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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.
27-SEP-2017, entry version 197.
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 adaptor
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 adaptor 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 ARBB1 AND ARBB2.
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 adaptor 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 WDR34.
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]
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).
[53]
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).
[54]
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).
[55]
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).
[56]
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).
[57]
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).
[58]
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).
[59]
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.
[60]
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:8837778}.
-!- CATALYTIC ACTIVITY: 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.
-!- 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 TRAF3IP2.
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 WDR34 (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). {ECO:0000250|UniProtKB:P70196,
ECO:0000269|PubMed:25736436, ECO:0000269|PubMed:25861989}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-359276, EBI-359276;
Q8V2D1:- (xeno); NbExp=3; IntAct=EBI-359276, EBI-8622036;
P25942:CD40; NbExp=2; IntAct=EBI-359276, EBI-525714;
P99999:CYCS; NbExp=2; IntAct=EBI-359276, EBI-446479;
Q9QZH6:Ecsit (xeno); NbExp=2; IntAct=EBI-359276, EBI-527020;
Q8WWZ3:EDARADD; NbExp=5; IntAct=EBI-359276, EBI-2949647;
P40939:HADHA; NbExp=2; IntAct=EBI-359276, EBI-356720;
P14778:IL1R1; NbExp=2; IntAct=EBI-359276, EBI-525905;
P51617:IRAK1; NbExp=3; IntAct=EBI-359276, EBI-358664;
O43187:IRAK2; NbExp=3; IntAct=EBI-359276, EBI-447733;
Q9Y616:IRAK3; NbExp=3; IntAct=EBI-359276, EBI-447690;
Q9UDY8:MALT1; NbExp=5; IntAct=EBI-359276, EBI-1047372;
Q99558:MAP3K14; NbExp=2; IntAct=EBI-359276, EBI-358011;
O43318:MAP3K7; NbExp=3; IntAct=EBI-359276, EBI-358684;
P50222:MEOX2; NbExp=3; IntAct=EBI-359276, EBI-748397;
P07174:Ngfr (xeno); NbExp=2; IntAct=EBI-359276, EBI-1038810;
Q9H8W4:PLEKHF2; NbExp=3; IntAct=EBI-359276, EBI-742388;
Q9UNA4:POLI; NbExp=3; IntAct=EBI-359276, EBI-741774;
P25786:PSMA1; NbExp=2; IntAct=EBI-359276, EBI-359352;
P28074:PSMB5; NbExp=2; IntAct=EBI-359276, EBI-357828;
P62191:PSMC1; NbExp=2; IntAct=EBI-359276, EBI-357598;
P62195:PSMC5; NbExp=2; IntAct=EBI-359276, EBI-357745;
O00232:PSMD12; NbExp=2; IntAct=EBI-359276, EBI-359733;
Q9UNM6:PSMD13; NbExp=2; IntAct=EBI-359276, EBI-356070;
Q13200:PSMD2; NbExp=2; IntAct=EBI-359276, EBI-357648;
Q15008:PSMD6; NbExp=2; IntAct=EBI-359276, EBI-359701;
P51665:PSMD7; NbExp=2; IntAct=EBI-359276, EBI-357659;
Q14257:RCN2; NbExp=2; IntAct=EBI-359276, EBI-356710;
Q9BVN2-2:RUSC1; NbExp=2; IntAct=EBI-359276, EBI-6257338;
Q9NYA1:SPHK1; NbExp=2; IntAct=EBI-359276, EBI-985303;
Q13501:SQSTM1; NbExp=2; IntAct=EBI-359276, EBI-307104;
Q86VP1:TAX1BP1; NbExp=8; IntAct=EBI-359276, EBI-529518;
Q13077:TRAF1; NbExp=13; IntAct=EBI-359276, EBI-359224;
Q12933:TRAF2; NbExp=12; IntAct=EBI-359276, EBI-355744;
O43734:TRAF3IP2; NbExp=4; IntAct=EBI-359276, EBI-744798;
O00463:TRAF5; NbExp=14; IntAct=EBI-359276, EBI-523498;
P0CG48:UBC; NbExp=3; IntAct=EBI-359276, EBI-3390054;
P15732:UBC5 (xeno); NbExp=3; IntAct=EBI-359276, EBI-2097669;
P51668:UBE2D1; NbExp=2; IntAct=EBI-359276, EBI-743540;
P62837:UBE2D2; NbExp=4; IntAct=EBI-359276, EBI-347677;
P61077:UBE2D3; NbExp=3; IntAct=EBI-359276, EBI-348268;
P61088:UBE2N; NbExp=5; IntAct=EBI-359276, EBI-1052908;
O75604:USP2; NbExp=3; IntAct=EBI-359276, EBI-743272;
Q01220:VACWR178 (xeno); NbExp=2; IntAct=EBI-359276, EBI-3863691;
P55072:VCP; NbExp=2; IntAct=EBI-359276, EBI-355164;
Q8N1B4:VPS52; NbExp=5; IntAct=EBI-359276, EBI-2799833;
P98170:XIAP; NbExp=2; IntAct=EBI-359276, EBI-517127;
P07947:YES1; NbExp=5; IntAct=EBI-359276, EBI-515331;
Q8TD23:ZNF675; NbExp=4; IntAct=EBI-359276, EBI-528190;
Q9UGI0:ZRANB1; NbExp=3; IntAct=EBI-359276, EBI-527853;
-!- 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; after cell stimulation with IL-
1-beta or TGF-beta. 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). {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: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.
UniGene; Hs.444172; -.
UniGene; Hs.591983; -.
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.
PDBsum; 1LB4; -.
PDBsum; 1LB5; -.
PDBsum; 1LB6; -.
PDBsum; 2ECI; -.
PDBsum; 2JMD; -.
PDBsum; 3HCS; -.
PDBsum; 3HCT; -.
PDBsum; 3HCU; -.
PDBsum; 4Z8M; -.
ProteinModelPortal; Q9Y4K3; -.
SMR; Q9Y4K3; -.
BioGrid; 113041; 293.
CORUM; Q9Y4K3; -.
DIP; DIP-27515N; -.
ELM; Q9Y4K3; -.
IntAct; Q9Y4K3; 390.
MINT; MINT-88585; -.
STRING; 9606.ENSP00000337853; -.
BindingDB; Q9Y4K3; -.
ChEMBL; CHEMBL3588728; -.
iPTMnet; Q9Y4K3; -.
PhosphoSitePlus; Q9Y4K3; -.
BioMuta; TRAF6; -.
DMDM; 30580642; -.
EPD; Q9Y4K3; -.
MaxQB; Q9Y4K3; -.
PaxDb; Q9Y4K3; -.
PeptideAtlas; Q9Y4K3; -.
PRIDE; Q9Y4K3; -.
DNASU; 7189; -.
Ensembl; ENST00000348124; ENSP00000337853; ENSG00000175104.
Ensembl; ENST00000526995; ENSP00000433623; ENSG00000175104.
GeneID; 7189; -.
KEGG; hsa:7189; -.
UCSC; uc001mwq.3; human.
CTD; 7189; -.
DisGeNET; 7189; -.
EuPathDB; HostDB:ENSG00000175104.14; -.
GeneCards; TRAF6; -.
HGNC; HGNC:12036; TRAF6.
HPA; CAB004605; -.
HPA; HPA019805; -.
HPA; HPA020599; -.
MalaCards; TRAF6; -.
MIM; 602355; gene.
neXtProt; NX_Q9Y4K3; -.
OpenTargets; ENSG00000175104; -.
Orphanet; 1810; Autosomal dominant hypohidrotic ectodermal dysplasia.
PharmGKB; PA36713; -.
eggNOG; ENOG410ISDW; Eukaryota.
eggNOG; ENOG410XTXK; LUCA.
GeneTree; ENSGT00550000074359; -.
HOGENOM; HOG000006625; -.
HOVERGEN; HBG060248; -.
InParanoid; Q9Y4K3; -.
KO; K03175; -.
OMA; PGYKLCL; -.
OrthoDB; EOG091G0GHD; -.
PhylomeDB; Q9Y4K3; -.
TreeFam; TF321154; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-166058; MyD88:Mal cascade initiated on plasma membrane.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
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-446652; Interleukin-1 family signaling.
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-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.
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; -.
ChiTaRS; TRAF6; human.
EvolutionaryTrace; Q9Y4K3; -.
GeneWiki; TRAF6; -.
GenomeRNAi; 7189; -.
PRO; PR:Q9Y4K3; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000175104; -.
CleanEx; HS_TRAF6; -.
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:0043234; C:protein 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; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
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:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
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:0070498; P:interleukin-1-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:0002756; P:MyD88-independent 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 from RNA polymerase II promoter; 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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IEA:Ensembl.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-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:0045672; P:positive regulation of osteoclast differentiation; IDA:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; NAS:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0050870; P:positive regulation of T cell activation; IC:UniProtKB.
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 from RNA polymerase II promoter; 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:0006461; P:protein complex assembly; IEA:Ensembl.
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:0051023; P:regulation of immunoglobulin secretion; 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.
Gene3D; 2.60.210.10; -; 1.
Gene3D; 3.30.40.10; -; 4.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR012227; TNF_rcpt--assoc_TRAF.
InterPro; IPR008974; TRAF-like.
InterPro; IPR027139; TRAF6.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
InterPro; IPR001293; Znf_TRAF.
PANTHER; PTHR10131:SF103; PTHR10131:SF103; 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; Complete proteome; 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 TNF receptor-associated factor 6.
/FTId=PRO_0000056407.
DOMAIN 350 499 MATH. {ECO:0000255|PROSITE-
ProRule:PRU00129}.
ZN_FING 70 109 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 150 202 TRAF-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00207}.
ZN_FING 203 259 TRAF-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00207}.
REGION 1 354 Interaction with TAX1BP1.
{ECO:0000269|PubMed:10920205}.
REGION 355 522 Interaction with TANK.
{ECO:0000269|PubMed:25861989}.
COILED 288 348 {ECO:0000255}.
CROSSLNK 124 124 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 124 124 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:17135271}.
CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:18093978}.
CROSSLNK 453 453 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:18093978}.
MUTAGEN 57 57 D->K: Loss of interaction with UBE2N.
{ECO:0000269|PubMed:19465916}.
MUTAGEN 70 70 C->A: Loss of ligase activity,
autoubiquitination and signaling
capacity. {ECO:0000269|PubMed:17135271,
ECO:0000269|PubMed:19465916}.
MUTAGEN 72 72 I->D: Loss of interaction with UBE2N.
{ECO:0000269|PubMed:19465916}.
MUTAGEN 74 74 L->E,K: Loss of interaction with UBE2N.
{ECO:0000269|PubMed:19465916}.
MUTAGEN 88 88 R->A: Loss of TRAF6 homodimerization and
impaired polyubiquitin synthesis. Loss of
TRAF6 homodimerization and impaired
polyubiquitin synthesis; when associated
with A-122.
{ECO:0000269|PubMed:19465916}.
MUTAGEN 118 118 F->A: Loss of TRAF6 homodimerization and
impaired polyubiquitin synthesis.
{ECO:0000269|PubMed:19465916}.
MUTAGEN 118 118 F->W: Partially impaired polyubiquitin
synthesis. {ECO:0000269|PubMed:19465916}.
MUTAGEN 118 118 F->Y: Partially impaired polyubiquitin
synthesis. {ECO:0000269|PubMed:19465916}.
MUTAGEN 122 122 F->A: Loss of TRAF6 homodimerization and
partially impaired polyubiquitin
synthesis. Loss of TRAF6 homodimerization
and impaired polyubiquitin synthesis;
when associated with A-88.
{ECO:0000269|PubMed:19465916}.
MUTAGEN 124 124 K->R: Loss of SUMO1-modification and c-
myb-mediated transcriptional repressive
activation. {ECO:0000269|PubMed:17135271,
ECO:0000269|PubMed:18093978,
ECO:0000269|PubMed:19465916}.
MUTAGEN 142 142 K->R: Loss of SUMO1-modification and c-
myb-mediated transcriptional repressive
activation.
{ECO:0000269|PubMed:18093978}.
MUTAGEN 453 453 K->R: Loss of SUMO1-modification and c-
myb-mediated transcriptional repressive
activation.
{ECO:0000269|PubMed:18093978}.
CONFLICT 12 12 S -> F (in Ref. 6; AAH31052).
{ECO:0000305}.
STRAND 60 62 {ECO:0000244|PDB:3HCT}.
HELIX 66 68 {ECO:0000244|PDB:3HCT}.
TURN 71 73 {ECO:0000244|PDB:3HCT}.
STRAND 78 82 {ECO:0000244|PDB:3HCT}.
TURN 84 86 {ECO:0000244|PDB:2ECI}.
STRAND 88 90 {ECO:0000244|PDB:3HCT}.
HELIX 91 101 {ECO:0000244|PDB:3HCT}.
TURN 106 108 {ECO:0000244|PDB:3HCT}.
HELIX 114 116 {ECO:0000244|PDB:3HCT}.
HELIX 121 128 {ECO:0000244|PDB:3HCT}.
STRAND 130 133 {ECO:0000244|PDB:3HCT}.
STRAND 135 138 {ECO:0000244|PDB:3HCU}.
STRAND 142 144 {ECO:0000244|PDB:3HCT}.
HELIX 145 147 {ECO:0000244|PDB:3HCT}.
HELIX 149 151 {ECO:0000244|PDB:3HCT}.
STRAND 153 155 {ECO:0000244|PDB:3HCT}.
STRAND 158 161 {ECO:0000244|PDB:3HCS}.
TURN 163 165 {ECO:0000244|PDB:3HCS}.
STRAND 168 170 {ECO:0000244|PDB:3HCS}.
HELIX 171 173 {ECO:0000244|PDB:3HCS}.
HELIX 174 180 {ECO:0000244|PDB:3HCS}.
STRAND 186 188 {ECO:0000244|PDB:3HCS}.
TURN 190 192 {ECO:0000244|PDB:3HCS}.
STRAND 195 197 {ECO:0000244|PDB:3HCS}.
HELIX 198 200 {ECO:0000244|PDB:3HCS}.
HELIX 201 205 {ECO:0000244|PDB:3HCS}.
STRAND 351 357 {ECO:0000244|PDB:1LB6}.
HELIX 360 368 {ECO:0000244|PDB:1LB6}.
STRAND 373 376 {ECO:0000244|PDB:1LB6}.
STRAND 380 385 {ECO:0000244|PDB:1LB6}.
STRAND 388 395 {ECO:0000244|PDB:1LB6}.
TURN 401 405 {ECO:0000244|PDB:1LB6}.
STRAND 406 414 {ECO:0000244|PDB:1LB6}.
HELIX 419 421 {ECO:0000244|PDB:1LB6}.
STRAND 428 434 {ECO:0000244|PDB:1LB6}.
HELIX 440 442 {ECO:0000244|PDB:1LB4}.
STRAND 446 451 {ECO:0000244|PDB:1LB6}.
HELIX 457 459 {ECO:0000244|PDB:1LB6}.
STRAND 463 466 {ECO:0000244|PDB:1LB6}.
STRAND 468 478 {ECO:0000244|PDB:1LB6}.
HELIX 479 483 {ECO:0000244|PDB:1LB6}.
TURN 484 486 {ECO:0000244|PDB:1LB5}.
STRAND 492 500 {ECO:0000244|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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