関: TRAF6

WordNet

having partial rights and privileges or subordinate status; "an associate member"; "an associate professor"
a person who joins with others in some activity or endeavor; "he had to consult his associate before continuing"
a person with subordinate membership in a society, institution, or commercial enterprise; "associates in the law firm bill at a lower rate than do partners"
any event that usually accompanies or is closely connected with another; "first was the lightning and then its thunderous associate"
make a logical or causal connection; "I cannot connect these two pieces of evidence in my mind"; "colligate these facts"; "I cannot relate these events at all" (同)tie_in, relate, link, colligate, link up, connect
be a contributing factor; "make things factor into a companys profitability"
any of the numbers (or symbols) that form a product when multiplied together
an independent variable in statistics
anything that contributes causally to a result; "a number of factors determined the outcome"
consider as relevant when making a decision; "You must factor in the recent developments" (同)factor in, factor out
resolve into factors; "a quantum computer can factor the number 15" (同)factor in, factor out
an event known to have happened or something known to have existed; "your fears have no basis in fact"; "how much of the story is fact and how much fiction is hard to tell"
a concept whose truth can be proved; "scientific hypotheses are not facts"
a piece of information about circumstances that exist or events that have occurred; "first you must collect all the facts of the case"
a statement or assertion of verified information about something that is the case or has happened; "he supported his argument with an impressive array of facts"
the 20th letter of the Roman alphabet (同)t
a cellular structure that is postulated to exist in order to mediate between a chemical agent that acts on nervous tissue and the physiological response

PrepTutorEJDIC

〈人〉'を'(…の)『仲間に加える』,(…に)連合させる《+『名』〈人〉+『with』+『名』》 / (…と)…'を'結びつけて考える(起こす)《+『名』+『with』+『名』》 / (…と)『仲間になる』,交際する《+『with』+『名』》 / (…と)合体する,提携する《+『with』+『名』》 / 『仲間』,『同僚』;組合員 / 準会員 / 付属物;連想されるもの / 連合した;仲間の,同僚の / 補助の,準…
(…の)『要因』,(…を生み出す)要素《+『in』+『名』(do『ing』)》 / 囲数,約数 / 代理人,《おもに英》仲買人 / =factorize
〈C〉『事実』,実際にある(あった)事 / 〈U〉真相,真実(truth) / 《the~》(法律用語で)犯行
tritiumの化学記号
=sense organ / 受信装置

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/07/15 04:13:01」(JST)

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TRAF6 is a TRAF human protein.

Function

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

TRAF6 has been shown to interact with:

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

Model organisms

Model organisms have been used in the study of TRAF6 function. A conditional knockout mouse line called Traf6^{tm2a(EUCOMM)Wtsi} was generated at the Wellcome Trust Sanger Institute.^[40] Male and female animals underwent a standardized phenotypic screen^[41] to determine the effects of deletion.^[42]^[43]^[44]^[45] Additional screens performed: - In-depth immunological phenotyping^[46]

*Traf6* knockout mouse phenotype
Characteristic	Phenotype
All data available at.^[41]^[46]
Peripheral blood leukocytes 6 Weeks	Normal
Insulin	Normal
Haematology 6 Weeks	Normal
Homozygous viability at P14	Abnormal
Recessive lethal study	Abnormal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Salmonella infection	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Epidermal Immune Composition	Normal

References

^ "Entrez Gene: TRAF6 TNF receptor-associated factor 6".
^ Nishitoh H, Saitoh M, Mochida Y, Takeda K, Nakano H, Rothe M et al. (September 1998). "ASK1 is essential for JNK/SAPK activation by TRAF2". Mol. Cell 2 (3): 389–95. doi:10.1016/s1097-2765(00)80283-x. PMID 9774977.
^ Hoeflich KP, Yeh WC, Yao Z, Mak TW, Woodgett JR (October 1999). "Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1)". Oncogene 18 (42): 5814–20. doi:10.1038/sj.onc.1202975. PMID 10523862.
^ ^a ^b Mochida Y, Takeda K, Saitoh M, Nishitoh H, Amagasa T, Ninomiya-Tsuji J et al. (October 2000). "ASK1 inhibits interleukin-1-induced NF-kappa B activity through disruption of TRAF6-TAK1 interaction". J. Biol. Chem. 275 (42): 32747–52. doi:10.1074/jbc.M003042200. PMID 10921914.
^ 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. 96 (4): 1234–9. doi:10.1073/pnas.96.4.1234. PMC 15446. PMID 9990007.
^ Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC (Dec 1997). "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". EMBO J. 16 (23): 6914–25. doi:10.1093/emboj/16.23.6914. PMC 1170295. PMID 9384571.
^ Bai S, Zha J, Zhao H, Ross FP, Teitelbaum SL (November 2008). "Tumor necrosis factor receptor-associated factor 6 is an intranuclear transcriptional coactivator in osteoclasts". J. Biol. Chem. 283 (45): 30861–7. doi:10.1074/jbc.M802525200. PMC 2662164. PMID 18768464.
^ Wu Y, Liu J, Zhang Z, Huang H, Shen J, Zhang S et al. (January 2009). "HSP27 regulates IL-1 stimulated IKK activation through interacting with TRAF6 and affecting its ubiquitination". Cell. Signal. 21 (1): 143–50. doi:10.1016/j.cellsig.2008.10.001. PMID 18950704.
^ ^a ^b Windheim M, Stafford M, Peggie M, Cohen P (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. 28 (5): 1783–91. doi:10.1128/MCB.02380-06. PMC 2258775. PMID 18180283.
^ ^a ^b Lamothe B, Campos AD, Webster WK, Gopinathan A, Hur L, Darnay BG (September 2008). "The RING domain and first zinc finger of TRAF6 coordinate signaling by interleukin-1, lipopolysaccharide, and RANKL". J. Biol. Chem. 283 (36): 24871–80. doi:10.1074/jbc.M802749200. PMC 2529010. PMID 18617513.
^ ^a ^b Chen F, Du Y, Zhang Z, Chen G, Zhang M, Shu HB et al. (April 2008). "Syntenin negatively regulates TRAF6-mediated IL-1R/TLR4 signaling". Cell. Signal. 20 (4): 666–74. doi:10.1016/j.cellsig.2007.12.002. PMID 18234474.
^ ^a ^b Wesche H, Gao X, Li X, Kirschning CJ, Stark GR, Cao Z (July 1999). "IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family". J. Biol. Chem. 274 (27): 19403–10. doi:10.1074/jbc.274.27.19403. PMID 10383454.
^ ^a ^b Muzio M, Ni J, Feng P, Dixit VM (November 1997). "IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling". Science 278 (5343): 1612–5. doi:10.1126/science.278.5343.1612. 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. 276 (45): 41661–7. doi:10.1074/jbc.M102262200. PMID 11518704.
^ Cao Z, Xiong J, Takeuchi M, Kurama T, Goeddel DV (October 1996). "TRAF6 is a signal transducer for interleukin-1". Nature 383 (6599): 443–6. doi:10.1038/383443a0. PMID 8837778.
^ Takatsuna H, Kato H, Gohda J, Akiyama T, Moriya A, Okamoto Y et al. (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. 278 (14): 12144–50. doi:10.1074/jbc.M300720200. PMID 12566447.
^ Li S, Strelow A, Fontana EJ, Wesche H (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. 99 (8): 5567–72. doi:10.1073/pnas.082100399. PMC 122810. PMID 11960013.
^ ^a ^b Ling L, Goeddel DV (August 2000). "T6BP, a TRAF6-interacting protein involved in IL-1 signaling". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9567–72. doi:10.1073/pnas.170279097. PMC 16905. PMID 10920205.
^ ^a ^b ^c Takaesu G, Ninomiya-Tsuji J, Kishida S, Li X, Stark GR, 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. 21 (7): 2475–84. doi:10.1128/MCB.21.7.2475-2484.2001. PMC 86880. PMID 11259596.
^ ^a ^b ^c Takaesu G, Kishida S, Hiyama A, Yamaguchi K, Shibuya H, Irie K et al. (April 2000). "TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway". Mol. Cell 5 (4): 649–58. doi:10.1016/s1097-2765(00)80244-0. PMID 10882101.
^ ^a ^b ^c Walsh MC, Kim GK, Maurizio PL, Molnar EE, Choi Y. Unutmaz D, ed. "TRAF6 autoubiquitination-independent activation of the NFkappaB and MAPK pathways in response to IL-1 and RANKL". PLoS ONE 3 (12): e4064. doi:10.1371/journal.pone.0004064. PMC 2603309. PMID 19112497.
^ ^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 398 (6724): 252–6. doi:10.1038/18465. PMID 10094049.
^ ^a ^b Ishitani T, Takaesu G, Ninomiya-Tsuji J, Shibuya H, Gaynor RB, Matsumoto K (Dec 2003). "Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling". EMBO J. 22 (23): 6277–88. doi:10.1093/emboj/cdg605. PMC 291846. PMID 14633987.
^ ^a ^b Ma Q, Zhou L, Shi H, Huo K (June 2008). "NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-kappaB activation". Cell. Signal. 20 (6): 1044–51. doi:10.1016/j.cellsig.2008.01.015. PMID 18299187.
^ Sorrentino A, Thakur N, Grimsby S, Marcusson A, von Bulow V, Schuster N et al. (October 2008). "The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner". Nat. Cell Biol. 10 (10): 1199–207. doi:10.1038/ncb1780. PMID 18758450.
^ ^a ^b Chen L, Dong W, Zou T, Ouyang L, He G, Liu Y et al. (August 2008). "Protein phosphatase 4 negatively regulates LPS cascade by inhibiting ubiquitination of TRAF6". FEBS Lett. 582 (19): 2843–9. doi:10.1016/j.febslet.2008.07.014. PMID 18634786.
^ Mizukami J, Takaesu G, Akatsuka H, Sakurai H, Ninomiya-Tsuji J, Matsumoto K et al. (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. 22 (4): 992–1000. doi:10.1128/mcb.22.4.992-1000.2002. PMC 134634. PMID 11809792.
^ Darnay BG, Haridas V, Ni J, Moore PA, Aggarwal BB (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. 273 (32): 20551–5. doi:10.1074/jbc.273.32.20551. PMID 9685412.
^ Darnay BG, Ni J, Moore PA, Aggarwal BB (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. 274 (12): 7724–31. doi:10.1074/jbc.274.12.7724. PMID 10075662.
^ Galibert L, Tometsko ME, Anderson DM, Cosman D, Dougall WC (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. 273 (51): 34120–7. doi:10.1074/jbc.273.51.34120. PMID 9852070.
^ Kim HH, Lee DE, Shin JN, Lee YS, Jeon YM, Chung CH et al. (January 1999). "Receptor activator of NF-kappaB recruits multiple TRAF family adaptors and activates c-Jun N-terminal kinase". FEBS Lett. 443 (3): 297–302. doi:10.1016/s0014-5793(98)01731-1. PMID 10025951.
^ Wald D, Qin J, Zhao Z, Qian Y, Naramura M, Tian L et al. (September 2003). "SIGIRR, a negative regulator of Toll-like receptor-interleukin 1 receptor signaling". Nat. Immunol. 4 (9): 920–7. doi:10.1038/ni968. PMID 12925853.
^ Sanz L, Diaz-Meco MT, Nakano H, Moscat J (April 2000). "The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway". EMBO J. 19 (7): 1576–86. doi:10.1093/emboj/19.7.1576. PMC 310227. PMID 10747026.
^ 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. 442 (2-3): 147–50. doi:10.1016/s0014-5793(98)01645-7. PMID 9928991.
^ Evans PC, Taylor ER, Coadwell J, Heyninck K, Beyaert R, Kilshaw PJ (August 2001). "Isolation and characterization of two novel A20-like proteins". Biochem. J. 357 (Pt 3): 617–23. doi:10.1042/0264-6021:3570617. PMC 1221992. PMID 11463333.
^ Xia XZ, Treanor J, Senaldi G, Khare SD, Boone T, Kelley M et al. (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. 192 (1): 137–43. doi:10.1084/jem.192.1.137. PMC 1887716. PMID 10880535.
^ Deng L, Wang C, Spencer E, Yang L, Braun A, You J et al. (October 2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell 103 (2): 351–61. doi:10.1016/s0092-8674(00)00126-4. PMID 11057907.
^ Newton K, Matsumoto ML, Wertz IE, Kirkpatrick DS, Lill JR, Tan J et al. (August 2008). "Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies". Cell 134 (4): 668–78. doi:10.1016/j.cell.2008.07.039. PMID 18724939.
^ Conze DB, Wu CJ, Thomas JA, Landstrom A, Ashwell JD (May 2008). "Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kappaB activation". Mol. Cell. Biol. 28 (10): 3538–47. doi:10.1128/MCB.02098-07. PMC 2423148. PMID 18347055.
^ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Opthalmologica 88: 925-7.doi:10.1111/j.1755-3768.2010.4142.x: Wiley.
^ ^a ^b "International Mouse Phenotyping Consortium".
^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V et al. (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337â€“42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
^ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
^ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell 128 (1): 9â€“13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
^ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN et al. (2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMID 23870131.
^ ^a ^b "Infection and Immunity Immunophenotyping (3i) Consortium".

External links

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

UpToDate Contents

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1. 腫瘍壊死因子受容体-1関連周期性発熱症候群（TRAPS） tumor necrosis factor receptor 1 associated periodic syndrome traps
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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

MicroRNA-146 inhibits pro-inflammatory cytokine secretion through IL-1 receptor-associated kinase 1 in human gingival fibroblasts.

Xie YF, Shu R, Jiang SY, Liu DL, Ni J, Zhang XL.SourceDepartment of Periodontology, Ninth People's Hospital, School of Medicine Shanghai Jiao Tong University, Shanghai Key Laboratory of Stomatology, 639 Zhi Zao Ju Road, Shanghai 200011, China. shurong123@hotmail.com.
Journal of inflammation (London, England).J Inflamm (Lond).2013 May 16;10(1):20. doi: 10.1186/1476-9255-10-20.
BACKGROUND: Although various microRNAs (miRNAs) regulate immune and inflammatory responses, the function of miRNAs in periodontitis has not been clearly illuminated. In this study, we measured miRNA-146 (miRNA-146a and miRNA-146b-5p) expression and explored its regulatory function in the inflammator
PMID 23680172

Herpes simplex virus US3 tegument protein inhibits Toll-like receptor 2 signaling at or before TRAF6 ubiquitination.

Sen J, Liu X, Roller R, Knipe DM.SourceDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, USA.
Virology.Virology.2013 May 10;439(2):65-73. doi: 10.1016/j.virol.2013.01.026. Epub 2013 Mar 7.
Herpes simplex virus (HSV) has evolved multiple strategies to modulate host immune responses. In a screen of HSV open reading frames to identify additional HSV-encoded proteins that affect NF-κB signaling, we identified the viral US3 tegument protein as an inhibitor of NF-κB signaling. We found th
PMID 23478027

Japanese Journal

Titanium Surface Roughness Accelerates RANKL-dependent Differentiation in the Osteoclast Precursor Cell Line, RAW264.7

MAKIHIRA Seicho,MINE Yuichi,KOSAKA Eduardo,NIKAWA Hiroki
Dental materials journal 26(5), 739-745, 2007-09
… Total RNA was extracted from cells cultured in the presence or absence of Receptor Activator of NF-κB Ligand (RANKL), prior to cDNA synthesis for real-time quantitative reverse transcriptase-polymerase chain reaction analysis. …
NAID 110006402837

TNF receptor-associated factor(TRAF)2依存性のNF-κBのcanonical経路はパイエル板の形成に必須である(アトピー疾患研究センター遺伝子解析モデル部門,一般演題(口頭発表),平成18年度順天堂大学大学院疾患モデル研究センター利用者研究発表会抄録)

朴将虎,中野裕康,奥村康
順天堂医学 53(2), 316, 2007-06
NAID 110007124885

「TRAF6」

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 transferase activity; • tumor necrosis factor receptor binding; • protein binding; • zinc ion binding; • ligase activity; • protein kinase binding; • mitogen-activated protein kinase kinase kinase binding; • ubiquitin conjugating enzyme binding; • ubiquitin protein ligase binding; • thioesterase binding; • identical protein binding; • histone deacetylase binding; • protein kinase B binding; • protein N-terminus binding; • ubiquitin protein ligase activity;
Cellular component	• nucleus; • nucleolus; • cytoplasm; • mitochondrion; • lipid particle; • cytosol; • plasma membrane; • cell cortex; • cytoplasmic side of plasma membrane; • endosome membrane; • CD40 receptor complex; • protein 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; • stimulatory C-type lectin receptor signaling pathway; • 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; • I-kappaB kinase/NF-kappaB signaling; • 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; • Fc-epsilon 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; • positive regulation of apoptotic process; • negative regulation of apoptotic process; • positive regulation of I-kappaB kinase/NF-kappaB signaling; • 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-templated; • 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; • cellular response to lipopolysaccharide; • apoptotic signaling pathway; • positive regulation of transcription regulatory region DNA binding;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;