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TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)

 TRAF6_HUMAN             Reviewed;         522 AA.
Q9Y4K3; A6NKI7; A8KAB3; D3DR16; Q8NEH5;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
02-JUN-2021, entry version 231.
RecName: Full=TNF receptor-associated factor 6;
EC=2.3.2.27;
AltName: Full=E3 ubiquitin-protein ligase TRAF6;
AltName: Full=Interleukin-1 signal transducer;
AltName: Full=RING finger protein 85;
AltName: Full=RING-type E3 ubiquitin transferase TRAF6 {ECO:0000305};
Name=TRAF6; Synonyms=RNF85;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH IRAK1.
PubMed=8837778; DOI=10.1038/383443a0;
Cao Z., Xiong J., Takeuchi M., Kurama T., Goeddel D.V.;
"TRAF6 is a signal transducer for interleukin-1.";
Nature 383:443-446(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
Hattori M., Rogers J., Lander E.S., Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH MAP3K14.
PubMed=9020361; DOI=10.1038/385540a0;
Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D.;
"MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-
1.";
Nature 385:540-544(1997).
[8]
INTERACTION WITH IRAK2.
PubMed=9374458; DOI=10.1126/science.278.5343.1612;
Muzio M., Ni J., Feng P., Dixit V.M.;
"IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1
signaling.";
Science 278:1612-1615(1997).
[9]
INTERACTION WITH RIPK2.
PubMed=9642260; DOI=10.1074/jbc.273.27.16968;
McCarthy J.V., Ni J., Dixit V.M.;
"RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase.";
J. Biol. Chem. 273:16968-16975(1998).
[10]
INTERACTION WITH TNFRSF11A.
PubMed=9774460; DOI=10.1074/jbc.273.43.28355;
Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.;
"The TRAF family of signal transducers mediates NF-kappaB activation by the
TRANCE receptor.";
J. Biol. Chem. 273:28355-28359(1998).
[11]
INTERACTION WITH TNFRSF5.
PubMed=9432981; DOI=10.1084/jem.187.2.237;
Kashiwada M., Shirakata Y., Inoue J., Nakano H., Okazaki K., Okumura K.,
Yamamoto T., Nagaoka H., Takemori T.;
"Tumor necrosis factor receptor-associated factor 6 (TRAF6) stimulates
extracellular signal-regulated kinase (ERK) activity in CD40 signaling
along a ras-independent pathway.";
J. Exp. Med. 187:237-244(1998).
[12]
INTERACTION WITH MAP3K5.
PubMed=9774977; DOI=10.1016/s1097-2765(00)80283-x;
Nishitoh H., Saitoh M., Mochida Y., Takeda K., Nakano H., Rothe M.,
Miyazono K., Ichijo H.;
"ASK1 is essential for JNK/SAPK activation by TRAF2.";
Mol. Cell 2:389-395(1998).
[13]
INTERACTION WITH MAP3K1.
PubMed=10346818; DOI=10.1101/gad.13.10.1297;
Baud V., Liu Z.-G., Bennett B., Suzuki N., Xia Y., Karin M.;
"Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6
is sufficient for JNK and IKK activation and target gene induction via an
amino-terminal effector domain.";
Genes Dev. 13:1297-1308(1999).
[14]
INTERACTION WITH NGFR.
PubMed=9915784; DOI=10.1074/jbc.274.5.2597;
Khursigara G., Orlinick J.R., Chao M.V.;
"Association of the p75 neurotrophin receptor with TRAF6.";
J. Biol. Chem. 274:2597-2600(1999).
[15]
INTERACTION WITH IRAK3.
PubMed=10383454; DOI=10.1074/jbc.274.27.19403;
Wesche H., Gao X., Li X., Kirschning C.J., Stark G.R., Cao Z.;
"IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated
kinase (IRAK) family.";
J. Biol. Chem. 274:19403-19410(1999).
[16]
INTERACTION WITH NGFR.
PubMed=10514511; DOI=10.1074/jbc.274.42.30202;
Ye X., Mehlen P., Rabizadeh S., VanArsdale T., Zhang H., Shin H.,
Wang J.J.L., Leo E., Zapata J.M., Hauser C.A., Reed J.C., Bredesen D.E.;
"TRAF family proteins interact with the common neurotrophin receptor and
modulate apoptosis induction.";
J. Biol. Chem. 274:30202-30208(1999).
[17]
INTERACTION WITH TNFRSF11A AND CSK.
PubMed=10635328; DOI=10.1016/s1097-2765(00)80232-4;
Wong B.R., Besser D., Kim N., Arron J.R., Vologodskaia M., Hanafusa H.,
Choi Y.;
"TRANCE, a TNF family member, activates Akt/PKB through a signaling complex
involving TRAF6 and c-Src.";
Mol. Cell 4:1041-1049(1999).
[18]
INTERACTION WITH MAP3K7 AND TAB1.
PubMed=10094049; DOI=10.1038/18465;
Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K.;
"The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase
cascade in the IL-1 signalling pathway.";
Nature 398:252-256(1999).
[19]
INTERACTION WITH MAP3K5.
PubMed=10523862; DOI=10.1038/sj.onc.1202975;
Hoeflich K.P., Yeh W.C., Yao Z., Mak T.W., Woodgett J.R.;
"Mediation of TNF receptor-associated factor effector functions by
apoptosis signal-regulating kinase-1 (ASK1).";
Oncogene 18:5814-5820(1999).
[20]
INTERACTION WITH UBE2V1, AND FUNCTION AS AN E3 UBIQUITIN LIGASE.
PubMed=11057907; DOI=10.1016/s0092-8674(00)00126-4;
Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C.,
Pickart C., Chen Z.J.;
"Activation of the IkappaB kinase complex by TRAF6 requires a dimeric
ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain.";
Cell 103:351-361(2000).
[21]
INTERACTION WITH TDP2.
PubMed=10764746; DOI=10.1074/jbc.m000531200;
Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I.,
Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.;
"TTRAP, a novel protein that associates with CD40, tumor necrosis factor
(TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that
inhibits nuclear factor-kappa B activation.";
J. Biol. Chem. 275:18586-18593(2000).
[22]
INTERACTION WITH TNFRSF17.
PubMed=10908663; DOI=10.1073/pnas.160213497;
Shu H.-B., Johnson H.;
"B cell maturation protein is a receptor for the tumor necrosis factor
family member TALL-1.";
Proc. Natl. Acad. Sci. U.S.A. 97:9156-9161(2000).
[23]
INTERACTION WITH TAX1BP1.
PubMed=10920205; DOI=10.1073/pnas.170279097;
Ling L., Goeddel D.V.;
"T6BP, a TRAF6-interacting protein involved in IL-1 signaling.";
Proc. Natl. Acad. Sci. U.S.A. 97:9567-9572(2000).
[24]
UBIQUITINATION.
PubMed=11460167; DOI=10.1038/35085597;
Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.;
"TAK1 is a ubiquitin-dependent kinase of MKK and IKK.";
Nature 412:346-351(2001).
[25]
INTERACTION WITH TRAF3IP2.
PubMed=12459498; DOI=10.1016/s0014-5793(02)03688-8;
Kanamori M., Kai C., Hayashizaki Y., Suzuki H.;
"NF-kappaB activator Act1 associates with IL-1/Toll pathway adapter
molecule TRAF6.";
FEBS Lett. 532:241-246(2002).
[26]
INTERACTION WITH ZNF675.
PubMed=11751921; DOI=10.1074/jbc.m110964200;
Shin J.N., Kim I., Lee J.S., Koh G.Y., Lee Z.H., Kim H.-H.;
"A novel zinc finger protein that inhibits osteoclastogenesis and the
function of tumor necrosis factor receptor-associated factor 6.";
J. Biol. Chem. 277:8346-8353(2002).
[27]
INTERACTION WITH IRAK4.
PubMed=11960013; DOI=10.1073/pnas.082100399;
Li S., Strelow A., Fontana E.J., Wesche H.;
"IRAK4: a novel member of the IRAK family with the properties of an IRAK-
kinase.";
Proc. Natl. Acad. Sci. U.S.A. 99:5567-5572(2002).
[28]
INTERACTION WITH PELI1.
PubMed=12496252; DOI=10.1074/jbc.m212112200;
Jiang Z., Johnson H.J., Nie H., Qin J., Bird T.A., Li X.;
"Pellino 1 is required for interleukin-1 (IL-1)-mediated signaling through
its interaction with the IL-1 receptor-associated kinase 4 (IRAK4)-IRAK-
tumor necrosis factor receptor-associated factor 6 (TRAF6) complex.";
J. Biol. Chem. 278:10952-10956(2003).
[29]
INTERACTION WITH PELI1 AND PELI2.
PubMed=12804775; DOI=10.1016/s0014-5793(03)00533-7;
Jensen L.E., Whitehead A.S.;
"Pellino2 activates the mitogen activated protein kinase pathway.";
FEBS Lett. 545:199-202(2003).
[30]
INTERACTION WITH TICAM2.
PubMed=12721283; DOI=10.1074/jbc.m303451200;
Bin L.-H., Xu L.-G., Shu H.-B.;
"TIRP, a novel Toll/interleukin-1 receptor (TIR) domain-containing adapter
protein involved in TIR signaling.";
J. Biol. Chem. 278:24526-24532(2003).
[31]
INTERACTION WITH PELI3.
PubMed=12874243; DOI=10.4049/jimmunol.171.3.1500;
Jensen L.E., Whitehead A.S.;
"Pellino3, a novel member of the Pellino protein family, promotes
activation of c-Jun and Elk-1 and may act as a scaffolding protein.";
J. Immunol. 171:1500-1506(2003).
[32]
INTERACTION WITH TICAM1.
PubMed=14530355; DOI=10.4049/jimmunol.171.8.4304;
Sato S., Sugiyama M., Yamamoto M., Watanabe Y., Kawai T., Takeda K.,
Akira S.;
"Toll/IL-1 receptor domain-containing adapter inducing IFN-beta (TRIF)
associates with TNF receptor-associated factor 6 and TANK-binding kinase 1,
and activates two distinct transcription factors, NF-kappa B and IFN-
regulatory factor-3, in the Toll-like receptor signaling.";
J. Immunol. 171:4304-4310(2003).
[33]
INTERACTION WITH TICAM1.
PubMed=14739303; DOI=10.1074/jbc.m311629200;
Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.;
"Mechanisms of the TRIF-induced interferon-stimulated response element and
NF-kappaB activation and apoptosis pathways.";
J. Biol. Chem. 279:15652-15661(2004).
[34]
INTERACTION WITH ZFAND5.
PubMed=14754897; DOI=10.1074/jbc.m309491200;
Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z.,
Shu H.-B.;
"ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor of
NFkappaB activation.";
J. Biol. Chem. 279:16847-16853(2004).
[35]
INTERACTION WITH EIF2AK2.
PubMed=15121867; DOI=10.1128/mcb.24.10.4502-4512.2004;
Gil J., Garcia M.A., Gomez-Puertas P., Guerra S., Rullas J., Nakano H.,
Alcami J., Esteban M.;
"TRAF family proteins link PKR with NF-kappa B activation.";
Mol. Cell. Biol. 24:4502-4512(2004).
[36]
INTERACTION WITH TICAM1.
PubMed=14982987; DOI=10.1073/pnas.0308496101;
Jiang Z., Mak T.W., Sen G., Li X.;
"Toll-like receptor 3-mediated activation of NF-kappaB and IRF3 diverges at
Toll-IL-1 receptor domain-containing adapter inducing IFN-beta.";
Proc. Natl. Acad. Sci. U.S.A. 101:3533-3538(2004).
[37]
INTERACTION WITH MAVS.
PubMed=16125763; DOI=10.1016/j.cell.2005.08.012;
Seth R.B., Sun L., Ea C.-K., Chen Z.J.;
"Identification and characterization of MAVS, a mitochondrial antiviral
signaling protein that activates NF-kappaB and IRF 3.";
Cell 122:669-682(2005).
[38]
INTERACTION WITH IL1RL1.
PubMed=16286016; DOI=10.1016/j.immuni.2005.09.015;
Schmitz J., Owyang A., Oldham E., Song Y., Murphy E., McClanahan T.K.,
Zurawski G., Moshrefi M., Qin J., Li X., Gorman D.M., Bazan J.F.,
Kastelein R.A.;
"IL-33, an interleukin-1-like cytokine that signals via the IL-1 receptor-
related protein ST 2 and induces T helper type 2-associated cytokines.";
Immunity 23:479-490(2005).
[39]
INTERACTION WITH TRAFD1.
PubMed=16221674; DOI=10.1074/jbc.m508221200;
Mashima R., Saeki K., Aki D., Minoda Y., Takaki H., Sanada T.,
Kobayashi T., Aburatani H., Yamanashi Y., Yoshimura A.;
"FLN29, a novel interferon- and LPS-inducible gene acting as a negative
regulator of toll-like receptor signaling.";
J. Biol. Chem. 280:41289-41297(2005).
[40]
INTERACTION WITH MAVS.
PubMed=16153868; DOI=10.1016/j.molcel.2005.08.014;
Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.;
"VISA is an adapter protein required for virus-triggered IFN-beta
Signaling.";
Mol. Cell 19:727-740(2005).
[41]
INTERACTION WITH AJUBA.
PubMed=15870274; DOI=10.1128/mcb.25.10.4010-4022.2005;
Feng Y., Longmore G.D.;
"The LIM protein Ajuba influences interleukin-1-induced NF-kappaB
activation by affecting the assembly and activity of the protein kinase
Czeta/p62/TRAF6 signaling complex.";
Mol. Cell. Biol. 25:4010-4022(2005).
[42]
FUNCTION IN TRANSCRIPTIONAL ACTIVATION OF NF-KAPPA-B AND JUN, AND
INTERACTION WITH ARRB1 AND ARRB2.
PubMed=16378096; DOI=10.1038/ni1294;
Wang Y., Tang Y., Teng L., Wu Y., Zhao X., Pei G.;
"Association of beta-arrestin and TRAF6 negatively regulates Toll-like
receptor-interleukin 1 receptor signaling.";
Nat. Immunol. 7:139-147(2006).
[43]
IDENTIFICATION IN COMPLEX WITH IRAK1; IRAK4; MYD88 AND PELI1.
PubMed=16951688; DOI=10.1038/ni1383;
Choi K.C., Lee Y.S., Lim S., Choi H.K., Lee C.H., Lee E.K., Hong S.,
Kim I.H., Kim S.J., Park S.H.;
"Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor
signaling through direct interaction with the adapter Pellino-1.";
Nat. Immunol. 7:1057-1065(2006).
[44]
MUTAGENESIS OF CYS-70 AND LYS-124, UBIQUITINATION AT LYS-124, AND FUNCTION.
PubMed=17135271; DOI=10.1074/jbc.m609503200;
Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., Darnay B.G.;
"Site-specific Lys-63-linked tumor necrosis factor receptor-associated
factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase
activation.";
J. Biol. Chem. 282:4102-4112(2007).
[45]
INTERACTION WITH RBCK1.
PubMed=17449468; DOI=10.1074/jbc.m701913200;
Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M.,
Chen D.Y., Zhai Z.H., Shu H.B.;
"RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-
triggered NF-kappaB activation by targeting TAB2/3 for degradation.";
J. Biol. Chem. 282:16776-16782(2007).
[46]
SUBCELLULAR LOCATION, FUNCTION, SUMOYLATION AT LYS-124; LYS-142 AND
LYS-453, UBIQUITINATION, INTERACTION WITH HDAC1 AND RANGAP1, AND
MUTAGENESIS OF LYS-124; LYS-142 AND LYS-453.
PubMed=18093978; DOI=10.1074/jbc.m706307200;
Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L.,
Darnay B.G., Ford R.J.;
"Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid
cells negatively regulates c-Myb-mediated transactivation through small
ubiquitin-related modifier-1 modification.";
J. Biol. Chem. 283:5081-5089(2008).
[47]
FUNCTION IN UBIQUITINATION OR IRAK1.
PubMed=18347055; DOI=10.1128/mcb.02098-07;
Conze D.B., Wu C.J., Thomas J.A., Landstrom A., Ashwell J.D.;
"Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1
receptor- and toll-like receptor-mediated NF-kappaB activation.";
Mol. Cell. Biol. 28:3538-3547(2008).
[48]
FUNCTION, INTERACTION WITH TGFBR1, AND UBIQUITINATION.
PubMed=18758450; DOI=10.1038/ncb1780;
Sorrentino A., Thakur N., Grimsby S., Marcusson A., von Bulow V.,
Schuster N., Zhang S., Heldin C.H., Landstrom M.;
"The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor
kinase-independent manner.";
Nat. Cell Biol. 10:1199-1207(2008).
[49]
INTERACTION WITH DYNC2I2.
PubMed=19521662; DOI=10.1007/s00018-009-0059-6;
Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.;
"WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced
NF-kappaB activation pathway.";
Cell. Mol. Life Sci. 66:2573-2584(2009).
[50]
FUNCTION, AND UBIQUITINATION.
PubMed=19675569; DOI=10.1038/nature08247;
Xia Z.-P., Sun L., Chen X., Pineda G., Jiang X., Adhikari A., Zeng W.,
Chen Z.J.;
"Direct activation of protein kinases by unanchored polyubiquitin chains.";
Nature 461:114-119(2009).
[51]
FUNCTION.
PubMed=19713527; DOI=10.1126/science.1175065;
Yang W.-L., Wang J., Chan C.-H., Lee S.-W., Campos A.D., Lamothe B.,
Hur L., Grabiner B.C., Lin X., Darnay B.G., Lin H.-K.;
"The E3 ligase TRAF6 regulates Akt ubiquitination and activation.";
Science 325:1134-1138(2009).
[52]
FUNCTION, UBIQUITINATION AT LYS-124, MUTAGENESIS OF CYS-70 AND LYS-124, AND
INTERACTION WITH IL17RA AND TRAF3IP2.
PubMed=19825828; DOI=10.1126/scisignal.2000382;
Liu C., Qian W., Qian Y., Giltiay N.V., Lu Y., Swaidani S., Misra S.,
Deng L., Chen Z.J., Li X.;
"Act1, a U-box E3 ubiquitin ligase for IL-17 signaling.";
Sci. Signal. 2:ra63-ra63(2009).
[53]
INTERACTION WITH NUMBL.
PubMed=20079715; DOI=10.1016/j.bbrc.2010.01.037;
Zhou L., Ma Q., Shi H., Huo K.;
"NUMBL interacts with TRAF6 and promotes the degradation of TRAF6.";
Biochem. Biophys. Res. Commun. 392:409-414(2010).
[54]
INTERACTION WITH TOMM70.
PubMed=20628368; DOI=10.1038/cr.2010.103;
Liu X.Y., Wei B., Shi H.X., Shan Y.F., Wang C.;
"Tom70 mediates activation of interferon regulatory factor 3 on
mitochondria.";
Cell Res. 20:994-1011(2010).
[55]
INTERACTION WITH CARD14.
PubMed=21302310; DOI=10.1002/jcp.22667;
Scudiero I., Zotti T., Ferravante A., Vessichelli M., Vito P., Stilo R.;
"Alternative splicing of CARMA2/CARD14 transcripts generates protein
variants with differential effect on NF-kappaB activation and endoplasmic
reticulum stress-induced cell death.";
J. Cell. Physiol. 226:3121-3131(2011).
[56]
INTERACTION WITH IFIT3.
PubMed=21813773; DOI=10.4049/jimmunol.1100963;
Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.;
"IFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging
MAVS and TBK1.";
J. Immunol. 187:2559-2568(2011).
[57]
INTERACTION WITH SASH1.
PubMed=23776175; DOI=10.4049/jimmunol.1200583;
Dauphinee S.M., Clayton A., Hussainkhel A., Yang C., Park Y.J.,
Fuller M.E., Blonder J., Veenstra T.D., Karsan A.;
"SASH1 is a scaffold molecule in endothelial TLR4 signaling.";
J. Immunol. 191:892-901(2013).
[58]
UBIQUITINATION, AND INTERACTION WITH LRRC19.
PubMed=25026888; DOI=10.1038/ncomms5434;
Su X., Min S., Cao S., Yan H., Zhao Y., Li H., Chai L., Mei S., Yang J.,
Zhang Y., Zhang Z., Liu F., Sun W., Che Y., Yang R.;
"LRRC19 expressed in the kidney induces TRAF2/6-mediated signals to prevent
infection by uropathogenic bacteria.";
Nat. Commun. 5:4434-4434(2014).
[59]
INTERACTION WITH TICAM1.
PubMed=25736436; DOI=10.15252/embr.201439637;
Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
Liu Y.;
"WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
EMBO Rep. 16:447-455(2015).
[60]
INTERACTION WITH TANK; USP10 AND ZC3H12A, AND DEUBIQUITINATION BY USP10.
PubMed=25861989; DOI=10.1074/jbc.m115.643767;
Wang W., Huang X., Xin H.B., Fu M., Xue A., Wu Z.H.;
"TRAF family member-associated NF-kappaB activator (TANK) inhibits
genotoxic nuclear factor kappaB activation by facilitating deubiquitinase
USP10-dependent deubiquitination of TRAF6 ligase.";
J. Biol. Chem. 290:13372-13385(2015).
[61]
INTERACTION WITH TRIM13.
PubMed=28087809; DOI=10.1124/mol.116.106716;
Huang B., Baek S.H.;
"Trim13 potentiates toll-like receptor 2-mediated nuclear factor kappaB
activation via K29-linked polyubiquitination of tumor necrosis factor
receptor-associated factor 6.";
Mol. Pharmacol. 91:307-316(2017).
[62]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 347-506 OF APOPROTEIN AND IN
COMPLEXES WITH TNFRSF5 AND TNFRSF11A PEPTIDES, FUNCTION, AND SUBUNIT.
PubMed=12140561; DOI=10.1038/nature00888;
Ye H., Arron J.R., Lamothe B., Cirilli M., Kobayashi T., Shevde N.K.,
Segal D., Dzivenu O.K., Vologodskaia M., Yim M., Du K., Singh S.,
Pike J.W., Darnay B.G., Choi Y., Wu H.;
"Distinct molecular mechanism for initiating TRAF6 signalling.";
Nature 418:443-447(2002).
[63]
STRUCTURE BY NMR OF 63-124 IN COMPLEX WITH ZINC IONS, AND INTERACTION WITH
UBE2N.
PubMed=17327397; DOI=10.1110/ps.062358007;
Mercier P., Lewis M.J., Hau D.D., Saltibus L.F., Xiao W., Spyracopoulos L.;
"Structure, interactions, and dynamics of the RING domain from human
TRAF6.";
Protein Sci. 16:602-614(2007).
[64]
STRUCTURE BY NMR OF 43-128.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RING domain of the human TNF receptor-associated
factor 6 protein.";
Submitted (MAR-2008) to the PDB data bank.
[65]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 50-211 IN COMPLEXES WITH ZINC IONS
AND UBE2N, SUBUNIT, FUNCTION, AUTOUBIQUITINATION, MUTAGENESIS OF ASP-57;
CYS-70; ILE-72; LEU-74; ARG-88; PHE-118; PHE-122 AND LYS-124, AND
ZINC-FINGER.
PubMed=19465916; DOI=10.1038/nsmb.1605;
Yin Q., Lin S.C., Lamothe B., Lu M., Lo Y.C., Hura G., Zheng L., Rich R.L.,
Campos A.D., Myszka D.G., Lenardo M.J., Darnay B.G., Wu H.;
"E2 interaction and dimerization in the crystal structure of TRAF6.";
Nat. Struct. Mol. Biol. 16:658-666(2009).
-!- FUNCTION: E3 ubiquitin ligase that, together with UBE2N and UBE2V1,
mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains
conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also
mediates ubiquitination of free/unanchored polyubiquitin chain that
leads to MAP3K7 activation. Leads to the activation of NF-kappa-B and
JUN. May be essential for the formation of functional osteoclasts.
Seems to also play a role in dendritic cells (DCs) maturation and/or
activation. Represses c-Myb-mediated transactivation, in B-lymphocytes.
Adapter protein that seems to play a role in signal transduction
initiated via TNF receptor, IL-1 receptor and IL-17 receptor. Regulates
osteoclast differentiation by mediating the activation of adapter
protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L
stimulation. Together with MAP3K8, mediates CD40 signals that activate
ERK in B-cells and macrophages, and thus may play a role in the
regulation of immunoglobulin production. {ECO:0000269|PubMed:11057907,
ECO:0000269|PubMed:12140561, ECO:0000269|PubMed:16378096,
ECO:0000269|PubMed:17135271, ECO:0000269|PubMed:18093978,
ECO:0000269|PubMed:18347055, ECO:0000269|PubMed:18758450,
ECO:0000269|PubMed:19465916, ECO:0000269|PubMed:19675569,
ECO:0000269|PubMed:19713527, ECO:0000269|PubMed:19825828,
ECO:0000269|PubMed:8837778}.
-!- CATALYTIC ACTIVITY:
Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
[acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
EC=2.3.2.27;
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homotrimer. Homooligomer. N-terminal region is dimeric while
C-terminal region is trimeric; maybe providing a mode of
oligomerization. Upon IL1B treatment, forms a complex with PELI1,
IRAK1, IRAK4 and MYD88; this complex recruits MAP3K7/TAK1, TAB1 and
TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to PELI1
prevents the complex formation and hence negatively regulates IL1R-TLR
signaling and eventually NF-kappa-B-mediated gene expression. Binds to
TNFRSF5/CD40 and TNFRSF11A/RANK. Associates with NGFR, TNFRSF17, IRAK2,
IRAK3, RIPK2, MAP3K1, MAP3K5, MAP3K14, CSK, TRAF, TRAF-interacting
protein TRIP and TNF receptor associated protein TDP2. Interacts with
IL17R. Interacts with SQSTM1 bridging NTRK1 and NGFR. Forms a ternary
complex with SQSTM1 and PRKCZ (By similarity). Interacts with PELI2 and
PELI3. Binds UBE2V1. Interacts with TAX1BP1. Interacts with ZNF675.
Interacts with ARRB1 and ARRB2. Interacts with MAP3K7 and
TAB1/MAP3K7IP1; during IL-1 signaling. Interacts with UBE2N. Interacts
with TGFBR1, HDAC1 and RANGAP1. Interacts with AKT1, AKT2 and AKT3.
Interacts (via TRAF domains) with NUMBL (via C-terminal). Interacts
with RBCK1. Interacts with LIMD1 (via LIM domains) (By similarity).
Interacts with RSAD2/viperin (By similarity). Interacts (via C-
terminus) with EIF2AK2/PKR (via the kinase catalytic domain) (By
similarity). Interacts with ZFAND5. Interacts with IL1RL1. Interacts
with TRAFD1. Interacts with AJUBA. Interacts with MAVS/IPS1. Interacts
(via TRAF domains) with DYNC2I2 (via WD domains). Interacts with IFIT3
(via N-terminus). Interacts with TICAM2. Interacts with CARD14.
Interacts with CD40 and MAP3K8; the interaction is required for ERK
activation (By similarity). Interacts with TICAM1 and this interaction
is enhanced in the presence of WDFY1 (PubMed:25736436). Interacts with
TANK; this interaction increases in response to DNA damage
(PubMed:25861989). Interacts with USP10; this interaction increases in
response to DNA damage (PubMed:25861989). Interacts with ZC3H12A; this
interaction increases in response to DNA damage and is stimulated by
TANK (PubMed:25861989). Interacts with WDFY3 (By similarity). Interacts
with TRIM13 (PubMed:28087809). Interacts with GPS2 (By similarity).
Interacts (via C-terminus) with SASH1 (PubMed:23776175). Interacts with
LRRC19 (PubMed:25026888). Interacts with IL17RA AND TRAF3IP2. Interacts
with TOMM70 (PubMed:20628368). {ECO:0000250|UniProtKB:P70196,
ECO:0000269|PubMed:19825828, ECO:0000269|PubMed:20628368,
ECO:0000269|PubMed:23776175, ECO:0000269|PubMed:25026888,
ECO:0000269|PubMed:25736436, ECO:0000269|PubMed:25861989,
ECO:0000269|PubMed:28087809}.
-!- INTERACTION:
Q9Y4K3; Q9C0C7-3: AMBRA1; NbExp=2; IntAct=EBI-359276, EBI-16042318;
Q9Y4K3; Q8IWQ3-3: BRSK2; NbExp=3; IntAct=EBI-359276, EBI-13085322;
Q9Y4K3; P25942: CD40; NbExp=2; IntAct=EBI-359276, EBI-525714;
Q9Y4K3; Q9HAV5: EDA2R; NbExp=2; IntAct=EBI-359276, EBI-526033;
Q9Y4K3; Q8WWZ3: EDARADD; NbExp=5; IntAct=EBI-359276, EBI-2949647;
Q9Y4K3; P14778: IL1R1; NbExp=2; IntAct=EBI-359276, EBI-525905;
Q9Y4K3; Q8NA54: IQUB; NbExp=3; IntAct=EBI-359276, EBI-10220600;
Q9Y4K3; P51617: IRAK1; NbExp=2; IntAct=EBI-359276, EBI-358664;
Q9Y4K3; O43187: IRAK2; NbExp=3; IntAct=EBI-359276, EBI-447733;
Q9Y4K3; Q9Y616: IRAK3; NbExp=3; IntAct=EBI-359276, EBI-447690;
Q9Y4K3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-359276, EBI-739832;
Q9Y4K3; Q9UDY8: MALT1; NbExp=5; IntAct=EBI-359276, EBI-1047372;
Q9Y4K3; O43318: MAP3K7; NbExp=2; IntAct=EBI-359276, EBI-358684;
Q9Y4K3; Q7Z434: MAVS; NbExp=4; IntAct=EBI-359276, EBI-995373;
Q9Y4K3; P50222: MEOX2; NbExp=3; IntAct=EBI-359276, EBI-748397;
Q9Y4K3; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-359276, EBI-11980301;
Q9Y4K3; Q96DC9: OTUB2; NbExp=3; IntAct=EBI-359276, EBI-746259;
Q9Y4K3; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-359276, EBI-742388;
Q9Y4K3; Q9UNA4: POLI; NbExp=3; IntAct=EBI-359276, EBI-741774;
Q9Y4K3; P54725: RAD23A; NbExp=3; IntAct=EBI-359276, EBI-746453;
Q9Y4K3; Q9BVN2-2: RUSC1; NbExp=2; IntAct=EBI-359276, EBI-6257338;
Q9Y4K3; P04271: S100B; NbExp=3; IntAct=EBI-359276, EBI-458391;
Q9Y4K3; Q9NYA1: SPHK1; NbExp=2; IntAct=EBI-359276, EBI-985303;
Q9Y4K3; Q13501: SQSTM1; NbExp=4; IntAct=EBI-359276, EBI-307104;
Q9Y4K3; P43405-2: SYK; NbExp=3; IntAct=EBI-359276, EBI-25892332;
Q9Y4K3; Q9NYJ8: TAB2; NbExp=3; IntAct=EBI-359276, EBI-358708;
Q9Y4K3; Q86VP1: TAX1BP1; NbExp=8; IntAct=EBI-359276, EBI-529518;
Q9Y4K3; Q96CG3: TIFA; NbExp=6; IntAct=EBI-359276, EBI-740711;
Q9Y4K3; Q9UKE5: TNIK; NbExp=3; IntAct=EBI-359276, EBI-1051794;
Q9Y4K3; Q13077: TRAF1; NbExp=17; IntAct=EBI-359276, EBI-359224;
Q9Y4K3; Q12933: TRAF2; NbExp=9; IntAct=EBI-359276, EBI-355744;
Q9Y4K3; O43734: TRAF3IP2; NbExp=4; IntAct=EBI-359276, EBI-744798;
Q9Y4K3; O00463: TRAF5; NbExp=15; IntAct=EBI-359276, EBI-523498;
Q9Y4K3; Q9Y4K3: TRAF6; NbExp=11; IntAct=EBI-359276, EBI-359276;
Q9Y4K3; P0CG48: UBC; NbExp=3; IntAct=EBI-359276, EBI-3390054;
Q9Y4K3; P51668: UBE2D1; NbExp=2; IntAct=EBI-359276, EBI-743540;
Q9Y4K3; P62837: UBE2D2; NbExp=5; IntAct=EBI-359276, EBI-347677;
Q9Y4K3; P61077: UBE2D3; NbExp=2; IntAct=EBI-359276, EBI-348268;
Q9Y4K3; P61088: UBE2N; NbExp=8; IntAct=EBI-359276, EBI-1052908;
Q9Y4K3; Q9HAC8: UBTD1; NbExp=3; IntAct=EBI-359276, EBI-745871;
Q9Y4K3; O94888: UBXN7; NbExp=3; IntAct=EBI-359276, EBI-1993627;
Q9Y4K3; P09936: UCHL1; NbExp=3; IntAct=EBI-359276, EBI-714860;
Q9Y4K3; O75385: ULK1; NbExp=2; IntAct=EBI-359276, EBI-908831;
Q9Y4K3; O75604: USP2; NbExp=3; IntAct=EBI-359276, EBI-743272;
Q9Y4K3; Q8N1B4: VPS52; NbExp=6; IntAct=EBI-359276, EBI-2799833;
Q9Y4K3; P61964: WDR5; NbExp=2; IntAct=EBI-359276, EBI-540834;
Q9Y4K3; P07947: YES1; NbExp=6; IntAct=EBI-359276, EBI-515331;
Q9Y4K3; Q5VVQ6: YOD1; NbExp=5; IntAct=EBI-359276, EBI-2510804;
Q9Y4K3; P24278: ZBTB25; NbExp=3; IntAct=EBI-359276, EBI-739899;
Q9Y4K3; Q8TD23: ZNF675; NbExp=4; IntAct=EBI-359276, EBI-528190;
Q9Y4K3; Q9UGI0: ZRANB1; NbExp=4; IntAct=EBI-359276, EBI-527853;
Q9Y4K3; Q9QZH6: Ecsit; Xeno; NbExp=2; IntAct=EBI-359276, EBI-527020;
Q9Y4K3; P07174: Ngfr; Xeno; NbExp=2; IntAct=EBI-359276, EBI-1038810;
Q9Y4K3; P10221: UL37; Xeno; NbExp=3; IntAct=EBI-359276, EBI-6880600;
Q9Y4K3; Q01220: VACWR178; Xeno; NbExp=2; IntAct=EBI-359276, EBI-3863691;
Q9Y4K3; Q8V2D1; Xeno; NbExp=3; IntAct=EBI-359276, EBI-8622036;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18093978}.
Cytoplasm, cell cortex {ECO:0000269|PubMed:18093978}. Nucleus
{ECO:0000269|PubMed:18093978}. Lipid droplet
{ECO:0000250|UniProtKB:P70196}. Note=Found in the nuclei of some
aggressive B-cell lymphoma cell lines as well as in the nuclei of both
resting and activated T- and B-lymphocytes. Found in punctate nuclear
body protein complexes. Ubiquitination may occur in the cytoplasm and
sumoylation in the nucleus. RSAD2/viperin recruits it to the lipid
droplet (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
skeletal muscle, kidney and pancreas.
-!- DOMAIN: The coiled coil domain mediates homo- and hetero-
oligomerization.
-!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic domains.
-!- PTM: Sumoylated on Lys-124, Lys-142 and Lys-453 with SUMO1.
{ECO:0000269|PubMed:18093978}.
-!- PTM: Polyubiquitinated on Lys-124 by TRAF3IP2; after cell stimulation
with IL17A (PubMed:19825828). Polyubiquitinated on Lys-124; after cell
stimulation with IL1B or TGFB. This ligand-induced cell stimulation
leads to dimerization/oligomerization of TRAF6 molecules, followed by
auto-ubiquitination which involves UBE2N and UBE2V1 and leads to TRAF6
activation. This 'Lys-63' site-specific poly-ubiquitination appears to
be associated with the activation of signaling molecules. Endogenous
autoubiquitination occurs only for the cytoplasmic form.
Deubiquitinated by USP10 in a TANK-dependent manner, leading to the
negative regulation of NF-kappaB signaling upon DNA damage
(PubMed:25861989). LRRC19 induces 'Lys-63' ubiquitination
(PubMed:25026888). {ECO:0000269|PubMed:11460167,
ECO:0000269|PubMed:17135271, ECO:0000269|PubMed:18093978,
ECO:0000269|PubMed:18758450, ECO:0000269|PubMed:19465916,
ECO:0000269|PubMed:19675569, ECO:0000269|PubMed:19825828,
ECO:0000269|PubMed:25026888, ECO:0000269|PubMed:25861989}.
-!- SIMILARITY: Belongs to the TNF receptor-associated factor family. A
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/traf6/";
---------------------------------------------------------------------------
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EMBL; U78798; AAB38751.1; -; mRNA.
EMBL; AY228337; AAO38054.1; -; Genomic_DNA.
EMBL; AK292978; BAF85667.1; -; mRNA.
EMBL; AC009656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC061999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68119.1; -; Genomic_DNA.
EMBL; CH471064; EAW68120.1; -; Genomic_DNA.
EMBL; CH471064; EAW68122.1; -; Genomic_DNA.
EMBL; BC031052; AAH31052.1; -; mRNA.
CCDS; CCDS7901.1; -.
PIR; S71821; S71821.
RefSeq; NP_004611.1; NM_004620.3.
RefSeq; NP_665802.1; NM_145803.2.
PDB; 1LB4; X-ray; 2.40 A; A=348-504.
PDB; 1LB5; X-ray; 2.40 A; A=347-504.
PDB; 1LB6; X-ray; 1.80 A; A=347-504.
PDB; 2ECI; NMR; -; A=50-128.
PDB; 2JMD; NMR; -; A=67-124.
PDB; 3HCS; X-ray; 2.20 A; A/B=50-211.
PDB; 3HCT; X-ray; 2.10 A; A=50-159.
PDB; 3HCU; X-ray; 2.60 A; A/C=50-159.
PDB; 4Z8M; X-ray; 2.95 A; A/B=346-504.
PDB; 5ZUJ; X-ray; 2.60 A; A=350-501.
PDB; 6A33; X-ray; 2.10 A; A=350-501.
PDB; 7L3L; X-ray; 2.80 A; B/D=52-158.
PDBsum; 1LB4; -.
PDBsum; 1LB5; -.
PDBsum; 1LB6; -.
PDBsum; 2ECI; -.
PDBsum; 2JMD; -.
PDBsum; 3HCS; -.
PDBsum; 3HCT; -.
PDBsum; 3HCU; -.
PDBsum; 4Z8M; -.
PDBsum; 5ZUJ; -.
PDBsum; 6A33; -.
PDBsum; 7L3L; -.
SMR; Q9Y4K3; -.
BioGRID; 113041; 372.
CORUM; Q9Y4K3; -.
DIP; DIP-27515N; -.
ELM; Q9Y4K3; -.
IntAct; Q9Y4K3; 124.
MINT; Q9Y4K3; -.
STRING; 9606.ENSP00000433623; -.
BindingDB; Q9Y4K3; -.
ChEMBL; CHEMBL3588728; -.
MoonDB; Q9Y4K3; Predicted.
iPTMnet; Q9Y4K3; -.
PhosphoSitePlus; Q9Y4K3; -.
BioMuta; TRAF6; -.
DMDM; 30580642; -.
EPD; Q9Y4K3; -.
jPOST; Q9Y4K3; -.
MassIVE; Q9Y4K3; -.
MaxQB; Q9Y4K3; -.
PaxDb; Q9Y4K3; -.
PeptideAtlas; Q9Y4K3; -.
PRIDE; Q9Y4K3; -.
ProteomicsDB; 86225; -.
Antibodypedia; 3895; 537 antibodies.
DNASU; 7189; -.
Ensembl; ENST00000348124; ENSP00000337853; ENSG00000175104.
Ensembl; ENST00000526995; ENSP00000433623; ENSG00000175104.
GeneID; 7189; -.
KEGG; hsa:7189; -.
UCSC; uc001mwq.3; human.
CTD; 7189; -.
DisGeNET; 7189; -.
GeneCards; TRAF6; -.
HGNC; HGNC:12036; TRAF6.
HPA; ENSG00000175104; Low tissue specificity.
MalaCards; TRAF6; -.
MIM; 602355; gene.
neXtProt; NX_Q9Y4K3; -.
OpenTargets; ENSG00000175104; -.
Orphanet; 1810; Autosomal dominant hypohidrotic ectodermal dysplasia.
PharmGKB; PA36713; -.
VEuPathDB; HostDB:ENSG00000175104.14; -.
eggNOG; KOG0297; Eukaryota.
GeneTree; ENSGT00940000155426; -.
HOGENOM; CLU_021061_5_0_1; -.
InParanoid; Q9Y4K3; -.
OMA; ECAICID; -.
OrthoDB; 918518at2759; -.
PhylomeDB; Q9Y4K3; -.
TreeFam; TF321154; -.
PathwayCommons; Q9Y4K3; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
Reactome; R-HSA-193692; Regulated proteolysis of p75NTR.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
Reactome; R-HSA-209560; NF-kB is activated and signals survival.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
Reactome; R-HSA-9645460; Alpha-protein kinase 1 signaling pathway.
Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-HSA-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
Reactome; R-HSA-975155; MyD88 dependent cascade initiated on endosome.
Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
Reactome; R-HSA-975871; MyD88 cascade initiated on plasma membrane.
SignaLink; Q9Y4K3; -.
SIGNOR; Q9Y4K3; -.
UniPathway; UPA00143; -.
BioGRID-ORCS; 7189; 29 hits in 996 CRISPR screens.
ChiTaRS; TRAF6; human.
EvolutionaryTrace; Q9Y4K3; -.
GeneWiki; TRAF6; -.
GenomeRNAi; 7189; -.
Pharos; Q9Y4K3; Tbio.
PRO; PR:Q9Y4K3; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; Q9Y4K3; protein.
Bgee; ENSG00000175104; Expressed in secondary oocyte and 187 other tissues.
Genevisible; Q9Y4K3; HS.
GO; GO:0035631; C:CD40 receptor complex; ISS:BHF-UCL.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:UniProtKB.
GO; GO:0043422; F:protein kinase B binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0031996; F:thioesterase binding; IPI:UniProtKB.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:UniProtKB.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IDA:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IMP:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0048468; P:cell development; IEA:Ensembl.
GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:ARUK-UCL.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IBA:GO_Central.
GO; GO:0097400; P:interleukin-17-mediated signaling pathway; IEA:Ensembl.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; TAS:Reactome.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IBA:GO_Central.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IMP:ARUK-UCL.
GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:ARUK-UCL.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; NAS:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0002726; P:positive regulation of T cell cytokine production; IMP:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0002637; P:regulation of immunoglobulin production; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IDA:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0042088; P:T-helper 1 type immune response; IEA:Ensembl.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
CDD; cd03776; MATH_TRAF6; 1.
Gene3D; 2.60.210.10; -; 1.
Gene3D; 3.30.40.10; -; 3.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR043211; TNF_rcpt-assoc_TRAF.
InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
InterPro; IPR008974; TRAF-like.
InterPro; IPR027139; TRAF6.
InterPro; IPR037309; TRAF6_MATH.
InterPro; IPR041310; TRAF6_Z2.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
InterPro; IPR001293; Znf_TRAF.
PANTHER; PTHR10131; PTHR10131; 1.
PANTHER; PTHR10131:SF131; PTHR10131:SF131; 1.
Pfam; PF18048; TRAF6_Z2; 1.
Pfam; PF02176; zf-TRAF; 1.
PIRSF; PIRSF015614; TRAF; 1.
SMART; SM00061; MATH; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF49599; SSF49599; 3.
PROSITE; PS50144; MATH; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
PROSITE; PS50145; ZF_TRAF; 2.
1: Evidence at protein level;
3D-structure; Coiled coil; Cytoplasm; DNA damage; Immunity;
Isopeptide bond; Lipid droplet; Metal-binding; Nucleus; Osteogenesis;
Reference proteome; Repeat; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1..522
/note="TNF receptor-associated factor 6"
/id="PRO_0000056407"
DOMAIN 350..499
/note="MATH"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
ZN_FING 70..109
/note="RING-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
ZN_FING 150..202
/note="TRAF-type 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
ZN_FING 203..259
/note="TRAF-type 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00207"
REGION 1..354
/note="Interaction with TAX1BP1"
/evidence="ECO:0000269|PubMed:10920205"
REGION 355..522
/note="Interaction with TANK"
/evidence="ECO:0000269|PubMed:25861989"
COILED 288..348
/evidence="ECO:0000255"
CROSSLNK 124
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
CROSSLNK 124
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:17135271,
ECO:0000269|PubMed:19825828"
CROSSLNK 142
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000269|PubMed:18093978"
CROSSLNK 453
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000269|PubMed:18093978"
MUTAGEN 57
/note="D->K: Loss of interaction with UBE2N."
/evidence="ECO:0000269|PubMed:19465916"
MUTAGEN 70
/note="C->A: Loss of ligase activity, autoubiquitination
and signaling capacity."
/evidence="ECO:0000269|PubMed:17135271,
ECO:0000269|PubMed:19465916"
MUTAGEN 72
/note="I->D: Loss of interaction with UBE2N. Has no effect
on TRAF3IP2-mediated 'Lys-63'-linked polyubiquitination."
/evidence="ECO:0000269|PubMed:19465916,
ECO:0000269|PubMed:19825828"
MUTAGEN 74
/note="L->E,K: Loss of interaction with UBE2N."
/evidence="ECO:0000269|PubMed:19465916"
MUTAGEN 88
/note="R->A: Loss of TRAF6 homodimerization and impaired
polyubiquitin synthesis. Loss of TRAF6 homodimerization and
impaired polyubiquitin synthesis; when associated with A-
122."
/evidence="ECO:0000269|PubMed:19465916"
MUTAGEN 118
/note="F->A: Loss of TRAF6 homodimerization and impaired
polyubiquitin synthesis."
/evidence="ECO:0000269|PubMed:19465916"
MUTAGEN 118
/note="F->W: Partially impaired polyubiquitin synthesis."
/evidence="ECO:0000269|PubMed:19465916"
MUTAGEN 118
/note="F->Y: Partially impaired polyubiquitin synthesis."
/evidence="ECO:0000269|PubMed:19465916"
MUTAGEN 122
/note="F->A: Loss of TRAF6 homodimerization and partially
impaired polyubiquitin synthesis. Loss of TRAF6
homodimerization and impaired polyubiquitin synthesis; when
associated with A-88."
/evidence="ECO:0000269|PubMed:19465916"
MUTAGEN 124
/note="K->R: Loss of SUMO1-modification and c-myb-mediated
transcriptional repressive activation. Loss of TRAF3IP2-
mediated 'Lys-63'-linked polyubiquitination."
/evidence="ECO:0000269|PubMed:17135271,
ECO:0000269|PubMed:18093978, ECO:0000269|PubMed:19465916,
ECO:0000269|PubMed:19825828"
MUTAGEN 142
/note="K->R: Loss of SUMO1-modification and c-myb-mediated
transcriptional repressive activation."
/evidence="ECO:0000269|PubMed:18093978"
MUTAGEN 453
/note="K->R: Loss of SUMO1-modification and c-myb-mediated
transcriptional repressive activation."
/evidence="ECO:0000269|PubMed:18093978"
CONFLICT 12
/note="S -> F (in Ref. 6; AAH31052)"
/evidence="ECO:0000305"
STRAND 60..62
/evidence="ECO:0007829|PDB:3HCT"
HELIX 66..68
/evidence="ECO:0007829|PDB:3HCT"
TURN 71..73
/evidence="ECO:0007829|PDB:3HCT"
STRAND 78..82
/evidence="ECO:0007829|PDB:3HCT"
TURN 84..86
/evidence="ECO:0007829|PDB:2ECI"
STRAND 88..90
/evidence="ECO:0007829|PDB:3HCT"
HELIX 91..101
/evidence="ECO:0007829|PDB:3HCT"
TURN 106..108
/evidence="ECO:0007829|PDB:3HCT"
HELIX 114..116
/evidence="ECO:0007829|PDB:3HCT"
HELIX 121..128
/evidence="ECO:0007829|PDB:3HCT"
STRAND 130..133
/evidence="ECO:0007829|PDB:3HCT"
STRAND 135..138
/evidence="ECO:0007829|PDB:3HCU"
STRAND 142..144
/evidence="ECO:0007829|PDB:3HCT"
HELIX 145..147
/evidence="ECO:0007829|PDB:3HCT"
HELIX 149..151
/evidence="ECO:0007829|PDB:3HCT"
STRAND 153..155
/evidence="ECO:0007829|PDB:3HCT"
STRAND 158..161
/evidence="ECO:0007829|PDB:3HCS"
TURN 163..165
/evidence="ECO:0007829|PDB:3HCS"
STRAND 168..170
/evidence="ECO:0007829|PDB:3HCS"
HELIX 171..173
/evidence="ECO:0007829|PDB:3HCS"
HELIX 174..180
/evidence="ECO:0007829|PDB:3HCS"
STRAND 186..188
/evidence="ECO:0007829|PDB:3HCS"
TURN 190..192
/evidence="ECO:0007829|PDB:3HCS"
STRAND 195..197
/evidence="ECO:0007829|PDB:3HCS"
HELIX 198..200
/evidence="ECO:0007829|PDB:3HCS"
HELIX 201..205
/evidence="ECO:0007829|PDB:3HCS"
STRAND 351..357
/evidence="ECO:0007829|PDB:1LB6"
HELIX 360..368
/evidence="ECO:0007829|PDB:1LB6"
STRAND 373..376
/evidence="ECO:0007829|PDB:1LB6"
STRAND 380..385
/evidence="ECO:0007829|PDB:1LB6"
STRAND 388..395
/evidence="ECO:0007829|PDB:1LB6"
TURN 401..405
/evidence="ECO:0007829|PDB:1LB6"
STRAND 406..414
/evidence="ECO:0007829|PDB:1LB6"
HELIX 419..421
/evidence="ECO:0007829|PDB:1LB6"
STRAND 428..434
/evidence="ECO:0007829|PDB:1LB6"
HELIX 440..442
/evidence="ECO:0007829|PDB:6A33"
STRAND 446..451
/evidence="ECO:0007829|PDB:1LB6"
HELIX 457..459
/evidence="ECO:0007829|PDB:1LB6"
STRAND 463..466
/evidence="ECO:0007829|PDB:1LB6"
STRAND 468..478
/evidence="ECO:0007829|PDB:1LB6"
HELIX 479..483
/evidence="ECO:0007829|PDB:1LB6"
TURN 484..486
/evidence="ECO:0007829|PDB:6A33"
STRAND 492..500
/evidence="ECO:0007829|PDB:1LB6"
SEQUENCE 522 AA; 59573 MW; 5AB9C255CCFEE749 CRC64;
MSLLNCENSC GSSQSESDCC VAMASSCSAV TKDDSVGGTA STGNLSSSFM EEIQGYDVEF
DPPLESKYEC PICLMALREA VQTPCGHRFC KACIIKSIRD AGHKCPVDNE ILLENQLFPD
NFAKREILSL MVKCPNEGCL HKMELRHLED HQAHCEFALM DCPQCQRPFQ KFHINIHILK
DCPRRQVSCD NCAASMAFED KEIHDQNCPL ANVICEYCNT ILIREQMPNH YDLDCPTAPI
PCTFSTFGCH EKMQRNHLAR HLQENTQSHM RMLAQAVHSL SVIPDSGYIS EVRNFQETIH
QLEGRLVRQD HQIRELTAKM ETQSMYVSEL KRTIRTLEDK VAEIEAQQCN GIYIWKIGNF
GMHLKCQEEE KPVVIHSPGF YTGKPGYKLC MRLHLQLPTA QRCANYISLF VHTMQGEYDS
HLPWPFQGTI RLTILDQSEA PVRQNHEEIM DAKPELLAFQ RPTIPRNPKG FGYVTFMHLE
ALRQRTFIKD DTLLVRCEVS TRFDMGSLRR EGFQPRSTDA GV


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EIAAB43998 GERP,Glioblastoma-expressed RING finger protein,Homo sapiens,Human,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,RNF27,TRIM8,Tripartite motif-containing protein 8
EIAAB34424 Constitutive photomorphogenesis protein 1 homolog,COP1,E3 ubiquitin-protein ligase RFWD2,hCOP1,Homo sapiens,Human,RFWD2,RING finger and WD repeat domain protein 2,RING finger protein 200,RNF200
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[TRAF6 RNF85] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (Interleukin-1 signal transducer) (RING finger protein 85) (RING-type E3 ubiquitin transferase TRAF6)
[Traf6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[Traf6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF6] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[traf6 si:dkey-56p7.3 zgc:63704] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[TRAF2 TRAP3] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2) (Tumor necrosis factor type 2 receptor-associated protein 3)
[Traf3 Craf1 Trafamn] TNF receptor-associated factor 3 (EC 2.3.2.27) (CD40 receptor-associated factor 1) (CRAF1) (RING-type E3 ubiquitin transferase TRAF3) (TRAFAMN)
[TRAF3 CAP1 CRAF1] TNF receptor-associated factor 3 (EC 2.3.2.27) (CAP-1) (CD40 receptor-associated factor 1) (CRAF1) (CD40-binding protein) (CD40BP) (LMP1-associated protein 1) (LAP1) (RING-type E3 ubiquitin transferase TRAF3)
[RBCK1 C20orf18 RNF54 UBCE7IP3 XAP3 XAP4] RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (HBV-associated factor 4) (Heme-oxidized IRP2 ubiquitin ligase 1) (HOIL-1) (Hepatitis B virus X-associated protein 4) (RING finger protein 54) (RING-type E3 ubiquitin transferase HOIL-1) (Ubiquitin-conjugating enzyme 7-interacting protein 3)
[Traf2] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2)
[TRIM13 LEU5 RFP2 RNF77] E3 ubiquitin-protein ligase TRIM13 (EC 2.3.2.27) (B-cell chronic lymphocytic leukemia tumor suppressor Leu5) (Leukemia-associated protein 5) (Putative tumor suppressor RFP2) (RING finger protein 77) (RING-type E3 ubiquitin transferase TRIM13) (Ret finger protein 2) (Tripartite motif-containing protein 13)
[Rbck1 Rbck Ubce7ip3 Uip28] RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (Heme-oxidized IRP2 ubiquitin ligase 1 homolog) (HOIL-1) (RING-type E3 ubiquitin transferase HOIL-1) (UbcM4-interacting protein 28) (Ubiquitin-conjugating enzyme 7-interacting protein 3)
[LNX1 LNX PDZRN2 UNQ574/PRO1136] E3 ubiquitin-protein ligase LNX (EC 2.3.2.27) (Ligand of Numb-protein X 1) (Numb-binding protein 1) (PDZ domain-containing RING finger protein 2) (RING-type E3 ubiquitin transferase LNX)
[traf6 TNeu045k15.1] TNF receptor-associated factor 6 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF6) (RING-type E3 ubiquitin transferase TRAF6)
[Rbck1 Pkcbpb15 Rbck Ubce7ip3] RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC 2.3.2.31) (Heme-oxidized IRP2 ubiquitin ligase 1 homolog) (HOIL-1) (Protein kinase C-binding protein beta-15) (RBCC protein interacting with PKC) (RING-type E3 ubiquitin transferase HOIL-1) (Ubiquitin-conjugating enzyme 7-interacting protein 3)
[Peli1] E3 ubiquitin-protein ligase pellino homolog 1 (Pellino-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase pellino homolog 1)
[PELI1 PRISM] E3 ubiquitin-protein ligase pellino homolog 1 (Pellino-1) (EC 2.3.2.27) (Pellino-related intracellular-signaling molecule) (RING-type E3 ubiquitin transferase pellino homolog 1)
[TRAF7 RFWD1 RNF119] E3 ubiquitin-protein ligase TRAF7 (EC 2.3.2.27) (RING finger and WD repeat-containing protein 1) (RING finger protein 119) (RING-type E3 ubiquitin transferase TRAF7) (TNF receptor-associated factor 7)
[RNF114 ZNF228 ZNF313] E3 ubiquitin-protein ligase RNF114 (EC 2.3.2.27) (RING finger protein 114) (RING-type E3 ubiquitin transferase RNF114) (Zinc finger protein 228) (Zinc finger protein 313)
[TRAF6] TNF receptor-associated factor (EC 2.3.2.27)
[TRAF6] TNF receptor-associated factor (EC 2.3.2.27)
[PELI3] E3 ubiquitin-protein ligase pellino homolog 3 (Pellino-3) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase pellino homolog 3)
[PELI2] E3 ubiquitin-protein ligase pellino homolog 2 (Pellino-2) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase pellino homolog 2)
[Peli3] E3 ubiquitin-protein ligase pellino homolog 3 (Pellino-3) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase pellino homolog 3)
[CBL CBL2 RNF55] E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene) (Proto-oncogene c-Cbl) (RING finger protein 55) (RING-type E3 ubiquitin transferase CBL) (Signal transduction protein CBL)
[Rnf2 DinG Ring1b] E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING-type E3 ubiquitin transferase RING2)
[TRAF3IP2 C6orf2 C6orf4 C6orf5 C6orf6] E3 ubiquitin ligase TRAF3IP2 (EC 2.3.2.27) (Adapter protein CIKS) (Connection to IKK and SAPK/JNK) (E3 ubiquitin-protein ligase CIKS) (Nuclear factor NF-kappa-B activator 1) (ACT1) (TRAF3-interacting protein 2)

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