dependent toll-like receptor signaling pathway; • MyD88-independent toll-like receptor signaling pathway; • protein complex assembly; • apoptotic process; • I-kappaB kinase/NF-kappaB cascade; • activation of NF-kappaB-inducing kinase activity; • JNK cascade; • antigen processing and presentation of exogenous peptide antigen via MHC class II; • osteoclast differentiation; • membrane protein intracellular domain proteolysis; • positive regulation of protein ubiquitination; • positive regulation of lipopolysaccharide-mediated signaling pathway; • activation of protein kinase activity; • positive regulation of interleukin-2 production; • toll-like receptor 2 signaling pathway; • toll-like receptor 3 signaling pathway; • toll-like receptor 4 signaling pathway; • toll-like receptor 5 signaling pathway; • toll-like receptor 9 signaling pathway; • toll-like receptor 10 signaling pathway; • TRIF-dependent toll-like receptor signaling pathway; • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; • toll-like receptor TLR1:TLR2 signaling pathway; • toll-like receptor TLR6:TLR2 signaling pathway; • T-helper 1 type immune response; • positive regulation of T cell proliferation; • odontogenesis of dentin-containing tooth; • myeloid dendritic cell differentiation; • negative regulation of apoptotic process; • positive regulation of I-kappaB kinase/NF-kappaB cascade; • positive regulation of JUN kinase activity; • positive regulation of interleukin-12 biosynthetic process; • innate immune response; • positive regulation of interleukin-6 biosynthetic process; • bone resorption; • positive regulation of osteoclast differentiation; • negative regulation of transcription, DNA-dependent; • positive regulation of transcription from RNA polymerase II promoter; • neurotrophin TRK receptor signaling pathway; • cell development; • positive regulation of smooth muscle cell proliferation; • T cell receptor signaling pathway; • positive regulation of T cell activation; • regulation of immunoglobulin secretion; • positive regulation of sequence-specific DNA binding transcription factor activity; • positive regulation of NF-kappaB transcription factor activity; • stress-activated MAPK cascade; • protein autoubiquitination; • nucleotide-binding oligomerization domain containing signaling pathway; • interleukin-1-mediated signaling pathway; • protein K63-linked ubiquitination; • response to interleukin-1; • apoptotic signaling pathway; • positive regulation of transcription regulatory region DNA binding;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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